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Entry: 5WB7
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HEADER    SIGNALING PROTEIN                       28-JUN-17   5WB7              
TITLE     CRYSTAL STRUCTURE OF THE EPIDERMAL GROWTH FACTOR RECEPTOR             
TITLE    2 EXTRACELLULAR REGION IN COMPLEX WITH EPIREGULIN                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPIDERMAL GROWTH FACTOR RECEPTOR;                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 SYNONYM: PROTO-ONCOGENE C-ERBB-1,RECEPTOR TYROSINE-PROTEIN KINASE    
COMPND   5 ERBB-1;                                                              
COMPND   6 EC: 2.7.10.1;                                                        
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: PROEPIREGULIN;                                             
COMPND  10 CHAIN: E, F, G, H;                                                   
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: EGFR, ERBB, ERBB1, HER1;                                       
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: SF9;                                       
SOURCE   9 MOL_ID: 2;                                                           
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606;                                                
SOURCE  13 GENE: EREG;                                                          
SOURCE  14 EXPRESSION_SYSTEM: DROSOPHILA MELANOGASTER;                          
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 7227;                                       
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: S2                                         
KEYWDS    RECEPTOR TYROSINE KINASE, GROWTH FACTOR, SIGNALING, MEMBRANE PROTEIN, 
KEYWDS   2 SIGNALING PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.M.FREED,N.J.BESSMAN,K.M.FERGUSON,M.A.LEMMON                         
REVDAT   3   01-NOV-17 5WB7    1       JRNL                                     
REVDAT   2   25-OCT-17 5WB7    1       JRNL                                     
REVDAT   1   18-OCT-17 5WB7    0                                                
JRNL        AUTH   D.M.FREED,N.J.BESSMAN,A.KIYATKIN,E.SALAZAR-CAVAZOS,          
JRNL        AUTH 2 P.O.BYRNE,J.O.MOORE,C.C.VALLEY,K.M.FERGUSON,D.J.LEAHY,       
JRNL        AUTH 3 D.S.LIDKE,M.A.LEMMON                                         
JRNL        TITL   EGFR LIGANDS DIFFERENTIALLY STABILIZE RECEPTOR DIMERS TO     
JRNL        TITL 2 SPECIFY SIGNALING KINETICS.                                  
JRNL        REF    CELL                          V. 171   683 2017              
JRNL        REFN                   ISSN 1097-4172                               
JRNL        PMID   28988771                                                     
JRNL        DOI    10.1016/J.CELL.2017.09.017                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.94 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.11.1_2575                                   
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 : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.94                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.68                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 53542                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.227                           
REMARK   3   R VALUE            (WORKING SET) : 0.225                           
REMARK   3   FREE R VALUE                     : 0.268                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.850                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2596                            
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 47.6906 -  7.8366    0.98     2757   144  0.2044 0.2150        
REMARK   3     2  7.8366 -  6.2245    0.99     2768   148  0.2284 0.2778        
REMARK   3     3  6.2245 -  5.4390    0.98     2718   150  0.2085 0.2335        
REMARK   3     4  5.4390 -  4.9423    0.99     2753   142  0.1919 0.2542        
REMARK   3     5  4.9423 -  4.5883    0.98     2731   147  0.1798 0.2176        
REMARK   3     6  4.5883 -  4.3180    0.98     2729   149  0.1798 0.2463        
REMARK   3     7  4.3180 -  4.1019    0.98     2711   139  0.1936 0.2369        
REMARK   3     8  4.1019 -  3.9234    0.97     2693   143  0.2047 0.2419        
REMARK   3     9  3.9234 -  3.7724    0.98     2744   119  0.2277 0.2592        
REMARK   3    10  3.7724 -  3.6423    0.98     2688   140  0.2370 0.2746        
REMARK   3    11  3.6423 -  3.5284    0.98     2721   145  0.2661 0.3173        
REMARK   3    12  3.5284 -  3.4276    0.97     2712   133  0.2668 0.3613        
REMARK   3    13  3.4276 -  3.3374    0.97     2664   129  0.2563 0.3021        
REMARK   3    14  3.3374 -  3.2560    0.97     2746   112  0.2633 0.3155        
REMARK   3    15  3.2560 -  3.1820    0.97     2704   133  0.2854 0.3216        
REMARK   3    16  3.1820 -  3.1143    0.98     2681   156  0.2979 0.3806        
REMARK   3    17  3.1143 -  3.0520    0.97     2687   124  0.3215 0.4359        
REMARK   3    18  3.0520 -  2.9944    0.93     2595   126  0.3492 0.4407        
REMARK   3    19  2.9944 -  2.9410    0.78     2144   117  0.3686 0.4682        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
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)     : 0.490            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 32.100           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 71.36                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 92.86                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.004          17485                                  
REMARK   3   ANGLE     :  0.902          23776                                  
REMARK   3   CHIRALITY :  0.065           2714                                  
REMARK   3   PLANARITY :  0.017           3061                                  
REMARK   3   DIHEDRAL  : 14.052           6664                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 2:164 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   76.945   -8.517   77.292              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5839 T22:   0.4245                                     
REMARK   3      T33:   0.4031 T12:  -0.0904                                     
REMARK   3      T13:  -0.1373 T23:   0.0136                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.9560 L22:   6.1218                                     
REMARK   3      L33:   4.1077 L12:  -2.1195                                     
REMARK   3      L13:  -1.0176 L23:   2.5209                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0350 S12:   0.1135 S13:   0.2189                       
REMARK   3      S21:  -0.2425 S22:  -0.0885 S23:   0.4289                       
REMARK   3      S31:   0.3194 S32:  -0.3422 S33:   0.0890                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 165:311 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   90.214    8.242   91.377              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8185 T22:   0.5115                                     
REMARK   3      T33:   0.7986 T12:  -0.0319                                     
REMARK   3      T13:  -0.2525 T23:  -0.1236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6993 L22:   1.0883                                     
REMARK   3      L33:   1.6391 L12:   0.2856                                     
REMARK   3      L13:  -0.0623 L23:   0.6515                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1862 S12:  -0.5061 S13:   0.7051                       
REMARK   3      S21:   0.2104 S22:   0.0623 S23:  -0.0673                       
REMARK   3      S31:  -0.0450 S32:   0.0672 S33:   0.0540                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 312:479 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  111.753  -11.616   69.822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4765 T22:   0.4384                                     
REMARK   3      T33:   0.3314 T12:  -0.0726                                     
REMARK   3      T13:  -0.0663 T23:   0.0520                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3052 L22:   2.5750                                     
REMARK   3      L33:   3.0405 L12:  -0.9326                                     
REMARK   3      L13:   0.5119 L23:  -0.1693                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0354 S12:   0.2842 S13:   0.2089                       
REMARK   3      S21:  -0.0028 S22:   0.1113 S23:  -0.1326                       
REMARK   3      S31:   0.0347 S32:  -0.0098 S33:  -0.0699                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: ( CHAIN A AND RESID 480:501 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  128.139  -22.192   75.774              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6666 T22:   0.6327                                     
REMARK   3      T33:   0.6244 T12:  -0.0573                                     
REMARK   3      T13:  -0.2626 T23:  -0.1430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.7261 L22:   7.2116                                     
REMARK   3      L33:   3.5876 L12:  -1.1431                                     
REMARK   3      L13:  -3.0421 L23:   1.7988                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3163 S12:  -0.7866 S13:   0.4059                       
REMARK   3      S21:   0.8590 S22:   0.6400 S23:  -1.9583                       
REMARK   3      S31:  -0.0411 S32:   1.0234 S33:  -0.5138                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 2:164 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   51.272  -19.720   21.624              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3179 T22:   0.3679                                     
REMARK   3      T33:   0.3401 T12:  -0.0067                                     
REMARK   3      T13:  -0.0158 T23:   0.0246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5095 L22:   6.0261                                     
REMARK   3      L33:   3.5799 L12:  -1.5624                                     
REMARK   3      L13:   0.7081 L23:   1.4341                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0574 S12:   0.1374 S13:   0.1474                       
REMARK   3      S21:  -0.1013 S22:   0.0448 S23:   0.2880                       
REMARK   3      S31:   0.1121 S32:  -0.0131 S33:  -0.0058                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 165:311 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   58.475   -3.221   40.425              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5772 T22:   0.4511                                     
REMARK   3      T33:   0.6063 T12:  -0.0193                                     
REMARK   3      T13:  -0.0460 T23:  -0.1403                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8431 L22:   2.4747                                     
REMARK   3      L33:   2.5468 L12:  -1.2251                                     
REMARK   3      L13:   1.0420 L23:   0.5864                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3982 S12:  -0.7228 S13:   1.2520                       
REMARK   3      S21:   0.1247 S22:   0.0308 S23:  -0.0137                       
REMARK   3      S31:  -0.3621 S32:  -0.2151 S33:   0.3767                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 312:479 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   85.781  -23.413   29.436              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2699 T22:   0.3559                                     
REMARK   3      T33:   0.3899 T12:   0.0091                                     
REMARK   3      T13:  -0.0633 T23:   0.0065                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1065 L22:   4.9055                                     
REMARK   3      L33:   3.9064 L12:  -0.7905                                     
REMARK   3      L13:   0.2936 L23:   0.5908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0074 S12:   0.0927 S13:   0.0857                       
REMARK   3      S21:   0.0412 S22:   0.0703 S23:  -0.4397                       
REMARK   3      S31:  -0.1698 S32:   0.0854 S33:  -0.0747                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: ( CHAIN B AND RESID 480:505 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   98.010  -35.038   44.045              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8516 T22:   0.8233                                     
REMARK   3      T33:   0.7106 T12:   0.1010                                     
REMARK   3      T13:  -0.3310 T23:  -0.0279                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0533 L22:   5.5970                                     
REMARK   3      L33:   0.7615 L12:   2.4514                                     
REMARK   3      L13:  -1.5723 L23:   0.9620                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0810 S12:  -1.1040 S13:  -0.4758                       
REMARK   3      S21:   1.1458 S22:   0.2523 S23:  -0.3410                       
REMARK   3      S31:   0.6237 S32:   0.8246 S33:  -0.1095                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: ( CHAIN C AND RESID 2:164 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   45.174   32.286   58.003              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4204 T22:   0.3451                                     
REMARK   3      T33:   0.3676 T12:  -0.0125                                     
REMARK   3      T13:   0.0554 T23:  -0.0116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.1761 L22:   7.7683                                     
REMARK   3      L33:   3.0435 L12:   1.4141                                     
REMARK   3      L13:   0.7592 L23:   2.9669                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0500 S12:  -0.0536 S13:  -0.2143                       
REMARK   3      S21:   0.4204 S22:  -0.3052 S23:   0.3064                       
REMARK   3      S31:   0.0605 S32:  -0.1820 S33:   0.3145                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 165:311 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   53.731   16.965   43.108              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6118 T22:   0.5105                                     
REMARK   3      T33:   0.7653 T12:  -0.0547                                     
REMARK   3      T13:  -0.1138 T23:  -0.1435                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5175 L22:   2.6435                                     
REMARK   3      L33:   2.2945 L12:  -3.2452                                     
REMARK   3      L13:  -1.9510 L23:   1.5888                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0495 S12:  -0.0703 S13:   0.1462                       
REMARK   3      S21:  -0.1162 S22:  -0.1433 S23:   0.2760                       
REMARK   3      S31:  -0.1552 S32:   0.1025 S33:   0.1293                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 312:479 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   79.086   35.989   64.097              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6087 T22:   0.6986                                     
REMARK   3      T33:   1.1554 T12:   0.1243                                     
REMARK   3      T13:  -0.3801 T23:  -0.2538                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.8676 L22:   3.7790                                     
REMARK   3      L33:   5.3932 L12:  -0.1845                                     
REMARK   3      L13:  -4.5254 L23:   0.8409                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0867 S12:  -1.1219 S13:   1.3542                       
REMARK   3      S21:   0.5777 S22:   0.7744 S23:  -1.3169                       
REMARK   3      S31:   0.3188 S32:   0.5961 S33:  -0.6169                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: ( CHAIN C AND RESID 480:501 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   94.681   45.808   55.434              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7801 T22:   0.8662                                     
REMARK   3      T33:   2.3999 T12:  -0.1188                                     
REMARK   3      T13:  -0.1290 T23:  -0.4754                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3948 L22:   2.6814                                     
REMARK   3      L33:   3.4979 L12:  -1.4642                                     
REMARK   3      L13:  -1.3187 L23:  -1.4231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1720 S12:  -1.1067 S13:   3.3172                       
REMARK   3      S21:  -0.2294 S22:   0.2893 S23:   1.2397                       
REMARK   3      S31:  -0.6156 S32:   0.7991 S33:  -0.5966                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 2:164 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   85.619   44.996  111.062              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0167 T22:   0.5811                                     
REMARK   3      T33:   0.4899 T12:  -0.1813                                     
REMARK   3      T13:  -0.2835 T23:   0.0068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8880 L22:   7.5543                                     
REMARK   3      L33:   1.9996 L12:   2.3195                                     
REMARK   3      L13:   0.3798 L23:   1.4982                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6135 S12:  -0.4460 S13:  -0.2284                       
REMARK   3      S21:   1.4119 S22:  -0.7663 S23:  -0.2268                       
REMARK   3      S31:   0.2202 S32:  -0.1601 S33:   0.0844                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 165:311 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):   87.366   28.565   95.073              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8529 T22:   0.5401                                     
REMARK   3      T33:   1.1105 T12:  -0.0200                                     
REMARK   3      T13:  -0.3254 T23:  -0.0869                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7247 L22:   4.6763                                     
REMARK   3      L33:   3.1470 L12:  -2.2958                                     
REMARK   3      L13:  -1.2477 L23:   2.8642                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4762 S12:   0.0068 S13:   0.1728                       
REMARK   3      S21:  -0.0369 S22:  -0.2818 S23:  -0.4465                       
REMARK   3      S31:  -0.0468 S32:  -0.1238 S33:  -0.1896                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 312:479 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  119.325   47.776  102.994              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0349 T22:   0.7951                                     
REMARK   3      T33:   2.2196 T12:   0.1080                                     
REMARK   3      T13:  -0.4382 T23:  -0.1560                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7333 L22:   3.1849                                     
REMARK   3      L33:   2.3646 L12:   0.5935                                     
REMARK   3      L13:  -1.0743 L23:   1.6068                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.6090 S12:  -0.0586 S13:  -1.8175                       
REMARK   3      S21:   0.3188 S22:   0.2915 S23:  -1.3065                       
REMARK   3      S31:   0.2345 S32:   0.6115 S33:  -0.6166                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: ( CHAIN D AND RESID 480:500 )                          
REMARK   3    ORIGIN FOR THE GROUP (A):  131.292   55.882   88.727              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7732 T22:   0.9734                                     
REMARK   3      T33:   1.8625 T12:  -0.0217                                     
REMARK   3      T13:   0.3580 T23:  -0.3907                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.0687 L22:   3.6127                                     
REMARK   3      L33:   1.6496 L12:   0.6557                                     
REMARK   3      L13:  -1.4363 L23:  -2.3387                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4530 S12:  -0.3069 S13:   0.9809                       
REMARK   3      S21:  -0.7770 S22:   0.0947 S23:  -1.2477                       
REMARK   3      S31:   0.5716 S32:   0.4752 S33:   0.2026                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: ( CHAIN E AND RESID 10:48 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   88.269  -15.188   60.450              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6994 T22:   0.7379                                     
REMARK   3      T33:   0.4927 T12:  -0.1072                                     
REMARK   3      T13:  -0.2381 T23:  -0.0287                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9090 L22:   6.3735                                     
REMARK   3      L33:   2.3068 L12:  -1.3533                                     
REMARK   3      L13:  -3.8464 L23:   0.1611                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5292 S12:   0.3419 S13:  -0.4636                       
REMARK   3      S21:  -0.0389 S22:  -0.5035 S23:   0.2320                       
REMARK   3      S31:   0.1283 S32:  -0.6532 S33:   0.0720                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: ( CHAIN F AND RESID 10:46 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   68.430  -25.961   10.903              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6590 T22:   0.7711                                     
REMARK   3      T33:   0.3115 T12:   0.0925                                     
REMARK   3      T13:   0.0054 T23:  -0.0075                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3770 L22:   7.8297                                     
REMARK   3      L33:   4.8156 L12:  -1.6194                                     
REMARK   3      L13:   3.2820 L23:  -2.2853                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1603 S12:   0.9109 S13:   0.0667                       
REMARK   3      S21:  -1.0522 S22:  -0.3048 S23:   0.2446                       
REMARK   3      S31:   0.7451 S32:   0.0498 S33:   0.2069                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: ( CHAIN G AND RESID 10:48 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):   57.630   37.570   76.174              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1189 T22:   1.2388                                     
REMARK   3      T33:   0.5433 T12:   0.1390                                     
REMARK   3      T13:  -0.0921 T23:   0.0290                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.7077 L22:   1.9166                                     
REMARK   3      L33:   2.5403 L12:   2.3399                                     
REMARK   3      L13:  -3.0941 L23:   0.4220                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0471 S12:  -2.8277 S13:   0.5320                       
REMARK   3      S21:   0.3989 S22:  -0.0723 S23:   0.0151                       
REMARK   3      S31:   1.0899 S32:   0.2222 S33:   0.1903                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: ( CHAIN H AND RESID 10:45 )                            
REMARK   3    ORIGIN FOR THE GROUP (A):  104.488   51.513  123.098              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.7410 T22:   1.3379                                     
REMARK   3      T33:   1.2548 T12:  -0.3381                                     
REMARK   3      T13:  -0.8090 T23:   0.0901                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9331 L22:   0.7707                                     
REMARK   3      L33:   0.4960 L12:   0.2568                                     
REMARK   3      L13:   0.5523 L23:  -0.3714                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4229 S12:  -0.7123 S13:   0.0840                       
REMARK   3      S21:   1.7779 S22:  -0.2689 S23:  -0.8027                       
REMARK   3      S31:  -0.5768 S32:   0.0014 S33:  -0.2024                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5WB7 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-JUN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000228702.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JUN-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.03                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53585                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.940                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY                : 2.800                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.3000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.94                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.99                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.45800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.700                              
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: EGFR DOMAINS I AND III FROM PDB ENTRY 3NJP           
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.61                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.03 M CITRIC ACID, 0.07 M BIS-TRIS      
REMARK 280  PROPANE, 16% PEG3350, PH 7.6, VAPOR DIFFUSION, HANGING DROP,        
REMARK 280  TEMPERATURE 294K                                                    
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       99.64400            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 11260 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 17.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D, E, H                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10400 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 49750 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -5.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, C, F, G                            
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     LEU A     1                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     HIS A   505                                                      
REMARK 465     HIS A   506                                                      
REMARK 465     HIS A   507                                                      
REMARK 465     LEU B     1                                                      
REMARK 465     HIS B   506                                                      
REMARK 465     HIS B   507                                                      
REMARK 465     LEU C     1                                                      
REMARK 465     HIS C   502                                                      
REMARK 465     HIS C   503                                                      
REMARK 465     HIS C   504                                                      
REMARK 465     HIS C   505                                                      
REMARK 465     HIS C   506                                                      
REMARK 465     HIS C   507                                                      
REMARK 465     LEU D     1                                                      
REMARK 465     SER D   501                                                      
REMARK 465     HIS D   502                                                      
REMARK 465     HIS D   503                                                      
REMARK 465     HIS D   504                                                      
REMARK 465     HIS D   505                                                      
REMARK 465     HIS D   506                                                      
REMARK 465     HIS D   507                                                      
REMARK 465     SER E    -7                                                      
REMARK 465     ASP E    -6                                                      
REMARK 465     ASN E    -5                                                      
REMARK 465     PRO E    -4                                                      
REMARK 465     ARG E    -3                                                      
REMARK 465     VAL E    -2                                                      
REMARK 465     ALA E    -1                                                      
REMARK 465     GLN E     0                                                      
REMARK 465     VAL E     1                                                      
REMARK 465     HIS E    49                                                      
REMARK 465     GLN E    50                                                      
REMARK 465     PRO E    51                                                      
REMARK 465     LEU E    52                                                      
REMARK 465     SER E    53                                                      
REMARK 465     LYS E    54                                                      
REMARK 465     SER F    -7                                                      
REMARK 465     ASP F    -6                                                      
REMARK 465     ASN F    -5                                                      
REMARK 465     PRO F    -4                                                      
REMARK 465     ARG F    -3                                                      
REMARK 465     VAL F    -2                                                      
REMARK 465     ALA F    -1                                                      
REMARK 465     GLN F     0                                                      
REMARK 465     VAL F     1                                                      
REMARK 465     THR F    47                                                      
REMARK 465     VAL F    48                                                      
REMARK 465     HIS F    49                                                      
REMARK 465     GLN F    50                                                      
REMARK 465     PRO F    51                                                      
REMARK 465     LEU F    52                                                      
REMARK 465     SER F    53                                                      
REMARK 465     LYS F    54                                                      
REMARK 465     SER G    -7                                                      
REMARK 465     ASP G    -6                                                      
REMARK 465     ASN G    -5                                                      
REMARK 465     PRO G    -4                                                      
REMARK 465     ARG G    -3                                                      
REMARK 465     VAL G    -2                                                      
REMARK 465     ALA G    -1                                                      
REMARK 465     GLN G     0                                                      
REMARK 465     VAL G     1                                                      
REMARK 465     HIS G    49                                                      
REMARK 465     GLN G    50                                                      
REMARK 465     PRO G    51                                                      
REMARK 465     LEU G    52                                                      
REMARK 465     SER G    53                                                      
REMARK 465     LYS G    54                                                      
REMARK 465     SER H    -7                                                      
REMARK 465     ASP H    -6                                                      
REMARK 465     ASN H    -5                                                      
REMARK 465     PRO H    -4                                                      
REMARK 465     ARG H    -3                                                      
REMARK 465     VAL H    -2                                                      
REMARK 465     ALA H    -1                                                      
REMARK 465     GLN H     0                                                      
REMARK 465     VAL H     1                                                      
REMARK 465     LEU H    46                                                      
REMARK 465     THR H    47                                                      
REMARK 465     VAL H    48                                                      
REMARK 465     HIS H    49                                                      
REMARK 465     GLN H    50                                                      
REMARK 465     PRO H    51                                                      
REMARK 465     LEU H    52                                                      
REMARK 465     SER H    53                                                      
REMARK 465     LYS H    54                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 202    CG   CD   CE   NZ                                   
REMARK 470     LEU A 245    CG   CD1  CD2                                       
REMARK 470     TYR A 251    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     GLN A 252    CG   CD   OE1  NE2                                  
REMARK 470     ASN A 256    CG   OD1  ND2                                       
REMARK 470     GLU A 258    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 269    CD   CE   NZ                                        
REMARK 470     LYS A 270    CG   CD   CE   NZ                                   
REMARK 470     HIS A 280    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 303    CD   CE   NZ                                        
REMARK 470     GLU A 306    CG   CD   OE1  OE2                                  
REMARK 470     ARG A 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU B 160    CG   CD1  CD2                                       
REMARK 470     LEU B 245    CG   CD1  CD2                                       
REMARK 470     GLN B 252    CG   CD   OE1  NE2                                  
REMARK 470     VAL B 255    CG1  CG2                                            
REMARK 470     GLU B 258    CG   CD   OE1  OE2                                  
REMARK 470     LYS B 269    CG   CD   CE   NZ                                   
REMARK 470     LYS B 270    CG   CD   CE   NZ                                   
REMARK 470     GLU B 306    CG   CD   OE1  OE2                                  
REMARK 470     GLU C   3    CG   CD   OE1  OE2                                  
REMARK 470     LYS C 105    CD   CE   NZ                                        
REMARK 470     HIS C 159    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS C 269    CG   CD   CE   NZ                                   
REMARK 470     ASP C 290    CG   OD1  OD2                                       
REMARK 470     ASP C 297    CG   OD1  OD2                                       
REMARK 470     LYS C 301    CG   CD   CE   NZ                                   
REMARK 470     LYS C 303    CG   CD   CE   NZ                                   
REMARK 470     LYS C 304    CG   CD   CE   NZ                                   
REMARK 470     ARG C 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 322    CG   CD   CE   NZ                                   
REMARK 470     LYS C 333    CG   CD   CE   NZ                                   
REMARK 470     GLN C 366    CG   CD   OE1  NE2                                  
REMARK 470     GLU C 388    CG   CD   OE1  OE2                                  
REMARK 470     ARG C 390    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C 430    CG   CD   CE   NZ                                   
REMARK 470     LYS C 443    CG   CD   CE   NZ                                   
REMARK 470     LYS C 455    CG   CD   CE   NZ                                   
REMARK 470     SER C 460    OG                                                  
REMARK 470     LYS C 465    CG   CD   CE   NZ                                   
REMARK 470     LYS D   5    CG   CD   CE   NZ                                   
REMARK 470     ASN D 104    CG   OD1  ND2                                       
REMARK 470     LYS D 105    CG   CD   CE   NZ                                   
REMARK 470     GLU D 136    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 141    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN D 158    CG   OD1  ND2                                       
REMARK 470     HIS D 159    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS D 188    CD   CE   NZ                                        
REMARK 470     GLN D 193    CG   CD   OE1  NE2                                  
REMARK 470     LYS D 202    CG   CD   CE   NZ                                   
REMARK 470     LYS D 270    CE   NZ                                             
REMARK 470     ASP D 290    CG   OD1  OD2                                       
REMARK 470     ASP D 297    CG   OD1  OD2                                       
REMARK 470     LYS D 301    CG   CD   CE   NZ                                   
REMARK 470     LYS D 304    CG   CD   CE   NZ                                   
REMARK 470     ARG D 310    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D 322    CG   CD   CE   NZ                                   
REMARK 470     LYS D 333    CG   CD   CE   NZ                                   
REMARK 470     GLN D 366    CG   CD   OE1  NE2                                  
REMARK 470     GLU D 388    CG   CD   OE1  OE2                                  
REMARK 470     LYS D 430    CG   CD   CE   NZ                                   
REMARK 470     LYS D 443    CG   CD   CE   NZ                                   
REMARK 470     LYS D 455    CG   CD   CE   NZ                                   
REMARK 470     SER D 460    OG                                                  
REMARK 470     LYS D 465    CG   CD   CE   NZ                                   
REMARK 470     GLU D 495    CG   CD   OE1  OE2                                  
REMARK 470     ARG D 497    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL D 500    CG1  CG2                                            
REMARK 470     LYS F   5    CD   CE   NZ                                        
REMARK 470     ASN F  11    CG   OD1  ND2                                       
REMARK 470     LEU F  46    CG   CD1  CD2                                       
REMARK 470     LYS G   5    CD   CE   NZ                                        
REMARK 470     GLN G  27    CG   CD   OE1  NE2                                  
REMARK 470     ARG G  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS H   5    CG   CD   CE   NZ                                   
REMARK 470     ARG H  31    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASN B   151     O5   NAG B   601              1.46            
REMARK 500   CG   ASN B   151     C1   NAG B   601              1.73            
REMARK 500   CG   ASN B   151     O5   NAG B   601              1.80            
REMARK 500   ND2  ASN B   151     O5   NAG B   601              1.86            
REMARK 500   OD1  ASP D   344     OG1  THR D   406              2.02            
REMARK 500   OH   TYR C   101     OD2  ASP G    24              2.03            
REMARK 500   O2   MAN B   607     O    HOH B   701              2.04            
REMARK 500   O    TYR H    13     NE   ARG H    40              2.07            
REMARK 500   OH   TYR B   101     OD2  ASP F    24              2.15            
REMARK 500   N    ASP C   102     O    THR C   106              2.17            
REMARK 500   NZ   LYS C     4     OE1  GLN C    59              2.18            
REMARK 500   OD1  ASN B   151     C1   NAG B   601              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   OE2  GLU A   180     O4   BMA B   605     1556     1.69            
REMARK 500   OE2  GLU A   489     OG   SER F    26     1656     1.99            
REMARK 500   NZ   LYS C    56     OD2  ASP H     9     1454     2.13            
REMARK 500   OE2  GLU D   180     NH1  ARG D   390     1455     2.19            
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    ILE A 327   N   -  CA  -  C   ANGL. DEV. = -17.9 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    LYS A  13     -119.28     57.96                                   
REMARK 500    ASN A  49       -4.10     72.91                                   
REMARK 500    SER A  92      -17.88   -151.24                                   
REMARK 500    LYS A 105        1.73     85.12                                   
REMARK 500    LEU A 116       96.60    -64.58                                   
REMARK 500    ASN A 134      -10.95     80.82                                   
REMARK 500    THR A 187       20.54   -141.48                                   
REMARK 500    LYS A 188      -53.79   -143.67                                   
REMARK 500    LYS A 229      -76.43   -137.39                                   
REMARK 500    GLU A 233     -114.99     53.32                                   
REMARK 500    ALA A 265       31.29    -91.29                                   
REMARK 500    ALA A 289     -128.89     58.46                                   
REMARK 500    MET A 294      148.05   -170.04                                   
REMARK 500    HIS A 409       27.61     49.63                                   
REMARK 500    GLN A 411      -30.53   -146.40                                   
REMARK 500    SER A 418       41.67     76.64                                   
REMARK 500    ASN A 469     -155.67    -99.61                                   
REMARK 500    GLN A 480       73.76   -107.86                                   
REMARK 500    SER B  11       42.95   -140.67                                   
REMARK 500    LYS B  13     -116.23     57.48                                   
REMARK 500    ASN B  91       16.76     56.04                                   
REMARK 500    SER B  92      -46.82   -146.00                                   
REMARK 500    ALA B 123     -159.40    -97.13                                   
REMARK 500    ASN B 134      -14.45     72.65                                   
REMARK 500    ALA B 178      -71.80    -84.10                                   
REMARK 500    LYS B 188      -57.81   -134.16                                   
REMARK 500    LYS B 229      -77.71   -134.71                                   
REMARK 500    GLU B 233     -114.68     45.07                                   
REMARK 500    ALA B 265       32.40    -98.03                                   
REMARK 500    ALA B 289     -113.32     54.05                                   
REMARK 500    ASP B 297       41.24   -153.76                                   
REMARK 500    ASN B 328     -161.40   -123.35                                   
REMARK 500    GLN B 411      -47.94   -144.97                                   
REMARK 500    ASN B 469     -157.51   -100.38                                   
REMARK 500    CYS B 486       40.29   -104.63                                   
REMARK 500    CYS B 491      137.25   -173.30                                   
REMARK 500    LYS C  13     -123.19     63.62                                   
REMARK 500    LEU C  17       78.95   -101.68                                   
REMARK 500    ASN C  91       -5.75     74.37                                   
REMARK 500    SER C  92       14.74   -154.62                                   
REMARK 500    ASN C 100       74.27   -100.02                                   
REMARK 500    LEU C 116       88.48    -69.60                                   
REMARK 500    ALA C 123     -161.98   -107.80                                   
REMARK 500    ASN C 134      -10.99     82.02                                   
REMARK 500    LEU C 149       -8.17    -59.64                                   
REMARK 500    LYS C 188      -54.09   -140.10                                   
REMARK 500    LYS C 229      -74.02   -130.41                                   
REMARK 500    GLU C 233     -112.63     52.58                                   
REMARK 500    ASN C 274       -5.15     71.97                                   
REMARK 500    HIS C 280       25.36    -77.37                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      87 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3201        
REMARK 800  bound to ASN A 32                                                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG A    
REMARK 800  3202 through MAN A 3205 bound to ASN A 328                          
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3206        
REMARK 800  bound to ASN A 389                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 3207        
REMARK 800  bound to ASN A 420                                                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 602 bound   
REMARK 800  to ASN B 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG B 601 bound   
REMARK 800  to ASN B 151                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  603 through MAN B 607 bound to ASN B 328                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG B    
REMARK 800  608 through BMA B 610 bound to ASN B 420                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG C 603 bound   
REMARK 800  to ASN C 32                                                         
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  601 through NAG C 602 bound to ASN C 151                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG C    
REMARK 800  604 through MAN C 607 bound to ASN C 328                            
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  602 through NAG D 603 bound to ASN D 32                             
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG D 601 bound   
REMARK 800  to ASN D 151                                                        
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Poly-Saccharide residues NAG D    
REMARK 800  604 through MAN D 607 bound to ASN D 328                            
DBREF  5WB7 A    1   501  UNP    P00533   EGFR_HUMAN      25    525             
DBREF  5WB7 B    1   501  UNP    P00533   EGFR_HUMAN      25    525             
DBREF  5WB7 C    1   501  UNP    P00533   EGFR_HUMAN      25    525             
DBREF  5WB7 D    1   501  UNP    P00533   EGFR_HUMAN      25    525             
DBREF  5WB7 E   -6    54  UNP    O14944   EREG_HUMAN      56    116             
DBREF  5WB7 F   -6    54  UNP    O14944   EREG_HUMAN      56    116             
DBREF  5WB7 G   -6    54  UNP    O14944   EREG_HUMAN      56    116             
DBREF  5WB7 H   -6    54  UNP    O14944   EREG_HUMAN      56    116             
SEQADV 5WB7 HIS A  502  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS A  503  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS A  504  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS A  505  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS A  506  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS A  507  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  502  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  503  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  504  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  505  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  506  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS B  507  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  502  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  503  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  504  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  505  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  506  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS C  507  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  502  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  503  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  504  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  505  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  506  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 HIS D  507  UNP  P00533              EXPRESSION TAG                 
SEQADV 5WB7 SER E   -7  UNP  O14944              EXPRESSION TAG                 
SEQADV 5WB7 SER F   -7  UNP  O14944              EXPRESSION TAG                 
SEQADV 5WB7 SER G   -7  UNP  O14944              EXPRESSION TAG                 
SEQADV 5WB7 SER H   -7  UNP  O14944              EXPRESSION TAG                 
SEQRES   1 A  507  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 A  507  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 A  507  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 A  507  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 A  507  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 A  507  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 A  507  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 A  507  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 A  507  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 A  507  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 A  507  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 A  507  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 A  507  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 A  507  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 A  507  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 A  507  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 A  507  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 A  507  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 A  507  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 A  507  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 A  507  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 A  507  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 A  507  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 A  507  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 A  507  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 A  507  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 A  507  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 A  507  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 A  507  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 A  507  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 A  507  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 A  507  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 A  507  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 A  507  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 A  507  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 A  507  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 A  507  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 A  507  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 A  507  GLU PRO ARG ASP CYS VAL SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 B  507  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 B  507  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 B  507  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 B  507  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 B  507  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 B  507  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 B  507  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 B  507  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 B  507  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 B  507  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 B  507  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 B  507  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 B  507  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 B  507  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 B  507  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 B  507  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 B  507  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 B  507  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 B  507  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 B  507  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 B  507  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 B  507  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 B  507  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 B  507  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 B  507  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 B  507  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 B  507  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 B  507  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 B  507  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 B  507  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 B  507  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 B  507  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 B  507  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 B  507  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 B  507  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 B  507  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 B  507  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 B  507  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 B  507  GLU PRO ARG ASP CYS VAL SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 C  507  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 C  507  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 C  507  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 C  507  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 C  507  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 C  507  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 C  507  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 C  507  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 C  507  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 C  507  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 C  507  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 C  507  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 C  507  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 C  507  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 C  507  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 C  507  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 C  507  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 C  507  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 C  507  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 C  507  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 C  507  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 C  507  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 C  507  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 C  507  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 C  507  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 C  507  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 C  507  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 C  507  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 C  507  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 C  507  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 C  507  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 C  507  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 C  507  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 C  507  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 C  507  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 C  507  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 C  507  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 C  507  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 C  507  GLU PRO ARG ASP CYS VAL SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 D  507  LEU GLU GLU LYS LYS VAL CYS GLN GLY THR SER ASN LYS          
SEQRES   2 D  507  LEU THR GLN LEU GLY THR PHE GLU ASP HIS PHE LEU SER          
SEQRES   3 D  507  LEU GLN ARG MET PHE ASN ASN CYS GLU VAL VAL LEU GLY          
SEQRES   4 D  507  ASN LEU GLU ILE THR TYR VAL GLN ARG ASN TYR ASP LEU          
SEQRES   5 D  507  SER PHE LEU LYS THR ILE GLN GLU VAL ALA GLY TYR VAL          
SEQRES   6 D  507  LEU ILE ALA LEU ASN THR VAL GLU ARG ILE PRO LEU GLU          
SEQRES   7 D  507  ASN LEU GLN ILE ILE ARG GLY ASN MET TYR TYR GLU ASN          
SEQRES   8 D  507  SER TYR ALA LEU ALA VAL LEU SER ASN TYR ASP ALA ASN          
SEQRES   9 D  507  LYS THR GLY LEU LYS GLU LEU PRO MET ARG ASN LEU GLN          
SEQRES  10 D  507  GLU ILE LEU HIS GLY ALA VAL ARG PHE SER ASN ASN PRO          
SEQRES  11 D  507  ALA LEU CYS ASN VAL GLU SER ILE GLN TRP ARG ASP ILE          
SEQRES  12 D  507  VAL SER SER ASP PHE LEU SER ASN MET SER MET ASP PHE          
SEQRES  13 D  507  GLN ASN HIS LEU GLY SER CYS GLN LYS CYS ASP PRO SER          
SEQRES  14 D  507  CYS PRO ASN GLY SER CYS TRP GLY ALA GLY GLU GLU ASN          
SEQRES  15 D  507  CYS GLN LYS LEU THR LYS ILE ILE CYS ALA GLN GLN CYS          
SEQRES  16 D  507  SER GLY ARG CYS ARG GLY LYS SER PRO SER ASP CYS CYS          
SEQRES  17 D  507  HIS ASN GLN CYS ALA ALA GLY CYS THR GLY PRO ARG GLU          
SEQRES  18 D  507  SER ASP CYS LEU VAL CYS ARG LYS PHE ARG ASP GLU ALA          
SEQRES  19 D  507  THR CYS LYS ASP THR CYS PRO PRO LEU MET LEU TYR ASN          
SEQRES  20 D  507  PRO THR THR TYR GLN MET ASP VAL ASN PRO GLU GLY LYS          
SEQRES  21 D  507  TYR SER PHE GLY ALA THR CYS VAL LYS LYS CYS PRO ARG          
SEQRES  22 D  507  ASN TYR VAL VAL THR ASP HIS GLY SER CYS VAL ARG ALA          
SEQRES  23 D  507  CYS GLY ALA ASP SER TYR GLU MET GLU GLU ASP GLY VAL          
SEQRES  24 D  507  ARG LYS CYS LYS LYS CYS GLU GLY PRO CYS ARG LYS VAL          
SEQRES  25 D  507  CYS ASN GLY ILE GLY ILE GLY GLU PHE LYS ASP SER LEU          
SEQRES  26 D  507  SER ILE ASN ALA THR ASN ILE LYS HIS PHE LYS ASN CYS          
SEQRES  27 D  507  THR SER ILE SER GLY ASP LEU HIS ILE LEU PRO VAL ALA          
SEQRES  28 D  507  PHE ARG GLY ASP SER PHE THR HIS THR PRO PRO LEU ASP          
SEQRES  29 D  507  PRO GLN GLU LEU ASP ILE LEU LYS THR VAL LYS GLU ILE          
SEQRES  30 D  507  THR GLY PHE LEU LEU ILE GLN ALA TRP PRO GLU ASN ARG          
SEQRES  31 D  507  THR ASP LEU HIS ALA PHE GLU ASN LEU GLU ILE ILE ARG          
SEQRES  32 D  507  GLY ARG THR LYS GLN HIS GLY GLN PHE SER LEU ALA VAL          
SEQRES  33 D  507  VAL SER LEU ASN ILE THR SER LEU GLY LEU ARG SER LEU          
SEQRES  34 D  507  LYS GLU ILE SER ASP GLY ASP VAL ILE ILE SER GLY ASN          
SEQRES  35 D  507  LYS ASN LEU CYS TYR ALA ASN THR ILE ASN TRP LYS LYS          
SEQRES  36 D  507  LEU PHE GLY THR SER GLY GLN LYS THR LYS ILE ILE SER          
SEQRES  37 D  507  ASN ARG GLY GLU ASN SER CYS LYS ALA THR GLY GLN VAL          
SEQRES  38 D  507  CYS HIS ALA LEU CYS SER PRO GLU GLY CYS TRP GLY PRO          
SEQRES  39 D  507  GLU PRO ARG ASP CYS VAL SER HIS HIS HIS HIS HIS HIS          
SEQRES   1 E   62  SER ASP ASN PRO ARG VAL ALA GLN VAL SER ILE THR LYS          
SEQRES   2 E   62  CYS SER SER ASP MET ASN GLY TYR CYS LEU HIS GLY GLN          
SEQRES   3 E   62  CYS ILE TYR LEU VAL ASP MET SER GLN ASN TYR CYS ARG          
SEQRES   4 E   62  CYS GLU VAL GLY TYR THR GLY VAL ARG CYS GLU HIS PHE          
SEQRES   5 E   62  PHE LEU THR VAL HIS GLN PRO LEU SER LYS                      
SEQRES   1 F   62  SER ASP ASN PRO ARG VAL ALA GLN VAL SER ILE THR LYS          
SEQRES   2 F   62  CYS SER SER ASP MET ASN GLY TYR CYS LEU HIS GLY GLN          
SEQRES   3 F   62  CYS ILE TYR LEU VAL ASP MET SER GLN ASN TYR CYS ARG          
SEQRES   4 F   62  CYS GLU VAL GLY TYR THR GLY VAL ARG CYS GLU HIS PHE          
SEQRES   5 F   62  PHE LEU THR VAL HIS GLN PRO LEU SER LYS                      
SEQRES   1 G   62  SER ASP ASN PRO ARG VAL ALA GLN VAL SER ILE THR LYS          
SEQRES   2 G   62  CYS SER SER ASP MET ASN GLY TYR CYS LEU HIS GLY GLN          
SEQRES   3 G   62  CYS ILE TYR LEU VAL ASP MET SER GLN ASN TYR CYS ARG          
SEQRES   4 G   62  CYS GLU VAL GLY TYR THR GLY VAL ARG CYS GLU HIS PHE          
SEQRES   5 G   62  PHE LEU THR VAL HIS GLN PRO LEU SER LYS                      
SEQRES   1 H   62  SER ASP ASN PRO ARG VAL ALA GLN VAL SER ILE THR LYS          
SEQRES   2 H   62  CYS SER SER ASP MET ASN GLY TYR CYS LEU HIS GLY GLN          
SEQRES   3 H   62  CYS ILE TYR LEU VAL ASP MET SER GLN ASN TYR CYS ARG          
SEQRES   4 H   62  CYS GLU VAL GLY TYR THR GLY VAL ARG CYS GLU HIS PHE          
SEQRES   5 H   62  PHE LEU THR VAL HIS GLN PRO LEU SER LYS                      
HET    NAG  A3201      14                                                       
HET    NAG  A3202      14                                                       
HET    NAG  A3203      14                                                       
HET    BMA  A3204      11                                                       
HET    MAN  A3205      11                                                       
HET    NAG  A3206      14                                                       
HET    NAG  A3207      14                                                       
HET    NAG  B 601      14                                                       
HET    NAG  B 602      14                                                       
HET    NAG  B 603      14                                                       
HET    NAG  B 604      14                                                       
HET    BMA  B 605      11                                                       
HET    MAN  B 606      11                                                       
HET    MAN  B 607      11                                                       
HET    NAG  B 608      14                                                       
HET    NAG  B 609      14                                                       
HET    BMA  B 610      11                                                       
HET    NAG  C 601      14                                                       
HET    NAG  C 602      14                                                       
HET    NAG  C 603      14                                                       
HET    NAG  C 604      14                                                       
HET    NAG  C 605      14                                                       
HET    BMA  C 606      11                                                       
HET    MAN  C 607      11                                                       
HET    NAG  D 601      14                                                       
HET    NAG  D 602      14                                                       
HET    NAG  D 603      14                                                       
HET    NAG  D 604      14                                                       
HET    NAG  D 605      14                                                       
HET    BMA  D 606      11                                                       
HET    MAN  D 607      11                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
FORMUL   9  NAG    21(C8 H15 N O6)                                              
FORMUL  10  BMA    5(C6 H12 O6)                                                 
FORMUL  10  MAN    5(C6 H12 O6)                                                 
FORMUL  23  HOH   *41(H2 O)                                                     
HELIX    1 AA1 THR A   19  ASN A   32  1                                  14    
HELIX    2 AA2 LEU A   52  ILE A   58  5                                   7    
HELIX    3 AA3 ASN A  134  ILE A  138  5                                   5    
HELIX    4 AA4 CYS A  170  SER A  174  5                                   5    
HELIX    5 AA5 GLY A  179  CYS A  183  5                                   5    
HELIX    6 AA6 SER A  203  CYS A  207  5                                   5    
HELIX    7 AA7 ILE A  318  LYS A  322  5                                   5    
HELIX    8 AA8 ASN A  331  LYS A  336  5                                   6    
HELIX    9 AA9 LEU A  348  GLY A  354  1                                   7    
HELIX   10 AB1 ASP A  364  VAL A  374  5                                  11    
HELIX   11 AB2 LEU A  393  GLU A  397  5                                   5    
HELIX   12 AB3 LYS A  407  GLY A  410  5                                   4    
HELIX   13 AB4 ASN A  452  PHE A  457  5                                   6    
HELIX   14 AB5 GLY A  471  THR A  478  1                                   8    
HELIX   15 AB6 THR B   19  ASN B   32  1                                  14    
HELIX   16 AB7 LEU B   52  ILE B   58  5                                   7    
HELIX   17 AB8 ASN B  134  ILE B  138  5                                   5    
HELIX   18 AB9 PHE B  148  MET B  152  5                                   5    
HELIX   19 AC1 CYS B  170  SER B  174  5                                   5    
HELIX   20 AC2 GLY B  179  CYS B  183  5                                   5    
HELIX   21 AC3 SER B  203  CYS B  207  5                                   5    
HELIX   22 AC4 ARG B  220  CYS B  224  5                                   5    
HELIX   23 AC5 ILE B  318  LYS B  322  5                                   5    
HELIX   24 AC6 ASN B  331  LYS B  336  5                                   6    
HELIX   25 AC7 LEU B  348  GLY B  354  1                                   7    
HELIX   26 AC8 ASP B  364  VAL B  374  5                                  11    
HELIX   27 AC9 LEU B  393  GLU B  397  5                                   5    
HELIX   28 AD1 LYS B  407  GLY B  410  5                                   4    
HELIX   29 AD2 ASN B  452  PHE B  457  5                                   6    
HELIX   30 AD3 GLY B  471  GLY B  479  1                                   9    
HELIX   31 AD4 THR C   19  ASN C   32  1                                  14    
HELIX   32 AD5 LEU C   52  ILE C   58  5                                   7    
HELIX   33 AD6 TYR C   88  ASN C   91  5                                   4    
HELIX   34 AD7 CYS C  170  SER C  174  5                                   5    
HELIX   35 AD8 SER C  203  CYS C  207  5                                   5    
HELIX   36 AD9 ARG C  220  CYS C  224  5                                   5    
HELIX   37 AE1 ILE C  318  LYS C  322  5                                   5    
HELIX   38 AE2 ASN C  331  LYS C  336  5                                   6    
HELIX   39 AE3 LEU C  348  GLY C  354  1                                   7    
HELIX   40 AE4 ASP C  355  HIS C  359  5                                   5    
HELIX   41 AE5 ASP C  364  VAL C  374  5                                  11    
HELIX   42 AE6 LEU C  393  GLU C  397  5                                   5    
HELIX   43 AE7 LYS C  407  GLY C  410  5                                   4    
HELIX   44 AE8 TYR C  447  ILE C  451  5                                   5    
HELIX   45 AE9 ASN C  452  LEU C  456  5                                   5    
HELIX   46 AF1 GLY C  471  THR C  478  1                                   8    
HELIX   47 AF2 THR D   19  PHE D   31  1                                  13    
HELIX   48 AF3 LEU D   52  ILE D   58  5                                   7    
HELIX   49 AF4 SER D  145  LEU D  149  5                                   5    
HELIX   50 AF5 CYS D  170  SER D  174  5                                   5    
HELIX   51 AF6 GLY D  179  CYS D  183  5                                   5    
HELIX   52 AF7 SER D  203  CYS D  207  5                                   5    
HELIX   53 AF8 ARG D  220  CYS D  224  5                                   5    
HELIX   54 AF9 ILE D  318  LYS D  322  5                                   5    
HELIX   55 AG1 ASN D  331  LYS D  336  5                                   6    
HELIX   56 AG2 LEU D  348  GLY D  354  1                                   7    
HELIX   57 AG3 ASP D  355  HIS D  359  5                                   5    
HELIX   58 AG4 ASP D  364  VAL D  374  5                                  11    
HELIX   59 AG5 LEU D  393  GLU D  397  5                                   5    
HELIX   60 AG6 LYS D  407  GLY D  410  5                                   4    
HELIX   61 AG7 ASN D  452  LEU D  456  5                                   5    
HELIX   62 AG8 GLY D  471  GLY D  479  1                                   9    
HELIX   63 AG9 GLU D  495  CYS D  499  5                                   5    
HELIX   64 AH1 SER E    7  ASN E   11  5                                   5    
SHEET    1 AA1 5 VAL A   6  CYS A   7  0                                        
SHEET    2 AA1 5 VAL A  36  VAL A  37  1  O  VAL A  36   N  CYS A   7           
SHEET    3 AA1 5 GLU A  60  VAL A  61  1  O  GLU A  60   N  VAL A  37           
SHEET    4 AA1 5 ILE A  82  ILE A  83  1  O  ILE A  82   N  VAL A  61           
SHEET    5 AA1 5 GLU A 118  ILE A 119  1  O  GLU A 118   N  ILE A  83           
SHEET    1 AA2 4 GLN A  16  LEU A  17  0                                        
SHEET    2 AA2 4 GLN E  27  CYS E  32  1  O  CYS E  32   N  GLN A  16           
SHEET    3 AA2 4 GLY E  17  LEU E  22 -1  N  ILE E  20   O  TYR E  29           
SHEET    4 AA2 4 ILE E   3  LYS E   5 -1  N  THR E   4   O  TYR E  21           
SHEET    1 AA3 5 LEU A  41  THR A  44  0                                        
SHEET    2 AA3 5 VAL A  65  ALA A  68  1  O  LEU A  66   N  ILE A  43           
SHEET    3 AA3 5 TYR A  93  LEU A  98  1  O  ALA A  96   N  VAL A  65           
SHEET    4 AA3 5 ALA A 123  SER A 127  1  O  ALA A 123   N  ALA A  94           
SHEET    5 AA3 5 SER A 153  MET A 154  1  O  SER A 153   N  VAL A 124           
SHEET    1 AA4 2 PHE A 230  ASP A 232  0                                        
SHEET    2 AA4 2 THR A 235  LYS A 237 -1  O  THR A 235   N  ASP A 232           
SHEET    1 AA5 2 MET A 244  TYR A 246  0                                        
SHEET    2 AA5 2 MET A 253  VAL A 255 -1  O  ASP A 254   N  LEU A 245           
SHEET    1 AA6 2 TYR A 261  PHE A 263  0                                        
SHEET    2 AA6 2 THR A 266  VAL A 268 -1  O  VAL A 268   N  TYR A 261           
SHEET    1 AA7 2 VAL A 276  VAL A 277  0                                        
SHEET    2 AA7 2 CYS A 283  VAL A 284 -1  O  VAL A 284   N  VAL A 276           
SHEET    1 AA8 2 SER A 291  GLU A 295  0                                        
SHEET    2 AA8 2 ARG A 300  LYS A 304 -1  O  LYS A 303   N  TYR A 292           
SHEET    1 AA9 5 CYS A 313  ASN A 314  0                                        
SHEET    2 AA9 5 SER A 340  SER A 342  1  O  SER A 342   N  CYS A 313           
SHEET    3 AA9 5 GLU A 376  ILE A 377  1  O  GLU A 376   N  ILE A 341           
SHEET    4 AA9 5 ILE A 401  ILE A 402  1  O  ILE A 401   N  ILE A 377           
SHEET    5 AA9 5 GLU A 431  ILE A 432  1  O  GLU A 431   N  ILE A 402           
SHEET    1 AB1 5 LEU A 345  ILE A 347  0                                        
SHEET    2 AB1 5 LEU A 381  ILE A 383  1  O  LEU A 382   N  LEU A 345           
SHEET    3 AB1 5 PHE A 412  VAL A 417  1  O  ALA A 415   N  ILE A 383           
SHEET    4 AB1 5 ASP A 436  SER A 440  1  O  ASP A 436   N  SER A 413           
SHEET    5 AB1 5 THR A 464  ILE A 467  1  O  LYS A 465   N  ILE A 439           
SHEET    1 AB2 5 VAL B   6  CYS B   7  0                                        
SHEET    2 AB2 5 VAL B  36  VAL B  37  1  O  VAL B  36   N  CYS B   7           
SHEET    3 AB2 5 GLU B  60  VAL B  61  1  O  GLU B  60   N  VAL B  37           
SHEET    4 AB2 5 ILE B  82  ILE B  83  1  O  ILE B  82   N  VAL B  61           
SHEET    5 AB2 5 GLU B 118  ILE B 119  1  O  GLU B 118   N  ILE B  83           
SHEET    1 AB3 4 GLN B  16  LEU B  17  0                                        
SHEET    2 AB3 4 GLN F  27  CYS F  32  1  O  CYS F  32   N  GLN B  16           
SHEET    3 AB3 4 GLY F  17  LEU F  22 -1  N  ILE F  20   O  TYR F  29           
SHEET    4 AB3 4 ILE F   3  LYS F   5 -1  N  THR F   4   O  TYR F  21           
SHEET    1 AB4 5 LEU B  41  THR B  44  0                                        
SHEET    2 AB4 5 VAL B  65  ALA B  68  1  O  LEU B  66   N  ILE B  43           
SHEET    3 AB4 5 TYR B  93  LEU B  98  1  O  ALA B  96   N  ILE B  67           
SHEET    4 AB4 5 ALA B 123  SER B 127  1  O  ALA B 123   N  ALA B  94           
SHEET    5 AB4 5 SER B 153  MET B 154  1  O  SER B 153   N  VAL B 124           
SHEET    1 AB5 4 THR B 235  LYS B 237  0                                        
SHEET    2 AB5 4 PHE B 230  ASP B 232 -1  N  ASP B 232   O  THR B 235           
SHEET    3 AB5 4 THR B 266  VAL B 268  1  O  CYS B 267   N  ARG B 231           
SHEET    4 AB5 4 TYR B 261  PHE B 263 -1  N  TYR B 261   O  VAL B 268           
SHEET    1 AB6 2 MET B 244  ASN B 247  0                                        
SHEET    2 AB6 2 GLN B 252  VAL B 255 -1  O  ASP B 254   N  LEU B 245           
SHEET    1 AB7 2 VAL B 276  VAL B 277  0                                        
SHEET    2 AB7 2 CYS B 283  VAL B 284 -1  O  VAL B 284   N  VAL B 276           
SHEET    1 AB8 2 SER B 291  GLU B 295  0                                        
SHEET    2 AB8 2 ARG B 300  LYS B 304 -1  O  LYS B 303   N  TYR B 292           
SHEET    1 AB9 5 VAL B 312  ASN B 314  0                                        
SHEET    2 AB9 5 SER B 340  SER B 342  1  O  SER B 342   N  CYS B 313           
SHEET    3 AB9 5 GLU B 376  ILE B 377  1  O  GLU B 376   N  ILE B 341           
SHEET    4 AB9 5 ILE B 401  ILE B 402  1  O  ILE B 401   N  ILE B 377           
SHEET    5 AB9 5 GLU B 431  ILE B 432  1  O  GLU B 431   N  ILE B 402           
SHEET    1 AC1 5 LEU B 345  ILE B 347  0                                        
SHEET    2 AC1 5 LEU B 381  ILE B 383  1  O  LEU B 382   N  LEU B 345           
SHEET    3 AC1 5 PHE B 412  VAL B 417  1  O  ALA B 415   N  ILE B 383           
SHEET    4 AC1 5 ASP B 436  SER B 440  1  O  ILE B 438   N  VAL B 416           
SHEET    5 AC1 5 THR B 464  ILE B 467  1  O  LYS B 465   N  ILE B 439           
SHEET    1 AC2 5 VAL C   6  CYS C   7  0                                        
SHEET    2 AC2 5 VAL C  36  VAL C  37  1  O  VAL C  36   N  CYS C   7           
SHEET    3 AC2 5 GLU C  60  VAL C  61  1  O  GLU C  60   N  VAL C  37           
SHEET    4 AC2 5 ILE C  82  ILE C  83  1  O  ILE C  82   N  VAL C  61           
SHEET    5 AC2 5 GLU C 118  ILE C 119  1  O  GLU C 118   N  ILE C  83           
SHEET    1 AC3 5 LEU C  41  THR C  44  0                                        
SHEET    2 AC3 5 VAL C  65  ALA C  68  1  O  LEU C  66   N  ILE C  43           
SHEET    3 AC3 5 TYR C  93  LEU C  98  1  O  ALA C  96   N  ILE C  67           
SHEET    4 AC3 5 ALA C 123  SER C 127  1  O  ARG C 125   N  VAL C  97           
SHEET    5 AC3 5 SER C 153  MET C 154  1  O  SER C 153   N  VAL C 124           
SHEET    1 AC4 2 PHE C 230  ASP C 232  0                                        
SHEET    2 AC4 2 THR C 235  LYS C 237 -1  O  THR C 235   N  ASP C 232           
SHEET    1 AC5 2 MET C 244  TYR C 246  0                                        
SHEET    2 AC5 2 MET C 253  VAL C 255 -1  O  ASP C 254   N  LEU C 245           
SHEET    1 AC6 2 TYR C 261  PHE C 263  0                                        
SHEET    2 AC6 2 THR C 266  VAL C 268 -1  O  VAL C 268   N  TYR C 261           
SHEET    1 AC7 2 GLU C 295  GLU C 296  0                                        
SHEET    2 AC7 2 VAL C 299  ARG C 300 -1  O  VAL C 299   N  GLU C 296           
SHEET    1 AC8 5 VAL C 312  ASN C 314  0                                        
SHEET    2 AC8 5 SER C 340  SER C 342  1  O  SER C 342   N  CYS C 313           
SHEET    3 AC8 5 GLU C 376  ILE C 377  1  O  GLU C 376   N  ILE C 341           
SHEET    4 AC8 5 ILE C 401  ILE C 402  1  O  ILE C 401   N  ILE C 377           
SHEET    5 AC8 5 GLU C 431  ILE C 432  1  O  GLU C 431   N  ILE C 402           
SHEET    1 AC9 5 LEU C 345  ILE C 347  0                                        
SHEET    2 AC9 5 LEU C 381  ILE C 383  1  O  LEU C 382   N  LEU C 345           
SHEET    3 AC9 5 PHE C 412  VAL C 417  1  O  ALA C 415   N  ILE C 383           
SHEET    4 AC9 5 ASP C 436  SER C 440  1  O  ASP C 436   N  SER C 413           
SHEET    5 AC9 5 THR C 464  ILE C 467  1  O  LYS C 465   N  VAL C 437           
SHEET    1 AD1 5 VAL D   6  CYS D   7  0                                        
SHEET    2 AD1 5 VAL D  36  VAL D  37  1  O  VAL D  36   N  CYS D   7           
SHEET    3 AD1 5 GLU D  60  VAL D  61  1  O  GLU D  60   N  VAL D  37           
SHEET    4 AD1 5 ILE D  82  ILE D  83  1  O  ILE D  82   N  VAL D  61           
SHEET    5 AD1 5 GLU D 118  ILE D 119  1  O  GLU D 118   N  ILE D  83           
SHEET    1 AD2 5 LEU D  41  THR D  44  0                                        
SHEET    2 AD2 5 VAL D  65  ALA D  68  1  O  LEU D  66   N  ILE D  43           
SHEET    3 AD2 5 TYR D  93  LEU D  98  1  O  ALA D  96   N  ILE D  67           
SHEET    4 AD2 5 ALA D 123  SER D 127  1  O  ALA D 123   N  ALA D  94           
SHEET    5 AD2 5 SER D 153  MET D 154  1  O  SER D 153   N  VAL D 124           
SHEET    1 AD3 4 THR D 235  LYS D 237  0                                        
SHEET    2 AD3 4 PHE D 230  ASP D 232 -1  N  PHE D 230   O  LYS D 237           
SHEET    3 AD3 4 THR D 266  VAL D 268  1  O  CYS D 267   N  ARG D 231           
SHEET    4 AD3 4 TYR D 261  PHE D 263 -1  N  PHE D 263   O  THR D 266           
SHEET    1 AD4 2 MET D 244  TYR D 246  0                                        
SHEET    2 AD4 2 MET D 253  VAL D 255 -1  O  ASP D 254   N  LEU D 245           
SHEET    1 AD5 2 VAL D 276  VAL D 277  0                                        
SHEET    2 AD5 2 CYS D 283  VAL D 284 -1  O  VAL D 284   N  VAL D 276           
SHEET    1 AD6 2 GLU D 295  GLU D 296  0                                        
SHEET    2 AD6 2 VAL D 299  ARG D 300 -1  O  VAL D 299   N  GLU D 296           
SHEET    1 AD7 5 CYS D 313  ASN D 314  0                                        
SHEET    2 AD7 5 SER D 340  SER D 342  1  O  SER D 342   N  CYS D 313           
SHEET    3 AD7 5 GLU D 376  ILE D 377  1  O  GLU D 376   N  ILE D 341           
SHEET    4 AD7 5 ILE D 401  ILE D 402  1  O  ILE D 401   N  ILE D 377           
SHEET    5 AD7 5 GLU D 431  ILE D 432  1  O  GLU D 431   N  ILE D 402           
SHEET    1 AD8 5 LEU D 345  ILE D 347  0                                        
SHEET    2 AD8 5 LEU D 381  ILE D 383  1  O  LEU D 382   N  LEU D 345           
SHEET    3 AD8 5 PHE D 412  VAL D 417  1  O  ALA D 415   N  ILE D 383           
SHEET    4 AD8 5 ASP D 436  SER D 440  1  O  ASP D 436   N  SER D 413           
SHEET    5 AD8 5 THR D 464  ILE D 467  1  O  LYS D 465   N  VAL D 437           
SHEET    1 AD9 2 TYR E  36  THR E  37  0                                        
SHEET    2 AD9 2 HIS E  43  PHE E  44 -1  O  HIS E  43   N  THR E  37           
SHEET    1 AE1 2 TYR F  36  THR F  37  0                                        
SHEET    2 AE1 2 HIS F  43  PHE F  44 -1  O  HIS F  43   N  THR F  37           
SHEET    1 AE2 3 THR G   4  LYS G   5  0                                        
SHEET    2 AE2 3 GLY G  17  LEU G  22 -1  O  TYR G  21   N  THR G   4           
SHEET    3 AE2 3 GLN G  27  CYS G  32 -1  O  TYR G  29   N  ILE G  20           
SHEET    1 AE3 2 TYR G  36  THR G  37  0                                        
SHEET    2 AE3 2 HIS G  43  PHE G  44 -1  O  HIS G  43   N  THR G  37           
SHEET    1 AE4 3 ILE H   3  LYS H   5  0                                        
SHEET    2 AE4 3 GLY H  17  LEU H  22 -1  O  TYR H  21   N  THR H   4           
SHEET    3 AE4 3 GLN H  27  CYS H  32 -1  O  TYR H  29   N  ILE H  20           
SHEET    1 AE5 2 TYR H  36  THR H  37  0                                        
SHEET    2 AE5 2 HIS H  43  PHE H  44 -1  O  HIS H  43   N  THR H  37           
SSBOND   1 CYS A    7    CYS A   34                          1555   1555  2.03  
SSBOND   2 CYS A  133    CYS A  163                          1555   1555  2.03  
SSBOND   3 CYS A  166    CYS A  175                          1555   1555  2.03  
SSBOND   4 CYS A  170    CYS A  183                          1555   1555  2.03  
SSBOND   5 CYS A  191    CYS A  199                          1555   1555  2.03  
SSBOND   6 CYS A  195    CYS A  207                          1555   1555  2.03  
SSBOND   7 CYS A  208    CYS A  216                          1555   1555  2.03  
SSBOND   8 CYS A  212    CYS A  224                          1555   1555  2.03  
SSBOND   9 CYS A  227    CYS A  236                          1555   1555  2.03  
SSBOND  10 CYS A  240    CYS A  267                          1555   1555  2.03  
SSBOND  11 CYS A  271    CYS A  283                          1555   1555  2.03  
SSBOND  12 CYS A  287    CYS A  302                          1555   1555  2.03  
SSBOND  13 CYS A  305    CYS A  309                          1555   1555  2.03  
SSBOND  14 CYS A  313    CYS A  338                          1555   1555  2.02  
SSBOND  15 CYS A  446    CYS A  475                          1555   1555  2.03  
SSBOND  16 CYS A  482    CYS A  491                          1555   1555  2.03  
SSBOND  17 CYS A  486    CYS A  499                          1555   1555  2.01  
SSBOND  18 CYS B    7    CYS B   34                          1555   1555  2.03  
SSBOND  19 CYS B  133    CYS B  163                          1555   1555  2.02  
SSBOND  20 CYS B  166    CYS B  175                          1555   1555  2.03  
SSBOND  21 CYS B  170    CYS B  183                          1555   1555  2.03  
SSBOND  22 CYS B  191    CYS B  199                          1555   1555  2.03  
SSBOND  23 CYS B  195    CYS B  207                          1555   1555  2.03  
SSBOND  24 CYS B  208    CYS B  216                          1555   1555  2.03  
SSBOND  25 CYS B  212    CYS B  224                          1555   1555  2.03  
SSBOND  26 CYS B  227    CYS B  236                          1555   1555  2.03  
SSBOND  27 CYS B  240    CYS B  267                          1555   1555  2.03  
SSBOND  28 CYS B  271    CYS B  283                          1555   1555  2.03  
SSBOND  29 CYS B  287    CYS B  302                          1555   1555  2.02  
SSBOND  30 CYS B  305    CYS B  309                          1555   1555  2.04  
SSBOND  31 CYS B  313    CYS B  338                          1555   1555  2.03  
SSBOND  32 CYS B  446    CYS B  475                          1555   1555  2.03  
SSBOND  33 CYS B  482    CYS B  491                          1555   1555  2.03  
SSBOND  34 CYS B  486    CYS B  499                          1555   1555  2.03  
SSBOND  35 CYS C    7    CYS C   34                          1555   1555  2.03  
SSBOND  36 CYS C  133    CYS C  163                          1555   1555  2.03  
SSBOND  37 CYS C  166    CYS C  175                          1555   1555  2.03  
SSBOND  38 CYS C  170    CYS C  183                          1555   1555  2.03  
SSBOND  39 CYS C  191    CYS C  199                          1555   1555  2.03  
SSBOND  40 CYS C  195    CYS C  207                          1555   1555  2.03  
SSBOND  41 CYS C  208    CYS C  216                          1555   1555  2.03  
SSBOND  42 CYS C  212    CYS C  224                          1555   1555  2.03  
SSBOND  43 CYS C  227    CYS C  236                          1555   1555  2.03  
SSBOND  44 CYS C  240    CYS C  267                          1555   1555  2.03  
SSBOND  45 CYS C  271    CYS C  283                          1555   1555  2.03  
SSBOND  46 CYS C  287    CYS C  302                          1555   1555  2.03  
SSBOND  47 CYS C  305    CYS C  309                          1555   1555  2.04  
SSBOND  48 CYS C  313    CYS C  338                          1555   1555  2.02  
SSBOND  49 CYS C  446    CYS C  475                          1555   1555  2.02  
SSBOND  50 CYS C  482    CYS C  491                          1555   1555  2.03  
SSBOND  51 CYS C  486    CYS C  499                          1555   1555  2.03  
SSBOND  52 CYS D    7    CYS D   34                          1555   1555  2.02  
SSBOND  53 CYS D  133    CYS D  163                          1555   1555  2.03  
SSBOND  54 CYS D  166    CYS D  175                          1555   1555  2.03  
SSBOND  55 CYS D  170    CYS D  183                          1555   1555  2.03  
SSBOND  56 CYS D  191    CYS D  199                          1555   1555  2.02  
SSBOND  57 CYS D  195    CYS D  207                          1555   1555  2.03  
SSBOND  58 CYS D  208    CYS D  216                          1555   1555  2.03  
SSBOND  59 CYS D  212    CYS D  224                          1555   1555  2.03  
SSBOND  60 CYS D  227    CYS D  236                          1555   1555  2.03  
SSBOND  61 CYS D  240    CYS D  267                          1555   1555  2.03  
SSBOND  62 CYS D  271    CYS D  283                          1555   1555  2.03  
SSBOND  63 CYS D  287    CYS D  302                          1555   1555  2.03  
SSBOND  64 CYS D  305    CYS D  309                          1555   1555  2.03  
SSBOND  65 CYS D  313    CYS D  338                          1555   1555  2.03  
SSBOND  66 CYS D  446    CYS D  475                          1555   1555  2.04  
SSBOND  67 CYS D  482    CYS D  491                          1555   1555  2.03  
SSBOND  68 CYS D  486    CYS D  499                          1555   1555  2.03  
SSBOND  69 CYS E    6    CYS E   19                          1555   1555  2.03  
SSBOND  70 CYS E   14    CYS E   30                          1555   1555  2.03  
SSBOND  71 CYS E   32    CYS E   41                          1555   1555  2.03  
SSBOND  72 CYS F    6    CYS F   19                          1555   1555  2.03  
SSBOND  73 CYS F   14    CYS F   30                          1555   1555  2.03  
SSBOND  74 CYS F   32    CYS F   41                          1555   1555  2.03  
SSBOND  75 CYS G    6    CYS G   19                          1555   1555  2.03  
SSBOND  76 CYS G   14    CYS G   30                          1555   1555  2.03  
SSBOND  77 CYS G   32    CYS G   41                          1555   1555  2.03  
SSBOND  78 CYS H    6    CYS H   19                          1555   1555  2.03  
SSBOND  79 CYS H   14    CYS H   30                          1555   1555  2.03  
SSBOND  80 CYS H   32    CYS H   41                          1555   1555  2.03  
LINK         ND2 ASN A  32                 C1  NAG A3201     1555   1555  1.44  
LINK         ND2 ASN A 328                 C1  NAG A3202     1555   1555  1.49  
LINK         ND2 ASN A 389                 C1  NAG A3206     1555   1555  1.44  
LINK         ND2 ASN A 420                 C1  NAG A3207     1555   1555  1.44  
LINK         ND2 ASN B  32                 C1  NAG B 602     1555   1555  1.44  
LINK         ND2 ASN B 151                 C1  NAG B 601     1555   1555  1.42  
LINK         ND2 ASN B 328                 C1  NAG B 603     1555   1555  1.50  
LINK         ND2 ASN B 420                 C1  NAG B 608     1555   1555  1.49  
LINK         ND2 ASN C  32                 C1  NAG C 603     1555   1555  1.44  
LINK         ND2 ASN C 151                 C1  NAG C 601     1555   1555  1.48  
LINK         ND2 ASN C 328                 C1  NAG C 604     1555   1555  1.49  
LINK         ND2 ASN D  32                 C1  NAG D 602     1555   1555  1.49  
LINK         ND2 ASN D 151                 C1  NAG D 601     1555   1555  1.44  
LINK         ND2 ASN D 328                 C1  NAG D 604     1555   1555  1.50  
LINK         O4  NAG A3202                 C1  NAG A3203     1555   1555  1.44  
LINK         O4  NAG A3203                 C1  BMA A3204     1555   1555  1.44  
LINK         O3  BMA A3204                 C1  MAN A3205     1555   1555  1.44  
LINK         O4  NAG B 603                 C1  NAG B 604     1555   1555  1.44  
LINK         O4  NAG B 604                 C1  BMA B 605     1555   1555  1.44  
LINK         O3  BMA B 605                 C1  MAN B 606     1555   1555  1.46  
LINK         O6  BMA B 605                 C1  MAN B 607     1555   1555  1.44  
LINK         O4  NAG B 608                 C1  NAG B 609     1555   1555  1.44  
LINK         O4  NAG B 609                 C1  BMA B 610     1555   1555  1.44  
LINK         O4  NAG C 601                 C1  NAG C 602     1555   1555  1.43  
LINK         O4  NAG C 604                 C1  NAG C 605     1555   1555  1.44  
LINK         O4  NAG C 605                 C1  BMA C 606     1555   1555  1.44  
LINK         O3  BMA C 606                 C1  MAN C 607     1555   1555  1.44  
LINK         O4  NAG D 602                 C1  NAG D 603     1555   1555  1.44  
LINK         O4  NAG D 604                 C1  NAG D 605     1555   1555  1.44  
LINK         O4  NAG D 605                 C1  BMA D 606     1555   1555  1.44  
LINK         O3  BMA D 606                 C1  MAN D 607     1555   1555  1.44  
SITE     1 AC1  3 GLN A  28  ASN A  32  ASN A  33                               
SITE     1 AC2 10 ASN A  91  PHE A 321  ASP A 323  SER A 324                    
SITE     2 AC2 10 LEU A 325  ASN A 328  ASN A 331  VAL A 350                    
SITE     3 AC2 10 THR A 358  THR A 360                                          
SITE     1 AC3  1 ASN A 389                                                     
SITE     1 AC4  2 GLU A 388  ASN A 420                                          
SITE     1 AC5  4 GLN B  28  ASN B  32  ASN B  33  HOH B 710                    
SITE     1 AC6  1 ASN B 151                                                     
SITE     1 AC7 12 GLU A 180  PHE B 321  ASP B 323  SER B 324                    
SITE     2 AC7 12 LEU B 325  SER B 326  ASN B 328  VAL B 350                    
SITE     3 AC7 12 ASP B 355  THR B 358  THR B 360  HOH B 701                    
SITE     1 AC8  4 GLU B 388  ASN B 420  THR B 422  ASN B 444                    
SITE     1 AC9  2 ASN C  32  ASN C  33                                          
SITE     1 AD1  3 ASN C  91  SER C  92  ASN C 151                               
SITE     1 AD2  8 ASP C 323  SER C 324  LEU C 325  ASN C 328                    
SITE     2 AD2  8 ASN C 331  THR C 358  THR C 360  HOH C 707                    
SITE     1 AD3  2 ASN D  32  ASN D  33                                          
SITE     1 AD4  1 ASN D 151                                                     
SITE     1 AD5  7 ASP D 323  SER D 324  LEU D 325  ASN D 328                    
SITE     2 AD5  7 ASN D 331  THR D 358  THR D 360                               
CRYST1   76.647  199.288   87.916  90.00  96.74  90.00 P 1 21 1      8          
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      0.013047  0.000000  0.001541        0.00000                         
SCALE2      0.000000  0.005018  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011454        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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