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Entry: 3T3M
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HEADER    CELL ADHESION                           25-JUL-11   3T3M              
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 SYNONYM: GPALPHA IIB, GPIIB, PLATELET MEMBRANE GLYCOPROTEIN IIB,     
COMPND   6 INTEGRIN ALPHA-IIB HEAVY CHAIN, INTEGRIN ALPHA-IIB LIGHT CHAIN, FORM 
COMPND   7 1, INTEGRIN ALPHA-IIB LIGHT CHAIN, FORM 2;                           
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  11 CHAIN: B, D;                                                         
COMPND  12 FRAGMENT: UNP RESIDUES 27-498;                                       
COMPND  13 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA;                
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: MONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                      
COMPND  17 CHAIN: E, H;                                                         
COMPND  18 ENGINEERED: YES;                                                     
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: MONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                      
COMPND  21 CHAIN: F, L;                                                         
COMPND  22 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_TAXID: 10090;                                               
SOURCE  18 MOL_ID: 4;                                                           
SOURCE  19 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  20 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 3T3M    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.    2.60 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) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.69                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.800                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 118689                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.180                           
REMARK   3   R VALUE            (WORKING SET) : 0.179                           
REMARK   3   FREE R VALUE                     : 0.222                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.860                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1022                            
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 59.7084 -  4.9728    1.00    17940   159  0.1781 0.2103        
REMARK   3     2  4.9728 -  3.9473    1.00    17496   161  0.1384 0.1609        
REMARK   3     3  3.9473 -  3.4484    0.99    17216   140  0.1690 0.2172        
REMARK   3     4  3.4484 -  3.1331    0.97    16831   144  0.1867 0.2562        
REMARK   3     5  3.1331 -  2.9086    0.95    16315   140  0.1988 0.2644        
REMARK   3     6  2.9086 -  2.7371    0.93    16023   142  0.2205 0.2525        
REMARK   3     7  2.7371 -  2.6000    0.92    15846   136  0.2524 0.3242        
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              : 0.38                                          
REMARK   3   B_SOL              : 44.76                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.540            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.600           
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) : -4.33560                                             
REMARK   3    B22 (A**2) : -3.00120                                             
REMARK   3    B33 (A**2) : -4.94500                                             
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      :  0.006          21673                                  
REMARK   3   ANGLE     :  0.696          29618                                  
REMARK   3   CHIRALITY :  0.043           3268                                  
REMARK   3   PLANARITY :  0.003           3805                                  
REMARK   3   DIHEDRAL  : 13.852           7866                                  
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):  51.5023  90.8549  54.4664              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2327 T22:   0.0093                                     
REMARK   3      T33:   0.1587 T12:  -0.0039                                     
REMARK   3      T13:   0.0936 T23:   0.0513                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6887 L22:   1.1179                                     
REMARK   3      L33:   0.9472 L12:   0.0910                                     
REMARK   3      L13:  -0.0438 L23:   0.2314                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0149 S12:  -0.0337 S13:  -0.0698                       
REMARK   3      S21:   0.1600 S22:  -0.0819 S23:   0.1398                       
REMARK   3      S31:   0.1735 S32:  -0.1584 S33:   0.0040                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: chain C and resid 1:450                                
REMARK   3    ORIGIN FOR THE GROUP (A):  85.1339  87.0699 117.7813              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2309 T22:   0.3372                                     
REMARK   3      T33:   0.1476 T12:   0.0630                                     
REMARK   3      T13:   0.0924 T23:   0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4593 L22:   0.6341                                     
REMARK   3      L33:   1.5799 L12:  -0.0065                                     
REMARK   3      L13:  -0.3828 L23:  -0.1078                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1624 S12:   0.0378 S13:  -0.1203                       
REMARK   3      S21:  -0.1315 S22:   0.0183 S23:  -0.1777                       
REMARK   3      S31:   0.3921 S32:   0.4057 S33:   0.1027                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: chain B and resid 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 124.1456  88.4989  35.2173              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7235 T22:   1.6866                                     
REMARK   3      T33:   0.9035 T12:   0.4948                                     
REMARK   3      T13:   0.0064 T23:  -0.2321                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7733 L22:   3.5076                                     
REMARK   3      L33:   0.0474 L12:  -3.2978                                     
REMARK   3      L13:  -0.2614 L23:   0.3820                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3034 S12:  -0.0527 S13:  -0.2160                       
REMARK   3      S21:   0.1098 S22:   0.1542 S23:  -0.7730                       
REMARK   3      S31:   0.3568 S32:   0.7508 S33:   0.1538                       
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): 101.9469 107.9009  52.8356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2436 T22:   0.6984                                     
REMARK   3      T33:   0.5625 T12:   0.0676                                     
REMARK   3      T13:  -0.0270 T23:  -0.0715                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0291 L22:   2.8692                                     
REMARK   3      L33:   5.7793 L12:  -1.0637                                     
REMARK   3      L13:  -2.3122 L23:   2.5205                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0360 S12:  -0.0147 S13:   0.3668                       
REMARK   3      S21:   0.0066 S22:   0.3534 S23:  -0.3310                       
REMARK   3      S31:   0.2137 S32:   1.1042 S33:  -0.2690                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: chain B and resid 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  68.5898 118.9030  63.5371              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2484 T22:   0.0208                                     
REMARK   3      T33:   0.1809 T12:   0.0193                                     
REMARK   3      T13:   0.0643 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0160 L22:   2.1878                                     
REMARK   3      L33:   1.0947 L12:   0.2843                                     
REMARK   3      L13:   0.2251 L23:   0.4215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0687 S12:  -0.1175 S13:   0.1729                       
REMARK   3      S21:   0.1304 S22:   0.0549 S23:  -0.0795                       
REMARK   3      S31:  -0.1809 S32:   0.0842 S33:  -0.0874                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: chain B and resid 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A): 117.8198  90.2200  19.9002              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6110 T22:   1.5366                                     
REMARK   3      T33:   0.8237 T12:   0.3312                                     
REMARK   3      T13:   0.1918 T23:   0.0260                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.6609 L22:   3.2146                                     
REMARK   3      L33:   6.1426 L12:   2.2805                                     
REMARK   3      L13:   0.9965 L23:  -1.1410                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0019 S12:  -0.4373 S13:   0.0188                       
REMARK   3      S21:  -0.4537 S22:  -0.0681 S23:  -1.0184                       
REMARK   3      S31:   0.1025 S32:   0.3069 S33:   0.0704                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: chain D and resid 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6065  70.9716 140.9913              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7654 T22:   1.1275                                     
REMARK   3      T33:   0.6606 T12:  -0.5396                                     
REMARK   3      T13:   0.1364 T23:  -0.0465                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2030 L22:   3.5154                                     
REMARK   3      L33:   1.1284 L12:   2.3444                                     
REMARK   3      L13:  -1.2791 L23:  -0.5857                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3848 S12:   0.1854 S13:  -0.7335                       
REMARK   3      S21:  -0.1387 S22:  -0.0121 S23:   0.3936                       
REMARK   3      S31:   0.4670 S32:  -0.5060 S33:   0.0567                       
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):  31.8639  88.0380 116.1018              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3722 T22:   0.9507                                     
REMARK   3      T33:   0.3547 T12:  -0.2933                                     
REMARK   3      T13:  -0.0038 T23:   0.1175                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6537 L22:   0.3455                                     
REMARK   3      L33:   3.5561 L12:  -0.3853                                     
REMARK   3      L13:  -0.1434 L23:  -0.2980                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2687 S12:   0.8321 S13:   0.0358                       
REMARK   3      S21:  -0.1075 S22:   0.1780 S23:   0.1091                       
REMARK   3      S31:   0.3646 S32:  -0.8167 S33:   0.0095                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: chain D and resid 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  61.1469 103.0600  99.6860              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2695 T22:   0.5261                                     
REMARK   3      T33:   0.1666 T12:  -0.0910                                     
REMARK   3      T13:   0.0174 T23:   0.1809                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8541 L22:   0.9506                                     
REMARK   3      L33:   2.1041 L12:  -0.2373                                     
REMARK   3      L13:   0.0326 L23:  -0.5144                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0304 S12:   0.3230 S13:   0.2400                       
REMARK   3      S21:  -0.1212 S22:   0.0724 S23:   0.0280                       
REMARK   3      S31:  -0.0933 S32:  -0.4078 S33:  -0.0511                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: chain D and resid 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.8107  80.7960 153.6684              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4295 T22:   0.7426                                     
REMARK   3      T33:   0.5467 T12:  -0.2537                                     
REMARK   3      T13:   0.1350 T23:  -0.1007                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4264 L22:   7.6489                                     
REMARK   3      L33:   0.6943 L12:   2.0639                                     
REMARK   3      L13:   0.2312 L23:   0.8007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2099 S12:   0.1147 S13:   0.2276                       
REMARK   3      S21:   0.0919 S22:   0.1846 S23:   0.8340                       
REMARK   3      S31:   0.4448 S32:  -0.9867 S33:  -0.0688                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: chain H and resid 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.4736  97.1205  82.9109              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4711 T22:   0.6161                                     
REMARK   3      T33:   0.3954 T12:  -0.0381                                     
REMARK   3      T13:   0.2021 T23:  -0.1012                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0647 L22:   0.6628                                     
REMARK   3      L33:   2.1638 L12:   0.0745                                     
REMARK   3      L13:  -1.7989 L23:  -0.7964                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0900 S12:  -0.5975 S13:  -0.0283                       
REMARK   3      S21:   0.7727 S22:  -0.0118 S23:   0.3208                       
REMARK   3      S31:   0.1343 S32:  -0.2278 S33:   0.0954                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: chain H and resid 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.8386  81.7287  93.0584              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6611 T22:   0.7103                                     
REMARK   3      T33:   1.7966 T12:   0.1531                                     
REMARK   3      T13:   0.2282 T23:   0.2833                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8431 L22:   0.1967                                     
REMARK   3      L33:   3.4985 L12:  -0.5729                                     
REMARK   3      L13:  -0.4997 L23:   0.4043                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0931 S12:  -0.3284 S13:  -1.6973                       
REMARK   3      S21:   0.3600 S22:   0.1169 S23:   0.3633                       
REMARK   3      S31:   0.9896 S32:   0.1935 S33:   0.0115                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: chain L and resid 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.1239  96.4252  64.4919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2840 T22:   0.7567                                     
REMARK   3      T33:   0.6634 T12:  -0.0336                                     
REMARK   3      T13:   0.1140 T23:  -0.2373                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9859 L22:   0.1954                                     
REMARK   3      L33:   0.5353 L12:   0.5250                                     
REMARK   3      L13:  -0.3578 L23:   0.0684                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0046 S12:   0.3609 S13:  -0.0859                       
REMARK   3      S21:   0.0269 S22:  -0.3361 S23:   0.7800                       
REMARK   3      S31:   0.1705 S32:  -0.7018 S33:  -0.0135                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: chain L and resid 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.2015  93.7895  86.2869              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2991 T22:   0.7425                                     
REMARK   3      T33:   1.0886 T12:   0.0430                                     
REMARK   3      T13:   0.2507 T23:   0.0565                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6346 L22:   0.8260                                     
REMARK   3      L33:   1.8549 L12:   0.0891                                     
REMARK   3      L13:   0.4052 L23:   0.3652                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3242 S12:   0.1143 S13:  -0.9231                       
REMARK   3      S21:   0.1591 S22:  -0.0394 S23:   0.3036                       
REMARK   3      S31:   0.2731 S32:  -0.4617 S33:   0.0764                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: chain E and resid 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 115.8483  90.2707  86.3730              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7772 T22:   0.9240                                     
REMARK   3      T33:   0.3858 T12:  -0.0442                                     
REMARK   3      T13:   0.2587 T23:   0.0659                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8595 L22:   0.6239                                     
REMARK   3      L33:   3.2389 L12:  -0.8249                                     
REMARK   3      L13:  -1.4013 L23:   1.3634                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0948 S12:   0.5990 S13:  -0.0342                       
REMARK   3      S21:  -0.6793 S22:   0.0022 S23:  -0.1826                       
REMARK   3      S31:   0.8827 S32:   0.0872 S33:   0.1383                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: chain E and resid 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 150.9936  82.1031  79.9761              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4342 T22:   2.0004                                     
REMARK   3      T33:   1.0045 T12:   0.7525                                     
REMARK   3      T13:   0.1664 T23:   0.1288                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7926 L22:   4.0169                                     
REMARK   3      L33:   3.1813 L12:   0.5114                                     
REMARK   3      L13:   0.9995 L23:   1.6856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5834 S12:   1.2312 S13:  -0.2402                       
REMARK   3      S21:  -0.7398 S22:  -0.1991 S23:  -0.9964                       
REMARK   3      S31:   0.6083 S32:   0.9299 S33:  -0.3645                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: chain F and resid 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 126.3063 100.4107 102.4090              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3785 T22:   1.1227                                     
REMARK   3      T33:   0.7981 T12:  -0.0776                                     
REMARK   3      T13:   0.1820 T23:   0.0691                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1502 L22:   0.9190                                     
REMARK   3      L33:   0.6341 L12:   0.5621                                     
REMARK   3      L13:  -0.5402 L23:   0.1096                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0658 S12:  -0.2193 S13:   0.6452                       
REMARK   3      S21:  -0.1324 S22:  -0.1904 S23:  -0.8557                       
REMARK   3      S31:   0.2088 S32:   0.5356 S33:   0.1240                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: chain F and resid 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 155.3639  98.2630  80.5370              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8456 T22:   1.8883                                     
REMARK   3      T33:   1.0642 T12:   0.2437                                     
REMARK   3      T13:   0.3409 T23:   0.2363                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2331 L22:   1.7981                                     
REMARK   3      L33:   2.4917 L12:   0.6282                                     
REMARK   3      L13:  -0.9855 L23:   0.7500                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:   0.4684 S13:   0.0634                       
REMARK   3      S21:  -0.8251 S22:   0.2809 S23:  -0.7135                       
REMARK   3      S31:  -0.0555 S32:   1.0777 S33:  -0.3417                       
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 3T3M COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-AUG-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB066994.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-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) : 1.0331                             
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   : 118868                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.700                             
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) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 92.3                               
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   (%): 63.17                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.34                     
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      130.57500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.66500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      130.57500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.66500            
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, 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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D, E, F                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   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   771     O    HOH A   772              1.76            
REMARK 500   O    HOH C   628     O    HOH C   735              1.93            
REMARK 500   O    HOH A   466     O    HOH A   686              1.93            
REMARK 500   O    HOH A   723     O    HOH A   771              2.02            
REMARK 500   O    HOH C   839     O    HOH C   840              2.03            
REMARK 500   O    HOH B   656     O    HOH B   766              2.04            
REMARK 500   O    HOH A   769     O    HOH A   770              2.06            
REMARK 500   O    HOH A   770     O    HOH A   771              2.06            
REMARK 500   O    HOH B   521     O    HOH B   675              2.07            
REMARK 500   O    HOH C   465     O    HOH C   851              2.08            
REMARK 500   O    HOH A   477     O    HOH A   751              2.09            
REMARK 500   O    HOH C   469     O    HOH C   731              2.10            
REMARK 500   O    HOH C   840     O    HOH C   841              2.13            
REMARK 500   O    HOH A   489     O    HOH A   728              2.13            
REMARK 500   O    HOH A   503     O    HOH A   670              2.14            
REMARK 500   O    HOH A   474     O    HOH A   699              2.14            
REMARK 500   O    HOH C   681     O    HOH C   798              2.17            
REMARK 500   O    HOH A   474     O    HOH B   478              2.17            
REMARK 500   O2   SO4 A   458     O    HOH A   756              2.19            
REMARK 500   OD2  ASP D   126     O    HOH D   760              2.19            
REMARK 500   ND2  ASN D   320     C2   NAG D  3320              2.19            
REMARK 500   O    TYR A   380     O    HOH A   749              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       27.28    -76.63                                   
REMARK 500    SER A 101     -134.21     58.21                                   
REMARK 500    LYS A 118     -117.76     59.06                                   
REMARK 500    GLU A 123      139.51     92.89                                   
REMARK 500    LEU A 212      -50.02     80.89                                   
REMARK 500    ALA A 286       -0.07     77.72                                   
REMARK 500    THR A 296      148.85   -174.46                                   
REMARK 500    ASP A 319       40.86     72.06                                   
REMARK 500    VAL A 325      -17.43   -143.30                                   
REMARK 500    PRO A 337       92.38    -64.23                                   
REMARK 500    SER B  20      146.92   -173.43                                   
REMARK 500    LEU B  33      -83.63    -42.07                                   
REMARK 500    ASP B  76      164.21     63.66                                   
REMARK 500    SER B  77       54.96    -97.28                                   
REMARK 500    SER B  78       51.11     72.03                                   
REMARK 500    VAL B 157      -80.70   -132.94                                   
REMARK 500    MET B 180     -159.02   -100.64                                   
REMARK 500    SER B 213     -164.58   -124.16                                   
REMARK 500    ASP B 241       73.39   -101.88                                   
REMARK 500    LYS B 253      170.62    -58.35                                   
REMARK 500    LEU B 258      -13.48     90.17                                   
REMARK 500    ASP B 361       31.07     70.26                                   
REMARK 500    LEU B 375      -97.30     47.89                                   
REMARK 500    ASN B 377       18.51     54.50                                   
REMARK 500    ALA B 439       20.98    -79.04                                   
REMARK 500    GLN B 440       43.09   -158.63                                   
REMARK 500    ASN B 449       24.10     47.37                                   
REMARK 500    ASN B 450       68.91     60.28                                   
REMARK 500    SER C  29        3.68    -68.49                                   
REMARK 500    GLN C  47       -6.40     80.20                                   
REMARK 500    SER C 101     -122.74     55.64                                   
REMARK 500    LYS C 118     -109.86     59.39                                   
REMARK 500    GLU C 123      137.45    100.23                                   
REMARK 500    VAL C 174      149.31   -170.14                                   
REMARK 500    LEU C 212      -38.21     71.36                                   
REMARK 500    SER C 222     -173.19    -66.02                                   
REMARK 500    ALA C 286       -1.43     76.20                                   
REMARK 500    THR D   7       47.48    -87.75                                   
REMARK 500    SER D  20      145.94   -172.76                                   
REMARK 500    ALA D  30       59.88    -96.07                                   
REMARK 500    PHE D  56       85.54   -150.98                                   
REMARK 500    LEU D  64      -79.01   -101.02                                   
REMARK 500    ASP D  66       43.90   -146.59                                   
REMARK 500    VAL D 157      -78.97   -131.20                                   
REMARK 500    PRO D 169     -177.77    -67.32                                   
REMARK 500    SER D 213     -159.54   -125.00                                   
REMARK 500    ASP D 241       78.09   -104.33                                   
REMARK 500    LEU D 258      -10.59     91.45                                   
REMARK 500    HIS D 274       35.49   -142.24                                   
REMARK 500    ASP D 361       31.71     71.42                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      91 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 D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 217   OD1                                                    
REMARK 620 2 PRO D 219   O    97.6                                              
REMARK 620 3 GLU D 220   OE1 163.5  80.0                                        
REMARK 620 4 ASP D 158   OD2  93.8  87.7 102.4                                  
REMARK 620 5 ASN D 215   OD1  90.7 165.4  88.6 103.8                            
REMARK 620 6 ASP D 217   O    73.1  81.8  90.4 161.9  89.2                      
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 157.4                                              
REMARK 620 3 ASP C 297   OD1  80.3  77.6                                        
REMARK 620 4 ASP C 305   OD2 101.1  83.5  89.1                                  
REMARK 620 5 ASP C 305   OD1  83.9 115.3 134.0  52.3                            
REMARK 620 6 ASP C 301   OD1  87.9  82.5  77.3 162.2 145.0                      
REMARK 620 7 HOH C 768   O   110.8  88.5 157.7 106.8  67.8  83.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA B2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP B 127   OD1                                                    
REMARK 620 2 SER B 123   O    92.9                                              
REMARK 620 3 ASP B 126   OD1  82.2  75.6                                        
REMARK 620 4 ASP B 126   OD2  90.1 126.7  52.2                                  
REMARK 620 5 MET B 335   O    87.8 160.1 124.1  73.1                            
REMARK 620 6 HOH B 503   O    92.9  87.8 162.3 145.2  72.4                      
REMARK 620 7 HOH B 517   O   171.6  86.2  89.4  83.7  95.9  95.5                
REMARK 620 N                    1     2     3     4     5     6                 
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 152.0                                              
REMARK 620 3 ASP A 426   OD1  76.6  75.9                                        
REMARK 620 4 ASN A 430   OD1  89.3  80.8  79.7                                  
REMARK 620 5 ASP A 434   OD1  94.6  90.3  89.8 167.6                            
REMARK 620 6 ASP A 434   OD2  84.6 119.7 136.9 139.1  53.2                      
REMARK 620 7 HOH A 621   O   126.2  78.4 150.3  81.8 105.1  69.9                
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 367   OD1 157.8                                              
REMARK 620 3 ASP C 365   OD2  74.9  82.9                                        
REMARK 620 4 ASP C 369   OD1  91.6  80.8  73.4                                  
REMARK 620 5 ASP C 373   OD1  93.1  89.3  93.4 164.3                            
REMARK 620 6 ASP C 373   OD2  79.6 118.3 135.2 144.0  51.7                      
REMARK 620 7 HOH C 654   O   100.2  97.8 147.1  74.3 119.5  73.2                
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 ASP C 245   OD2                                                    
REMARK 620 2 ASP C 247   O    89.8                                              
REMARK 620 3 THR C 250   O   168.2  85.6                                        
REMARK 620 4 GLU C 243   OE2  64.3  79.4 125.1                                  
REMARK 620 5 GLU C 252   OE2  83.5 147.5  94.5 124.6                            
REMARK 620 6 THR C 250   OG1  87.0  77.3  81.4 142.8  70.7                      
REMARK 620 7 GLU C 243   OE1 118.3  80.6  71.6  54.0 130.2 146.2                
REMARK 620 8 GLU C 252   OE1  79.5 156.3 108.5  77.0  52.6 122.6  85.9          
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 ARG A 303   O                                                      
REMARK 620 2 ASN A 299   OD1 157.8                                              
REMARK 620 3 ASP A 297   OD1  79.7  79.1                                        
REMARK 620 4 ASP A 305   OD1  83.5 115.0 128.1                                  
REMARK 620 5 ASP A 305   OD2  96.6  86.3  80.6  53.1                            
REMARK 620 6 ASP A 301   OD1  90.1  78.6  76.0 152.8 154.1                      
REMARK 620 7 HOH A 535   O   116.6  80.1 150.1  80.4 119.2  79.0                
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 ASP C 428   OD1                                                    
REMARK 620 2 TYR C 432   O   147.8                                              
REMARK 620 3 ASP C 426   OD1  72.5  75.6                                        
REMARK 620 4 ASN C 430   OD1  89.4  80.6  79.6                                  
REMARK 620 5 ASP C 434   OD2 115.6  91.5 139.0 137.3                            
REMARK 620 6 ASP C 434   OD1  83.9 100.9  90.7 169.5  53.2                      
REMARK 620 7 HOH C 475   O    79.5 127.9 145.4  80.2  71.9 106.3                
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 365   OD2  73.4                                              
REMARK 620 3 ASP A 367   OD1 160.2  86.7                                        
REMARK 620 4 ASP A 373   OD2  80.1 133.2 114.5                                  
REMARK 620 5 ASP A 373   OD1  89.7  89.5  89.6  52.0                            
REMARK 620 6 ASP A 369   OD1  89.1  75.2  86.3 142.8 164.3                      
REMARK 620 7 HOH A 478   O    99.1 147.4  97.9  73.8 122.6  73.0                
REMARK 620 N                    1     2     3     4     5     6                 
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 THR A 250   O                                                      
REMARK 620 2 ASP A 245   OD2 156.9                                              
REMARK 620 3 GLU A 243   OE2 130.5  68.7                                        
REMARK 620 4 ASP A 247   O    83.9  87.0  82.1                                  
REMARK 620 5 THR A 250   OG1  75.7  81.6 144.5  77.2                            
REMARK 620 6 GLU A 243   OE1  76.3 122.4  54.4  78.0 144.2                      
REMARK 620 7 GLU A 252   OE2  83.9  92.5 128.0 147.2  70.2 127.9                
REMARK 620 8 GLU A 252   OE1 108.9  86.1  77.8 160.0 120.2  89.9  52.1          
REMARK 620 N                    1     2     3     4     5     6     7           
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 GLU B 220   OE1 171.8                                              
REMARK 620 3 ASP B 158   OD2  95.4  92.0                                        
REMARK 620 4 PRO B 219   O   102.9  81.6  82.4                                  
REMARK 620 5 ASP B 217   O    76.3  97.1 166.9  89.5                            
REMARK 620 6 ASN B 215   OD1  84.7  90.2 102.9 170.4  86.6                      
REMARK 620 N                    1     2     3     4     5                       
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 MET D 335   O                                                      
REMARK 620 2 ASP D 127   OD1  93.2                                              
REMARK 620 3 ASP D 126   OD1 127.8  80.1                                        
REMARK 620 4 SER D 123   O   157.0  90.6  75.3                                  
REMARK 620 5 ASP D 126   OD2  75.5  88.7  52.8 127.3                            
REMARK 620 6 HOH D 647   O    76.7  98.7 155.5  80.3 151.6                      
REMARK 620 7 HOH D 484   O    87.7 178.7  98.6  88.9  90.8  82.4                
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 CA A 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RC2 A 5000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA B 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3324                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL B 473                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RC2 C 5000                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL C 458                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA D 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE BMA D 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN D 3323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CL D 473                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC9                                                 
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: NDB                                   
DBREF  3T3M A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3T3M B    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3T3M C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3T3M D    1   472  UNP    P05106   ITB3_HUMAN      27    498             
DBREF  3T3M E    1   221  PDB    3T3M     3T3M             1    221             
DBREF  3T3M H    1   221  PDB    3T3M     3T3M             1    221             
DBREF  3T3M F    1   214  PDB    3T3M     3T3M             1    214             
DBREF  3T3M L    1   214  PDB    3T3M     3T3M             1    214             
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 3T3M ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3M ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3M ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3M ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3M ASN D  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3T3M ASN B  320  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    RC2  A5000      27                                                       
HET    SO4  A 458       5                                                       
HET    SO4  A 459       5                                                       
HET    SO4  A 460       5                                                       
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     CL  B 473       1                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    RC2  C5000      27                                                       
HET     CL  C 458       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     CL  D 473       1                                                       
HET    SO4  L 215       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     RC2 N-{3-[5-OXO-7-(PIPERAZIN-1-YL)-5H-[1,3,4]THIADIAZOLO[3,          
HETNAM   2 RC2  2-A]PYRIMIDIN-2-YL]PHENYL}GLYCINAMIDE                           
HETNAM     SO4 SULFATE ION                                                      
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     BMA BETA-D-MANNOSE                                                   
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETNAM      CL CHLORIDE ION                                                     
FORMUL   9   CA    12(CA 2+)                                                    
FORMUL  13  RC2    2(C17 H19 N7 O2 S)                                           
FORMUL  14  SO4    4(O4 S 2-)                                                   
FORMUL  19  NAG    10(C8 H15 N O6)                                              
FORMUL  20  BMA    2(C6 H12 O6)                                                 
FORMUL  20  MAN    3(C6 H12 O6)                                                 
FORMUL  22   CL    3(CL 1-)                                                     
FORMUL  36  HOH   *855(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 CYS B    5  GLY B    9  5                                   5    
HELIX    8   8 SER B   12  ALA B   18  1                                   7    
HELIX    9   9 LEU B   40  LYS B   46  1                                   7    
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  170  ASN B  175  1                                   6    
HELIX   15  15 VAL B  200  LYS B  208  1                                   9    
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  GLU B  323  1                                  10    
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 SER D   12  SER D   20  1                                   9    
HELIX   30  30 LEU D   40  ASP D   47  1                                   8    
HELIX   31  31 ALA D   50  GLU D   52  5                                   3    
HELIX   32  32 ASP D   76  VAL D   80  5                                   5    
HELIX   33  33 SER D  121  SER D  123  5                                   3    
HELIX   34  34 MET D  124  ILE D  131  1                                   8    
HELIX   35  35 ASN D  133  ARG D  143  1                                  11    
HELIX   36  36 PRO D  169  ASN D  175  1                                   7    
HELIX   37  37 VAL D  200  LYS D  209  1                                  10    
HELIX   38  38 GLY D  221  CYS D  232  1                                  12    
HELIX   39  39 CYS D  232  GLY D  237  1                                   6    
HELIX   40  40 LEU D  258  GLY D  264  5                                   7    
HELIX   41  41 SER D  291  ASN D  303  1                                  13    
HELIX   42  42 VAL D  314  GLU D  323  1                                  10    
HELIX   43  43 ASN D  339  ARG D  352  1                                  14    
HELIX   44  44 CYS D  435  ALA D  441  5                                   7    
HELIX   45  45 ASN E   28  THR E   32  5                                   5    
HELIX   46  46 THR E   87  THR E   91  5                                   5    
HELIX   47  47 ASP F   79  PHE F   83  5                                   5    
HELIX   48  48 SER F  121  SER F  127  1                                   7    
HELIX   49  49 LYS F  183  GLU F  187  1                                   5    
HELIX   50  50 ASN H   28  THR H   32  5                                   5    
HELIX   51  51 PRO H   62  GLN H   65  5                                   4    
HELIX   52  52 THR H   74  SER H   76  5                                   3    
HELIX   53  53 ASP L   79  PHE L   83  5                                   5    
HELIX   54  54 SER L  121  THR L  126  1                                   6    
HELIX   55  55 LYS L  183  GLU L  187  1                                   5    
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  VAL A 425   O  ASP A 434           
SHEET    1   B 3 LEU A  23  LYS A  27  0                                        
SHEET    2   B 3 VAL A  33  ALA A  39 -1  O  ALA A  34   N  HIS A  26           
SHEET    3   B 3 GLY A  52  PRO A  57 -1  O  CYS A  56   N  ILE A  35           
SHEET    1   C 4 GLU A  75  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  HIS A 112   N  PHE A  87           
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 173  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  LEU A 270   N  TYR A 253           
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  ARG A 327   N  ALA A 310           
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  GLY A 364           
SHEET    3   I 4 GLN A 388  PHE A 392 -1  O  GLN A 388   N  ALA A 378           
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  ILE B 416   O  LEU B 425           
SHEET    5   L 6 LYS B 354  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   L 6 SER B 385  MET B 387 -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  LYS B 402 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   M 5 SER B 367  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  ILE B 151   O  THR B 197           
SHEET    3   N 6 VAL B 112  ASP B 119  1  N  TYR B 116   O  GLY B 152           
SHEET    4   N 6 SER B 243  THR B 250  1  O  LEU B 245   N  ASP B 113           
SHEET    5   N 6 ILE B 304  VAL B 310  1  O  ILE B 307   N  LEU B 246           
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 SER C  22  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  HIS C 112   N  PHE C  87           
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 103   N  TRP C 100           
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 173  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 280   N  VAL C 267           
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  ALA C 323   N  GLU C 315           
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  LEU C 363           
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  ILE D 416   O  LEU D 425           
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  MET D 118   O  GLY D 154           
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  LEU D 333   N  VAL D 310           
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  SER E  25   N  GLN E   3           
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  VAL E  37   O  TYR E  95           
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  PRO E 129  0                                        
SHEET    2  AH 4 SER E 141  LYS E 149 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AH 4 TYR E 181  LEU E 183 -1  O  LEU E 183   N  VAL E 148           
SHEET    4  AH 4 VAL E 175  LEU E 176 -1  N  VAL E 175   O  THR E 182           
SHEET    1  AI 3 SER E 126  PRO E 129  0                                        
SHEET    2  AI 3 SER E 141  LYS E 149 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AI 3 SER E 186  THR E 190 -1  O  VAL E 187   N  LEU E 144           
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  MET F  11           
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  MET F  45   N  GLN F  37           
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  MET F  11           
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 2 THR F 114  VAL F 115  0                                        
SHEET    2  AN 2 LEU F 136  ASN F 137 -1  O  ASN F 137   N  THR F 114           
SHEET    1  AO 3 GLY F 129  VAL F 133  0                                        
SHEET    2  AO 3 MET F 175  THR F 182 -1  O  LEU F 179   N  VAL F 132           
SHEET    3  AO 3 VAL F 159  TRP F 163 -1  N  LEU F 160   O  THR F 178           
SHEET    1  AP 4 SER F 153  ARG F 155  0                                        
SHEET    2  AP 4 ASN F 145  ILE F 150 -1  N  TRP F 148   O  ARG F 155           
SHEET    3  AP 4 SER F 191  THR F 197 -1  O  GLU F 195   N  LYS F 147           
SHEET    4  AP 4 PHE F 209  ASN F 210 -1  O  PHE F 209   N  TYR F 192           
SHEET    1  AQ 4 GLN H   3  GLN H   6  0                                        
SHEET    2  AQ 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  AQ 4 THR H  78  LEU H  83 -1  O  LEU H  83   N  VAL H  18           
SHEET    4  AQ 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1  AR 6 GLU H  10  VAL H  12  0                                        
SHEET    2  AR 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AR 6 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 115           
SHEET    4  AR 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5  AR 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AR 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  AS 4 GLU H  10  VAL H  12  0                                        
SHEET    2  AS 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AS 4 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 115           
SHEET    4  AS 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
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 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1  AU 4 SER H 126  LEU H 130  0                                        
SHEET    2  AU 4 SER H 141  TYR H 151 -1  O  LEU H 147   N  TYR H 128           
SHEET    3  AU 4 LEU H 180  THR H 190 -1  O  LEU H 183   N  VAL H 148           
SHEET    4  AU 4 VAL H 175  GLN H 177 -1  N  GLN H 177   O  LEU H 180           
SHEET    1  AV 3 THR H 157  TRP H 160  0                                        
SHEET    2  AV 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  AV 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  AW 4 MET L   4  SER L   7  0                                        
SHEET    2  AW 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3  AW 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4  AW 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1  AX 6 SER L  10  VAL L  13  0                                        
SHEET    2  AX 6 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AX 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AX 6 ILE L  33  GLN L  38 -1  N  LEU L  36   O  TYR L  87           
SHEET    5  AX 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6  AX 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  AY 4 SER L  10  VAL L  13  0                                        
SHEET    2  AY 4 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AY 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AY 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AZ 4 THR L 114  PHE L 118  0                                        
SHEET    2  AZ 4 GLY L 129  PHE L 139 -1  O  PHE L 135   N  SER L 116           
SHEET    3  AZ 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4  AZ 4 VAL L 159  TRP L 163 -1  N  LEU L 160   O  THR L 178           
SHEET    1  BA 4 SER L 153  ARG L 155  0                                        
SHEET    2  BA 4 ASN L 145  ILE L 150 -1  N  ILE L 150   O  SER L 153           
SHEET    3  BA 4 SER L 191  THR L 197 -1  O  THR L 197   N  ASN L 145           
SHEET    4  BA 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  2.05  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.04  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.04  
SSBOND   4 CYS B    5    CYS B   23                          1555   1555  2.04  
SSBOND   5 CYS B   13    CYS B  435                          1555   1555  2.03  
SSBOND   6 CYS B   16    CYS B   38                          1555   1555  2.03  
SSBOND   7 CYS B   26    CYS B   49                          1555   1555  2.03  
SSBOND   8 CYS B  177    CYS B  184                          1555   1555  2.05  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.05  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.04  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.03  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.03  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.04  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.03  
SSBOND  17 CYS D    5    CYS D   23                          1555   1555  2.04  
SSBOND  18 CYS D   13    CYS D  435                          1555   1555  2.03  
SSBOND  19 CYS D   16    CYS D   38                          1555   1555  2.03  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.03  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.04  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.04  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.03  
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  2.04  
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  2.03  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.03  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.04  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.04  
LINK         O4  NAG B3321                 C1  BMA B3322     1555   1555  1.44  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.44  
LINK         O3  BMA D3322                 C1  MAN D3323     1555   1555  1.44  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.44  
LINK         O4  NAG B3371                 C1  NAG B3372     1555   1555  1.44  
LINK         ND2 ASN D 371                 C1  NAG D3371     1555   1555  1.44  
LINK         O4  NAG D3321                 C1  BMA D3322     1555   1555  1.44  
LINK         O4  NAG D3371                 C1  NAG D3372     1555   1555  1.44  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.44  
LINK         ND2 ASN D 320                 C1  NAG D3320     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  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.45  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.21  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.26  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.26  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.28  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.28  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.28  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.28  
LINK         OD2 ASP C 245                CA    CA C2004     1555   1555  2.29  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.30  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.30  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.30  
LINK         OE1 GLU D 220                CA    CA D2003     1555   1555  2.31  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.31  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.31  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.31  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.32  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.32  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.33  
LINK         OE1 GLU B 220                CA    CA B2003     1555   1555  2.33  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.34  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.34  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.34  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.34  
LINK         O   MET D 335                CA    CA D2002     1555   1555  2.35  
LINK         OD2 ASP A 245                CA    CA A2004     1555   1555  2.35  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.35  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.35  
LINK         OD2 ASP C 365                CA    CA C2006     1555   1555  2.35  
LINK         OD2 ASP A 365                CA    CA A2006     1555   1555  2.36  
LINK         OE2 GLU A 243                CA    CA A2004     1555   1555  2.36  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.36  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.37  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.37  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.38  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.38  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.38  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.38  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.39  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.40  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.41  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.41  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.41  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.41  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.42  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.42  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.42  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.43  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.43  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.43  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.44  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.45  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.45  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.45  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.46  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.46  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.46  
LINK         OE1 GLU C 243                CA    CA C2004     1555   1555  2.46  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.47  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.48  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.48  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.48  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.49  
LINK         OD2 ASP B 126                CA    CA B2002     1555   1555  2.50  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.50  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.50  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.50  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.51  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.52  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.52  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.52  
LINK         OD2 ASP D 126                CA    CA D2002     1555   1555  2.52  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.52  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.53  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.56  
LINK        CA    CA A2005                 O   HOH A 535     1555   1555  2.28  
LINK        CA    CA C2006                 O   HOH C 654     1555   1555  2.29  
LINK        CA    CA C2005                 O   HOH C 768     1555   1555  2.32  
LINK        CA    CA A2006                 O   HOH A 478     1555   1555  2.33  
LINK        CA    CA D2002                 O   HOH D 647     1555   1555  2.36  
LINK        CA    CA D2002                 O   HOH D 484     1555   1555  2.39  
LINK        CA    CA A2007                 O   HOH A 621     1555   1555  2.40  
LINK        CA    CA C2007                 O   HOH C 475     1555   1555  2.41  
LINK        CA    CA B2002                 O   HOH B 503     1555   1555  2.42  
LINK        CA    CA B2002                 O   HOH B 517     1555   1555  2.44  
CISPEP   1 SER B   84    PRO B   85          0        -4.46                     
CISPEP   2 SER B  162    PRO B  163          0         6.41                     
CISPEP   3 SER B  168    PRO B  169          0        -4.98                     
CISPEP   4 SER D   84    PRO D   85          0        -3.14                     
CISPEP   5 SER D  162    PRO D  163          0        10.26                     
CISPEP   6 SER D  168    PRO D  169          0        -4.16                     
CISPEP   7 PHE E  152    PRO E  153          0        -2.28                     
CISPEP   8 GLU E  154    PRO E  155          0        -5.29                     
CISPEP   9 TRP E  194    PRO E  195          0        -0.78                     
CISPEP  10 SER F    7    PRO F    8          0        -2.76                     
CISPEP  11 LEU F   94    PRO F   95          0        -0.28                     
CISPEP  12 TYR F  140    PRO F  141          0         2.86                     
CISPEP  13 PHE H  152    PRO H  153          0        -4.23                     
CISPEP  14 GLU H  154    PRO H  155          0        -2.74                     
CISPEP  15 TRP H  194    PRO H  195          0         0.67                     
CISPEP  16 SER L    7    PRO L    8          0        -3.80                     
CISPEP  17 LEU L   94    PRO L   95          0        -0.04                     
CISPEP  18 TYR L  140    PRO L  141          0         2.72                     
SITE     1 AC1  5 GLU A 243  ASP A 245  ASP A 247  THR A 250                    
SITE     2 AC1  5 GLU A 252                                                     
SITE     1 AC2  6 ASP A 297  ASN A 299  ASP A 301  ARG A 303                    
SITE     2 AC2  6 ASP A 305  HOH A 535                                          
SITE     1 AC3  6 ASP A 365  ASP A 367  ASP A 369  TYR A 371                    
SITE     2 AC3  6 ASP A 373  HOH A 478                                          
SITE     1 AC4  6 ASP A 426  ASP A 428  ASN A 430  TYR A 432                    
SITE     2 AC4  6 ASP A 434  HOH A 621                                          
SITE     1 AC5 17 PHE A 160  TYR A 190  LEU A 192  ASP A 224                    
SITE     2 AC5 17 SER A 225  PHE A 231  HOH A 514  HOH A 648                    
SITE     3 AC5 17 HOH A 658  TYR B 166  ARG B 214  ASN B 215                    
SITE     4 AC5 17 ARG B 216  ASP B 217  GLU B 220   CL B 473                    
SITE     5 AC5 17 HOH B 506                                                     
SITE     1 AC6  4 ARG A 279  ARG A 281  HOH A 756  MAN B3323                    
SITE     1 AC7  4 ARG A 400  SER A 401  ARG A 402  HOH A 662                    
SITE     1 AC8  2 PHE A  10  GLN A 444                                          
SITE     1 AC9  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 AC9  6 HOH B 503  HOH B 517                                          
SITE     1 BC1  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC1  5 GLU B 220                                                     
SITE     1 BC2  3 LYS B  98  ASN B  99  HOH B 546                               
SITE     1 BC3  7 MET A 285  ASN B 320  HOH B 519  HOH B 572                    
SITE     2 BC3  7 HOH B 575  HOH B 680  NAG B3321                               
SITE     1 BC4  3 ARG A 281  NAG B3320  BMA B3322                               
SITE     1 BC5  3 NAG B3321  MAN B3323  MAN B3324                               
SITE     1 BC6  4 ARG A 281  SO4 A 458  HOH B 530  BMA B3322                    
SITE     1 BC7  1 BMA B3322                                                     
SITE     1 BC8  6 ASN B 371  PRO B 381  SER B 398  ILE B 399                    
SITE     2 BC8  6 GLU B 400  NAG B3372                                          
SITE     1 BC9  1 NAG B3371                                                     
SITE     1 CC1  4 RC2 A5000  TYR B 122  ARG B 214  ASN B 215                    
SITE     1 CC2  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 CC2  5 GLU C 252                                                     
SITE     1 CC3  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 CC3  6 ASP C 305  HOH C 768                                          
SITE     1 CC4  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 CC4  6 ASP C 373  HOH C 654                                          
SITE     1 CC5  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 CC5  6 ASP C 434  HOH C 475                                          
SITE     1 CC6 15 PHE C 160  TYR C 190  LEU C 192  ASP C 224                    
SITE     2 CC6 15 SER C 225  PHE C 231  HOH C 461  HOH C 620                    
SITE     3 CC6 15 HOH C 794  ARG D 214  ASN D 215  ARG D 216                    
SITE     4 CC6 15 ASP D 217  GLU D 220   CL D 473                               
SITE     1 CC7  4 ARG C 279  ARG C 281  HOH C 807  MAN D3323                    
SITE     1 CC8  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 CC8  6 HOH D 484  HOH D 647                                          
SITE     1 CC9  5 ASP D 158  ASN D 215  ASP D 217  PRO D 219                    
SITE     2 CC9  5 GLU D 220                                                     
SITE     1 DC1  6 LYS D  98  ASN D  99  PHE D 100  SER D 101                    
SITE     2 DC1  6 HOH D 528  NAG D3372                                          
SITE     1 DC2  5 MET C 285  ASN D 320  HOH D 527  HOH D 533                    
SITE     2 DC2  5 NAG D3321                                                     
SITE     1 DC3  4 ARG C 281  HOH D 533  NAG D3320  BMA D3322                    
SITE     1 DC4  2 NAG D3321  MAN D3323                                          
SITE     1 DC5  3 ARG C 281   CL C 458  BMA D3322                               
SITE     1 DC6  4 ASN D 371  SER D 398  GLU D 400  NAG D3372                    
SITE     1 DC7  2 NAG D3099  NAG D3371                                          
SITE     1 DC8  5 HOH C 793  RC2 C5000  TYR D 122  ARG D 214                    
SITE     2 DC8  5 ASN D 215                                                     
SITE     1 DC9  6 ARG C  73  GLU L 154  ARG L 155  GLN L 156                    
SITE     2 DC9  6 ASN L 157  HOH L 519                                          
CRYST1  261.150  145.330  104.680  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      0.003829  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006881  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009553        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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