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Entry: 3NIG
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HEADER    CELL ADHESION/BLOOD CLOTTING            15-JUN-10   3NIG              
TITLE     THE CLOSED HEADPIECE OF INTEGRIN IIB 3 AND ITS COMPLEX WITH AN IIB 3 -
TITLE    2 SPECIFIC ANTAGONIST THAT DOES NOT INDUCE OPENING                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INTEGRIN ALPHA-IIB;                                        
COMPND   3 CHAIN: A, C;                                                         
COMPND   4 FRAGMENT: INTEGRIN ALPHA-IIB, RESIDUES 32-488;                       
COMPND   5 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIB, GPALPHA IIB, GPIIB,     
COMPND   6 INTEGRIN ALPHA-IIB HEAVY CHAIN;                                      
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: INTEGRIN BETA-3;                                           
COMPND  10 CHAIN: B, D;                                                         
COMPND  11 FRAGMENT: INTEGRIN BETA-3, RESIDUES 27-497;                          
COMPND  12 SYNONYM: PLATELET MEMBRANE GLYCOPROTEIN IIIA, GPIIIA, CD61;          
COMPND  13 ENGINEERED: YES;                                                     
COMPND  14 MOL_ID: 3;                                                           
COMPND  15 MOLECULE: MMONOCLONAL ANTIBODY 10E5 HEAVY CHAIN;                     
COMPND  16 CHAIN: E, H;                                                         
COMPND  17 ENGINEERED: YES;                                                     
COMPND  18 MOL_ID: 4;                                                           
COMPND  19 MOLECULE: MMONOCLONAL ANTIBODY 10E5 LIGHT CHAIN;                     
COMPND  20 CHAIN: F, L;                                                         
COMPND  21 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_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: CHO LEC 3.2.8.1;                           
SOURCE  10 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  11 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;                          
SOURCE  14 MOL_ID: 2;                                                           
SOURCE  15 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  16 ORGANISM_COMMON: HUMAN;                                              
SOURCE  17 ORGANISM_TAXID: 9606;                                                
SOURCE  18 GENE: ITGB3, GP3A;                                                   
SOURCE  19 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE  20 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE  21 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE  22 EXPRESSION_SYSTEM_CELL_LINE: LEC 3.2.8.1;                            
SOURCE  23 EXPRESSION_SYSTEM_CELL: CHO;                                         
SOURCE  24 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  25 EXPRESSION_SYSTEM_PLASMID: PCDNA 3.1, PEF1;                          
SOURCE  26 MOL_ID: 3;                                                           
SOURCE  27 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  28 ORGANISM_COMMON: MOUSE;                                              
SOURCE  29 ORGANISM_TAXID: 10090;                                               
SOURCE  30 STRAIN: BALB/C;                                                      
SOURCE  31 CELL_LINE: 10E5 HYBRIDOMA;                                           
SOURCE  32 MOL_ID: 4;                                                           
SOURCE  33 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  34 ORGANISM_COMMON: MOUSE;                                              
SOURCE  35 ORGANISM_TAXID: 10090;                                               
SOURCE  36 STRAIN: BALB/C;                                                      
SOURCE  37 CELL_LINE: 10E5 HYBRIDOMA                                            
KEYWDS    INTEGRIN, HEADPIECE, ALPHAIIB, BETA3, CELL ADHESION-IMMUNE SYSTEM     
KEYWDS   2 COMPLEX, CELL ADHESION-BLOOD CLOTTING COMPLEX                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.H.ZHU,J.Q.ZHU,T.A.SPRINGER                                          
REVDAT   1   22-DEC-10 3NIG    0                                                
JRNL        AUTH   J.ZHU,J.ZHU,A.NEGRI,D.PROVASI,M.FILIZOLA,B.S.COLLER,         
JRNL        AUTH 2 T.A.SPRINGER                                                 
JRNL        TITL   CLOSED HEADPIECE OF INTEGRIN {ALPHA}IIB{BETA}3 AND ITS       
JRNL        TITL 2 COMPLEX WITH AN {ALPHA}IIB{BETA}3-SPECIFIC ANTAGONIST THAT   
JRNL        TITL 3 DOES NOT INDUCE OPENING.                                     
JRNL        REF    BLOOD                         V. 116  5050 2010              
JRNL        REFN                   ISSN 0006-4971                               
JRNL        PMID   20679525                                                     
JRNL        DOI    10.1182/BLOOD-2010-04-281154                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6_289)                      
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.49                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 187662                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.172                           
REMARK   3   FREE R VALUE                     : 0.212                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 0.540                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1009                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.5026 -  4.3033    1.00    27438   150  0.1569 0.1850        
REMARK   3     2  4.3033 -  3.4159    1.00    26772   155  0.1503 0.1741        
REMARK   3     3  3.4159 -  2.9842    1.00    26563   153  0.1603 0.2383        
REMARK   3     4  2.9842 -  2.7114    1.00    26594   136  0.1629 0.2130        
REMARK   3     5  2.7114 -  2.5170    1.00    26453   140  0.1703 0.2404        
REMARK   3     6  2.5170 -  2.3686    1.00    26447   129  0.1901 0.2532        
REMARK   3     7  2.3686 -  2.2500    1.00    26386   146  0.2138 0.2560        
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              : 44.27                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.330            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
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) : -2.08430                                             
REMARK   3    B22 (A**2) : 3.05830                                              
REMARK   3    B33 (A**2) : -0.97400                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.00000                                             
REMARK   3    B23 (A**2) : -0.00000                                             
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.009          21518                                  
REMARK   3   ANGLE     :  1.153          29249                                  
REMARK   3   CHIRALITY :  0.071           3252                                  
REMARK   3   PLANARITY :  0.005           3795                                  
REMARK   3   DIHEDRAL  : 16.385           7692                                  
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):  51.3613  90.9646  54.3938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1608 T22:  -0.0197                                     
REMARK   3      T33:   0.1245 T12:   0.0063                                     
REMARK   3      T13:   0.0538 T23:   0.0499                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5303 L22:   0.4988                                     
REMARK   3      L33:   0.6514 L12:  -0.0187                                     
REMARK   3      L13:  -0.1490 L23:   0.3933                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0126 S12:  -0.0168 S13:  -0.0299                       
REMARK   3      S21:   0.0636 S22:  -0.0078 S23:   0.0230                       
REMARK   3      S31:   0.1431 S32:  -0.0262 S33:   0.0200                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN C AND RESID 1:450                                
REMARK   3    ORIGIN FOR THE GROUP (A):  84.9773  86.9114 117.5757              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2033 T22:   0.2029                                     
REMARK   3      T33:   0.1340 T12:   0.0570                                     
REMARK   3      T13:   0.0716 T23:   0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3473 L22:   0.4964                                     
REMARK   3      L33:   1.2867 L12:   0.2875                                     
REMARK   3      L13:  -0.5320 L23:  -0.3513                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0901 S12:  -0.0744 S13:  -0.0675                       
REMARK   3      S21:  -0.1104 S22:  -0.0256 S23:  -0.0593                       
REMARK   3      S31:   0.2669 S32:   0.3099 S33:   0.1219                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A): 123.9426  88.7267  35.2145              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4733 T22:   1.6711                                     
REMARK   3      T33:   0.9053 T12:   0.4182                                     
REMARK   3      T13:   0.0453 T23:  -0.3924                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.9538 L22:   1.3354                                     
REMARK   3      L33:   1.0358 L12:  -1.3818                                     
REMARK   3      L13:   1.3288 L23:  -0.7231                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3116 S12:   0.6837 S13:   0.5466                       
REMARK   3      S21:   0.2251 S22:   0.0657 S23:  -0.5124                       
REMARK   3      S31:   0.1870 S32:   1.3116 S33:  -0.0131                       
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): 101.6846 108.0573  52.6381              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2276 T22:   0.6070                                     
REMARK   3      T33:   0.6054 T12:   0.0869                                     
REMARK   3      T13:   0.0114 T23:  -0.2477                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2747 L22:   0.3170                                     
REMARK   3      L33:   1.3540 L12:  -0.0672                                     
REMARK   3      L13:  -0.3881 L23:   0.3908                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0085 S12:  -0.0984 S13:   0.3100                       
REMARK   3      S21:  -0.0261 S22:   0.3525 S23:  -0.1703                       
REMARK   3      S31:   0.1141 S32:   0.9141 S33:  -0.3826                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  68.2942 119.0274  63.3295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2181 T22:   0.0506                                     
REMARK   3      T33:   0.2047 T12:   0.0102                                     
REMARK   3      T13:   0.0462 T23:   0.0018                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6443 L22:   1.1537                                     
REMARK   3      L33:   0.5236 L12:   0.2311                                     
REMARK   3      L13:  -0.0516 L23:   0.4564                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0316 S12:  -0.0234 S13:   0.1191                       
REMARK   3      S21:  -0.0081 S22:   0.0780 S23:  -0.0826                       
REMARK   3      S31:  -0.1161 S32:   0.0270 S33:  -0.0509                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A): 117.6261  90.2055  19.8589              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3959 T22:   1.4701                                     
REMARK   3      T33:   0.7437 T12:   0.2528                                     
REMARK   3      T13:   0.1294 T23:  -0.1611                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1686 L22:   0.3950                                     
REMARK   3      L33:   0.1515 L12:   0.2471                                     
REMARK   3      L13:  -0.1128 L23:  -0.0994                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1645 S12:  -1.0057 S13:   0.2120                       
REMARK   3      S21:  -0.1366 S22:  -0.4804 S23:  -0.0674                       
REMARK   3      S31:   0.1065 S32:   0.4237 S33:   0.2345                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 1:57                                 
REMARK   3    ORIGIN FOR THE GROUP (A):  15.5861  70.9675 140.7228              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6119 T22:   1.0559                                     
REMARK   3      T33:   0.4547 T12:  -0.6411                                     
REMARK   3      T13:   0.1777 T23:  -0.0145                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2787 L22:   1.2559                                     
REMARK   3      L33:   1.2203 L12:   1.1320                                     
REMARK   3      L13:   0.2698 L23:  -0.1139                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3800 S12:  -0.0222 S13:  -0.1525                       
REMARK   3      S21:  -0.3072 S22:  -0.1114 S23:   0.2415                       
REMARK   3      S31:   0.6495 S32:  -1.1262 S33:   0.2315                       
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):  31.8466  87.8586 115.8306              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3468 T22:   0.6914                                     
REMARK   3      T33:   0.2498 T12:  -0.2496                                     
REMARK   3      T13:   0.0243 T23:   0.1116                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9256 L22:   0.3203                                     
REMARK   3      L33:   1.9122 L12:   0.1841                                     
REMARK   3      L13:  -0.9632 L23:  -0.3743                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2992 S12:   0.5466 S13:  -0.0012                       
REMARK   3      S21:  -0.1172 S22:   0.2293 S23:  -0.0010                       
REMARK   3      S31:   0.4490 S32:  -1.0005 S33:  -0.0037                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN D AND RESID 109:352                              
REMARK   3    ORIGIN FOR THE GROUP (A):  61.0605 102.7883  99.3917              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1984 T22:   0.2125                                     
REMARK   3      T33:   0.1335 T12:  -0.0742                                     
REMARK   3      T13:   0.0253 T23:   0.0768                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9902 L22:   0.2283                                     
REMARK   3      L33:   1.4439 L12:  -0.1538                                     
REMARK   3      L13:   0.0264 L23:  -0.3510                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0241 S12:   0.2252 S13:   0.1069                       
REMARK   3      S21:  -0.0411 S22:   0.0950 S23:  -0.0037                       
REMARK   3      S31:   0.0680 S32:  -0.2386 S33:  -0.0533                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 433:461                              
REMARK   3    ORIGIN FOR THE GROUP (A):  19.7323  80.8706 153.3467              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4355 T22:   0.6250                                     
REMARK   3      T33:   0.3865 T12:  -0.2578                                     
REMARK   3      T13:   0.1166 T23:  -0.0774                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2160 L22:   0.0976                                     
REMARK   3      L33:   3.1732 L12:   0.1980                                     
REMARK   3      L13:  -0.9027 L23:  -0.1378                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3481 S12:  -0.0293 S13:   0.5558                       
REMARK   3      S21:  -0.0563 S22:  -0.0792 S23:   0.1447                       
REMARK   3      S31:   0.3789 S32:  -0.2698 S33:   0.2981                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.3644  97.2739  82.6918              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3541 T22:   0.4370                                     
REMARK   3      T33:   0.2923 T12:  -0.1063                                     
REMARK   3      T13:   0.1644 T23:  -0.0875                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.4127 L22:   1.3024                                     
REMARK   3      L33:   0.7510 L12:  -0.1364                                     
REMARK   3      L13:  -0.7886 L23:   0.3800                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1498 S12:  -0.1767 S13:   0.0400                       
REMARK   3      S21:   0.4858 S22:  -0.2690 S23:   0.1446                       
REMARK   3      S31:   0.2394 S32:  -0.2643 S33:   0.1207                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN H AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): -13.7797  81.8670  92.8544              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3605 T22:   0.3576                                     
REMARK   3      T33:   1.5889 T12:   0.0697                                     
REMARK   3      T13:   0.2388 T23:   0.0766                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9402 L22:   0.6150                                     
REMARK   3      L33:   2.8180 L12:  -1.3359                                     
REMARK   3      L13:   0.7469 L23:  -0.2959                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2799 S12:   0.0339 S13:  -1.6790                       
REMARK   3      S21:   0.2556 S22:   0.1555 S23:   0.5058                       
REMARK   3      S31:   0.8016 S32:   0.4030 S33:   0.1490                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A):   7.0514  96.5009  64.3021              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1307 T22:   0.6580                                     
REMARK   3      T33:   0.6109 T12:  -0.0263                                     
REMARK   3      T13:   0.0530 T23:  -0.2727                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2638 L22:   1.8022                                     
REMARK   3      L33:   1.3626 L12:   0.2718                                     
REMARK   3      L13:  -0.2794 L23:   0.7240                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0273 S12:   0.1909 S13:   0.0486                       
REMARK   3      S21:  -0.0640 S22:  -0.5460 S23:   0.8597                       
REMARK   3      S31:   0.0136 S32:  -0.8488 S33:   0.5063                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN L AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): -22.1780  93.8591  86.1368              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1540 T22:   0.4951                                     
REMARK   3      T33:   0.9255 T12:   0.0314                                     
REMARK   3      T13:   0.2369 T23:  -0.0864                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3704 L22:   0.2682                                     
REMARK   3      L33:   0.7912 L12:  -0.1037                                     
REMARK   3      L13:  -0.4124 L23:   0.3909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4249 S12:   0.3680 S13:  -1.5104                       
REMARK   3      S21:   0.0572 S22:  -0.1206 S23:   0.4163                       
REMARK   3      S31:   0.0297 S32:  -0.4374 S33:   0.5319                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 1:119                                
REMARK   3    ORIGIN FOR THE GROUP (A): 115.6334  90.1745  86.1974              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8467 T22:   0.7989                                     
REMARK   3      T33:   0.3600 T12:   0.0102                                     
REMARK   3      T13:   0.2746 T23:   0.0059                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.1170 L22:   1.0556                                     
REMARK   3      L33:   0.6431 L12:  -0.3152                                     
REMARK   3      L13:   0.3789 L23:  -0.7136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0537 S12:   0.2873 S13:  -0.0110                       
REMARK   3      S21:  -0.8477 S22:  -0.1376 S23:  -0.1463                       
REMARK   3      S31:   1.0628 S32:   0.2565 S33:   0.1594                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN E AND RESID 120:221                              
REMARK   3    ORIGIN FOR THE GROUP (A): 151.0473  82.2590  79.7093              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2746 T22:   1.4912                                     
REMARK   3      T33:   0.7839 T12:   0.8762                                     
REMARK   3      T13:   0.0844 T23:   0.0528                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3856 L22:   0.0001                                     
REMARK   3      L33:   0.0384 L12:  -0.0277                                     
REMARK   3      L13:  -0.0451 L23:   0.0210                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3915 S12:   0.3139 S13:  -0.0281                       
REMARK   3      S21:  -0.1959 S22:  -0.1246 S23:  -0.1544                       
REMARK   3      S31:   0.5536 S32:   0.2121 S33:  -0.1337                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 1:108                                
REMARK   3    ORIGIN FOR THE GROUP (A): 126.0399 100.3007 102.2099              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1945 T22:   0.8715                                     
REMARK   3      T33:   0.5967 T12:  -0.0599                                     
REMARK   3      T13:   0.1679 T23:   0.0522                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.5807 L22:   1.6921                                     
REMARK   3      L33:   1.3636 L12:  -1.5404                                     
REMARK   3      L13:   0.7883 L23:  -0.4055                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1456 S12:  -0.2552 S13:   0.8793                       
REMARK   3      S21:  -0.0266 S22:  -0.1530 S23:  -0.7551                       
REMARK   3      S31:   0.0970 S32:   0.6065 S33:   0.2330                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN F AND RESID 109:214                              
REMARK   3    ORIGIN FOR THE GROUP (A): 155.1109  98.2611  80.3064              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3789 T22:   1.5323                                     
REMARK   3      T33:   0.7915 T12:   0.2512                                     
REMARK   3      T13:   0.4200 T23:   0.3127                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0085 L22:   0.2637                                     
REMARK   3      L33:   1.2072 L12:  -0.0551                                     
REMARK   3      L13:   0.0256 L23:   0.1395                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0630 S12:  -0.2128 S13:   0.0787                       
REMARK   3      S21:  -0.2116 S22:  -0.0568 S23:  -0.5257                       
REMARK   3      S31:  -0.0092 S32:   1.5632 S33:   0.0552                       
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 3NIG COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-DEC-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB059869.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-JUL-09                          
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) : 0.97948                            
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   : 187671                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.630                              
REMARK 200  R MERGE                    (I) : 0.09400                            
REMARK 200  R SYM                      (I) : 0.09400                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.1100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.31                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.98                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.99400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 3NID                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.01                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
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      130.33500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       72.58500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000      130.33500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       72.58500            
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     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     VAL C   454                                                      
REMARK 465     LYS C   455                                                      
REMARK 465     ALA C   456                                                      
REMARK 465     SER C   457                                                      
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 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 L   765     O    HOH L  1141              2.00            
REMARK 500   ND2  ASN B   371     C2   NAG B  3371              2.06            
REMARK 500   O    HOH B   514     O    HOH B  1038              2.12            
REMARK 500   O3   SO4 A   461     O    HOH A  1036              2.13            
REMARK 500   O    HOH A  1053     O    HOH A  1142              2.14            
REMARK 500   O    HOH C  1051     O    HOH C  1146              2.14            
REMARK 500   O    HOH A  1173     O    HOH B  1174              2.16            
REMARK 500   O    HOH C  1190     O    HOH D   766              2.18            
REMARK 500   O    HOH A  1054     O    HOH A  1142              2.18            
REMARK 500   O    HOH A   820     O    HOH A  1118              2.19            
REMARK 500   O    HOH C   583     O    HOH C  1191              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B 202   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG B 202   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  46       32.88    -83.34                                   
REMARK 500    GLN A  47       28.31     48.09                                   
REMARK 500    SER A 101     -129.85     54.20                                   
REMARK 500    LYS A 118     -119.41     59.01                                   
REMARK 500    GLU A 123      138.09     93.49                                   
REMARK 500    LEU A 212      -43.86     73.29                                   
REMARK 500    SER A 222     -167.00    -78.17                                   
REMARK 500    ASP A 319       39.55     78.76                                   
REMARK 500    PRO A 337      100.08    -50.14                                   
REMARK 500    PHE A 417      121.18    -39.36                                   
REMARK 500    PRO B   2       92.50    -49.01                                   
REMARK 500    ASN B   3     -173.97    -65.61                                   
REMARK 500    ALA B  30       54.47   -104.37                                   
REMARK 500    PRO B  32      177.41    -52.64                                   
REMARK 500    PHE B  56       85.25   -156.12                                   
REMARK 500    ASP B  66       28.67   -143.11                                   
REMARK 500    ARG B  67      133.34    -36.04                                   
REMARK 500    ASP B  76      100.90    -50.26                                   
REMARK 500    VAL B 157      -77.30   -125.38                                   
REMARK 500    MET B 180     -163.04   -101.18                                   
REMARK 500    SER B 213     -159.88   -121.66                                   
REMARK 500    ASP B 241       72.32   -117.41                                   
REMARK 500    LYS B 253      173.81    -57.42                                   
REMARK 500    LEU B 258      -10.88     88.81                                   
REMARK 500    CYS B 374      -92.52   -109.58                                   
REMARK 500    PRO B 381      151.27    -48.19                                   
REMARK 500    GLN B 440       47.64   -140.23                                   
REMARK 500    ASN B 450       69.08     66.38                                   
REMARK 500    SER C 101     -130.87     59.55                                   
REMARK 500    LYS C 118     -111.11     58.05                                   
REMARK 500    GLU C 123      137.10     98.59                                   
REMARK 500    PHE C 191       13.33     81.39                                   
REMARK 500    LEU C 212      -51.85     73.14                                   
REMARK 500    ASP C 319       34.17     79.38                                   
REMARK 500    ALA C 424        9.57     81.52                                   
REMARK 500    ASN D   3     -174.15   -172.67                                   
REMARK 500    ASP D  47       33.90    -99.58                                   
REMARK 500    PHE D  56       76.92   -153.30                                   
REMARK 500    ASP D  66       42.14   -143.25                                   
REMARK 500    PRO D  85      170.96    -59.88                                   
REMARK 500    VAL D 157      -80.70   -126.61                                   
REMARK 500    LYS D 181       33.51    -88.36                                   
REMARK 500    SER D 213     -159.21   -121.76                                   
REMARK 500    ASP D 241       74.58   -111.11                                   
REMARK 500    LYS D 253      173.22    -53.04                                   
REMARK 500    LEU D 258      -13.97     88.15                                   
REMARK 500    SER D 337       15.12     56.35                                   
REMARK 500    CYS D 374      -87.48   -103.58                                   
REMARK 500    ASN D 376     -157.68     54.26                                   
REMARK 500    ASP E  73       92.89   -168.40                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      86 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 SER B   78     GLN B   79                  138.50                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH B1037   O                                                      
REMARK 620 2 GLU B 220   OE2 108.8                                              
REMARK 620 3 HOH B1039   O    97.2  89.6                                        
REMARK 620 4 HOH B 514   O   167.3  76.1  94.6                                  
REMARK 620 5 SER B 121   OG   71.3  88.4 167.0  97.4                            
REMARK 620 6 HOH B 897   O   113.1 131.3 108.2  58.1  82.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D2001  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D 475   O                                                      
REMARK 620 2 HOH D 505   O   105.2                                              
REMARK 620 3 GLU D 220   OE2 104.9  95.9                                        
REMARK 620 4 HOH D 864   O    86.7  94.6 161.7                                  
REMARK 620 5 HOH D1092   O   160.9  93.8  74.4  89.9                            
REMARK 620 6 SER D 121   OG   71.5 170.9  77.1  93.7  90.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2003  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 217   OD1                                                    
REMARK 620 2 GLU D 220   OE1 162.7                                              
REMARK 620 3 PRO D 219   O    98.8  81.1                                        
REMARK 620 4 ASN D 215   OD1  93.8  85.1 166.1                                  
REMARK 620 5 ASP D 158   OD2  97.5  99.5  81.7 102.5                            
REMARK 620 6 ASP D 217   O    75.4  87.3  87.4  90.1 166.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2004  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR C 250   O                                                      
REMARK 620 2 ASP C 245   OD2 155.5                                              
REMARK 620 3 ASP C 247   O    90.4  95.4                                        
REMARK 620 4 GLU C 243   OE1  78.4 125.4  89.7                                  
REMARK 620 5 GLU C 243   OE2 128.5  75.2  91.8  50.2                            
REMARK 620 6 GLU C 252   OE2  88.7  71.7 140.1 129.0 119.2                      
REMARK 620 7 GLU C 252   OE1 101.3  76.3 167.0  87.1  76.4  47.1                
REMARK 620 8 THR C 250   OG1  77.0  82.2  71.9 148.9 150.8  69.1 116.1          
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 PRO B 219   O   101.1                                              
REMARK 620 3 ASP B 158   OD2  94.7  84.9                                        
REMARK 620 4 GLU B 220   OE1 168.1  82.1  97.0                                  
REMARK 620 5 ASN B 215   OD1  89.4 168.8  98.2  86.9                            
REMARK 620 6 ASP B 217   O    76.1  88.6 167.6  92.6  90.2                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA C2007  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR C 432   O                                                      
REMARK 620 2 HOH C 566   O   129.8                                              
REMARK 620 3 ASP C 428   OD1 154.7  73.9                                        
REMARK 620 4 ASP C 426   OD1  79.3 148.0  75.7                                  
REMARK 620 5 ASP C 434   OD2  83.7  72.1 115.8 131.9                            
REMARK 620 6 ASN C 430   OD1  85.9  83.0  89.4  86.8 136.5                      
REMARK 620 7 ASP C 434   OD1  95.1 100.1  87.5  88.3  48.7 174.8                
REMARK 620 N                    1     2     3     4     5     6                 
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 155.3                                              
REMARK 620 3 ASP C 297   OD1  73.5  81.8                                        
REMARK 620 4 HOH C 810   O   116.1  87.3 157.9                                  
REMARK 620 5 ASP C 305   OD2  93.6  85.3  88.7 109.5                            
REMARK 620 6 ASP C 305   OD1  89.1 108.3 134.2  67.5  49.6                      
REMARK 620 7 ASP C 301   OD1  86.7  87.6  75.6  84.8 163.6 146.7                
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 ASP A 245   OD2                                                    
REMARK 620 2 THR A 250   O   156.8                                              
REMARK 620 3 GLU A 243   OE1 128.2  74.7                                        
REMARK 620 4 GLU A 243   OE2  75.7 127.4  52.7                                  
REMARK 620 5 THR A 250   OG1  80.7  77.0 142.5 147.8                            
REMARK 620 6 ASP A 247   O    93.6  87.2  78.8  84.2  75.7                      
REMARK 620 7 GLU A 252   OE2  76.7  90.0 131.9 122.4  71.6 147.0                
REMARK 620 8 GLU A 252   OE1  83.8 102.0  88.9  78.1 121.0 162.2  49.4          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2005  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASN A 299   OD1                                                    
REMARK 620 2 ARG A 303   O   155.6                                              
REMARK 620 3 ASP A 297   OD1  81.0  74.7                                        
REMARK 620 4 HOH A 559   O    92.3 109.0 155.8                                  
REMARK 620 5 ASP A 305   OD1 114.0  83.4 127.4  76.6                            
REMARK 620 6 ASP A 305   OD2  85.6  93.5  82.7 120.2  51.2                      
REMARK 620 7 ASP A 301   OD1  84.9  86.8  75.1  81.1 151.1 157.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2006  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 371   O                                                      
REMARK 620 2 ASP A 367   OD1 160.7                                              
REMARK 620 3 HOH A 491   O   101.0  96.9                                        
REMARK 620 4 ASP A 365   OD2  76.7  84.0 154.5                                  
REMARK 620 5 ASP A 373   OD2  77.7 114.6  74.6 128.2                            
REMARK 620 6 ASP A 369   OD1  91.8  84.6  77.9  76.8 147.9                      
REMARK 620 7 ASP A 373   OD1  89.1  88.4 120.1  85.3  50.0 161.4                
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 157.3                                              
REMARK 620 3 ASP A 426   OD1  82.8  74.5                                        
REMARK 620 4 HOH A 478   O   123.5  77.9 149.6                                  
REMARK 620 5 ASN A 430   OD1  88.8  88.1  87.0  79.4                            
REMARK 620 6 ASP A 434   OD1  94.1  87.5  88.9 102.6 174.7                      
REMARK 620 7 ASP A 434   OD2  77.7 119.4 132.7  73.0 134.6  50.6                
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 HOH C 495   O                                                      
REMARK 620 2 TYR C 371   O   103.9                                              
REMARK 620 3 ASP C 367   OD1 102.1 148.3                                        
REMARK 620 4 ASP C 373   OD2  76.8  86.5 117.1                                  
REMARK 620 5 ASP C 365   OD2 149.8  75.3  73.1 132.5                            
REMARK 620 6 ASP C 369   OD1  75.1  85.3  84.2 147.7  74.8                      
REMARK 620 7 ASP C 373   OD1 123.4  92.4  88.2  50.2  86.6 161.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA D2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP D 127   OD1                                                    
REMARK 620 2 MET D 335   O    89.6                                              
REMARK 620 3 HOH D 515   O   173.4  92.7                                        
REMARK 620 4 SER D 123   O    88.7 162.2  90.9                                  
REMARK 620 5 HOH D 503   O    91.9  80.2  94.5  82.2                            
REMARK 620 6 ASP D 126   OD1  79.4 121.5  94.2  75.6 156.2                      
REMARK 620 7 ASP D 126   OD2  90.5  75.8  84.1 121.9 155.8  47.4                
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 MET B 335   O                                                      
REMARK 620 2 HOH B 537   O    98.8                                              
REMARK 620 3 ASP B 127   OD1  91.2 170.0                                        
REMARK 620 4 HOH B 750   O    73.5  90.2  93.4                                  
REMARK 620 5 SER B 123   O   156.6  80.1  91.1  83.2                            
REMARK 620 6 ASP B 126   OD1 123.1  88.2  85.7 163.4  80.2                      
REMARK 620 7 ASP B 126   OD2  75.4  91.7  90.0 148.8 127.8  47.9                
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 GOL A 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 461                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 2001                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2002                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA B 2003                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3099                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3320                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3321                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MAN B 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG B 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2004                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2005                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2006                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA C 2007                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL C 458                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 459                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 C 460                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: CC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 2001                 
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 MAN D 3322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3371                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NAG D 3372                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 472                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: DC8                                                 
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: 2VDR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NID   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3NIF   RELATED DB: PDB                                   
DBREF  3NIG A    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3NIG B    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  3NIG C    1   457  UNP    P08514   ITA2B_HUMAN     32    488             
DBREF  3NIG D    1   471  UNP    P05106   ITB3_HUMAN      27    497             
DBREF  3NIG E    1   221  PDB    3NIG     3NIG             1    221             
DBREF  3NIG H    1   221  PDB    3NIG     3NIG             1    221             
DBREF  3NIG F    1   214  PDB    3NIG     3NIG             1    214             
DBREF  3NIG L    1   214  PDB    3NIG     3NIG             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  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 B  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 B  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 B  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 B  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 B  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 B  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 B  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 B  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 B  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 B  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 B  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 B  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 B  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 B  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 B  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 B  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 B  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 B  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 B  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 B  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 B  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 B  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 B  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 B  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 B  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 B  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 B  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 B  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 B  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 B  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 B  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 B  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 B  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 B  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 B  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 B  471  SER GLN CYS                                                  
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  471  GLY PRO ASN ILE CYS THR THR ARG GLY VAL SER SER CYS          
SEQRES   2 D  471  GLN GLN CYS LEU ALA VAL SER PRO MET CYS ALA TRP CYS          
SEQRES   3 D  471  SER ASP GLU ALA LEU PRO LEU GLY SER PRO ARG CYS ASP          
SEQRES   4 D  471  LEU LYS GLU ASN LEU LEU LYS ASP ASN CYS ALA PRO GLU          
SEQRES   5 D  471  SER ILE GLU PHE PRO VAL SER GLU ALA ARG VAL LEU GLU          
SEQRES   6 D  471  ASP ARG PRO LEU SER ASP LYS GLY SER GLY ASP SER SER          
SEQRES   7 D  471  GLN VAL THR GLN VAL SER PRO GLN ARG ILE ALA LEU ARG          
SEQRES   8 D  471  LEU ARG PRO ASP ASP SER LYS ASN PHE SER ILE GLN VAL          
SEQRES   9 D  471  ARG GLN VAL GLU ASP TYR PRO VAL ASP ILE TYR TYR LEU          
SEQRES  10 D  471  MET ASP LEU SER TYR SER MET LYS ASP ASP LEU TRP SER          
SEQRES  11 D  471  ILE GLN ASN LEU GLY THR LYS LEU ALA THR GLN MET ARG          
SEQRES  12 D  471  LYS LEU THR SER ASN LEU ARG ILE GLY PHE GLY ALA PHE          
SEQRES  13 D  471  VAL ASP LYS PRO VAL SER PRO TYR MET TYR ILE SER PRO          
SEQRES  14 D  471  PRO GLU ALA LEU GLU ASN PRO CYS TYR ASP MET LYS THR          
SEQRES  15 D  471  THR CYS LEU PRO MET PHE GLY TYR LYS HIS VAL LEU THR          
SEQRES  16 D  471  LEU THR ASP GLN VAL THR ARG PHE ASN GLU GLU VAL LYS          
SEQRES  17 D  471  LYS GLN SER VAL SER ARG ASN ARG ASP ALA PRO GLU GLY          
SEQRES  18 D  471  GLY PHE ASP ALA ILE MET GLN ALA THR VAL CYS ASP GLU          
SEQRES  19 D  471  LYS ILE GLY TRP ARG ASN ASP ALA SER HIS LEU LEU VAL          
SEQRES  20 D  471  PHE THR THR ASP ALA LYS THR HIS ILE ALA LEU ASP GLY          
SEQRES  21 D  471  ARG LEU ALA GLY ILE VAL GLN PRO ASN ASP GLY GLN CYS          
SEQRES  22 D  471  HIS VAL GLY SER ASP ASN HIS TYR SER ALA SER THR THR          
SEQRES  23 D  471  MET ASP TYR PRO SER LEU GLY LEU MET THR GLU LYS LEU          
SEQRES  24 D  471  SER GLN LYS ASN ILE ASN LEU ILE PHE ALA VAL THR GLU          
SEQRES  25 D  471  ASN VAL VAL ASN LEU TYR GLN ASN TYR SER GLU LEU ILE          
SEQRES  26 D  471  PRO GLY THR THR VAL GLY VAL LEU SER MET ASP SER SER          
SEQRES  27 D  471  ASN VAL LEU GLN LEU ILE VAL ASP ALA TYR GLY LYS ILE          
SEQRES  28 D  471  ARG SER LYS VAL GLU LEU GLU VAL ARG ASP LEU PRO GLU          
SEQRES  29 D  471  GLU LEU SER LEU SER PHE ASN ALA THR CYS LEU ASN ASN          
SEQRES  30 D  471  GLU VAL ILE PRO GLY LEU LYS SER CYS MET GLY LEU LYS          
SEQRES  31 D  471  ILE GLY ASP THR VAL SER PHE SER ILE GLU ALA LYS VAL          
SEQRES  32 D  471  ARG GLY CYS PRO GLN GLU LYS GLU LYS SER PHE THR ILE          
SEQRES  33 D  471  LYS PRO VAL GLY PHE LYS ASP SER LEU ILE VAL GLN VAL          
SEQRES  34 D  471  THR PHE ASP CYS ASP CYS ALA CYS GLN ALA GLN ALA GLU          
SEQRES  35 D  471  PRO ASN SER HIS ARG CYS ASN ASN GLY ASN GLY THR PHE          
SEQRES  36 D  471  GLU CYS GLY VAL CYS ARG CYS GLY PRO GLY TRP LEU GLY          
SEQRES  37 D  471  SER GLN CYS                                                  
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 3NIG ASN D   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3NIG ASN B   99  ASN  GLYCOSYLATION SITE                                 
MODRES 3NIG ASN D  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3NIG ASN B  371  ASN  GLYCOSYLATION SITE                                 
MODRES 3NIG ASN B  320  ASN  GLYCOSYLATION SITE                                 
MODRES 3NIG ASN D  320  ASN  GLYCOSYLATION SITE                                 
HET     CA  A2004       1                                                       
HET     CA  A2005       1                                                       
HET     CA  A2006       1                                                       
HET     CA  A2007       1                                                       
HET    GOL  A 458       6                                                       
HET    GOL  A 459       6                                                       
HET    SO4  A 460       5                                                       
HET    SO4  A 461       5                                                       
HET     MG  B2001       1                                                       
HET     CA  B2002       1                                                       
HET     CA  B2003       1                                                       
HET    NAG  B3099      14                                                       
HET    NAG  B3320      14                                                       
HET    NAG  B3321      14                                                       
HET    MAN  B3322      11                                                       
HET    NAG  B3371      14                                                       
HET    NAG  B3372      14                                                       
HET     CA  C2004       1                                                       
HET     CA  C2005       1                                                       
HET     CA  C2006       1                                                       
HET     CA  C2007       1                                                       
HET    GOL  C 458       6                                                       
HET    SO4  C 459       5                                                       
HET    SO4  C 460       5                                                       
HET     MG  D2001       1                                                       
HET     CA  D2002       1                                                       
HET     CA  D2003       1                                                       
HET    NAG  D3099      14                                                       
HET    NAG  D3320      14                                                       
HET    NAG  D3321      14                                                       
HET    MAN  D3322      11                                                       
HET    NAG  D3371      14                                                       
HET    NAG  D3372      14                                                       
HET    SO4  D 472       5                                                       
HET    SO4  L 215       5                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     MAN ALPHA-D-MANNOSE                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   9   CA    12(CA 2+)                                                    
FORMUL  13  GOL    3(C3 H8 O3)                                                  
FORMUL  15  SO4    6(O4 S 2-)                                                   
FORMUL  17   MG    2(MG 2+)                                                     
FORMUL  20  NAG    10(C8 H15 N O6)                                              
FORMUL  21  MAN    2(C6 H12 O6)                                                 
FORMUL  38  HOH   *1227(H2 O)                                                   
HELIX    1   1 LEU A  151  ASN A  158  1                                   8    
HELIX    2   2 GLY A  187  LEU A  192  1                                   6    
HELIX    3   3 VAL A  200  TYR A  207  1                                   8    
HELIX    4   4 ASN A  227  PHE A  231  5                                   5    
HELIX    5   5 THR A  259  LEU A  264  1                                   6    
HELIX    6   6 TYR A  440  ALA A  442  5                                   3    
HELIX    7   7 ASN B    3  GLY B    9  1                                   7    
HELIX    8   8 SER B   12  SER B   20  1                                   9    
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  169  ASN B  175  1                                   7    
HELIX   15  15 GLN B  199  LYS B  209  1                                  11    
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  ILE B  325  1                                  12    
HELIX   21  21 ASN B  339  ARG B  352  1                                  14    
HELIX   22  22 CYS B  435  ALA B  441  5                                   7    
HELIX   23  23 LEU C  151  ASN C  158  1                                   8    
HELIX   24  24 GLY C  187  LEU C  192  1                                   6    
HELIX   25  25 VAL C  200  TYR C  207  1                                   8    
HELIX   26  26 ASN C  227  PHE C  231  5                                   5    
HELIX   27  27 THR C  259  LEU C  264  1                                   6    
HELIX   28  28 TYR C  440  ALA C  442  5                                   3    
HELIX   29  29 ASN D    3  ARG D    8  1                                   6    
HELIX   30  30 SER D   12  SER D   20  1                                   9    
HELIX   31  31 LYS D   41  ASP D   47  1                                   7    
HELIX   32  32 ALA D   50  GLU D   52  5                                   3    
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 GLN D  199  GLN D  210  1                                  12    
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  LYS D  302  1                                  12    
HELIX   42  42 VAL D  314  ILE D  325  1                                  12    
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 PRO E   62  GLN E   65  5                                   4    
HELIX   47  47 THR E   87  THR E   91  5                                   5    
HELIX   48  48 ASP F   79  PHE F   83  5                                   5    
HELIX   49  49 SER F  121  THR F  126  1                                   6    
HELIX   50  50 THR F  182  GLU F  187  1                                   6    
HELIX   51  51 ASN H   28  THR H   32  5                                   5    
HELIX   52  52 PRO H   62  GLN H   65  5                                   4    
HELIX   53  53 THR H   74  SER H   76  5                                   3    
HELIX   54  54 THR H   87  THR H   91  5                                   5    
HELIX   55  55 PRO H  206  SER H  209  5                                   4    
HELIX   56  56 ASP L   79  PHE L   83  5                                   5    
HELIX   57  57 SER L  121  SER L  127  1                                   7    
HELIX   58  58 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 445   N  TYR A  11           
SHEET    3   A 4 ASP A 434  ALA A 439 -1  N  LEU A 435   O  TYR A 448           
SHEET    4   A 4 SER A 420  VAL A 425 -1  N  ARG A 422   O  ILE A 436           
SHEET    1   B 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  LEU A 116   N  THR A  83           
SHEET    4   C 4 GLU A 120  GLU A 121 -1  O  GLU A 120   N  GLU A 117           
SHEET    1   D 4 VAL A  97  TRP A 100  0                                        
SHEET    2   D 4 VAL A 103  ALA A 108 -1  O  VAL A 105   N  VAL A  98           
SHEET    3   D 4 SER A 129  ALA A 133 -1  O  SER A 129   N  ALA A 108           
SHEET    4   D 4 ARG A 140  TYR A 143 -1  O  ALA A 141   N  LEU A 132           
SHEET    1   E 4 SER A 172  VAL A 175  0                                        
SHEET    2   E 4 GLU A 180  ALA A 185 -1  O  VAL A 182   N  VAL A 174           
SHEET    3   E 4 LEU A 194  PRO A 199 -1  O  ALA A 196   N  LEU A 183           
SHEET    4   E 4 SER A 220  LEU A 221 -1  O  SER A 220   N  GLN A 197           
SHEET    1   F 4 VAL A 239  GLY A 242  0                                        
SHEET    2   F 4 GLU A 252  ALA A 257 -1  O  VAL A 254   N  ALA A 240           
SHEET    3   F 4 ALA A 266  LEU A 270 -1  O  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  LEU A 363           
SHEET    3   I 4 GLN A 388  PHE A 392 -1  O  LEU A 390   N  VAL A 376           
SHEET    4   I 4 GLN A 405  ASP A 408 -1  O  LEU A 407   N  VAL A 389           
SHEET    1   J 2 GLY A 394  GLN A 395  0                                        
SHEET    2   J 2 GLY A 398  LEU A 399 -1  O  GLY A 398   N  GLN A 395           
SHEET    1   K 3 CYS B  38  ASP B  39  0                                        
SHEET    2   K 3 ALA B  24  CYS B  26 -1  N  ALA B  24   O  ASP B  39           
SHEET    3   K 3 ILE B  54  GLU B  55 -1  O  GLU B  55   N  TRP B  25           
SHEET    1   L 6 GLU B  60  GLU B  65  0                                        
SHEET    2   L 6 ARG B  87  LEU B  92 -1  O  ALA B  89   N  ARG B  62           
SHEET    3   L 6 LEU B 425  PHE B 431  1  O  GLN B 428   N  LEU B  90           
SHEET    4   L 6 GLU B 411  PRO B 418 -1  N  LYS B 412   O  VAL B 429           
SHEET    5   L 6 VAL B 355  ARG B 360 -1  N  GLU B 358   O  LYS B 417           
SHEET    6   L 6 SER B 385  CYS B 386 -1  O  CYS B 386   N  VAL B 355           
SHEET    1   M 5 VAL B  83  SER B  84  0                                        
SHEET    2   M 5 SER B  97  ARG B 105 -1  O  GLN B 103   N  SER B  84           
SHEET    3   M 5 THR B 394  VAL B 403 -1  O  ILE B 399   N  PHE B 100           
SHEET    4   M 5 LEU B 366  THR B 373 -1  N  ASN B 371   O  SER B 398           
SHEET    5   M 5 VAL B 379  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  PHE B 153   O  LEU B 194           
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  VAL B 247   N  LEU B 117           
SHEET    5   N 6 ASN B 305  VAL B 310  1  O  ILE B 307   N  PHE B 248           
SHEET    6   N 6 THR B 329  VAL B 332  1  O  THR B 329   N  PHE B 308           
SHEET    1   O 2 GLY B 453  GLU B 456  0                                        
SHEET    2   O 2 VAL B 459  CYS B 462 -1  O  ARG B 461   N  THR B 454           
SHEET    1   P 4 THR C   9  ALA C  12  0                                        
SHEET    2   P 4 GLN C 444  TYR C 448 -1  O  VAL C 445   N  TYR C  11           
SHEET    3   P 4 ASP C 434  ALA C 439 -1  N  LEU C 435   O  TYR C 448           
SHEET    4   P 4 SER C 420  VAL C 425 -1  N  ARG C 422   O  ILE C 436           
SHEET    1   Q 3 LEU C  23  LYS C  27  0                                        
SHEET    2   Q 3 VAL C  33  GLY C  38 -1  O  ALA C  34   N  HIS C  26           
SHEET    3   Q 3 VAL C  53  PRO C  57 -1  O  CYS C  56   N  ILE C  35           
SHEET    1   R 4 THR C  76  VAL C  79  0                                        
SHEET    2   R 4 GLN C  82  PHE C  87 -1  O  LEU C  84   N  ARG C  77           
SHEET    3   R 4 HIS C 112  GLU C 117 -1  O  LEU C 116   N  THR C  83           
SHEET    4   R 4 GLU C 120  GLU C 121 -1  O  GLU C 120   N  GLU C 117           
SHEET    1   S 4 VAL C  97  TRP C 100  0                                        
SHEET    2   S 4 VAL C 103  ALA C 108 -1  O  VAL C 105   N  VAL C  98           
SHEET    3   S 4 SER C 129  ALA C 133 -1  O  SER C 129   N  ALA C 108           
SHEET    4   S 4 ARG C 140  TYR C 143 -1  O  ALA C 141   N  LEU C 132           
SHEET    1   T 4 SER C 172  VAL C 175  0                                        
SHEET    2   T 4 GLU C 180  ALA C 185 -1  O  GLY C 184   N  SER C 172           
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  LYS C 321   N  ARG C 317           
SHEET    1   X 4 ILE C 360  GLY C 364  0                                        
SHEET    2   X 4 ASP C 373  ALA C 378 -1  O  ASP C 373   N  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  LEU D  40  0                                        
SHEET    2   Z 3 CYS D  23  CYS D  26 -1  N  ALA D  24   O  ASP D  39           
SHEET    3   Z 3 ILE D  54  GLU D  55 -1  O  GLU D  55   N  TRP D  25           
SHEET    1  AA 6 GLU D  60  GLU D  65  0                                        
SHEET    2  AA 6 ARG D  87  LEU D  92 -1  O  ALA D  89   N  ARG D  62           
SHEET    3  AA 6 LEU D 425  PHE D 431  1  O  GLN D 428   N  LEU D  90           
SHEET    4  AA 6 GLU D 411  PRO D 418 -1  N  PHE D 414   O  VAL D 427           
SHEET    5  AA 6 VAL D 355  ARG D 360 -1  N  ARG D 360   O  THR D 415           
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  VAL D 395   N  VAL D 104           
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  TYR D 116   O  GLY D 152           
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  ILE D 307   N  PHE D 248           
SHEET    6  AC 6 THR D 329  LEU D 333  1  O  THR D 329   N  PHE D 308           
SHEET    1  AD 2 GLY D 453  GLU D 456  0                                        
SHEET    2  AD 2 VAL D 459  CYS D 462 -1  O  ARG D 461   N  THR D 454           
SHEET    1  AE 4 GLN E   3  GLN E   6  0                                        
SHEET    2  AE 4 VAL E  18  SER E  25 -1  O  THR E  23   N  GLN E   5           
SHEET    3  AE 4 THR E  78  LEU E  83 -1  O  ALA E  79   N  CYS E  22           
SHEET    4  AE 4 ALA E  68  ASP E  73 -1  N  THR E  71   O  TYR E  80           
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  ALA E  92   O  VAL E 115           
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  ALA E  92   O  VAL E 115           
SHEET    4  AG 4 TYR E 108  TRP E 109 -1  O  TYR E 108   N  ARG E  98           
SHEET    1  AH 4 SER E 126  LEU E 130  0                                        
SHEET    2  AH 4 SER E 141  TYR E 151 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AH 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  TYR E 151           
SHEET    4  AH 4 VAL E 169  THR E 171 -1  N  HIS E 170   O  SER E 186           
SHEET    1  AI 4 SER E 126  LEU E 130  0                                        
SHEET    2  AI 4 SER E 141  TYR E 151 -1  O  LEU E 147   N  TYR E 128           
SHEET    3  AI 4 LEU E 180  THR E 190 -1  O  TYR E 181   N  TYR E 151           
SHEET    4  AI 4 VAL E 175  GLN E 177 -1  N  GLN E 177   O  LEU E 180           
SHEET    1  AJ 2 THR E 159  TRP E 160  0                                        
SHEET    2  AJ 2 CYS E 201  ASN E 202 -1  O  ASN E 202   N  THR E 159           
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  ILE F  75   N  VAL F  19           
SHEET    4  AK 4 PHE F  62  SER F  67 -1  N  SER F  63   O  THR F  74           
SHEET    1  AL 6 SER F  10  VAL F  13  0                                        
SHEET    2  AL 6 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AL 6 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AL 6 ILE F  33  GLN F  38 -1  N  GLN F  38   O  ASP F  85           
SHEET    5  AL 6 PHE F  44  TYR F  49 -1  O  LEU F  47   N  TRP F  35           
SHEET    6  AL 6 ASN F  53  LEU F  54 -1  O  ASN F  53   N  TYR F  49           
SHEET    1  AM 4 SER F  10  VAL F  13  0                                        
SHEET    2  AM 4 THR F 102  ILE F 106  1  O  GLU F 105   N  VAL F  13           
SHEET    3  AM 4 ASP F  85  GLN F  90 -1  N  TYR F  86   O  THR F 102           
SHEET    4  AM 4 THR F  97  PHE F  98 -1  O  THR F  97   N  GLN F  90           
SHEET    1  AN 4 THR F 114  PHE F 118  0                                        
SHEET    2  AN 4 ALA F 130  PHE F 139 -1  O  VAL F 133   N  PHE F 118           
SHEET    3  AN 4 TYR F 173  LEU F 181 -1  O  MET F 175   N  LEU F 136           
SHEET    4  AN 4 VAL F 159  TRP F 163 -1  N  SER F 162   O  SER F 176           
SHEET    1  AO 4 SER F 153  ARG F 155  0                                        
SHEET    2  AO 4 ASN F 145  ILE F 150 -1  N  ILE F 150   O  SER F 153           
SHEET    3  AO 4 TYR F 192  HIS F 198 -1  O  GLU F 195   N  LYS F 147           
SHEET    4  AO 4 SER F 201  ILE F 205 -1  O  ILE F 205   N  ALA F 196           
SHEET    1  AP 4 GLN H   3  GLN H   6  0                                        
SHEET    2  AP 4 VAL H  18  SER H  25 -1  O  THR H  23   N  GLN H   5           
SHEET    3  AP 4 THR H  78  LEU H  83 -1  O  LEU H  81   N  LEU H  20           
SHEET    4  AP 4 ALA H  68  ASP H  73 -1  N  THR H  71   O  TYR H  80           
SHEET    1  AQ 6 GLU H  10  VAL H  12  0                                        
SHEET    2  AQ 6 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AQ 6 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 115           
SHEET    4  AQ 6 VAL H  34  ARG H  40 -1  N  HIS H  35   O  VAL H  97           
SHEET    5  AQ 6 GLY H  44  ILE H  51 -1  O  GLU H  46   N  LYS H  38           
SHEET    6  AQ 6 THR H  58  TYR H  60 -1  O  LYS H  59   N  ARG H  50           
SHEET    1  AR 4 GLU H  10  VAL H  12  0                                        
SHEET    2  AR 4 THR H 113  VAL H 117  1  O  SER H 114   N  GLU H  10           
SHEET    3  AR 4 ALA H  92  ARG H  98 -1  N  ALA H  92   O  VAL H 115           
SHEET    4  AR 4 TYR H 108  TRP H 109 -1  O  TYR H 108   N  ARG H  98           
SHEET    1  AS 4 SER H 126  LEU H 130  0                                        
SHEET    2  AS 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3  AS 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  AS 4 VAL H 169  THR H 171 -1  N  HIS H 170   O  SER H 186           
SHEET    1  AT 4 SER H 126  LEU H 130  0                                        
SHEET    2  AT 4 SER H 141  TYR H 151 -1  O  LYS H 149   N  SER H 126           
SHEET    3  AT 4 LEU H 180  THR H 190 -1  O  TYR H 181   N  TYR H 151           
SHEET    4  AT 4 VAL H 175  GLN H 177 -1  N  GLN H 177   O  LEU H 180           
SHEET    1  AU 3 THR H 157  TRP H 160  0                                        
SHEET    2  AU 3 THR H 200  HIS H 205 -1  O  ASN H 202   N  THR H 159           
SHEET    3  AU 3 THR H 210  LYS H 215 -1  O  THR H 210   N  HIS H 205           
SHEET    1  AV 4 MET L   4  SER L   7  0                                        
SHEET    2  AV 4 VAL L  19  ALA L  25 -1  O  HIS L  24   N  THR L   5           
SHEET    3  AV 4 ASP L  70  ILE L  75 -1  O  LEU L  73   N  ILE L  21           
SHEET    4  AV 4 PHE L  62  SER L  67 -1  N  SER L  63   O  THR L  74           
SHEET    1  AW 6 SER L  10  VAL L  13  0                                        
SHEET    2  AW 6 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AW 6 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AW 6 ILE L  33  GLN L  38 -1  N  GLY L  34   O  VAL L  89           
SHEET    5  AW 6 PHE L  44  TYR L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6  AW 6 ASN L  53  LEU L  54 -1  O  ASN L  53   N  TYR L  49           
SHEET    1  AX 4 SER L  10  VAL L  13  0                                        
SHEET    2  AX 4 THR L 102  ILE L 106  1  O  GLU L 105   N  MET L  11           
SHEET    3  AX 4 ASP L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4  AX 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1  AY 4 THR L 114  PHE L 118  0                                        
SHEET    2  AY 4 GLY L 129  PHE L 139 -1  O  VAL L 133   N  PHE L 118           
SHEET    3  AY 4 TYR L 173  THR L 182 -1  O  LEU L 181   N  ALA L 130           
SHEET    4  AY 4 VAL L 159  TRP L 163 -1  N  SER L 162   O  SER L 176           
SHEET    1  AZ 4 SER L 153  ARG L 155  0                                        
SHEET    2  AZ 4 ASN L 145  ILE L 150 -1  N  TRP L 148   O  ARG L 155           
SHEET    3  AZ 4 SER L 191  THR L 197 -1  O  THR L 197   N  ASN L 145           
SHEET    4  AZ 4 ILE L 205  ASN L 210 -1  O  ILE L 205   N  ALA L 196           
SSBOND   1 CYS A   56    CYS A   65                          1555   1555  2.09  
SSBOND   2 CYS A  107    CYS A  130                          1555   1555  2.08  
SSBOND   3 CYS A  146    CYS A  167                          1555   1555  2.12  
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  2.13  
SSBOND   9 CYS B  232    CYS B  273                          1555   1555  2.13  
SSBOND  10 CYS B  374    CYS B  386                          1555   1555  2.04  
SSBOND  11 CYS B  406    CYS B  433                          1555   1555  2.03  
SSBOND  12 CYS B  437    CYS B  457                          1555   1555  2.04  
SSBOND  13 CYS B  448    CYS B  460                          1555   1555  2.04  
SSBOND  14 CYS C   56    CYS C   65                          1555   1555  2.06  
SSBOND  15 CYS C  107    CYS C  130                          1555   1555  2.07  
SSBOND  16 CYS C  146    CYS C  167                          1555   1555  2.07  
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  2.04  
SSBOND  20 CYS D   26    CYS D   49                          1555   1555  2.04  
SSBOND  21 CYS D  177    CYS D  184                          1555   1555  2.11  
SSBOND  22 CYS D  232    CYS D  273                          1555   1555  2.09  
SSBOND  23 CYS D  374    CYS D  386                          1555   1555  2.04  
SSBOND  24 CYS D  406    CYS D  433                          1555   1555  2.03  
SSBOND  25 CYS D  437    CYS D  457                          1555   1555  2.05  
SSBOND  26 CYS D  448    CYS D  460                          1555   1555  2.06  
SSBOND  27 CYS D  462    CYS D  471                          1555   1555  2.04  
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  2.04  
SSBOND  31 CYS F   23    CYS F   88                          1555   1555  2.05  
SSBOND  32 CYS F  134    CYS F  194                          1555   1555  2.03  
SSBOND  33 CYS H   22    CYS H   96                          1555   1555  2.05  
SSBOND  34 CYS H  134    CYS L  214                          1555   1555  2.03  
SSBOND  35 CYS H  146    CYS H  201                          1555   1555  2.04  
SSBOND  36 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND  37 CYS L  134    CYS L  194                          1555   1555  2.03  
LINK         ND2 ASN D  99                 C1  NAG D3099     1555   1555  1.43  
LINK         ND2 ASN B  99                 C1  NAG B3099     1555   1555  1.43  
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 D3371                 C1  NAG D3372     1555   1555  1.44  
LINK         ND2 ASN B 371                 C1  NAG B3371     1555   1555  1.44  
LINK         ND2 ASN B 320                 C1  NAG B3320     1555   1555  1.44  
LINK         O4  NAG D3320                 C1  NAG D3321     1555   1555  1.45  
LINK         ND2 ASN D 320                 C1  NAG D3320     1555   1555  1.45  
LINK         O4  NAG B3320                 C1  NAG B3321     1555   1555  1.45  
LINK         O4  NAG B3321                 C1  MAN B3322     1555   1555  1.45  
LINK         O4  NAG D3321                 C1  MAN D3322     1555   1555  1.46  
LINK        MG    MG B2001                 O   HOH B1037     1555   1555  2.05  
LINK        MG    MG D2001                 O   HOH D 475     1555   1555  2.19  
LINK         OD1 ASP D 217                CA    CA D2003     1555   1555  2.20  
LINK         OE2 GLU B 220                MG    MG B2001     1555   1555  2.25  
LINK        MG    MG D2001                 O   HOH D 505     1555   1555  2.26  
LINK         O   THR C 250                CA    CA C2004     1555   1555  2.26  
LINK         OD1 ASP B 217                CA    CA B2003     1555   1555  2.28  
LINK        MG    MG B2001                 O   HOH B1039     1555   1555  2.28  
LINK         O   TYR C 432                CA    CA C2007     1555   1555  2.29  
LINK         OE2 GLU D 220                MG    MG D2001     1555   1555  2.31  
LINK         O   ARG C 303                CA    CA C2005     1555   1555  2.32  
LINK         OD2 ASP A 245                CA    CA A2004     1555   1555  2.32  
LINK         OD1 ASN A 299                CA    CA A2005     1555   1555  2.33  
LINK         O   TYR A 371                CA    CA A2006     1555   1555  2.33  
LINK         O   TYR A 432                CA    CA A2007     1555   1555  2.34  
LINK         OD1 ASP A 367                CA    CA A2006     1555   1555  2.35  
LINK         O   PRO B 219                CA    CA B2003     1555   1555  2.35  
LINK         OD1 ASP A 428                CA    CA A2007     1555   1555  2.35  
LINK        CA    CA C2006                 O   HOH C 495     1555   1555  2.35  
LINK         OE1 GLU D 220                CA    CA D2003     1555   1555  2.36  
LINK         O   PRO D 219                CA    CA D2003     1555   1555  2.36  
LINK         O   THR A 250                CA    CA A2004     1555   1555  2.37  
LINK         OD2 ASP B 158                CA    CA B2003     1555   1555  2.37  
LINK         O   ARG A 303                CA    CA A2005     1555   1555  2.37  
LINK        CA    CA A2006                 O   HOH A 491     1555   1555  2.37  
LINK         OE1 GLU B 220                CA    CA B2003     1555   1555  2.38  
LINK         OD1 ASN C 299                CA    CA C2005     1555   1555  2.39  
LINK         OD1 ASP A 297                CA    CA A2005     1555   1555  2.39  
LINK         O   TYR C 371                CA    CA C2006     1555   1555  2.39  
LINK         OD1 ASP D 127                CA    CA D2002     1555   1555  2.40  
LINK         OD1 ASN B 215                CA    CA B2003     1555   1555  2.40  
LINK         OD1 ASP A 426                CA    CA A2007     1555   1555  2.41  
LINK        MG    MG D2001                 O   HOH D 864     1555   1555  2.41  
LINK         OD2 ASP C 245                CA    CA C2004     1555   1555  2.42  
LINK         O   MET B 335                CA    CA B2002     1555   1555  2.42  
LINK        CA    CA A2005                 O   HOH A 559     1555   1555  2.42  
LINK        CA    CA B2002                 O   HOH B 537     1555   1555  2.43  
LINK         O   MET D 335                CA    CA D2002     1555   1555  2.43  
LINK         OD1 ASP B 127                CA    CA B2002     1555   1555  2.43  
LINK         OD1 ASP C 297                CA    CA C2005     1555   1555  2.43  
LINK         OD2 ASP A 365                CA    CA A2006     1555   1555  2.44  
LINK         O   ASP B 217                CA    CA B2003     1555   1555  2.45  
LINK        CA    CA D2002                 O   HOH D 515     1555   1555  2.45  
LINK         OD1 ASP C 367                CA    CA C2006     1555   1555  2.45  
LINK        MG    MG D2001                 O   HOH D1092     1555   1555  2.45  
LINK         OE1 GLU A 243                CA    CA A2004     1555   1555  2.47  
LINK        MG    MG B2001                 O   HOH B 514     1555   1555  2.48  
LINK         O   SER D 123                CA    CA D2002     1555   1555  2.49  
LINK        CA    CA A2007                 O   HOH A 478     1555   1555  2.49  
LINK         OD1 ASN D 215                CA    CA D2003     1555   1555  2.49  
LINK        CA    CA C2007                 O   HOH C 566     1555   1555  2.50  
LINK         OD2 ASP D 158                CA    CA D2003     1555   1555  2.51  
LINK        CA    CA D2002                 O   HOH D 503     1555   1555  2.52  
LINK        CA    CA B2002                 O   HOH B 750     1555   1555  2.52  
LINK         OD1 ASP A 305                CA    CA A2005     1555   1555  2.52  
LINK         OD1 ASP C 428                CA    CA C2007     1555   1555  2.52  
LINK         O   ASP C 247                CA    CA C2004     1555   1555  2.52  
LINK         OD2 ASP A 373                CA    CA A2006     1555   1555  2.52  
LINK         OE2 GLU A 243                CA    CA A2004     1555   1555  2.53  
LINK         OD1 ASN A 430                CA    CA A2007     1555   1555  2.53  
LINK         OD1 ASP D 126                CA    CA D2002     1555   1555  2.53  
LINK        CA    CA C2005                 O   HOH C 810     1555   1555  2.53  
LINK         OD1 ASP C 426                CA    CA C2007     1555   1555  2.54  
LINK         OG1 THR A 250                CA    CA A2004     1555   1555  2.55  
LINK         OG  SER B 121                MG    MG B2001     1555   1555  2.55  
LINK         O   ASP D 217                CA    CA D2003     1555   1555  2.56  
LINK         OD2 ASP C 373                CA    CA C2006     1555   1555  2.56  
LINK         OE1 GLU C 243                CA    CA C2004     1555   1555  2.56  
LINK         OD1 ASP A 434                CA    CA A2007     1555   1555  2.56  
LINK         O   SER B 123                CA    CA B2002     1555   1555  2.57  
LINK         OD2 ASP A 305                CA    CA A2005     1555   1555  2.57  
LINK         OD2 ASP C 365                CA    CA C2006     1555   1555  2.58  
LINK         OD1 ASP A 369                CA    CA A2006     1555   1555  2.58  
LINK         OD2 ASP A 434                CA    CA A2007     1555   1555  2.58  
LINK         OD2 ASP C 305                CA    CA C2005     1555   1555  2.60  
LINK         OD1 ASP B 126                CA    CA B2002     1555   1555  2.62  
LINK         O   ASP A 247                CA    CA A2004     1555   1555  2.62  
LINK         OD1 ASP C 369                CA    CA C2006     1555   1555  2.62  
LINK         OG  SER D 121                MG    MG D2001     1555   1555  2.63  
LINK         OE2 GLU C 243                CA    CA C2004     1555   1555  2.64  
LINK         OD2 ASP C 434                CA    CA C2007     1555   1555  2.65  
LINK         OD1 ASN C 430                CA    CA C2007     1555   1555  2.65  
LINK         OD1 ASP A 373                CA    CA A2006     1555   1555  2.66  
LINK         OE2 GLU A 252                CA    CA A2004     1555   1555  2.66  
LINK         OD1 ASP C 373                CA    CA C2006     1555   1555  2.67  
LINK         OE1 GLU A 252                CA    CA A2004     1555   1555  2.67  
LINK         OE2 GLU C 252                CA    CA C2004     1555   1555  2.68  
LINK         OD1 ASP C 434                CA    CA C2007     1555   1555  2.69  
LINK         OD1 ASP C 305                CA    CA C2005     1555   1555  2.71  
LINK         OD1 ASP C 301                CA    CA C2005     1555   1555  2.73  
LINK        MG    MG B2001                 O   HOH B 897     1555   1555  2.75  
LINK         OD2 ASP B 126                CA    CA B2002     1555   1555  2.76  
LINK         OD1 ASP A 301                CA    CA A2005     1555   1555  2.77  
LINK         OE1 GLU C 252                CA    CA C2004     1555   1555  2.79  
LINK         OG1 THR C 250                CA    CA C2004     1555   1555  2.79  
LINK         OD2 ASP D 126                CA    CA D2002     1555   1555  2.86  
CISPEP   1 SER B   77    SER B   78          0         5.71                     
CISPEP   2 SER B   84    PRO B   85          0        -4.85                     
CISPEP   3 SER B  162    PRO B  163          0         8.79                     
CISPEP   4 SER B  168    PRO B  169          0       -10.73                     
CISPEP   5 PRO B  464    GLY B  465          0        -6.92                     
CISPEP   6 SER D   77    SER D   78          0        -3.68                     
CISPEP   7 SER D   84    PRO D   85          0        -6.50                     
CISPEP   8 SER D  162    PRO D  163          0         8.88                     
CISPEP   9 SER D  168    PRO D  169          0        -6.15                     
CISPEP  10 PHE E  152    PRO E  153          0        -5.58                     
CISPEP  11 GLU E  154    PRO E  155          0        -3.45                     
CISPEP  12 TRP E  194    PRO E  195          0        -4.68                     
CISPEP  13 SER F    7    PRO F    8          0       -10.96                     
CISPEP  14 LEU F   94    PRO F   95          0        -0.01                     
CISPEP  15 TYR F  140    PRO F  141          0         5.63                     
CISPEP  16 PHE H  152    PRO H  153          0        -2.58                     
CISPEP  17 GLU H  154    PRO H  155          0        -4.44                     
CISPEP  18 TRP H  194    PRO H  195          0         4.69                     
CISPEP  19 SER L    7    PRO L    8          0        -9.93                     
CISPEP  20 LEU L   94    PRO L   95          0         0.15                     
CISPEP  21 TYR L  140    PRO L  141          0         9.44                     
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 559                                          
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 491                                          
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 478                                          
SITE     1 AC5  3 ARG A  90  LYS A 124  HOH A 581                               
SITE     1 AC6  4 GLN A 395  ARG A 400  SER A 401  ARG A 402                    
SITE     1 AC7  4 PHE A  10  PHE A 411  GLN A 444  HOH A 474                    
SITE     1 AC8  7 ARG A 386  PRO A 412  HOH A 894  HOH A1036                    
SITE     2 AC8  7 ARG C 386  PRO C 412  THR C 413                               
SITE     1 AC9  6 SER B 121  GLU B 220  HOH B 514  HOH B 897                    
SITE     2 AC9  6 HOH B1037  HOH B1039                                          
SITE     1 BC1  6 SER B 123  ASP B 126  ASP B 127  MET B 335                    
SITE     2 BC1  6 HOH B 537  HOH B 750                                          
SITE     1 BC2  5 ASP B 158  ASN B 215  ASP B 217  PRO B 219                    
SITE     2 BC2  5 GLU B 220                                                     
SITE     1 BC3  1 ASN B  99                                                     
SITE     1 BC4  7 MET A 285  ASN B 320  HOH B 482  HOH B 534                    
SITE     2 BC4  7 HOH B 536  HOH B 552  NAG B3321                               
SITE     1 BC5  2 NAG B3320  MAN B3322                                          
SITE     1 BC6  2 HOH B 725  NAG B3321                                          
SITE     1 BC7  7 SER B 369  ASN B 371  PRO B 381  SER B 398                    
SITE     2 BC7  7 ILE B 399  GLU B 400  NAG B3372                               
SITE     1 BC8  1 NAG B3371                                                     
SITE     1 BC9  5 GLU C 243  ASP C 245  ASP C 247  THR C 250                    
SITE     2 BC9  5 GLU C 252                                                     
SITE     1 CC1  6 ASP C 297  ASN C 299  ASP C 301  ARG C 303                    
SITE     2 CC1  6 ASP C 305  HOH C 810                                          
SITE     1 CC2  6 ASP C 365  ASP C 367  ASP C 369  TYR C 371                    
SITE     2 CC2  6 ASP C 373  HOH C 495                                          
SITE     1 CC3  6 ASP C 426  ASP C 428  ASN C 430  TYR C 432                    
SITE     2 CC3  6 ASP C 434  HOH C 566                                          
SITE     1 CC4  3 ALA C  89  HIS C 112  HOH C 504                               
SITE     1 CC5  5 PRO A 383  PHE C  10  PRO C 410  GLN C 444                    
SITE     2 CC5  5 HOH C 985                                                     
SITE     1 CC6  3 ASN C 227  TYR C 230  ARG C 276                               
SITE     1 CC7  6 SER D 121  GLU D 220  HOH D 475  HOH D 505                    
SITE     2 CC7  6 HOH D 864  HOH D1092                                          
SITE     1 CC8  6 SER D 123  ASP D 126  ASP D 127  MET D 335                    
SITE     2 CC8  6 HOH D 503  HOH D 515                                          
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  4 ASN D  99  PHE D 100  SER D 101  NAG D3372                    
SITE     1 DC2  8 MET C 285  ASN D 320  HOH D 541  HOH D 581                    
SITE     2 DC2  8 HOH D 583  HOH D 818  HOH D 893  NAG D3321                    
SITE     1 DC3  4 ARG C 281  HOH D 581  NAG D3320  MAN D3322                    
SITE     1 DC4  1 NAG D3321                                                     
SITE     1 DC5  3 ASN D 371  SER D 398  NAG D3372                               
SITE     1 DC6  2 NAG D3099  NAG D3371                                          
SITE     1 DC7  7 GLN D 106  TYR D 110  SER D 243  ARG D 352                    
SITE     2 DC7  7 GLY D 420  HOH D1019  HOH D1065                               
SITE     1 DC8  5 ARG C  73  GLU L 154  ARG L 155  GLN L 156                    
SITE     2 DC8  5 ASN L 157                                                     
CRYST1  260.670  145.170  104.440  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      0.003836  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006888  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009575        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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