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Entry: 3T3P
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HEADER    CELL ADHESION                           25-JUL-11   3T3P              
TITLE     A NOVEL HIGH AFFINITY INTEGRIN ALPHAIIBBETA3 RECEPTOR ANTAGONIST THAT 
TITLE    2 UNEXPECTEDLY DISPLACES MG2+ FROM THE BETA3 MIDAS                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: UNP RESIDUES 32-488;                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: INTEGRIN BETA-3;                                           
COMPND   8 CHAIN: B, D;                                                         
COMPND   9 FRAGMENT: UNP RESIDUES 27-498;                                       
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MOL_ID: 3;                                                           
COMPND  12 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  13 CHAIN: E, H;                                                         
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 4;                                                           
COMPND  16 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  17 CHAIN: F, L;                                                         
COMPND  18 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: ITGA2B, GP2B, ITGAB;                                           
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ITGB3, GP3A;                                                   
SOURCE  13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  15 MOL_ID: 3;                                                           
SOURCE  16 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  17 ORGANISM_COMMON: MOUSE;                                              
SOURCE  18 ORGANISM_TAXID: 10090;                                               
SOURCE  19 MOL_ID: 4;                                                           
SOURCE  20 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  21 ORGANISM_COMMON: MOUSE;                                              
SOURCE  22 ORGANISM_TAXID: 10090                                                
KEYWDS    INTEGRIN, CELL ADHESION, BLOOD CLOTTING, FIBRINOGEN, PLATELET         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.ZHU,J.ZHU,T.A.SPRINGER                                              
REVDAT   1   28-MAR-12 3T3P    0                                                
JRNL        AUTH   J.ZHU,W.S.CHOI,J.G.MCCOY,A.NEGRI,J.ZHU,S.NAINI,J.LI,M.SHEN,  
JRNL        AUTH 2 W.HUANG,D.BOUGIE,M.RASMUSSEN,R.ASTER,C.J.THOMAS,M.FILIZOLA,  
JRNL        AUTH 3 T.A.SPRINGER,B.S.COLLER                                      
JRNL        TITL   STRUCTURE-GUIDED DESIGN OF A HIGH-AFFINITY PLATELET INTEGRIN 
JRNL        TITL 2 ALPHAIIBBETA3 RECEPTOR ANTAGONIST THAT DISRUPTS MG2+ BINDING 
JRNL        TITL 3 TO THE MIDAS                                                 
JRNL        REF    SCI TRANSL MED                V.   4 5RA32 2012              
JRNL        REFN                   ISSN 1946-6234                               
JRNL        PMID   22422993                                                     
JRNL        DOI    10.1126/SCITRANSLMED.3003576                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.1_743)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.39                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 199280                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.189                           
REMARK   3   FREE R VALUE                     : 0.220                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.500                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 991                             
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 48.3986 -  4.2077    0.99    29172   148  0.1694 0.1914        
REMARK   3     2  4.2077 -  3.3400    0.99    28515   147  0.1698 0.2033        
REMARK   3     3  3.3400 -  2.9179    0.99    28275   164  0.1853 0.2050        
REMARK   3     4  2.9179 -  2.6511    1.00    28282   131  0.1958 0.2370        
REMARK   3     5  2.6511 -  2.4611    1.00    28243   140  0.2180 0.2650        
REMARK   3     6  2.4611 -  2.3160    1.00    28117   132  0.2389 0.2709        
REMARK   3     7  2.3160 -  2.2000    0.98    27685   129  0.2701 0.3270        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.40                                          
REMARK   3   B_SOL              : 40.00                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.700            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.370           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.27750                                             
REMARK   3    B22 (A**2) : 13.77460                                             
REMARK   3    B33 (A**2) : 13.83080                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
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      :  0.009          21749                                  
REMARK   3   ANGLE     :  0.850          29744                                  
REMARK   3   CHIRALITY :  0.052           3280                                  
REMARK   3   PLANARITY :  0.004           3825                                  
REMARK   3   DIHEDRAL  : 14.543           7897                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 18                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: chain A and resid 1:450                                
REMARK   3    ORIGIN FOR THE GROUP (A):  51.1300  90.6727  54.3053              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1110 T22:  -0.3990                                     
REMARK   3      T33:  -0.2010 T12:   0.0409                                     
REMARK   3      T13:   0.1980 T23:   0.1452                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0345 L22:   0.0611                                     
REMARK   3      L33:   0.0683 L12:   0.0008                                     
REMARK   3      L13:  -0.0329 L23:   0.0411                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0102 S12:  -0.0825 S13:  -0.0353                       
REMARK   3      S21:   0.0968 S22:  -0.0235 S23:   0.0877                       
REMARK   3      S31:   0.1419 S32:  -0.0909 S33:  -0.1230                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain C and resid 1:450                                
REMARK   3    ORIGIN FOR THE GROUP (A):  84.8740  86.9672 117.9781              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.1061 T22:   0.2293                                     
REMARK   3      T33:  -0.1678 T12:   0.1014                                     
REMARK   3      T13:   0.2384 T23:  -0.0333                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1216 L22:   0.1558                                     
REMARK   3      L33:   0.3417 L12:   0.0174                                     
REMARK   3      L13:  -0.0737 L23:  -0.0234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0503 S12:   0.0913 S13:  -0.0638                       
REMARK   3      S21:  -0.1178 S22:   0.0091 S23:  -0.1813                       
REMARK   3      S31:   0.1619 S32:   0.3108 S33:   0.0296                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain B and resid 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 123.7801  88.7332  35.1695              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4183 T22:   0.9474                                     
REMARK   3      T33:   0.6438 T12:   0.3067                                     
REMARK   3      T13:  -0.0011 T23:  -0.1408                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.9657 L22:   4.9349                                     
REMARK   3      L33:   1.4760 L12:  -1.0271                                     
REMARK   3      L13:  -0.8755 L23:  -0.6823                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2084 S12:   0.0060 S13:  -0.6187                       
REMARK   3      S21:  -0.1877 S22:  -0.1222 S23:  -1.0363                       
REMARK   3      S31:   0.2515 S32:   0.3339 S33:   0.3228                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: chain B and (resid 58:107 or resid 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A): 101.5006 107.9434  52.8595              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1140 T22:   0.3902                                     
REMARK   3      T33:   0.3141 T12:   0.0672                                     
REMARK   3      T13:  -0.0517 T23:  -0.1163                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0601 L22:   1.0923                                     
REMARK   3      L33:   1.1977 L12:  -0.5379                                     
REMARK   3      L13:  -0.4986 L23:   0.3974                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0338 S12:  -0.0052 S13:   0.1576                       
REMARK   3      S21:   0.0150 S22:   0.0423 S23:  -0.0959                       
REMARK   3      S31:   0.0411 S32:   0.1446 S33:  -0.0566                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain B and resid 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  68.1358 118.8061  63.8023              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0080 T22:  -0.2051                                     
REMARK   3      T33:   0.0171 T12:   0.0176                                     
REMARK   3      T13:   0.0477 T23:  -0.0326                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1640 L22:   0.1986                                     
REMARK   3      L33:   0.1437 L12:  -0.1055                                     
REMARK   3      L13:  -0.0652 L23:   0.0271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0464 S12:  -0.0354 S13:   0.1171                       
REMARK   3      S21:   0.0243 S22:   0.0361 S23:  -0.0483                       
REMARK   3      S31:  -0.1032 S32:   0.0344 S33:   0.0996                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and resid 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A): 117.5010  90.3532  19.8517              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2912 T22:   0.7528                                     
REMARK   3      T33:   0.5023 T12:   0.1691                                     
REMARK   3      T13:   0.0832 T23:  -0.0899                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8150 L22:   3.6415                                     
REMARK   3      L33:   4.9664 L12:   0.3334                                     
REMARK   3      L13:  -2.1042 L23:  -2.1995                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0887 S12:  -0.1741 S13:  -0.1110                       
REMARK   3      S21:  -0.3868 S22:   0.0494 S23:  -0.9285                       
REMARK   3      S31:   0.1069 S32:   0.2016 S33:  -0.1393                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain D and resid 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5145  70.6928 141.0641              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4418 T22:   0.6083                                     
REMARK   3      T33:   0.4342 T12:  -0.3195                                     
REMARK   3      T13:   0.0626 T23:  -0.0122                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.0415 L22:   4.7360                                     
REMARK   3      L33:   1.8488 L12:   0.9524                                     
REMARK   3      L13:  -1.1770 L23:  -1.0849                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1849 S12:  -0.0253 S13:  -0.7064                       
REMARK   3      S21:  -0.0480 S22:   0.1148 S23:   0.6681                       
REMARK   3      S31:   0.2482 S32:  -0.2452 S33:   0.0440                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: chain D and (resid 58:107 or resid 354:432)            
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6803  87.5761 116.0653              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1904 T22:   0.4901                                     
REMARK   3      T33:   0.1529 T12:  -0.1716                                     
REMARK   3      T13:  -0.0116 T23:   0.0655                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0094 L22:   0.3178                                     
REMARK   3      L33:   3.0520 L12:   0.2168                                     
REMARK   3      L13:  -0.9019 L23:  -0.6588                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0917 S12:   0.1660 S13:  -0.0328                       
REMARK   3      S21:  -0.0476 S22:   0.0318 S23:   0.0074                       
REMARK   3      S31:   0.1448 S32:  -0.1752 S33:   0.0372                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain D and resid 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  60.9133 102.6524  99.5730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0904 T22:   0.2466                                     
REMARK   3      T33:  -0.0435 T12:  -0.0721                                     
REMARK   3      T13:   0.0478 T23:   0.1068                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2123 L22:   0.1816                                     
REMARK   3      L33:   0.5261 L12:  -0.0402                                     
REMARK   3      L13:   0.0294 L23:  -0.0527                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0073 S12:   0.1353 S13:   0.0853                       
REMARK   3      S21:  -0.0820 S22:   0.0316 S23:   0.0272                       
REMARK   3      S31:  -0.0764 S32:  -0.1410 S33:  -0.0775                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain D and resid 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.5643  80.5564 153.7085              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1802 T22:   0.3382                                     
REMARK   3      T33:   0.2739 T12:  -0.1238                                     
REMARK   3      T13:   0.0715 T23:  -0.0134                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.5701 L22:   4.1000                                     
REMARK   3      L33:   1.2041 L12:   1.2830                                     
REMARK   3      L13:  -0.5479 L23:   1.0230                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0058 S12:  -0.0233 S13:   0.0026                       
REMARK   3      S21:   0.1105 S22:   0.2406 S23:   0.4118                       
REMARK   3      S31:   0.0803 S32:  -0.2909 S33:  -0.2494                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain H and resid 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3847  96.9792  82.7917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3252 T22:   0.4289                                     
REMARK   3      T33:   0.2151 T12:   0.0141                                     
REMARK   3      T13:   0.1490 T23:  -0.0750                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6123 L22:   0.3045                                     
REMARK   3      L33:   2.0494 L12:   0.3983                                     
REMARK   3      L13:  -0.3725 L23:  -0.5264                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1413 S12:  -0.4464 S13:  -0.0065                       
REMARK   3      S21:   0.4342 S22:   0.0732 S23:   0.1920                       
REMARK   3      S31:   0.1015 S32:  -0.0086 S33:   0.0505                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain H and resid 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.6762  81.5543  93.4142              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4041 T22:   0.4868                                     
REMARK   3      T33:   1.1394 T12:   0.0823                                     
REMARK   3      T13:   0.2039 T23:   0.1641                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4640 L22:   0.7850                                     
REMARK   3      L33:   4.4357 L12:  -0.0981                                     
REMARK   3      L13:   0.9319 L23:   1.2248                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0187 S12:  -0.3435 S13:  -1.1221                       
REMARK   3      S21:   0.2138 S22:   0.0142 S23:   0.0746                       
REMARK   3      S31:   0.6843 S32:  -0.1549 S33:  -0.0427                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain L and resid 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   6.8917  96.1019  64.5145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0848 T22:   0.4169                                     
REMARK   3      T33:   0.3429 T12:  -0.0084                                     
REMARK   3      T13:   0.0811 T23:  -0.1250                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5907 L22:   0.3026                                     
REMARK   3      L33:   0.4104 L12:   0.1617                                     
REMARK   3      L13:  -0.0590 L23:  -0.1645                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0608 S12:   0.1752 S13:  -0.1713                       
REMARK   3      S21:   0.0129 S22:  -0.0210 S23:   0.2982                       
REMARK   3      S31:   0.0966 S32:  -0.3205 S33:   0.0071                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain L and resid 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.0736  93.5481  86.6806              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1460 T22:   0.4800                                     
REMARK   3      T33:   0.5755 T12:   0.0110                                     
REMARK   3      T13:   0.1723 T23:   0.0014                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3280 L22:   0.6033                                     
REMARK   3      L33:   2.3618 L12:   0.0948                                     
REMARK   3      L13:  -0.6156 L23:   0.1840                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0926 S12:  -0.0383 S13:  -0.2490                       
REMARK   3      S21:   0.0555 S22:  -0.0145 S23:   0.0824                       
REMARK   3      S31:   0.1464 S32:  -0.0993 S33:   0.1071                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain E and resid 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 115.5604  90.3136  86.5574              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5941 T22:   0.6559                                     
REMARK   3      T33:   0.3731 T12:  -0.0871                                     
REMARK   3      T13:   0.2694 T23:  -0.0128                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6300 L22:   0.6002                                     
REMARK   3      L33:   3.4031 L12:  -0.8788                                     
REMARK   3      L13:  -0.9564 L23:   1.1138                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1919 S12:   0.4681 S13:  -0.2678                       
REMARK   3      S21:  -0.3509 S22:  -0.0593 S23:  -0.1181                       
REMARK   3      S31:   0.6525 S32:  -0.0475 S33:   0.2973                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain E and resid 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 151.4353  82.9927  80.0385              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9147 T22:   1.1268                                     
REMARK   3      T33:   1.1023 T12:   0.3202                                     
REMARK   3      T13:   0.2816 T23:   0.1210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1436 L22:   3.7941                                     
REMARK   3      L33:   3.3905 L12:  -0.1935                                     
REMARK   3      L13:   0.7826 L23:   2.0382                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2198 S12:   1.1242 S13:  -0.7982                       
REMARK   3      S21:  -0.3155 S22:  -0.1196 S23:  -1.0255                       
REMARK   3      S31:   0.5760 S32:   1.2000 S33:  -0.1019                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain F and resid 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 125.8902 100.5827 102.5532              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1840 T22:   0.6480                                     
REMARK   3      T33:   0.5571 T12:  -0.0546                                     
REMARK   3      T13:   0.1482 T23:   0.0179                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2792 L22:   0.2825                                     
REMARK   3      L33:   0.2763 L12:   0.2564                                     
REMARK   3      L13:   0.4093 L23:   0.1034                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0312 S12:  -0.0724 S13:   0.0886                       
REMARK   3      S21:  -0.0779 S22:  -0.0050 S23:  -0.4562                       
REMARK   3      S31:   0.0187 S32:   0.3655 S33:  -0.0055                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain F and resid 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 154.8666  98.9069  80.6566              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7721 T22:   1.2149                                     
REMARK   3      T33:   1.1278 T12:   0.1657                                     
REMARK   3      T13:   0.3641 T23:   0.3062                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0184 L22:   2.2580                                     
REMARK   3      L33:   5.6044 L12:   1.3399                                     
REMARK   3      L13:  -1.9952 L23:   1.7295                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0004 S12:   0.3091 S13:   0.0944                       
REMARK   3      S21:  -0.8932 S22:   0.2842 S23:  -0.9231                       
REMARK   3      S31:  -0.2536 S32:   1.2454 S33:  -0.2919                       
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 3T3P COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-SEP-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066997.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.9                                
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) : 1.0332                             
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 300 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 199292                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.32                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.96                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 0.2 M AMMONIUM SULFATE,    
REMARK 280  0.1 M TRIS-HCL, PH 8.9, VAPOR DIFFUSION, HANGING DROP,              
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000      129.76650            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.62850            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      129.76650            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.62850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 APPLY THE FOLLOWING TO CHAINS: A, B, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, H, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   455                                                      
REMARK 465     ALA A   456                                                      
REMARK 465     SER A   457                                                      
REMARK 465     LEU B   467                                                      
REMARK 465     GLY B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     GLN B   470                                                      
REMARK 465     CYS B   471                                                      
REMARK 465     GLU B   472                                                      
REMARK 465     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
REMARK 465     GLU D   472                                                      
REMARK 465     GLY E   135                                                      
REMARK 465     ASP E   136                                                      
REMARK 465     THR E   137                                                      
REMARK 465     THR E   138                                                      
REMARK 465     GLY E   139                                                      
REMARK 465     GLY E   220                                                      
REMARK 465     PRO E   221                                                      
REMARK 465     GLY H   135                                                      
REMARK 465     ASP H   136                                                      
REMARK 465     THR H   137                                                      
REMARK 465     GLY H   220                                                      
REMARK 465     PRO H   221                                                      
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     GLU B  174   CG   CD   OE1  OE2                                  
REMARK 480     LYS D  350   CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1282     O    HOH A  1284              1.70            
REMARK 500   O    HOH A   475     O    HOH A  1141              1.75            
REMARK 500   O    HOH A   484     O    HOH A  1234              1.77            
REMARK 500   O    HOH C  1237     O    HOH C  1287              1.78            
REMARK 500   O    HOH A  1127     O    HOH A  1234              1.84            
REMARK 500   O    HOH A   593     O    HOH A  1154              1.88            
REMARK 500   O    HOH L   216     O    HOH L  1197              1.89            
REMARK 500   O    HOH A  1280     O    HOH A  1282              1.91            
REMARK 500   O    HOH C  1247     O    HOH D  1117              1.96            
REMARK 500   O    HOH A  1282     O    HOH A  1288              1.96            
REMARK 500   O    HOH D   513     O    HOH D  1126              2.01            
REMARK 500   O    HOH B   563     O    HOH B  1213              2.02            
REMARK 500   O    HOH C   926     O    HOH D  1171              2.02            
REMARK 500   O    HOH C   510     O    HOH C  1135              2.02            
REMARK 500   O    HOH A  1128     O    HOH A  1188              2.05            
REMARK 500   O    HOH A   518     O    HOH A   593              2.05            
REMARK 500   O    HOH B   935     O    HOH B  1136              2.05            
REMARK 500   O    HOH A  1280     O    HOH A  1281              2.06            
REMARK 500   O    HOH A   517     O    HOH B   673              2.07            
REMARK 500   ND2  ASN D   371     C2   NAG D  3371              2.08            
REMARK 500   O    HOH B   555     O    HOH B  1166              2.08            
REMARK 500   O    HOH C   970     O    HOH C  1291              2.10            
REMARK 500   O    HOH D  1158     O    HOH D  1160              2.10            
REMARK 500   O    HOH A   669     O    HOH A  1162              2.12            
REMARK 500   O    HOH A  1128     O    HOH A  1190              2.14            
REMARK 500   O    HOH C   929     O    HOH C  1131              2.14            
REMARK 500   O    HOH A   604     O    HOH D  1238              2.14            
REMARK 500   O4   SO4 A   460     O    HOH A   691              2.14            
REMARK 500   O    HOH A   517     O    HOH A  1111              2.15            
REMARK 500   O    HOH A  1151     O    HOH B  1113              2.15            
REMARK 500   O    HOH A   566     O    HOH A  1279              2.15            
REMARK 500   O    HOH C   586     O    HOH C  1179              2.16            
REMARK 500   O    HOH L  1132     O    HOH L  1175              2.18            
REMARK 500   O    HOH A   928     O    HOH A  1122              2.18            
REMARK 500   O    HOH A   928     O    HOH A  1110              2.18            
REMARK 500   O    HOH B   541     O    HOH B   925              2.18            
REMARK 500   O    HOH A   859     O    HOH A   977              2.18            
REMARK 500   O    HOH C  1148     O    HOH C  1236              2.19            
REMARK 500   O    HOH B   526     O    HOH B  1264              2.19            
REMARK 500   OG   SER F   201     O    SER F   203              2.19            
REMARK 500   O    HOH A   592     O    HOH B   974              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  46       28.58    -79.39                                   
REMARK 500    SER A 101     -128.70     52.47                                   
REMARK 500    LYS A 118     -115.43     57.33                                   
REMARK 500    GLU A 123      135.70     98.03                                   
REMARK 500    LEU A 212      -44.64     74.49                                   
REMARK 500    SER A 222     -167.50    -77.49                                   
REMARK 500    ASP A 319       39.38     75.51                                   
REMARK 500    PRO A 337      104.85    -58.32                                   
REMARK 500    PHE A 417      117.03    -38.54                                   
REMARK 500    PHE B  56       79.56   -161.89                                   
REMARK 500    ASP B  66       43.67   -144.56                                   
REMARK 500    ASP B  76      165.88     65.47                                   
REMARK 500    SER B  77       62.13   -100.33                                   
REMARK 500    VAL B 157      -80.77   -127.38                                   
REMARK 500    MET B 180     -164.45   -100.84                                   
REMARK 500    SER B 213     -160.85   -122.71                                   
REMARK 500    ASP B 241       77.03   -109.67                                   
REMARK 500    LEU B 258       -9.60     87.02                                   
REMARK 500    LEU B 375      -94.39     48.51                                   
REMARK 500    ASN B 377       18.70     45.59                                   
REMARK 500    SER C 101     -128.70     54.28                                   
REMARK 500    LYS C 118     -115.88     60.86                                   
REMARK 500    GLU C 123      135.51     98.33                                   
REMARK 500    LEU C 212      -52.04     76.68                                   
REMARK 500    SER C 222     -174.58    -69.06                                   
REMARK 500    ALA D  30       40.72    -95.77                                   
REMARK 500    ASP D  47       35.66    -87.00                                   
REMARK 500    ASN D  48       16.78     55.50                                   
REMARK 500    PHE D  56       81.94   -161.01                                   
REMARK 500    ASP D  66       40.19   -144.62                                   
REMARK 500    VAL D 157      -77.09   -130.68                                   
REMARK 500    PRO D 169     -175.83    -69.35                                   
REMARK 500    SER D 213     -163.21   -120.96                                   
REMARK 500    ASP D 241       74.75   -108.23                                   
REMARK 500    LEU D 258      -13.97     94.18                                   
REMARK 500    CYS D 374     -123.06    -97.69                                   
REMARK 500    ASN D 376     -136.84     58.95                                   
REMARK 500    ASN E  55      -18.93   -162.84                                   
REMARK 500    PHE E 152      141.10   -171.93                                   
REMARK 500    SER E 167       94.77    -66.20                                   
REMARK 500    SER F  43     -158.98    -85.63                                   
REMARK 500    SER F  77       75.31     57.51                                   
REMARK 500    SER F 127       33.53    -91.59                                   
REMARK 500    LEU F 136       78.06   -117.11                                   
REMARK 500    ASN F 138       82.70     57.99                                   
REMARK 500    PRO F 141     -168.62    -72.71                                   
REMARK 500    LEU F 181     -169.26   -167.71                                   
REMARK 500    GLU F 187       36.75    -77.32                                   
REMARK 500    ASN F 190      -52.24   -125.65                                   
REMARK 500    ALA F 196      124.79   -171.47                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      64 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 245   OD2                                                    
REMARK 620 2 THR A 250   O   166.0                                              
REMARK 620 3 GLU A 243   OE1 119.4  74.5                                        
REMARK 620 4 THR A 250   OG1  87.2  79.1 146.4                                  
REMARK 620 5 GLU A 243   OE2  64.5 129.4  54.9 146.0                            
REMARK 620 6 GLU A 252   OE2  89.2  83.1 126.4  69.3 125.1                      
REMARK 620 7 ASP A 247   O    89.8  90.1  82.5  77.1  84.1 146.4                
REMARK 620 8 GLU A 252   OE1  80.6 103.3  87.1 119.3  76.1  51.5 160.2          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 220   OE2                                                    
REMARK 620 2 SER B 121   OG   91.8                                              
REMARK 620 3 HOH B 477   O   106.0  70.2                                        
REMARK 620 4 HOH B1120   O    78.2 101.6 170.6                                  
REMARK 620 5 HOH B1121   O    94.9 166.4  96.5  91.4                            
REMARK 620 6 HOH B 920   O   168.5  86.8  84.3  90.9  89.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 217   OD1                                                    
REMARK 620 2 PRO D 219   O   102.3                                              
REMARK 620 3 GLU D 220   OE1 163.9  78.2                                        
REMARK 620 4 ASN D 215   OD1  91.0 163.3  86.2                                  
REMARK 620 5 ASP D 158   OD2  96.2  87.2  99.9 101.5                            
REMARK 620 6 ASP D 217   O    73.8  85.7  90.2  88.4 166.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU D 220   OE2                                                    
REMARK 620 2 SER D 121   OG   92.7                                              
REMARK 620 3 HOH D1118   O   113.4  72.4                                        
REMARK 620 4 HOH D 476   O    89.4 172.9 100.6                                  
REMARK 620 5 HOH D1126   O    79.9  99.0 164.0  88.0                            
REMARK 620 6 HOH D1115   O   167.0  92.5  79.6  87.0  87.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ARG C 303   O                                                      
REMARK 620 2 ASN C 299   OD1 154.8                                              
REMARK 620 3 ASP C 297   OD1  77.7  77.6                                        
REMARK 620 4 ASP C 305   OD2  92.4  90.2  84.4                                  
REMARK 620 5 ASP C 305   OD1  92.6 108.5 135.1  51.9                            
REMARK 620 6 ASP C 301   OD1  88.1  81.1  76.0 159.8 148.2                      
REMARK 620 7 HOH C1134   O   113.9  87.5 156.0 114.7  67.5  83.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 371   O                                                      
REMARK 620 2 ASP A 367   OD1 158.7                                              
REMARK 620 3 ASP A 365   OD2  74.2  84.6                                        
REMARK 620 4 ASP A 369   OD1  90.1  86.2  77.0                                  
REMARK 620 5 ASP A 373   OD2  82.6 111.4 130.9 146.6                            
REMARK 620 6 ASP A 373   OD1  91.7  85.9  87.2 162.9  50.4                      
REMARK 620 7 HOH A 486   O   103.2  96.5 154.9  78.0  72.1 118.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 127   OD1                                                    
REMARK 620 2 MET D 335   O    90.9                                              
REMARK 620 3 ASP D 126   OD1  78.1 126.0                                        
REMARK 620 4 SER D 123   O    91.9 161.9  72.1                                  
REMARK 620 5 ASP D 126   OD2  91.0  76.5  51.4 121.3                            
REMARK 620 6 HOH D 509   O   177.6  90.7  99.5  87.1  87.5                      
REMARK 620 7 HOH D 488   O    98.0  78.4 154.9  83.4 153.5  84.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 432   O                                                      
REMARK 620 2 ASP C 428   OD1 151.2                                              
REMARK 620 3 ASN C 430   OD1  88.2  86.8                                        
REMARK 620 4 ASP C 434   OD2  86.3 116.5 135.5                                  
REMARK 620 5 ASP C 426   OD1  77.3  74.1  85.9 135.2                            
REMARK 620 6 ASP C 434   OD1  98.7  83.3 169.5  53.4  87.9                      
REMARK 620 7 HOH C 478   O   127.4  78.6  75.9  72.9 147.9 105.5                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 250   O                                                      
REMARK 620 2 ASP C 245   OD2 165.4                                              
REMARK 620 3 GLU C 243   OE1  76.7 114.8                                        
REMARK 620 4 ASP C 247   O    88.6  84.0  83.3                                  
REMARK 620 5 GLU C 243   OE2 131.7  60.3  55.1  85.3                            
REMARK 620 6 THR C 250   OG1  84.6  81.0 147.9  70.3 136.3                      
REMARK 620 7 GLU C 252   OE2  91.5  86.4 134.4 141.1 121.6  71.0                
REMARK 620 8 GLU C 252   OE1 115.8  73.9  94.0 154.2  72.4 117.7  51.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ARG A 303   O   160.5                                              
REMARK 620 3 ASP A 297   OD1  84.9  75.6                                        
REMARK 620 4 ASP A 305   OD2  88.2  90.4  83.6                                  
REMARK 620 5 ASP A 305   OD1 112.9  80.8 128.4  51.1                            
REMARK 620 6 ASP A 301   OD1  88.5  86.8  78.4 161.9 145.2                      
REMARK 620 7 HOH A 478   O    90.4 107.3 157.4 118.4  73.6  79.4                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 371   O                                                      
REMARK 620 2 ASP C 365   OD2  75.7                                              
REMARK 620 3 ASP C 367   OD1 152.4  77.9                                        
REMARK 620 4 ASP C 369   OD1  91.4  78.9  75.8                                  
REMARK 620 5 ASP C 373   OD2  85.5 134.9 119.3 143.1                            
REMARK 620 6 ASP C 373   OD1  93.8  87.9  92.9 164.1  52.4                      
REMARK 620 7 HOH C 494   O    97.8 150.2 101.2  72.1  71.9 121.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 217   OD1                                                    
REMARK 620 2 PRO B 219   O   103.6                                              
REMARK 620 3 ASN B 215   OD1  86.9 168.2                                        
REMARK 620 4 ASP B 217   O    76.3  89.8  87.4                                  
REMARK 620 5 ASP B 158   OD2  94.2  84.3 100.6 167.4                            
REMARK 620 6 GLU B 220   OE1 170.1  80.1  88.7  94.6  95.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 432   O                                                      
REMARK 620 2 ASP A 428   OD1 156.8                                              
REMARK 620 3 ASP A 426   OD1  79.2  78.0                                        
REMARK 620 4 ASP A 434   OD1  95.1  90.7  93.7                                  
REMARK 620 5 ASN A 430   OD1  86.2  86.6  82.8 175.9                            
REMARK 620 6 ASP A 434   OD2  79.5 121.2 138.1  53.0 131.0                      
REMARK 620 7 HOH A 467   O   127.3  72.6 145.9 103.4  78.7  73.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 MET B 335   O    87.9                                              
REMARK 620 3 ASP B 126   OD1  85.3 124.8                                        
REMARK 620 4 SER B 123   O    94.7 160.2  75.0                                  
REMARK 620 5 ASP B 126   OD2  93.6  74.2  51.7 125.0                            
REMARK 620 6 HOH B 525   O   175.8  94.4  90.5  84.3  83.7                      
REMARK 620 7 HOH B 502   O    93.8  77.0 158.0  83.2 150.0  90.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 473                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3324                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 461                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 462                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 473                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: EC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 L 215                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3NID   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NIF   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NIG   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3T3M   RELATED DB: PDB                                   
DBREF  3T3P A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3T3P B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3T3P C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3T3P D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
SEQRES   1 A  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 A  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 A  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 A  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 A  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 A  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 A  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 A  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 A  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 A  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 A  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 A  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 A  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 A  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 A  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 A  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 A  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 A  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 A  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 A  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 A  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 A  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 A  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 A  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 A  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 A  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 A  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 A  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 A  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 A  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 A  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 A  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 A  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 A  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 A  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 A  457  ALA SER                                                      
SEQRES   1 B  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  472  SER GLN CYS GLU                                              
SEQRES   1 C  457  LEU ASN LEU ASP PRO VAL GLN LEU THR PHE TYR ALA GLY          
SEQRES   2 C  457  PRO ASN GLY SER GLN PHE GLY PHE SER LEU ASP PHE HIS          
SEQRES   3 C  457  LYS ASP SER HIS GLY ARG VAL ALA ILE VAL VAL GLY ALA          
SEQRES   4 C  457  PRO ARG THR LEU GLY PRO SER GLN GLU GLU THR GLY GLY          
SEQRES   5 C  457  VAL PHE LEU CYS PRO TRP ARG ALA GLU GLY GLY GLN CYS          
SEQRES   6 C  457  PRO SER LEU LEU PHE ASP LEU ARG ASP GLU THR ARG ASN          
SEQRES   7 C  457  VAL GLY SER GLN THR LEU GLN THR PHE LYS ALA ARG GLN          
SEQRES   8 C  457  GLY LEU GLY ALA SER VAL VAL SER TRP SER ASP VAL ILE          
SEQRES   9 C  457  VAL ALA CYS ALA PRO TRP GLN HIS TRP ASN VAL LEU GLU          
SEQRES  10 C  457  LYS THR GLU GLU ALA GLU LYS THR PRO VAL GLY SER CYS          
SEQRES  11 C  457  PHE LEU ALA GLN PRO GLU SER GLY ARG ARG ALA GLU TYR          
SEQRES  12 C  457  SER PRO CYS ARG GLY ASN THR LEU SER ARG ILE TYR VAL          
SEQRES  13 C  457  GLU ASN ASP PHE SER TRP ASP LYS ARG TYR CYS GLU ALA          
SEQRES  14 C  457  GLY PHE SER SER VAL VAL THR GLN ALA GLY GLU LEU VAL          
SEQRES  15 C  457  LEU GLY ALA PRO GLY GLY TYR TYR PHE LEU GLY LEU LEU          
SEQRES  16 C  457  ALA GLN ALA PRO VAL ALA ASP ILE PHE SER SER TYR ARG          
SEQRES  17 C  457  PRO GLY ILE LEU LEU TRP HIS VAL SER SER GLN SER LEU          
SEQRES  18 C  457  SER PHE ASP SER SER ASN PRO GLU TYR PHE ASP GLY TYR          
SEQRES  19 C  457  TRP GLY TYR SER VAL ALA VAL GLY GLU PHE ASP GLY ASP          
SEQRES  20 C  457  LEU ASN THR THR GLU TYR VAL VAL GLY ALA PRO THR TRP          
SEQRES  21 C  457  SER TRP THR LEU GLY ALA VAL GLU ILE LEU ASP SER TYR          
SEQRES  22 C  457  TYR GLN ARG LEU HIS ARG LEU ARG GLY GLU GLN MET ALA          
SEQRES  23 C  457  SER TYR PHE GLY HIS SER VAL ALA VAL THR ASP VAL ASN          
SEQRES  24 C  457  GLY ASP GLY ARG HIS ASP LEU LEU VAL GLY ALA PRO LEU          
SEQRES  25 C  457  TYR MET GLU SER ARG ALA ASP ARG LYS LEU ALA GLU VAL          
SEQRES  26 C  457  GLY ARG VAL TYR LEU PHE LEU GLN PRO ARG GLY PRO HIS          
SEQRES  27 C  457  ALA LEU GLY ALA PRO SER LEU LEU LEU THR GLY THR GLN          
SEQRES  28 C  457  LEU TYR GLY ARG PHE GLY SER ALA ILE ALA PRO LEU GLY          
SEQRES  29 C  457  ASP LEU ASP ARG ASP GLY TYR ASN ASP ILE ALA VAL ALA          
SEQRES  30 C  457  ALA PRO TYR GLY GLY PRO SER GLY ARG GLY GLN VAL LEU          
SEQRES  31 C  457  VAL PHE LEU GLY GLN SER GLU GLY LEU ARG SER ARG PRO          
SEQRES  32 C  457  SER GLN VAL LEU ASP SER PRO PHE PRO THR GLY SER ALA          
SEQRES  33 C  457  PHE GLY PHE SER LEU ARG GLY ALA VAL ASP ILE ASP ASP          
SEQRES  34 C  457  ASN GLY TYR PRO ASP LEU ILE VAL GLY ALA TYR GLY ALA          
SEQRES  35 C  457  ASN GLN VAL ALA VAL TYR ARG ALA GLN PRO VAL VAL LYS          
SEQRES  36 C  457  ALA SER                                                      
SEQRES   1 D  472  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  472  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  472  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  472  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  472  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  472  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  472  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  472  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  472  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  472  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  472  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  472  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  472  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  472  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  472  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  472  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  472  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  472  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  472  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  472  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  472  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  472  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  472  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  472  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  472  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  472  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  472  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  472  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  472  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  472  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  472  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  472  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  472  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  472  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  472  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  472  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  472  SER GLN CYS GLU                                              
SEQRES   1 E  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 E  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 E  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 E  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 E  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 E  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 E  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 E  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 E  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 E  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 E  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 E  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 E  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 E  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 E  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 E  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 E  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 F  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 F  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 F  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 F  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 F  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 F  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 F  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 F  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 F  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 F  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 F  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 F  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 F  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 F  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 F  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 F  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 F  214  PHE ASN ARG ASN GLU CYS                                      
SEQRES   1 H  221  GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS          
SEQRES   2 H  221  PRO GLY ALA SER VAL LYS LEU SER CYS THR ALA SER GLY          
SEQRES   3 H  221  PHE ASN ILE LYS ASP THR TYR VAL HIS TRP VAL LYS GLN          
SEQRES   4 H  221  ARG PRO GLU GLN GLY LEU GLU TRP ILE GLY ARG ILE ASP          
SEQRES   5 H  221  PRO ALA ASN GLY TYR THR LYS TYR ASP PRO LYS PHE GLN          
SEQRES   6 H  221  GLY LYS ALA THR ILE THR ALA ASP THR SER SER ASN THR          
SEQRES   7 H  221  ALA TYR LEU GLN LEU SER SER LEU THR SER GLU ASP THR          
SEQRES   8 H  221  ALA VAL TYR TYR CYS VAL ARG PRO LEU TYR ASP TYR TYR          
SEQRES   9 H  221  ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR VAL          
SEQRES  10 H  221  SER SER ALA LYS THR THR ALA PRO SER VAL TYR PRO LEU          
SEQRES  11 H  221  ALA PRO VAL CYS GLY ASP THR THR GLY SER SER VAL THR          
SEQRES  12 H  221  LEU GLY CYS LEU VAL LYS GLY TYR PHE PRO GLU PRO VAL          
SEQRES  13 H  221  THR LEU THR TRP ASN SER GLY SER LEU SER SER GLY VAL          
SEQRES  14 H  221  HIS THR PHE PRO ALA VAL LEU GLN SER ASP LEU TYR THR          
SEQRES  15 H  221  LEU SER SER SER VAL THR VAL THR SER SER THR TRP PRO          
SEQRES  16 H  221  SER GLN SER ILE THR CYS ASN VAL ALA HIS PRO ALA SER          
SEQRES  17 H  221  SER THR LYS VAL ASP LYS LYS ILE GLU PRO ARG GLY PRO          
SEQRES   1 L  214  ASP ILE LEU MET THR GLN SER PRO SER SER MET SER VAL          
SEQRES   2 L  214  SER LEU GLY ASP THR VAL SER ILE THR CYS HIS ALA SER          
SEQRES   3 L  214  GLN GLY ILE SER SER ASN ILE GLY TRP LEU GLN GLN LYS          
SEQRES   4 L  214  PRO GLY LYS SER PHE MET GLY LEU ILE TYR TYR GLY THR          
SEQRES   5 L  214  ASN LEU VAL ASP GLY VAL PRO SER ARG PHE SER GLY SER          
SEQRES   6 L  214  GLY SER GLY ALA ASP TYR SER LEU THR ILE SER SER LEU          
SEQRES   7 L  214  ASP SER GLU ASP PHE ALA ASP TYR TYR CYS VAL GLN TYR          
SEQRES   8 L  214  ALA GLN LEU PRO TYR THR PHE GLY GLY GLY THR LYS LEU          
SEQRES   9 L  214  GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE          
SEQRES  10 L  214  PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA          
SEQRES  11 L  214  SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP          
SEQRES  12 L  214  ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN          
SEQRES  13 L  214  ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR          
SEQRES  15 L  214  LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU          
SEQRES  16 L  214  ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER          
SEQRES  17 L  214  PHE ASN ARG ASN GLU CYS                                      
MODRES 3T3P ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3P ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3P ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3P ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3P ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3P ASN B  320  ASN  GLYCOSYLATION SITE                                 
HET    SO4  A 458       5                                                       
HET    SO4  A 459       5                                                       
HET    SO4  A 460       5                                                       
HET    GOL  A 461       6                                                       
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET     CL  B 473       1                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    BMA  B3322      11                                                       
HET    MAN  B3323      11                                                       
HET    MAN  B3324      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET    SO4  C 458       5                                                       
HET    SO4  C 459       5                                                       
HET    SO4  C 460       5                                                       
HET     CL  C 461       1                                                       
HET     CL  C 462       1                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET     CL  D 473       1                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3099      14                                                       
HET    NAG  D3320      14                                                       
HET    NAG  D3321      14                                                       
HET    BMA  D3322      11                                                       
HET    MAN  D3323      11                                                       
HET    NAG  D3371      14                                                       
HET    NAG  D3372      14                                                       
HET    SO4  L 215       5                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM      CA CALCIUM ION                                                      
HETNAM      CL CHLORIDE ION                                                     
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9  SO4    7(O4 S 2-)                                                   
FORMUL  12  GOL    C3 H8 O3                                                     
FORMUL  13   CA    12(CA 2+)                                                    
FORMUL  17   CL    4(CL 1-)                                                     
FORMUL  18   MG    2(MG 2+)                                                     
FORMUL  21  NAG    10(C8 H15 N O6)                                              
FORMUL  22  BMA    2(C6 H12 O6)                                                 
FORMUL  22  MAN    3(C6 H12 O6)                                                 
FORMUL  41  HOH   *1291(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 ASN B    3  ARG B    8  1                                   6    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
HELIX    9   9 LEU B   40  ASP B   47  1                                   8    
HELIX   10  10 ALA B   50  GLU B   52  5                                   3    
HELIX   11  11 SER B  121  SER B  123  5                                   3    
HELIX   12  12 MET B  124  ILE B  131  1                                   8    
HELIX   13  13 ASN B  133  ARG B  143  1                                  11    
HELIX   14  14 PRO B  169  ASN B  175  1                                   7    
HELIX   15  15 GLN B  199  GLN B  210  1                                  12    
HELIX   16  16 GLY B  221  CYS B  232  1                                  12    
HELIX   17  17 CYS B  232  GLY B  237  1                                   6    
HELIX   18  18 LEU B  258  GLY B  264  5                                   7    
HELIX   19  19 SER B  291  LYS B  302  1                                  12    
HELIX   20  20 VAL B  314  LEU B  324  1                                  11    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  441  5                                   7    
HELIX   23  23 LEU C  151  ASN C  158  1                                   8    
HELIX   24  24 GLY C  187  LEU C  192  1                                   6    
HELIX   25  25 VAL C  200  TYR C  207  1                                   8    
HELIX   26  26 ASN C  227  PHE C  231  5                                   5    
HELIX   27  27 THR C  259  LEU C  264  1                                   6    
HELIX   28  28 TYR C  440  ALA C  442  5                                   3    
HELIX   29  29 ASN D    3  ARG D    8  1                                   6    
HELIX   30  30 SER D   12  ALA D   18  1                                   7    
HELIX   31  31 LEU D   40  ASP D   47  1                                   8    
HELIX   32  32 ALA D   50  GLU D   52  5                                   3    
HELIX   33  33 ASP D   76  VAL D   80  5                                   5    
HELIX   34  34 SER D  121  SER D  123  5                                   3    
HELIX   35  35 MET D  124  GLN D  132  1                                   9    
HELIX   36  36 ASN D  133  ARG D  143  1                                  11    
HELIX   37  37 PRO D  169  ASN D  175  1                                   7    
HELIX   38  38 GLN D  199  GLN D  210  1                                  12    
HELIX   39  39 GLY D  221  CYS D  232  1                                  12    
HELIX   40  40 CYS D  232  GLY D  237  1                                   6    
HELIX   41  41 LEU D  258  GLY D  264  5                                   7    
HELIX   42  42 SER D  291  LYS D  302  1                                  12    
HELIX   43  43 VAL D  314  GLU D  323  1                                  10    
HELIX   44  44 ASN D  339  ARG D  352  1                                  14    
HELIX   45  45 CYS D  435  ALA D  441  5                                   7    
HELIX   46  46 PRO E   62  GLN E   65  5                                   4    
HELIX   47  47 THR E   87  THR E   91  5                                   5    
HELIX   48  48 HIS E  205  SER E  209  5                                   5    
HELIX   49  49 ASP F   79  PHE F   83  5                                   5    
HELIX   50  50 SER F  121  SER F  127  1                                   7    
HELIX   51  51 LYS F  183  GLU F  187  1                                   5    
HELIX   52  52 ASN H   28  THR H   32  5                                   5    
HELIX   53  53 PRO H   62  GLN H   65  5                                   4    
HELIX   54  54 THR H   74  SER H   76  5                                   3    
HELIX   55  55 THR H   87  THR H   91  5                                   5    
HELIX   56  56 PRO H  206  SER H  209  5                                   4    
HELIX   57  57 ASP L   79  PHE L   83  5                                   5    
HELIX   58  58 SER L  121  SER L  127  1                                   7    
HELIX   59  59 LYS L  183  ARG L  188  1                                   6    
SHEET    1   A 4 THR A   9  ALA A  12  0                                        
SHEET    2   A 4 GLN A 444  TYR A 448 -1  O  VAL A 447   N  THR A   9           
SHEET    3   A 4 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    4   A 4 SER A 420  VAL A 425 -1  N  ARG A 422   O  ILE A 436           
SHEET    1   B 4 LEU A  23  LYS A  27  0                                        
SHEET    2   B 4 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3   B 4 GLY A  52  PRO A  57 -1  O  CYS A  56   N  ILE A  35           
SHEET    4   B 4 SER A  67  LEU A  68 -1  O  LEU A  68   N  VAL A  53           
SHEET    1   C 4 THR A  76  VAL A  79  0                                        
SHEET    2   C 4 GLN A  82  PHE A  87 -1  O  LEU A  84   N  ARG A  77           
SHEET    3   C 4 HIS A 112  GLU A 117 -1  O  LEU A 116   N  THR A  83           
SHEET    4   C 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1   D 4 VAL A  97  TRP A 100  0                                        
SHEET    2   D 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3   D 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4   D 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1   E 4 SER A 172  VAL A 175  0                                        
SHEET    2   E 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3   E 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4   E 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1   F 4 VAL A 239  GLY A 242  0                                        
SHEET    2   F 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3   F 4 ALA A 266  LEU A 270 -1  O  ALA A 266   N  ALA A 257           
SHEET    4   F 4 ARG A 276  ARG A 281 -1  O  LEU A 280   N  VAL A 267           
SHEET    1   G 4 VAL A 293  THR A 296  0                                        
SHEET    2   G 4 ASP A 305  ALA A 310 -1  O  LEU A 307   N  ALA A 294           
SHEET    3   G 4 ARG A 327  PHE A 331 -1  O  PHE A 331   N  LEU A 306           
SHEET    4   G 4 LEU A 345  THR A 348 -1  O  LEU A 347   N  VAL A 328           
SHEET    1   H 2 MET A 314  ARG A 317  0                                        
SHEET    2   H 2 LYS A 321  GLU A 324 -1  O  LYS A 321   N  ARG A 317           
SHEET    1   I 4 ILE A 360  GLY A 364  0                                        
SHEET    2   I 4 ASP A 373  ALA A 378 -1  O  ASP A 373   N  LEU A 363           
SHEET    3   I 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4   I 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1   J 2 GLY A 394  GLN A 395  0                                        
SHEET    2   J 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1   K 3 CYS B  38  ASP B  39  0                                        
SHEET    2   K 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   K 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   L 6 GLU B  60  GLU B  65  0                                        
SHEET    2   L 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3   L 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   L 6 GLU B 411  PRO B 418 -1  N  LYS B 412   O  VAL B 429           
SHEET    5   L 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   L 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   M 5 VAL B  83  SER B  84  0                                        
SHEET    2   M 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   M 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   M 5 LEU B 366  CYS B 374 -1  N  ASN B 371   O  SER B 398           
SHEET    5   M 5 GLU B 378  PRO B 381 -1  O  ILE B 380   N  ALA B 372           
SHEET    1   N 6 TYR B 190  THR B 197  0                                        
SHEET    2   N 6 LEU B 149  PHE B 156 -1  N  ALA B 155   O  LYS B 191           
SHEET    3   N 6 VAL B 112  ASP B 119  1  N  MET B 118   O  GLY B 154           
SHEET    4   N 6 SER B 243  THR B 250  1  O  VAL B 247   N  LEU B 117           
SHEET    5   N 6 ASN B 305  VAL B 310  1  O  ALA B 309   N  PHE B 248           
SHEET    6   N 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1   O 2 GLY B 453  GLU B 456  0                                        
SHEET    2   O 2 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1   P 4 THR C   9  ALA C  12  0                                        
SHEET    2   P 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3   P 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4   P 4 SER C 420  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1   Q 3 LEU C  23  LYS C  27  0                                        
SHEET    2   Q 3 VAL C  33  ALA C  39 -1  O  ALA C  34   N  HIS C  26           
SHEET    3   Q 3 GLY C  52  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    1   R 4 THR C  76  VAL C  79  0                                        
SHEET    2   R 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3   R 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4   R 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1   S 4 VAL C  97  TRP C 100  0                                        
SHEET    2   S 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3   S 4 SER C 129  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4   S 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   T 4 SER C 172  VAL C 175  0                                        
SHEET    2   T 4 GLU C 180  ALA C 185 -1  O  VAL C 182   N  VAL C 174           
SHEET    3   T 4 LEU C 194  PRO C 199 -1  O  ALA C 196   N  LEU C 183           
SHEET    4   T 4 SER C 220  LEU C 221 -1  O  SER C 220   N  GLN C 197           
SHEET    1   U 4 VAL C 239  GLY C 242  0                                        
SHEET    2   U 4 GLU C 252  ALA C 257 -1  O  VAL C 254   N  ALA C 240           
SHEET    3   U 4 ALA C 266  LEU C 270 -1  O  LEU C 270   N  TYR C 253           
SHEET    4   U 4 ARG C 276  ARG C 281 -1  O  LEU C 277   N  ILE C 269           
SHEET    1   V 4 VAL C 293  THR C 296  0                                        
SHEET    2   V 4 ASP C 305  ALA C 310 -1  O  LEU C 307   N  ALA C 294           
SHEET    3   V 4 ARG C 327  PHE C 331 -1  O  PHE C 331   N  LEU C 306           
SHEET    4   V 4 LEU C 345  THR C 348 -1  O  LEU C 347   N  VAL C 328           
SHEET    1   W 2 MET C 314  ARG C 317  0                                        
SHEET    2   W 2 LYS C 321  GLU C 324 -1  O  LYS C 321   N  ARG C 317           
SHEET    1   X 4 ILE C 360  GLY C 364  0                                        
SHEET    2   X 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  GLY C 364           
SHEET    3   X 4 GLN C 388  PHE C 392 -1  O  LEU C 390   N  VAL C 376           
SHEET    4   X 4 GLN C 405  ASP C 408 -1  O  LEU C 407   N  VAL C 389           
SHEET    1   Y 2 GLY C 394  GLN C 395  0                                        
SHEET    2   Y 2 GLY C 398  LEU C 399 -1  O  GLY C 398   N  GLN C 395           
SHEET    1   Z 3 CYS D  38  ASP D  39  0                                        
SHEET    2   Z 3 ALA D  24  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3   Z 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  AA 6 GLU D  60  GLU D  65  0                                        
SHEET    2  AA 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3  AA 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4  AA 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5  AA 6 VAL D 355  ARG D 360 -1  N  GLU D 358   O  LYS D 417           
SHEET    6  AA 6 SER D 385  CYS D 386 -1  O  CYS D 386   N  VAL D 355           
SHEET    1  AB 5 VAL D  83  SER D  84  0                                        
SHEET    2  AB 5 SER D  97  ARG D 105 -1  O  GLN D 103   N  SER D  84           
SHEET    3  AB 5 THR D 394  VAL D 403 -1  O  ILE D 399   N  PHE D 100           
SHEET    4  AB 5 LEU D 366  THR D 373 -1  N  ASN D 371   O  SER D 398           
SHEET    5  AB 5 VAL D 379  PRO D 381 -1  O  ILE D 380   N  ALA D 372           
SHEET    1  AC 6 TYR D 190  THR D 197  0                                        
SHEET    2  AC 6 LEU D 149  PHE D 156 -1  N  ILE D 151   O  THR D 197           
SHEET    3  AC 6 VAL D 112  ASP D 119  1  N  ILE D 114   O  ARG D 150           
SHEET    4  AC 6 SER D 243  THR D 250  1  O  SER D 243   N  ASP D 113           
SHEET    5  AC 6 ASN D 305  THR D 311  1  O  ALA D 309   N  PHE D 248           
SHEET    6  AC 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  AD 2 GLY D 453  GLU D 456  0                                        
SHEET    2  AD 2 VAL D 459  CYS D 462 -1  O  ARG D 461   N  THR D 454           
SHEET    1  AE 4 GLN E   3  GLN E   6  0                                        
SHEET    2  AE 4 VAL E  18  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3  AE 4 THR E  78  LEU E  83 -1  O  LEU E  83   N  VAL E  18           
SHEET    4  AE 4 ALA E  68  ASP E  73 -1  N  THR E  69   O  GLN E  82           
SHEET    1  AF 6 GLU E  10  VAL E  12  0                                        
SHEET    2  AF 6 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  AF 6 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4  AF 6 VAL E  34  ARG E  40 -1  N  GLN E  39   O  VAL E  93           
SHEET    5  AF 6 GLY E  44  ILE E  51 -1  O  GLU E  46   N  LYS E  38           
SHEET    6  AF 6 THR E  58  TYR E  60 -1  O  LYS E  59   N  ARG E  50           
SHEET    1  AG 4 GLU E  10  VAL E  12  0                                        
SHEET    2  AG 4 THR E 113  VAL E 117  1  O  SER E 114   N  GLU E  10           
SHEET    3  AG 4 ALA E  92  ARG E  98 -1  N  TYR E  94   O  THR E 113           
SHEET    4  AG 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1  AH 4 SER E 126  LEU E 130  0                                        
SHEET    2  AH 4 SER E 141  LYS E 149 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AH 4 LEU E 180  THR E 190 -1  O  VAL E 189   N  VAL E 142           
SHEET    4  AH 4 VAL E 169  THR E 171 -1  N  HIS E 170   O  SER E 186           
SHEET    1  AI 4 SER E 126  LEU E 130  0                                        
SHEET    2  AI 4 SER E 141  LYS E 149 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AI 4 LEU E 180  THR E 190 -1  O  VAL E 189   N  VAL E 142           
SHEET    4  AI 4 VAL E 175  GLN E 177 -1  N  GLN E 177   O  LEU E 180           
SHEET    1  AJ 3 THR E 157  TRP E 160  0                                        
SHEET    2  AJ 3 THR E 200  ALA E 204 -1  O  ALA E 204   N  THR E 157           
SHEET    3  AJ 3 ASP E 213  LYS E 215 -1  O  LYS E 214   N  CYS E 201           
SHEET    1  AK 4 MET F   4  SER F   7  0                                        
SHEET    2  AK 4 VAL F  19  ALA F  25 -1  O  HIS F  24   N  THR F   5           
SHEET    3  AK 4 ASP F  70  ILE F  75 -1  O  LEU F  73   N  ILE F  21           
SHEET    4  AK 4 PHE F  62  SER F  67 -1  N  SER F  65   O  SER F  72           
SHEET    1  AL 6 SER F  10  VAL F  13  0                                        
SHEET    2  AL 6 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AL 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AL 6 ILE F  33  GLN F  38 -1  N  GLY F  34   O  VAL F  89           
SHEET    5  AL 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6  AL 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1  AM 4 SER F  10  VAL F  13  0                                        
SHEET    2  AM 4 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AM 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AM 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1  AN 4 THR F 114  PHE F 118  0                                        
SHEET    2  AN 4 GLY F 129  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3  AN 4 TYR F 173  THR F 182 -1  O  MET F 175   N  LEU F 136           
SHEET    4  AN 4 VAL F 159  TRP F 163 -1  N  LEU F 160   O  THR F 178           
SHEET    1  AO 3 SER F 153  ARG F 155  0                                        
SHEET    2  AO 3 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3  AO 3 TYR F 192  THR F 197 -1  O  THR F 197   N  ASN F 145           
SHEET    1  AP 4 GLN H   3  GLN H   6  0                                        
SHEET    2  AP 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  AP 4 THR H  78  LEU H  83 -1  O  LEU H  83   N  VAL H  18           
SHEET    4  AP 4 ALA H  68  ASP H  73 -1  N  THR H  69   O  GLN H  82           
SHEET    1  AQ 6 GLU H  10  VAL H  12  0                                        
SHEET    2  AQ 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AQ 6 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4  AQ 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5  AQ 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AQ 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  AR 4 GLU H  10  VAL H  12  0                                        
SHEET    2  AR 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AR 4 ALA H  92  ARG H  98 -1  N  TYR H  94   O  THR H 113           
SHEET    4  AR 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  AS 4 SER H 126  LEU H 130  0                                        
SHEET    2  AS 4 SER H 141  TYR H 151 -1  O  LEU H 147   N  TYR H 128           
SHEET    3  AS 4 LEU H 180  THR H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4  AS 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1  AT 4 SER H 126  LEU H 130  0                                        
SHEET    2  AT 4 SER H 141  TYR H 151 -1  O  LEU H 147   N  TYR H 128           
SHEET    3  AT 4 LEU H 180  THR H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4  AT 4 VAL H 175  GLN H 177 -1  N  GLN H 177   O  LEU H 180           
SHEET    1  AU 3 THR H 157  TRP H 160  0                                        
SHEET    2  AU 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  AU 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  AV 4 MET L   4  SER L   7  0                                        
SHEET    2  AV 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3  AV 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4  AV 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1  AW 6 SER L  10  VAL L  13  0                                        
SHEET    2  AW 6 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AW 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AW 6 ILE L  33  GLN L  38 -1  N  GLY L  34   O  VAL L  89           
SHEET    5  AW 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6  AW 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  AX 4 SER L  10  VAL L  13  0                                        
SHEET    2  AX 4 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AX 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AX 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AY 4 THR L 114  PHE L 118  0                                        
SHEET    2  AY 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  AY 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4  AY 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1  AZ 4 SER L 153  ARG L 155  0                                        
SHEET    2  AZ 4 ASN L 145  ILE L 150 -1  N  TRP L 148   O  ARG L 155           
SHEET    3  AZ 4 SER L 191  THR L 197 -1  O  THR L 197   N  ASN L 145           
SHEET    4  AZ 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.06  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.06  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.06  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.04  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.04  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.07  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.08  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.05  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.06  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.04  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.04  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.02  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.05  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.05  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.04  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.04  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.05  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.03  
SSBOND  28 CYS E   22    CYS E   96                          1555   1555  2.04  
SSBOND  29 CYS E  134    CYS F  214                          1555   1555  2.03  
SSBOND  30 CYS E  146    CYS E  201                          1555   1555  2.03  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.04  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.04  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.04  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.45  
LINK         OD2 ASP A 245                CA    CA A2004     1555   1555  2.14  
LINK         OE2 GLU B 220                MG    MG B2001     1555   1555  2.16  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.17  
LINK         OE2 GLU D 220                MG    MG D2001     1555   1555  2.19  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.22  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.23  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.24  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.24  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.25  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.25  
LINK         OD2 ASP C 245                CA    CA C2004     1555   1555  2.26  
LINK         O   MET D 335                CA    CA D2002     1555   1555  2.27  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.27  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.27  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.28  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.28  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.29  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.29  
LINK         OG  SER D 121                MG    MG D2001     1555   1555  2.30  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.30  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.30  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.31  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.31  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.31  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.32  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.33  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.34  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.34  
LINK         OE1 GLU D 220                CA    CA D2003     1555   1555  2.34  
LINK         OE1 GLU C 243                CA    CA C2004     1555   1555  2.35  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.36  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.36  
LINK         OG  SER B 121                MG    MG B2001     1555   1555  2.37  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.37  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.37  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.38  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.38  
LINK         OD2 ASP C 365                CA    CA C2006     1555   1555  2.38  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.39  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.39  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.39  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.39  
LINK         OD2 ASP A 365                CA    CA A2006     1555   1555  2.40  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.40  
LINK         OE1 GLU B 220                CA    CA B2003     1555   1555  2.40  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.40  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.41  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.41  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.41  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.43  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.43  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.43  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.44  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.44  
LINK         OE2 GLU A 243                CA    CA A2004     1555   1555  2.45  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.45  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.45  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.46  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.47  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.48  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.48  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.49  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.49  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.49  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.50  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.50  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.51  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.51  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.53  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.53  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.54  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.54  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.56  
LINK         OD2 ASP B 126                CA    CA B2002     1555   1555  2.57  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.59  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.59  
LINK         OD2 ASP D 126                CA    CA D2002     1555   1555  2.61  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.63  
LINK        MG    MG D2001                 O   HOH D1118     1555   1555  2.00  
LINK        MG    MG B2001                 O   HOH B 477     1555   1555  2.02  
LINK        MG    MG B2001                 O   HOH B1120     1555   1555  2.06  
LINK        MG    MG D2001                 O   HOH D 476     1555   1555  2.08  
LINK        MG    MG D2001                 O   HOH D1126     1555   1555  2.09  
LINK        MG    MG B2001                 O   HOH B1121     1555   1555  2.10  
LINK        MG    MG B2001                 O   HOH B 920     1555   1555  2.11  
LINK        MG    MG D2001                 O   HOH D1115     1555   1555  2.11  
LINK        CA    CA C2006                 O   HOH C 494     1555   1555  2.26  
LINK        CA    CA B2002                 O   HOH B 525     1555   1555  2.34  
LINK        CA    CA A2007                 O   HOH A 467     1555   1555  2.36  
LINK        CA    CA A2005                 O   HOH A 478     1555   1555  2.36  
LINK        CA    CA A2006                 O   HOH A 486     1555   1555  2.39  
LINK        CA    CA D2002                 O   HOH D 509     1555   1555  2.41  
LINK        CA    CA C2005                 O   HOH C1134     1555   1555  2.42  
LINK        CA    CA B2002                 O   HOH B 502     1555   1555  2.44  
LINK        CA    CA D2002                 O   HOH D 488     1555   1555  2.44  
LINK        CA    CA C2007                 O   HOH C 478     1555   1555  2.48  
LINK         O4  NAG D3321                 C1  BMA D3322     1555   1555  1.44  
LINK         O4  NAG B3321                 C1  BMA B3322     1555   1555  1.44  
LINK         O3  BMA D3322                 C1  MAN D3323     1555   1555  1.44  
LINK         O3  BMA B3322                 C1  MAN B3323     1555   1555  1.44  
LINK         O6  BMA B3322                 C1  MAN B3324     1555   1555  1.44  
CISPEP   1 SER B   84    PRO B   85          0        -4.72                     
CISPEP   2 SER B  162    PRO B  163          0         5.27                     
CISPEP   3 SER B  168    PRO B  169          0        -6.34                     
CISPEP   4 SER D   84    PRO D   85          0        -3.20                     
CISPEP   5 SER D  162    PRO D  163          0         8.46                     
CISPEP   6 SER D  168    PRO D  169          0        -5.87                     
CISPEP   7 PHE E  152    PRO E  153          0        -5.54                     
CISPEP   8 GLU E  154    PRO E  155          0        -2.32                     
CISPEP   9 TRP E  194    PRO E  195          0         0.72                     
CISPEP  10 SER F    7    PRO F    8          0        -5.93                     
CISPEP  11 LEU F   94    PRO F   95          0        -3.65                     
CISPEP  12 TYR F  140    PRO F  141          0         2.72                     
CISPEP  13 PHE H  152    PRO H  153          0        -3.41                     
CISPEP  14 GLU H  154    PRO H  155          0        -5.41                     
CISPEP  15 TRP H  194    PRO H  195          0        -1.76                     
CISPEP  16 SER L    7    PRO L    8          0        -4.85                     
CISPEP  17 LEU L   94    PRO L   95          0         1.14                     
CISPEP  18 TYR L  140    PRO L  141          0         0.12                     
SITE     1 AC1  2 TYR A 155  SER A 161                                          
SITE     1 AC2  3 PHE A  10  GLN A 444  PRO C 383                               
SITE     1 AC3  5 ARG A 400  SER A 401  ARG A 402  HOH A 691                    
SITE     2 AC3  5 HOH A 696                                                     
SITE     1 AC4  4 ASN A 227  ARG A 276  ARG A 279  HOH A1172                    
SITE     1 AC5  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC5  5 GLU A 252                                                     
SITE     1 AC6  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC6  6 ASP A 305  HOH A 478                                          
SITE     1 AC7  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC7  6 ASP A 373  HOH A 486                                          
SITE     1 AC8  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC8  6 ASP A 434  HOH A 467                                          
SITE     1 AC9  6 SER B 121  TYR B 122  ARG B 214  ASN B 215                    
SITE     2 AC9  6 HOH B1120  HOH B1123                                          
SITE     1 BC1  6 SER B 121  GLU B 220  HOH B 477  HOH B 920                    
SITE     2 BC1  6 HOH B1120  HOH B1121                                          
SITE     1 BC2  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 BC2  6 HOH B 502  HOH B 525                                          
SITE     1 BC3  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC3  5 GLU B 220                                                     
SITE     1 BC4  2 ASN B  99  PHE B 100                                          
SITE     1 BC5  7 MET A 285  ASN B 320  HOH B 486  HOH B 534                    
SITE     2 BC5  7 HOH B 538  HOH B 547  NAG B3321                               
SITE     1 BC6  5 ARG A 281  HOH A1178  NAG B3320  BMA B3322                    
SITE     2 BC6  5 MAN B3324                                                     
SITE     1 BC7  4 HOH B 826  NAG B3321  MAN B3323  MAN B3324                    
SITE     1 BC8  3 ARG A 281  HOH B 826  BMA B3322                               
SITE     1 BC9  2 NAG B3321  BMA B3322                                          
SITE     1 CC1  4 ASN B 371  SER B 398  GLU B 400  NAG B3372                    
SITE     1 CC2  1 NAG B3371                                                     
SITE     1 CC3  3 ALA C  89  HIS C 112  HOH C 576                               
SITE     1 CC4  4 ARG C 400  SER C 401  ARG C 402  HOH C1250                    
SITE     1 CC5  5 ASN C 227  TYR C 230  ARG C 276  ARG C 279                    
SITE     2 CC5  5 HOH C1239                                                     
SITE     1 CC6  1 GLN C 444                                                     
SITE     1 CC7  1 TRP C  58                                                     
SITE     1 CC8  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 CC8  5 GLU C 252                                                     
SITE     1 CC9  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 CC9  6 ASP C 305  HOH C1134                                          
SITE     1 DC1  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 DC1  6 ASP C 373  HOH C 494                                          
SITE     1 DC2  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 DC2  6 ASP C 434  HOH C 478                                          
SITE     1 DC3  5 SER D 121  TYR D 122  ARG D 214  ASN D 215                    
SITE     2 DC3  5 HOH D1126                                                     
SITE     1 DC4  6 SER D 121  GLU D 220  HOH D 476  HOH D1115                    
SITE     2 DC4  6 HOH D1118  HOH D1126                                          
SITE     1 DC5  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 DC5  6 HOH D 488  HOH D 509                                          
SITE     1 DC6  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 DC6  5 GLU D 220                                                     
SITE     1 DC7  2 ASN D  99  NAG D3372                                          
SITE     1 DC8  7 MET C 285  ASN D 320  HOH D 529  HOH D 533                    
SITE     2 DC8  7 HOH D 551  HOH D 978  NAG D3321                               
SITE     1 DC9  4 ARG C 281  HOH C1016  NAG D3320  BMA D3322                    
SITE     1 EC1  2 NAG D3321  MAN D3323                                          
SITE     1 EC2  2 ARG C 281  BMA D3322                                          
SITE     1 EC3  5 ASN D 371  SER D 398  ILE D 399  GLU D 400                    
SITE     2 EC3  5 NAG D3372                                                     
SITE     1 EC4  2 NAG D3099  NAG D3371                                          
SITE     1 EC5  4 SER L  30  SER L  67  GLY L  68  HOH L 961                    
CRYST1  259.533  145.257  104.798  90.00  90.00  90.00 P 21 21 2     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      0.003853  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006884  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009542        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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