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Entry: 5FO8
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HEADER    LIPID BINDING                           18-NOV-15   5FO8              
TITLE     CRYSTAL STRUCTURE OF HUMAN COMPLEMENT C3B IN COMPLEX WITH MCP (CCP1-4)
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COMPLEMENT C3;                                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 23-667;                                       
COMPND   5 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND   6 PROTEIN 1, C3ADESARG, COMPLEMENT C3B;                                
COMPND   7 EC: 3.4.21.47;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: COMPLEMENT C3;                                             
COMPND  10 CHAIN: B;                                                            
COMPND  11 FRAGMENT: UNP RESIDUES 749-1663;                                     
COMPND  12 SYNONYM: C3 AND PZP-LIKE ALPHA-2-MACROGLOBULIN DOMAIN-CONTAINING     
COMPND  13 PROTEIN 1, C3ADESARG, COMPLEMENT C3B;                                
COMPND  14 EC: 3.4.21.47;                                                       
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: MEMBRANE COFACTOR PROTEIN;                                 
COMPND  17 CHAIN: C;                                                            
COMPND  18 FRAGMENT: CCP DOMAINS 1-4, UNP RESIDUES 35-286;                      
COMPND  19 SYNONYM: TLX, TROPHOBLAST LEUKOCYTE COMMON ANTIGEN, MEMBRANE COFACTOR
COMPND  20 PROTEIN MCP, CD46;                                                   
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 OTHER_DETAILS: PURIFIED FROM HUMAN PLASMA;                           
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 OTHER_DETAILS: PURIFIED FROM HUMAN PLASMA;                           
SOURCE  11 MOL_ID: 3;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  16 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    LIPID BINDING, LIPID BIANDING, COMPLEMENT SYSTEM, IMMUNE SYSTEM,      
KEYWDS   2 PLASMA PROTEIN, COFA ACTIVITY, REGULATORS OF COMPLEMENT ACTIVITY     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.FORNERIS,J.WU,X.XUE,P.GROS                                          
REVDAT   3   29-JUL-20 5FO8    1       COMPND REMARK HETNAM LINK                
REVDAT   3 2                   1       SITE   ATOM                              
REVDAT   2   01-JUN-16 5FO8    1       JRNL                                     
REVDAT   1   06-APR-16 5FO8    0                                                
JRNL        AUTH   F.FORNERIS,J.WU,X.XUE,D.RICKLIN,Z.LIN,G.SFYROERA,A.TZEKOU,   
JRNL        AUTH 2 E.VOLOKHINA,J.C.GRANNEMAN,R.HAUHART,P.BERTRAM,M.K.LISZEWSKI, 
JRNL        AUTH 3 J.P.ATKINSON,J.D.LAMBRIS,P.GROS                              
JRNL        TITL   REGULATORS OF COMPLEMENT ACTIVITY MEDIATE INHIBITORY         
JRNL        TITL 2 MECHANISMS THROUGH A COMMON C3B-BINDING MODE.                
JRNL        REF    EMBO J.                       V.  35  1133 2016              
JRNL        REFN                   ISSN 0261-4189                               
JRNL        PMID   27013439                                                     
JRNL        DOI    10.15252/EMBJ.201593673                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 57.02                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 98766                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.190                           
REMARK   3   R VALUE            (WORKING SET) : 0.188                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4925                            
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 57.0365 -  7.4520    0.98     3332   189  0.1720 0.1400        
REMARK   3     2  7.4520 -  5.9169    0.99     3256   159  0.1825 0.2075        
REMARK   3     3  5.9169 -  5.1695    1.00     3229   157  0.1688 0.2049        
REMARK   3     4  5.1695 -  4.6971    1.00     3219   170  0.1440 0.1566        
REMARK   3     5  4.6971 -  4.3605    1.00     3178   193  0.1407 0.1704        
REMARK   3     6  4.3605 -  4.1035    1.00     3172   176  0.1509 0.1820        
REMARK   3     7  4.1035 -  3.8981    1.00     3195   153  0.1722 0.2067        
REMARK   3     8  3.8981 -  3.7284    1.00     3185   166  0.1778 0.2149        
REMARK   3     9  3.7284 -  3.5849    0.96     3032   158  0.1950 0.2377        
REMARK   3    10  3.5849 -  3.4612    1.00     3139   166  0.2014 0.2292        
REMARK   3    11  3.4612 -  3.3530    1.00     3153   171  0.1988 0.2305        
REMARK   3    12  3.3530 -  3.2572    1.00     3142   178  0.2091 0.2824        
REMARK   3    13  3.2572 -  3.1714    1.00     3168   149  0.2149 0.2388        
REMARK   3    14  3.1714 -  3.0941    0.99     3083   190  0.2070 0.2488        
REMARK   3    15  3.0941 -  3.0237    0.99     3118   191  0.2076 0.2745        
REMARK   3    16  3.0237 -  2.9594    1.00     3123   155  0.2085 0.2552        
REMARK   3    17  2.9594 -  2.9002    0.99     3126   169  0.2113 0.2488        
REMARK   3    18  2.9002 -  2.8455    0.99     3121   151  0.2111 0.2505        
REMARK   3    19  2.8455 -  2.7947    0.99     3110   159  0.2165 0.2578        
REMARK   3    20  2.7947 -  2.7473    0.99     3078   165  0.2157 0.2865        
REMARK   3    21  2.7473 -  2.7030    0.99     3098   159  0.2256 0.2748        
REMARK   3    22  2.7030 -  2.6614    0.99     3090   152  0.2213 0.2594        
REMARK   3    23  2.6614 -  2.6222    0.98     3072   144  0.2167 0.2764        
REMARK   3    24  2.6222 -  2.5853    0.99     3109   149  0.2162 0.2743        
REMARK   3    25  2.5853 -  2.5504    0.97     3083   157  0.2238 0.3108        
REMARK   3    26  2.5504 -  2.5172    0.99     3067   154  0.2210 0.2770        
REMARK   3    27  2.5172 -  2.4858    0.97     3038   155  0.2269 0.3002        
REMARK   3    28  2.4858 -  2.4558    0.98     3069   162  0.2410 0.2725        
REMARK   3    29  2.4558 -  2.4273    0.98     3049   179  0.2526 0.3105        
REMARK   3    30  2.4273 -  2.4000    0.96     3007   149  0.2635 0.3043        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.240            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.760           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 42.69                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 67.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005          13578                                  
REMARK   3   ANGLE     :  0.851          18342                                  
REMARK   3   CHIRALITY :  0.057           2079                                  
REMARK   3   PLANARITY :  0.004           2352                                  
REMARK   3   DIHEDRAL  : 15.853           5104                                  
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 THROUGH 67 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   9.9311  10.0084  11.8608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3721 T22:   0.6682                                     
REMARK   3      T33:   0.3648 T12:  -0.0043                                     
REMARK   3      T13:   0.1110 T23:   0.0137                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0143 L22:   0.0060                                     
REMARK   3      L33:   0.0034 L12:   0.0065                                     
REMARK   3      L13:   0.0060 L23:  -0.0008                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0034 S12:   0.2030 S13:  -0.0546                       
REMARK   3      S21:  -0.0082 S22:   0.0161 S23:   0.0554                       
REMARK   3      S31:  -0.0089 S32:  -0.0791 S33:  -0.0000                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 68 THROUGH 112 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  10.6637  18.5166  23.3981              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4156 T22:   0.4670                                     
REMARK   3      T33:   0.3277 T12:  -0.0135                                     
REMARK   3      T13:   0.1207 T23:  -0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0061 L22:   0.0010                                     
REMARK   3      L33:   0.0118 L12:   0.0018                                     
REMARK   3      L13:  -0.0056 L23:  -0.0041                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0369 S12:   0.0196 S13:  -0.0703                       
REMARK   3      S21:   0.0193 S22:  -0.0161 S23:   0.0214                       
REMARK   3      S31:  -0.0903 S32:  -0.1307 S33:  -0.0002                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 113 THROUGH 347 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4996  48.7004  27.8136              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6897 T22:   0.3874                                     
REMARK   3      T33:   0.4003 T12:   0.0783                                     
REMARK   3      T13:   0.1281 T23:   0.0001                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0814 L22:   0.0269                                     
REMARK   3      L33:   0.0158 L12:   0.0399                                     
REMARK   3      L13:   0.0581 L23:   0.0251                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0396 S12:   0.0657 S13:  -0.0264                       
REMARK   3      S21:  -0.0205 S22:   0.0445 S23:  -0.0627                       
REMARK   3      S31:  -0.2169 S32:   0.0168 S33:   0.0000                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 348 THROUGH 432 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  48.7780  21.4362  15.9283              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4381 T22:   0.5835                                     
REMARK   3      T33:   0.3827 T12:   0.0198                                     
REMARK   3      T13:   0.1184 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0320 L22:   0.0108                                     
REMARK   3      L33:   0.0254 L12:  -0.0103                                     
REMARK   3      L13:  -0.0040 L23:   0.0030                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0151 S12:  -0.0443 S13:  -0.1709                       
REMARK   3      S21:   0.0168 S22:   0.0582 S23:  -0.0010                       
REMARK   3      S31:  -0.0916 S32:  -0.0589 S33:   0.0001                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 433 THROUGH 515 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5680  13.5660   3.4808              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4149 T22:   0.5229                                     
REMARK   3      T33:   0.3655 T12:   0.0551                                     
REMARK   3      T13:   0.1870 T23:   0.0232                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0373 L22:   0.0057                                     
REMARK   3      L33:   0.0494 L12:   0.0110                                     
REMARK   3      L13:   0.0389 L23:   0.0133                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0120 S12:   0.0736 S13:  -0.0938                       
REMARK   3      S21:  -0.0581 S22:  -0.0935 S23:  -0.0570                       
REMARK   3      S31:  -0.0621 S32:  -0.0274 S33:  -0.0111                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 516 THROUGH 560 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9399  36.7153   6.4248              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6685 T22:   0.3898                                     
REMARK   3      T33:   0.3935 T12:  -0.0231                                     
REMARK   3      T13:   0.1535 T23:   0.0842                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0174 L22:   0.0022                                     
REMARK   3      L33:   0.0103 L12:   0.0012                                     
REMARK   3      L13:   0.0088 L23:   0.0051                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0382 S12:   0.0802 S13:  -0.0887                       
REMARK   3      S21:  -0.0283 S22:  -0.0039 S23:  -0.0036                       
REMARK   3      S31:  -0.1756 S32:   0.0616 S33:   0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 561 THROUGH 643 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  24.0652  30.3232  17.8282              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5203 T22:   0.4299                                     
REMARK   3      T33:   0.3010 T12:   0.0098                                     
REMARK   3      T13:   0.1170 T23:   0.0121                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0765 L22:   0.0168                                     
REMARK   3      L33:   0.0208 L12:  -0.0249                                     
REMARK   3      L13:  -0.0043 L23:   0.0190                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0355 S12:  -0.0068 S13:  -0.1391                       
REMARK   3      S21:  -0.0464 S22:  -0.0361 S23:  -0.0164                       
REMARK   3      S31:  -0.2085 S32:  -0.0639 S33:   0.0131                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 731 THROUGH 1011 )                
REMARK   3    ORIGIN FOR THE GROUP (A):  18.0043  60.0664  28.2928              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6780 T22:  -0.0445                                     
REMARK   3      T33:   0.1692 T12:   0.1454                                     
REMARK   3      T13:   0.0353 T23:   0.0276                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2784 L22:   0.3352                                     
REMARK   3      L33:   0.1022 L12:   0.0207                                     
REMARK   3      L13:   0.0884 L23:   0.0663                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0156 S12:  -0.0050 S13:   0.0500                       
REMARK   3      S21:  -0.2476 S22:  -0.1860 S23:   0.1780                       
REMARK   3      S31:  -0.2438 S32:  -0.1785 S33:  -0.1974                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1012 THROUGH 1237 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.5919   1.2983  49.9512              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1303 T22:   0.3020                                     
REMARK   3      T33:   0.2753 T12:  -0.0087                                     
REMARK   3      T13:   0.0102 T23:  -0.0304                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2049 L22:   0.1068                                     
REMARK   3      L33:   0.1143 L12:  -0.0341                                     
REMARK   3      L13:   0.0295 L23:  -0.0223                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0082 S12:   0.0471 S13:  -0.0107                       
REMARK   3      S21:   0.0104 S22:   0.0218 S23:  -0.0210                       
REMARK   3      S31:   0.0126 S32:  -0.0906 S33:   0.0000                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1238 THROUGH 1496 )               
REMARK   3    ORIGIN FOR THE GROUP (A):  26.9885  66.4210  42.3006              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5427 T22:   0.0765                                     
REMARK   3      T33:   0.2719 T12:   0.0311                                     
REMARK   3      T13:   0.0770 T23:  -0.0114                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2177 L22:   0.0567                                     
REMARK   3      L33:   0.0432 L12:  -0.0373                                     
REMARK   3      L13:   0.0840 L23:   0.0033                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0210 S12:  -0.0198 S13:   0.1661                       
REMARK   3      S21:  -0.0100 S22:  -0.0486 S23:   0.0939                       
REMARK   3      S31:  -0.2069 S32:  -0.0632 S33:  -0.0213                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1497 THROUGH 1543 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   8.2796  96.1093  53.3772              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4554 T22:   0.2101                                     
REMARK   3      T33:   0.4902 T12:   0.0556                                     
REMARK   3      T13:  -0.0663 T23:  -0.0249                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0075 L22:   0.0131                                     
REMARK   3      L33:   0.0140 L12:   0.0025                                     
REMARK   3      L13:  -0.0028 L23:   0.0048                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0223 S12:  -0.0065 S13:  -0.0989                       
REMARK   3      S21:   0.0149 S22:  -0.0765 S23:  -0.0014                       
REMARK   3      S31:   0.1358 S32:  -0.0062 S33:   0.0001                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1544 THROUGH 1641 )               
REMARK   3    ORIGIN FOR THE GROUP (A):   5.9712  96.9825  57.3938              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3436 T22:   0.2163                                     
REMARK   3      T33:   0.5100 T12:  -0.0235                                     
REMARK   3      T13:  -0.0003 T23:  -0.0263                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0052 L22:   0.0319                                     
REMARK   3      L33:   0.0216 L12:   0.0008                                     
REMARK   3      L13:  -0.0114 L23:  -0.0124                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0311 S12:  -0.0964 S13:  -0.0548                       
REMARK   3      S21:   0.1066 S22:   0.0261 S23:   0.0179                       
REMARK   3      S31:   0.1579 S32:   0.0177 S33:   0.0000                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 124 THROUGH 166 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.0177  40.4189  30.4738              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7323 T22:   0.5413                                     
REMARK   3      T33:   0.5736 T12:   0.2190                                     
REMARK   3      T13:   0.0834 T23:   0.1341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0014 L22:   0.0037                                     
REMARK   3      L33:   0.0021 L12:  -0.0032                                     
REMARK   3      L13:  -0.0034 L23:   0.0029                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0022 S12:  -0.0183 S13:   0.0846                       
REMARK   3      S21:  -0.0143 S22:  -0.0360 S23:   0.0125                       
REMARK   3      S31:  -0.0757 S32:  -0.0127 S33:   0.0000                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 167 THROUGH 190 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3746  37.5724  22.2321              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5774 T22:   0.6388                                     
REMARK   3      T33:   0.5222 T12:   0.2608                                     
REMARK   3      T13:   0.0530 T23:   0.1604                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0004 L22:   0.0007                                     
REMARK   3      L33:   0.0003 L12:   0.0003                                     
REMARK   3      L13:   0.0005 L23:  -0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0028 S12:   0.0044 S13:   0.0206                       
REMARK   3      S21:  -0.0367 S22:   0.0146 S23:  -0.0121                       
REMARK   3      S31:  -0.0496 S32:   0.0107 S33:  -0.0000                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 191 THROUGH 201 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -16.0375   8.2922  27.5460              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4384 T22:   0.6692                                     
REMARK   3      T33:   0.4331 T12:   0.0117                                     
REMARK   3      T13:   0.0154 T23:  -0.0015                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0006 L22:   0.0022                                     
REMARK   3      L33:   0.0005 L12:  -0.0003                                     
REMARK   3      L13:  -0.0000 L23:   0.0021                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0137 S12:   0.0091 S13:  -0.0057                       
REMARK   3      S21:  -0.0094 S22:   0.0189 S23:   0.0111                       
REMARK   3      S31:   0.0379 S32:  -0.0313 S33:   0.0000                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 202 THROUGH 222 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.7060   8.8825  25.8837              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4701 T22:   0.7005                                     
REMARK   3      T33:   0.3511 T12:   0.0007                                     
REMARK   3      T13:   0.0652 T23:   0.0188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0004 L22:   0.0043                                     
REMARK   3      L33:   0.0024 L12:   0.0018                                     
REMARK   3      L13:  -0.0005 L23:   0.0026                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0005 S12:   0.0125 S13:   0.0512                       
REMARK   3      S21:  -0.0173 S22:  -0.0102 S23:   0.0013                       
REMARK   3      S31:   0.0291 S32:  -0.0329 S33:  -0.0001                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 223 THROUGH 235 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.7969  -0.3163  15.0600              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6349 T22:   0.6227                                     
REMARK   3      T33:   0.4475 T12:  -0.0246                                     
REMARK   3      T13:  -0.0120 T23:  -0.0872                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.0004 L22:   0.0003                                     
REMARK   3      L33:   0.0006 L12:  -0.0002                                     
REMARK   3      L13:  -0.0001 L23:   0.0007                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0053 S12:   0.0100 S13:  -0.0079                       
REMARK   3      S21:  -0.0093 S22:  -0.0041 S23:   0.0002                       
REMARK   3      S31:   0.0068 S32:  -0.0100 S33:  -0.0000                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'C' AND (RESID 236 THROUGH 252 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -15.9492   8.7903  19.4420              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5104 T22:   0.6812                                     
REMARK   3      T33:   0.5089 T12:  -0.0296                                     
REMARK   3      T13:  -0.0777 T23:  -0.0268                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0000 L22:   0.0011                                     
REMARK   3      L33:   0.0024 L12:   0.0006                                     
REMARK   3      L13:   0.0010 L23:   0.0019                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0285 S12:  -0.0130 S13:   0.0442                       
REMARK   3      S21:  -0.0301 S22:   0.0141 S23:   0.0088                       
REMARK   3      S31:   0.0332 S32:  -0.0634 S33:   0.0000                       
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 5FO8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 18-NOV-15.                  
REMARK 100 THE DEPOSITION ID IS D_1290065589.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID29                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.933                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : IMOSFLM                            
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 98854                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 69.950                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 3.800                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 6.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.44                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.90                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.000                              
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: PDB ENTRY 2I07, PDB ENTRY 3O8E                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM AMMONIUM CITRATE 7% PEG 3350 5MM   
REMARK 280  GLUTATHIONE 50MM BIS-TRIS PROPANE, PH 6.5                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
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,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
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       41.41500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      116.91500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       41.41500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      116.91500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 18170 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 76110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 16.1 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E                         
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     GLU A    95                                                      
REMARK 465     PHE A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     ALA A   666                                                      
REMARK 465     ALA A   667                                                      
REMARK 465     SER B   749                                                      
REMARK 465     ASN B   750                                                      
REMARK 465     LEU B   751                                                      
REMARK 465     ASP B   752                                                      
REMARK 465     GLU B  1372                                                      
REMARK 465     THR B  1373                                                      
REMARK 465     GLU B  1374                                                      
REMARK 465     LYS B  1375                                                      
REMARK 465     ARG B  1376                                                      
REMARK 465     PRO B  1377                                                      
REMARK 465     GLN B  1378                                                      
REMARK 465     ASP B  1379                                                      
REMARK 465     ALA B  1380                                                      
REMARK 465     GLU B  1498                                                      
REMARK 465     ASP B  1499                                                      
REMARK 465     GLY B  1500                                                      
REMARK 465     LYS B  1501                                                      
REMARK 465     LEU B  1502                                                      
REMARK 465     ASN B  1503                                                      
REMARK 465     LYS B  1504                                                      
REMARK 465     LEU B  1505                                                      
REMARK 465     CYS C    35                                                      
REMARK 465     GLU C    36                                                      
REMARK 465     GLU C    37                                                      
REMARK 465     PRO C    38                                                      
REMARK 465     PRO C    39                                                      
REMARK 465     THR C    40                                                      
REMARK 465     PHE C    41                                                      
REMARK 465     GLU C    42                                                      
REMARK 465     ALA C    43                                                      
REMARK 465     MET C    44                                                      
REMARK 465     GLU C    45                                                      
REMARK 465     LEU C    46                                                      
REMARK 465     ILE C    47                                                      
REMARK 465     GLY C    48                                                      
REMARK 465     LYS C    49                                                      
REMARK 465     PRO C    50                                                      
REMARK 465     LYS C    51                                                      
REMARK 465     PRO C    52                                                      
REMARK 465     TYR C    53                                                      
REMARK 465     TYR C    54                                                      
REMARK 465     GLU C    55                                                      
REMARK 465     ILE C    56                                                      
REMARK 465     GLY C    57                                                      
REMARK 465     GLU C    58                                                      
REMARK 465     ARG C    59                                                      
REMARK 465     VAL C    60                                                      
REMARK 465     ASP C    61                                                      
REMARK 465     TYR C    62                                                      
REMARK 465     LYS C    63                                                      
REMARK 465     CYS C    64                                                      
REMARK 465     LYS C    65                                                      
REMARK 465     LYS C    66                                                      
REMARK 465     GLY C    67                                                      
REMARK 465     TYR C    68                                                      
REMARK 465     PHE C    69                                                      
REMARK 465     TYR C    70                                                      
REMARK 465     ILE C    71                                                      
REMARK 465     PRO C    72                                                      
REMARK 465     PRO C    73                                                      
REMARK 465     LEU C    74                                                      
REMARK 465     ALA C    75                                                      
REMARK 465     THR C    76                                                      
REMARK 465     HIS C    77                                                      
REMARK 465     THR C    78                                                      
REMARK 465     ILE C    79                                                      
REMARK 465     CYS C    80                                                      
REMARK 465     ASP C    81                                                      
REMARK 465     ARG C    82                                                      
REMARK 465     ASN C    83                                                      
REMARK 465     HIS C    84                                                      
REMARK 465     THR C    85                                                      
REMARK 465     TRP C    86                                                      
REMARK 465     LEU C    87                                                      
REMARK 465     PRO C    88                                                      
REMARK 465     VAL C    89                                                      
REMARK 465     SER C    90                                                      
REMARK 465     ASP C    91                                                      
REMARK 465     ASP C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     CYS C    94                                                      
REMARK 465     TYR C    95                                                      
REMARK 465     ARG C    96                                                      
REMARK 465     GLU C    97                                                      
REMARK 465     THR C    98                                                      
REMARK 465     CYS C    99                                                      
REMARK 465     PRO C   100                                                      
REMARK 465     TYR C   101                                                      
REMARK 465     ILE C   102                                                      
REMARK 465     ARG C   103                                                      
REMARK 465     ASP C   104                                                      
REMARK 465     PRO C   105                                                      
REMARK 465     LEU C   106                                                      
REMARK 465     ASN C   107                                                      
REMARK 465     GLY C   108                                                      
REMARK 465     GLN C   109                                                      
REMARK 465     ALA C   110                                                      
REMARK 465     VAL C   111                                                      
REMARK 465     PRO C   112                                                      
REMARK 465     ALA C   113                                                      
REMARK 465     ASN C   114                                                      
REMARK 465     GLY C   115                                                      
REMARK 465     THR C   116                                                      
REMARK 465     TYR C   117                                                      
REMARK 465     GLU C   118                                                      
REMARK 465     PHE C   119                                                      
REMARK 465     GLY C   120                                                      
REMARK 465     TYR C   121                                                      
REMARK 465     GLN C   122                                                      
REMARK 465     MET C   123                                                      
REMARK 465     HIS C   124                                                      
REMARK 465     PHE C   125                                                      
REMARK 465     ILE C   126                                                      
REMARK 465     CYS C   127                                                      
REMARK 465     ASN C   128                                                      
REMARK 465     GLU C   129                                                      
REMARK 465     GLY C   130                                                      
REMARK 465     TYR C   131                                                      
REMARK 465     TYR C   132                                                      
REMARK 465     LEU C   133                                                      
REMARK 465     ILE C   134                                                      
REMARK 465     GLY C   135                                                      
REMARK 465     GLU C   136                                                      
REMARK 465     GLU C   137                                                      
REMARK 465     ILE C   138                                                      
REMARK 465     LEU C   139                                                      
REMARK 465     TYR C   140                                                      
REMARK 465     CYS C   141                                                      
REMARK 465     GLU C   142                                                      
REMARK 465     LEU C   143                                                      
REMARK 465     LYS C   144                                                      
REMARK 465     GLY C   145                                                      
REMARK 465     SER C   146                                                      
REMARK 465     VAL C   147                                                      
REMARK 465     ALA C   148                                                      
REMARK 465     ILE C   149                                                      
REMARK 465     TRP C   150                                                      
REMARK 465     SER C   151                                                      
REMARK 465     GLY C   152                                                      
REMARK 465     LYS C   153                                                      
REMARK 465     PRO C   154                                                      
REMARK 465     PRO C   155                                                      
REMARK 465     ILE C   156                                                      
REMARK 465     CYS C   157                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU C 158    CG   CD   OE1  OE2                                  
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   SG   CYS B  1506     CB   CYS B  1511              1.74            
REMARK 500   OG   SER B  1586     O    HOH B  2246              1.83            
REMARK 500   O    HOH A  2023     O    HOH B  2091              1.83            
REMARK 500   O    HOH A  2010     O    HOH A  2050              1.85            
REMARK 500   O    HOH A  2016     O    HOH A  2031              1.86            
REMARK 500   O    HOH A  2105     O    HOH A  2106              1.90            
REMARK 500   O    HOH B  2019     O    HOH B  2191              1.91            
REMARK 500   O    HOH A  2040     O    HOH A  2081              1.97            
REMARK 500   O    HOH B  2010     O    HOH B  2166              1.97            
REMARK 500   O    HOH B  2118     O    HOH C  2019              1.98            
REMARK 500   O    HOH B  2222     O    HOH B  2288              2.00            
REMARK 500   O    SER A   351     O    HOH A  2090              2.00            
REMARK 500   O    HOH B  2219     O    HOH B  2220              2.01            
REMARK 500   O    ASP B   819     O    HOH B  2035              2.03            
REMARK 500   ND1  HIS B  1026     O    HOH B  2082              2.04            
REMARK 500   O    HOH A  2011     O    HOH A  2012              2.05            
REMARK 500   O    HOH A  2054     O    HOH A  2116              2.05            
REMARK 500   O    HOH B  2015     O    HOH B  2016              2.06            
REMARK 500   O    TRP B  1313     O    HOH B  2231              2.07            
REMARK 500   OE1  GLU B   822     O    HOH B  2037              2.08            
REMARK 500   O    HOH B  2247     O    HOH B  2270              2.10            
REMARK 500   O    HOH B  2162     O    HOH C  2010              2.10            
REMARK 500   O    HOH A  2017     O    HOH B  2090              2.11            
REMARK 500   OH   TYR B  1483     O    HOH B  2238              2.12            
REMARK 500   O    HOH B  2007     O    HOH B  2119              2.13            
REMARK 500   N    SER B   976     O    HOH B  2056              2.13            
REMARK 500   O    HOH A  2072     O    HOH A  2076              2.14            
REMARK 500   O    HOH B  2013     O    HOH B  2184              2.15            
REMARK 500   OD1  ASN A    32     O    HOH A  2004              2.16            
REMARK 500   O    HOH A  2064     O    HOH A  2146              2.16            
REMARK 500   O    HOH A  2042     O    HOH A  2043              2.16            
REMARK 500   O    HOH A  2076     O    HOH A  2166              2.17            
REMARK 500   NE2  GLN B  1290     O    HOH B  2229              2.17            
REMARK 500   OD1  ASN A   378     O    HOH A  2091              2.18            
REMARK 500   O2   EDO B  2666     O    HOH B  2190              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B  2137     O    HOH B  2291     1545     2.02            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS A 100       -0.51     66.06                                   
REMARK 500    PRO A 170        0.08    -60.46                                   
REMARK 500    LYS A 241       36.98    -84.29                                   
REMARK 500    PRO A 415       47.84    -80.64                                   
REMARK 500    GLU A 464      106.15    -57.01                                   
REMARK 500    SER A 541       23.53     85.11                                   
REMARK 500    SER A 558     -154.47   -157.80                                   
REMARK 500    GLU A 571     -114.52     54.08                                   
REMARK 500    SER A 631     -159.47     51.44                                   
REMARK 500    GLU A 659      120.13    173.95                                   
REMARK 500    SER B 765      -10.12   -143.69                                   
REMARK 500    THR B 800     -171.80   -171.38                                   
REMARK 500    GLN B 858      115.47   -163.63                                   
REMARK 500    HIS B 882      109.26    -52.94                                   
REMARK 500    HIS B 918       -5.89     80.57                                   
REMARK 500    ASP B 948       75.96   -160.98                                   
REMARK 500    CYS B1010     -157.04    -91.30                                   
REMARK 500    SER B1064        4.63     82.39                                   
REMARK 500    ASN B1135       18.33     58.34                                   
REMARK 500    ASP B1216       23.44     49.16                                   
REMARK 500    THR B1399     -156.31    -77.47                                   
REMARK 500    ALA B1437       28.41   -164.96                                   
REMARK 500    SER B1439       -4.56     62.41                                   
REMARK 500    GLU B1509      -49.95     67.85                                   
REMARK 500    LYS B1595       44.68     39.96                                   
REMARK 500    LYS B1599      -13.07     78.73                                   
REMARK 500    PRO B1616       51.99    -94.06                                   
REMARK 500    PRO B1662      155.67    -48.20                                   
REMARK 500    LEU C 184       -3.11     69.94                                   
REMARK 500    PRO C 279      157.24    -49.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH B2015        DISTANCE =  6.35 ANGSTROMS                       
REMARK 525    HOH B2016        DISTANCE =  6.81 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5FO7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COMPLEMENT C3B AT 2.8 ANGSTROM RESOLUTION 
REMARK 900 RELATED ID: 5FO9   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COMPLEMENT C3B IN COMPLEX WITH CR1        
REMARK 900 (CCP15-17)                                                           
REMARK 900 RELATED ID: 5FOA   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COMPLEMENT C3B IN COMPLEX WITH DAF (CCP2- 
REMARK 900 4)                                                                   
REMARK 900 RELATED ID: 5FOB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HUMAN COMPLEMENT C3B IN COMPLEX WITH SMALLPOX   
REMARK 900 INHIBITOR OF COMPLEMENT (SPICE)                                      
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE 1013 HAS BEEN CONVERTED FROM GLN TO GLU IN                   
REMARK 999 CONVERSION OF C3 PROTEIN TO C3B                                      
DBREF  5FO8 A   23   667  UNP    P01024   CO3_HUMAN       23    667             
DBREF  5FO8 B  749  1663  UNP    P01024   CO3_HUMAN      749   1663             
DBREF  5FO8 C   35   286  UNP    P15529   MCP_HUMAN       35    286             
SEQADV 5FO8 GLU B 1013  UNP  P01024    GLN  1013 SEE REMARK 999                 
SEQRES   1 A  645  SER PRO MET TYR SER ILE ILE THR PRO ASN ILE LEU ARG          
SEQRES   2 A  645  LEU GLU SER GLU GLU THR MET VAL LEU GLU ALA HIS ASP          
SEQRES   3 A  645  ALA GLN GLY ASP VAL PRO VAL THR VAL THR VAL HIS ASP          
SEQRES   4 A  645  PHE PRO GLY LYS LYS LEU VAL LEU SER SER GLU LYS THR          
SEQRES   5 A  645  VAL LEU THR PRO ALA THR ASN HIS MET GLY ASN VAL THR          
SEQRES   6 A  645  PHE THR ILE PRO ALA ASN ARG GLU PHE LYS SER GLU LYS          
SEQRES   7 A  645  GLY ARG ASN LYS PHE VAL THR VAL GLN ALA THR PHE GLY          
SEQRES   8 A  645  THR GLN VAL VAL GLU LYS VAL VAL LEU VAL SER LEU GLN          
SEQRES   9 A  645  SER GLY TYR LEU PHE ILE GLN THR ASP LYS THR ILE TYR          
SEQRES  10 A  645  THR PRO GLY SER THR VAL LEU TYR ARG ILE PHE THR VAL          
SEQRES  11 A  645  ASN HIS LYS LEU LEU PRO VAL GLY ARG THR VAL MET VAL          
SEQRES  12 A  645  ASN ILE GLU ASN PRO GLU GLY ILE PRO VAL LYS GLN ASP          
SEQRES  13 A  645  SER LEU SER SER GLN ASN GLN LEU GLY VAL LEU PRO LEU          
SEQRES  14 A  645  SER TRP ASP ILE PRO GLU LEU VAL ASN MET GLY GLN TRP          
SEQRES  15 A  645  LYS ILE ARG ALA TYR TYR GLU ASN SER PRO GLN GLN VAL          
SEQRES  16 A  645  PHE SER THR GLU PHE GLU VAL LYS GLU TYR VAL LEU PRO          
SEQRES  17 A  645  SER PHE GLU VAL ILE VAL GLU PRO THR GLU LYS PHE TYR          
SEQRES  18 A  645  TYR ILE TYR ASN GLU LYS GLY LEU GLU VAL THR ILE THR          
SEQRES  19 A  645  ALA ARG PHE LEU TYR GLY LYS LYS VAL GLU GLY THR ALA          
SEQRES  20 A  645  PHE VAL ILE PHE GLY ILE GLN ASP GLY GLU GLN ARG ILE          
SEQRES  21 A  645  SER LEU PRO GLU SER LEU LYS ARG ILE PRO ILE GLU ASP          
SEQRES  22 A  645  GLY SER GLY GLU VAL VAL LEU SER ARG LYS VAL LEU LEU          
SEQRES  23 A  645  ASP GLY VAL GLN ASN PRO ARG ALA GLU ASP LEU VAL GLY          
SEQRES  24 A  645  LYS SER LEU TYR VAL SER ALA THR VAL ILE LEU HIS SER          
SEQRES  25 A  645  GLY SER ASP MET VAL GLN ALA GLU ARG SER GLY ILE PRO          
SEQRES  26 A  645  ILE VAL THR SER PRO TYR GLN ILE HIS PHE THR LYS THR          
SEQRES  27 A  645  PRO LYS TYR PHE LYS PRO GLY MET PRO PHE ASP LEU MET          
SEQRES  28 A  645  VAL PHE VAL THR ASN PRO ASP GLY SER PRO ALA TYR ARG          
SEQRES  29 A  645  VAL PRO VAL ALA VAL GLN GLY GLU ASP THR VAL GLN SER          
SEQRES  30 A  645  LEU THR GLN GLY ASP GLY VAL ALA LYS LEU SER ILE ASN          
SEQRES  31 A  645  THR HIS PRO SER GLN LYS PRO LEU SER ILE THR VAL ARG          
SEQRES  32 A  645  THR LYS LYS GLN GLU LEU SER GLU ALA GLU GLN ALA THR          
SEQRES  33 A  645  ARG THR MET GLN ALA LEU PRO TYR SER THR VAL GLY ASN          
SEQRES  34 A  645  SER ASN ASN TYR LEU HIS LEU SER VAL LEU ARG THR GLU          
SEQRES  35 A  645  LEU ARG PRO GLY GLU THR LEU ASN VAL ASN PHE LEU LEU          
SEQRES  36 A  645  ARG MET ASP ARG ALA HIS GLU ALA LYS ILE ARG TYR TYR          
SEQRES  37 A  645  THR TYR LEU ILE MET ASN LYS GLY ARG LEU LEU LYS ALA          
SEQRES  38 A  645  GLY ARG GLN VAL ARG GLU PRO GLY GLN ASP LEU VAL VAL          
SEQRES  39 A  645  LEU PRO LEU SER ILE THR THR ASP PHE ILE PRO SER PHE          
SEQRES  40 A  645  ARG LEU VAL ALA TYR TYR THR LEU ILE GLY ALA SER GLY          
SEQRES  41 A  645  GLN ARG GLU VAL VAL ALA ASP SER VAL TRP VAL ASP VAL          
SEQRES  42 A  645  LYS ASP SER CYS VAL GLY SER LEU VAL VAL LYS SER GLY          
SEQRES  43 A  645  GLN SER GLU ASP ARG GLN PRO VAL PRO GLY GLN GLN MET          
SEQRES  44 A  645  THR LEU LYS ILE GLU GLY ASP HIS GLY ALA ARG VAL VAL          
SEQRES  45 A  645  LEU VAL ALA VAL ASP LYS GLY VAL PHE VAL LEU ASN LYS          
SEQRES  46 A  645  LYS ASN LYS LEU THR GLN SER LYS ILE TRP ASP VAL VAL          
SEQRES  47 A  645  GLU LYS ALA ASP ILE GLY CYS THR PRO GLY SER GLY LYS          
SEQRES  48 A  645  ASP TYR ALA GLY VAL PHE SER ASP ALA GLY LEU THR PHE          
SEQRES  49 A  645  THR SER SER SER GLY GLN GLN THR ALA GLN ARG ALA GLU          
SEQRES  50 A  645  LEU GLN CYS PRO GLN PRO ALA ALA                              
SEQRES   1 B  915  SER ASN LEU ASP GLU ASP ILE ILE ALA GLU GLU ASN ILE          
SEQRES   2 B  915  VAL SER ARG SER GLU PHE PRO GLU SER TRP LEU TRP ASN          
SEQRES   3 B  915  VAL GLU ASP LEU LYS GLU PRO PRO LYS ASN GLY ILE SER          
SEQRES   4 B  915  THR LYS LEU MET ASN ILE PHE LEU LYS ASP SER ILE THR          
SEQRES   5 B  915  THR TRP GLU ILE LEU ALA VAL SER MET SER ASP LYS LYS          
SEQRES   6 B  915  GLY ILE CYS VAL ALA ASP PRO PHE GLU VAL THR VAL MET          
SEQRES   7 B  915  GLN ASP PHE PHE ILE ASP LEU ARG LEU PRO TYR SER VAL          
SEQRES   8 B  915  VAL ARG ASN GLU GLN VAL GLU ILE ARG ALA VAL LEU TYR          
SEQRES   9 B  915  ASN TYR ARG GLN ASN GLN GLU LEU LYS VAL ARG VAL GLU          
SEQRES  10 B  915  LEU LEU HIS ASN PRO ALA PHE CYS SER LEU ALA THR THR          
SEQRES  11 B  915  LYS ARG ARG HIS GLN GLN THR VAL THR ILE PRO PRO LYS          
SEQRES  12 B  915  SER SER LEU SER VAL PRO TYR VAL ILE VAL PRO LEU LYS          
SEQRES  13 B  915  THR GLY LEU GLN GLU VAL GLU VAL LYS ALA ALA VAL TYR          
SEQRES  14 B  915  HIS HIS PHE ILE SER ASP GLY VAL ARG LYS SER LEU LYS          
SEQRES  15 B  915  VAL VAL PRO GLU GLY ILE ARG MET ASN LYS THR VAL ALA          
SEQRES  16 B  915  VAL ARG THR LEU ASP PRO GLU ARG LEU GLY ARG GLU GLY          
SEQRES  17 B  915  VAL GLN LYS GLU ASP ILE PRO PRO ALA ASP LEU SER ASP          
SEQRES  18 B  915  GLN VAL PRO ASP THR GLU SER GLU THR ARG ILE LEU LEU          
SEQRES  19 B  915  GLN GLY THR PRO VAL ALA GLN MET THR GLU ASP ALA VAL          
SEQRES  20 B  915  ASP ALA GLU ARG LEU LYS HIS LEU ILE VAL THR PRO SER          
SEQRES  21 B  915  GLY CYS GLY GLU GLU ASN MET ILE GLY MET THR PRO THR          
SEQRES  22 B  915  VAL ILE ALA VAL HIS TYR LEU ASP GLU THR GLU GLN TRP          
SEQRES  23 B  915  GLU LYS PHE GLY LEU GLU LYS ARG GLN GLY ALA LEU GLU          
SEQRES  24 B  915  LEU ILE LYS LYS GLY TYR THR GLN GLN LEU ALA PHE ARG          
SEQRES  25 B  915  GLN PRO SER SER ALA PHE ALA ALA PHE VAL LYS ARG ALA          
SEQRES  26 B  915  PRO SER THR TRP LEU THR ALA TYR VAL VAL LYS VAL PHE          
SEQRES  27 B  915  SER LEU ALA VAL ASN LEU ILE ALA ILE ASP SER GLN VAL          
SEQRES  28 B  915  LEU CYS GLY ALA VAL LYS TRP LEU ILE LEU GLU LYS GLN          
SEQRES  29 B  915  LYS PRO ASP GLY VAL PHE GLN GLU ASP ALA PRO VAL ILE          
SEQRES  30 B  915  HIS GLN GLU MET ILE GLY GLY LEU ARG ASN ASN ASN GLU          
SEQRES  31 B  915  LYS ASP MET ALA LEU THR ALA PHE VAL LEU ILE SER LEU          
SEQRES  32 B  915  GLN GLU ALA LYS ASP ILE CYS GLU GLU GLN VAL ASN SER          
SEQRES  33 B  915  LEU PRO GLY SER ILE THR LYS ALA GLY ASP PHE LEU GLU          
SEQRES  34 B  915  ALA ASN TYR MET ASN LEU GLN ARG SER TYR THR VAL ALA          
SEQRES  35 B  915  ILE ALA GLY TYR ALA LEU ALA GLN MET GLY ARG LEU LYS          
SEQRES  36 B  915  GLY PRO LEU LEU ASN LYS PHE LEU THR THR ALA LYS ASP          
SEQRES  37 B  915  LYS ASN ARG TRP GLU ASP PRO GLY LYS GLN LEU TYR ASN          
SEQRES  38 B  915  VAL GLU ALA THR SER TYR ALA LEU LEU ALA LEU LEU GLN          
SEQRES  39 B  915  LEU LYS ASP PHE ASP PHE VAL PRO PRO VAL VAL ARG TRP          
SEQRES  40 B  915  LEU ASN GLU GLN ARG TYR TYR GLY GLY GLY TYR GLY SER          
SEQRES  41 B  915  THR GLN ALA THR PHE MET VAL PHE GLN ALA LEU ALA GLN          
SEQRES  42 B  915  TYR GLN LYS ASP ALA PRO ASP HIS GLN GLU LEU ASN LEU          
SEQRES  43 B  915  ASP VAL SER LEU GLN LEU PRO SER ARG SER SER LYS ILE          
SEQRES  44 B  915  THR HIS ARG ILE HIS TRP GLU SER ALA SER LEU LEU ARG          
SEQRES  45 B  915  SER GLU GLU THR LYS GLU ASN GLU GLY PHE THR VAL THR          
SEQRES  46 B  915  ALA GLU GLY LYS GLY GLN GLY THR LEU SER VAL VAL THR          
SEQRES  47 B  915  MET TYR HIS ALA LYS ALA LYS ASP GLN LEU THR CYS ASN          
SEQRES  48 B  915  LYS PHE ASP LEU LYS VAL THR ILE LYS PRO ALA PRO GLU          
SEQRES  49 B  915  THR GLU LYS ARG PRO GLN ASP ALA LYS ASN THR MET ILE          
SEQRES  50 B  915  LEU GLU ILE CYS THR ARG TYR ARG GLY ASP GLN ASP ALA          
SEQRES  51 B  915  THR MET SER ILE LEU ASP ILE SER MET MET THR GLY PHE          
SEQRES  52 B  915  ALA PRO ASP THR ASP ASP LEU LYS GLN LEU ALA ASN GLY          
SEQRES  53 B  915  VAL ASP ARG TYR ILE SER LYS TYR GLU LEU ASP LYS ALA          
SEQRES  54 B  915  PHE SER ASP ARG ASN THR LEU ILE ILE TYR LEU ASP LYS          
SEQRES  55 B  915  VAL SER HIS SER GLU ASP ASP CYS LEU ALA PHE LYS VAL          
SEQRES  56 B  915  HIS GLN TYR PHE ASN VAL GLU LEU ILE GLN PRO GLY ALA          
SEQRES  57 B  915  VAL LYS VAL TYR ALA TYR TYR ASN LEU GLU GLU SER CYS          
SEQRES  58 B  915  THR ARG PHE TYR HIS PRO GLU LYS GLU ASP GLY LYS LEU          
SEQRES  59 B  915  ASN LYS LEU CYS ARG ASP GLU LEU CYS ARG CYS ALA GLU          
SEQRES  60 B  915  GLU ASN CYS PHE ILE GLN LYS SER ASP ASP LYS VAL THR          
SEQRES  61 B  915  LEU GLU GLU ARG LEU ASP LYS ALA CYS GLU PRO GLY VAL          
SEQRES  62 B  915  ASP TYR VAL TYR LYS THR ARG LEU VAL LYS VAL GLN LEU          
SEQRES  63 B  915  SER ASN ASP PHE ASP GLU TYR ILE MET ALA ILE GLU GLN          
SEQRES  64 B  915  THR ILE LYS SER GLY SER ASP GLU VAL GLN VAL GLY GLN          
SEQRES  65 B  915  GLN ARG THR PHE ILE SER PRO ILE LYS CYS ARG GLU ALA          
SEQRES  66 B  915  LEU LYS LEU GLU GLU LYS LYS HIS TYR LEU MET TRP GLY          
SEQRES  67 B  915  LEU SER SER ASP PHE TRP GLY GLU LYS PRO ASN LEU SER          
SEQRES  68 B  915  TYR ILE ILE GLY LYS ASP THR TRP VAL GLU HIS TRP PRO          
SEQRES  69 B  915  GLU GLU ASP GLU CYS GLN ASP GLU GLU ASN GLN LYS GLN          
SEQRES  70 B  915  CYS GLN ASP LEU GLY ALA PHE THR GLU SER MET VAL VAL          
SEQRES  71 B  915  PHE GLY CYS PRO ASN                                          
SEQRES   1 C  252  CYS GLU GLU PRO PRO THR PHE GLU ALA MET GLU LEU ILE          
SEQRES   2 C  252  GLY LYS PRO LYS PRO TYR TYR GLU ILE GLY GLU ARG VAL          
SEQRES   3 C  252  ASP TYR LYS CYS LYS LYS GLY TYR PHE TYR ILE PRO PRO          
SEQRES   4 C  252  LEU ALA THR HIS THR ILE CYS ASP ARG ASN HIS THR TRP          
SEQRES   5 C  252  LEU PRO VAL SER ASP ASP ALA CYS TYR ARG GLU THR CYS          
SEQRES   6 C  252  PRO TYR ILE ARG ASP PRO LEU ASN GLY GLN ALA VAL PRO          
SEQRES   7 C  252  ALA ASN GLY THR TYR GLU PHE GLY TYR GLN MET HIS PHE          
SEQRES   8 C  252  ILE CYS ASN GLU GLY TYR TYR LEU ILE GLY GLU GLU ILE          
SEQRES   9 C  252  LEU TYR CYS GLU LEU LYS GLY SER VAL ALA ILE TRP SER          
SEQRES  10 C  252  GLY LYS PRO PRO ILE CYS GLU LYS VAL LEU CYS THR PRO          
SEQRES  11 C  252  PRO PRO LYS ILE LYS ASN GLY LYS HIS THR PHE SER GLU          
SEQRES  12 C  252  VAL GLU VAL PHE GLU TYR LEU ASP ALA VAL THR TYR SER          
SEQRES  13 C  252  CYS ASP PRO ALA PRO GLY PRO ASP PRO PHE SER LEU ILE          
SEQRES  14 C  252  GLY GLU SER THR ILE TYR CYS GLY ASP ASN SER VAL TRP          
SEQRES  15 C  252  SER ARG ALA ALA PRO GLU CYS LYS VAL VAL LYS CYS ARG          
SEQRES  16 C  252  PHE PRO VAL VAL GLU ASN GLY LYS GLN ILE SER GLY PHE          
SEQRES  17 C  252  GLY LYS LYS PHE TYR TYR LYS ALA THR VAL MET PHE GLU          
SEQRES  18 C  252  CYS ASP LYS GLY PHE TYR LEU ASP GLY SER ASP THR ILE          
SEQRES  19 C  252  VAL CYS ASP SER ASN SER THR TRP ASP PRO PRO VAL PRO          
SEQRES  20 C  252  LYS CYS LEU LYS VAL                                          
MODRES 5FO8 ASN A   85  ASN  GLYCOSYLATION SITE                                 
MODRES 5FO8 ASN B  939  ASN  GLYCOSYLATION SITE                                 
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    BMA  E   3      11                                                       
HET    EDO  A1666       4                                                       
HET    EDO  A1667       4                                                       
HET    EDO  A1668       4                                                       
HET    EDO  A1669       4                                                       
HET    EDO  B2664       4                                                       
HET    EDO  B2665       4                                                       
HET    EDO  B2666       4                                                       
HET    EDO  B2667       4                                                       
HET    EDO  B2668       4                                                       
HET    EDO  B2669       4                                                       
HET    EDO  B2670       4                                                       
HET    EDO  B2671       4                                                       
HET    EDO  B2672       4                                                       
HET    EDO  B2673       4                                                       
HET    EDO  B2674       4                                                       
HET    EDO  B2675       4                                                       
HET    EDO  B2676       4                                                       
HET    EDO  B2677       4                                                       
HET    EDO  B2678       4                                                       
HET    EDO  B2679       4                                                       
HET    EDO  B2680       4                                                       
HET    EDO  B2681       4                                                       
HET    EDO  B2682       4                                                       
HET    EDO  B2683       4                                                       
HET    EDO  B2684       4                                                       
HET    EDO  B2685       4                                                       
HET    EDO  B2686       4                                                       
HET    EDO  B2687       4                                                       
HET    EDO  B2688       4                                                       
HET    EDO  B2689       4                                                       
HET    EDO  B2690       4                                                       
HET    EDO  B2691       4                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     BMA BETA-D-MANNOPYRANOSE                                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   4  NAG    4(C8 H15 N O6)                                               
FORMUL   5  BMA    C6 H12 O6                                                    
FORMUL   6  EDO    32(C2 H6 O2)                                                 
FORMUL  38  HOH   *492(H2 O)                                                    
HELIX    1   1 THR A   77  ASN A   81  5                                   5    
HELIX    2   2 SER A  303  GLY A  310  1                                   8    
HELIX    3   3 ARG A  315  VAL A  320  5                                   6    
HELIX    4   4 SER A  432  GLN A  436  5                                   5    
HELIX    5   5 THR A  448  SER A  452  5                                   5    
HELIX    6   6 HIS A  483  ILE A  487  5                                   5    
HELIX    7   7 THR A  522  ILE A  526  5                                   5    
HELIX    8   8 LYS A  600  ASN A  606  1                                   7    
HELIX    9   9 THR A  612  ALA A  623  1                                  12    
HELIX   10  10 ASP A  634  ALA A  642  1                                   9    
HELIX   11  11 ALA B  757  ILE B  761  5                                   5    
HELIX   12  12 ASP B  948  GLY B  953  1                                   6    
HELIX   13  13 ASP B  996  ILE B 1004  5                                   9    
HELIX   14  14 GLU B 1012  GLU B 1032  1                                  21    
HELIX   15  15 GLN B 1033  GLY B 1038  1                                   6    
HELIX   16  16 LYS B 1041  LEU B 1057  1                                  17    
HELIX   17  17 SER B 1075  VAL B 1090  1                                  16    
HELIX   18  18 ASP B 1096  GLN B 1112  1                                  17    
HELIX   19  19 HIS B 1126  ARG B 1134  5                                   9    
HELIX   20  20 GLU B 1138  LYS B 1155  1                                  18    
HELIX   21  21 SER B 1164  TYR B 1180  1                                  17    
HELIX   22  22 MET B 1181  LEU B 1183  5                                   3    
HELIX   23  23 ARG B 1185  GLN B 1198  1                                  14    
HELIX   24  24 LYS B 1203  THR B 1213  1                                  11    
HELIX   25  25 ASP B 1216  ASN B 1218  5                                   3    
HELIX   26  26 LYS B 1225  LEU B 1243  1                                  19    
HELIX   27  27 PHE B 1248  GLN B 1259  1                                  12    
HELIX   28  28 SER B 1268  ALA B 1286  1                                  19    
HELIX   29  29 ASP B 1414  ASN B 1423  1                                  10    
HELIX   30  30 LYS B 1431  ASP B 1435  5                                   5    
HELIX   31  31 SER B 1439  ARG B 1441  5                                   3    
HELIX   32  32 GLU B 1509  GLU B 1516  1                                   8    
HELIX   33  33 ASN B 1517  PHE B 1519  5                                   3    
HELIX   34  34 THR B 1528  CYS B 1537  1                                  10    
HELIX   35  35 CYS B 1590  LYS B 1595  1                                   6    
HELIX   36  36 GLU B 1633  GLN B 1638  1                                   6    
HELIX   37  37 ASP B 1639  GLU B 1641  5                                   3    
HELIX   38  38 ASN B 1642  PHE B 1659  1                                  18    
HELIX   39  39 GLY C  211  VAL C  215  5                                   5    
SHEET    1  AA 4 MET A  83  PHE A  88  0                                        
SHEET    2  AA 4 GLU A  40  HIS A  47 -1  O  GLU A  40   N  PHE A  88           
SHEET    3  AA 4 MET A  25  PRO A  31 -1  O  MET A  25   N  HIS A  47           
SHEET    4  AA 4 LEU A 644  SER A 648 -1  O  THR A 645   N  THR A  30           
SHEET    1  AB 5 ILE A  33  ARG A  35  0                                        
SHEET    2  AB 5 GLN A 115  SER A 124  1  O  LEU A 122   N  LEU A  34           
SHEET    3  AB 5 LYS A 104  PHE A 112 -1  O  LYS A 104   N  VAL A 123           
SHEET    4  AB 5 VAL A  53  ASP A  61 -1  O  THR A  56   N  THR A 111           
SHEET    5  AB 5 VAL A  68  LEU A  76 -1  N  LEU A  69   O  VAL A  59           
SHEET    1  AC 3 TYR A 129  THR A 134  0                                        
SHEET    2  AC 3 THR A 144  VAL A 152 -1  O  ARG A 148   N  GLN A 133           
SHEET    3  AC 3 VAL A 188  ASP A 194 -1  O  LEU A 189   N  ILE A 149           
SHEET    1  AD 5 ILE A 138  TYR A 139  0                                        
SHEET    2  AD 5 PHE A 218  VAL A 224  1  O  GLU A 223   N  TYR A 139           
SHEET    3  AD 5 GLY A 202  TYR A 210 -1  O  GLY A 202   N  VAL A 224           
SHEET    4  AD 5 THR A 162  GLU A 168 -1  O  MET A 164   N  TYR A 209           
SHEET    5  AD 5 PRO A 174  SER A 181 -1  N  VAL A 175   O  ILE A 167           
SHEET    1  AE 3 PHE A 232  PRO A 238  0                                        
SHEET    2  AE 3 LEU A 251  PHE A 259 -1  O  THR A 254   N  GLU A 237           
SHEET    3  AE 3 SER A 297  LEU A 302 -1  O  GLY A 298   N  ILE A 255           
SHEET    1  AF 5 TYR A 243  TYR A 244  0                                        
SHEET    2  AF 5 MET A 338  VAL A 349  1  O  PRO A 347   N  TYR A 243           
SHEET    3  AF 5 SER A 323  LEU A 332 -1  O  LEU A 324   N  ILE A 346           
SHEET    4  AF 5 GLY A 267  ASP A 277 -1  O  THR A 268   N  ILE A 331           
SHEET    5  AF 5 GLN A 280  ILE A 293 -1  O  GLN A 280   N  ASP A 277           
SHEET    1  AG 3 GLN A 354  HIS A 356  0                                        
SHEET    2  AG 3 PRO A 369  THR A 377 -1  O  PHE A 375   N  HIS A 356           
SHEET    3  AG 3 VAL A 406  ASN A 412 -1  O  ALA A 407   N  VAL A 374           
SHEET    1  AH 5 TYR A 363  PHE A 364  0                                        
SHEET    2  AH 5 THR A 438  PRO A 445  1  O  LEU A 444   N  PHE A 364           
SHEET    3  AH 5 LEU A 420  THR A 426 -1  O  LEU A 420   N  ALA A 443           
SHEET    4  AH 5 PRO A 388  VAL A 391 -1  O  ALA A 390   N  ARG A 425           
SHEET    5  AH 5 GLN A 398  LEU A 400 -1  O  SER A 399   N  VAL A 389           
SHEET    1  AI 3 TYR A 455  SER A 459  0                                        
SHEET    2  AI 3 THR A 470  ARG A 478 -1  O  ASN A 474   N  SER A 459           
SHEET    3  AI 3 LEU A 514  SER A 520 -1  O  VAL A 515   N  PHE A 475           
SHEET    1  AJ 4 ARG A 499  VAL A 507  0                                        
SHEET    2  AJ 4 TYR A 489  ASN A 496 -1  O  TYR A 490   N  GLN A 506           
SHEET    3  AJ 4 SER A 528  LEU A 537 -1  O  ARG A 530   N  MET A 495           
SHEET    4  AJ 4 GLU A 545  ASP A 554 -1  O  GLU A 545   N  LEU A 537           
SHEET    1  AK 3 VAL A 564  SER A 567  0                                        
SHEET    2  AK 3 GLN A 580  ASP A 588 -1  O  LYS A 584   N  LYS A 566           
SHEET    3  AK 3 ILE B 786  PHE B 794 -1  O  SER B 787   N  GLY A 587           
SHEET    1  BA 2 SER B 770  TRP B 771  0                                        
SHEET    2  BA 2 ARG A 592  ASP A 599 -1  O  ALA A 597   N  TRP B 771           
SHEET    1  BB 2 VAL B 775  ASP B 777  0                                        
SHEET    2  BB 2 ARG A 592  ASP A 599 -1  O  VAL A 593   N  GLU B 776           
SHEET    1  BC 2 GLY B 814  VAL B 817  0                                        
SHEET    2  BC 2 THR B 801  SER B 810 -1  O  SER B 808   N  CYS B 816           
SHEET    1  BD 2 PHE B 821  THR B 824  0                                        
SHEET    2  BD 2 THR B 801  SER B 810 -1  O  TRP B 802   N  VAL B 823           
SHEET    1  BE 4 PHE B 829  ARG B 834  0                                        
SHEET    2  BE 4 VAL B 845  ASN B 853 -1  O  ARG B 848   N  ARG B 834           
SHEET    3  BE 4 SER B 892  PRO B 902 -1  O  SER B 892   N  ASN B 853           
SHEET    4  BE 4 PHE B 872  CYS B 873 -1  O  CYS B 873   N  VAL B 901           
SHEET    1  BF 5 VAL B 839  VAL B 840  0                                        
SHEET    2  BF 5 SER B 922  VAL B 932  1  O  LYS B 930   N  VAL B 839           
SHEET    3  BF 5 GLY B 906  VAL B 916 -1  O  GLY B 906   N  VAL B 931           
SHEET    4  BF 5 LEU B 860  LEU B 866 -1  O  ARG B 863   N  ALA B 915           
SHEET    5  BF 5 GLN B 883  ILE B 888 -1  O  GLN B 884   N  VAL B 864           
SHEET    1  BG 4 ILE B 936  LEU B 947  0                                        
SHEET    2  BG 4 GLY B1340  ALA B1350 -1  O  GLY B1340   N  LEU B 947           
SHEET    3  BG 4 GLU B 977  GLY B 984 -1  O  GLU B 977   N  MET B1347           
SHEET    4  BG 4 ARG B1320  THR B1324 -1  O  ARG B1320   N  LEU B 982           
SHEET    1  BH 4 VAL B 957  ILE B 962  0                                        
SHEET    2  BH 4 PHE B1330  LYS B1337 -1  O  PHE B1330   N  ILE B 962           
SHEET    3  BH 4 ASN B1293  GLN B1299 -1  O  ASN B1293   N  LYS B1337           
SHEET    4  BH 4 ILE B1307  HIS B1312 -1  O  ILE B1307   N  LEU B1298           
SHEET    1  BI 4 PHE B1361  PRO B1369  0                                        
SHEET    2  BI 4 THR B1383  TYR B1392 -1  O  ILE B1385   N  LYS B1368           
SHEET    3  BI 4 ASP B1457  GLN B1465 -1  O  ASP B1457   N  THR B1390           
SHEET    4  BI 4 PHE B1411  PRO B1413 -1  O  ALA B1412   N  HIS B1464           
SHEET    1  BJ 5 ARG B1427  TYR B1428  0                                        
SHEET    2  BJ 5 THR B1443  LEU B1448 -1  O  TYR B1447   N  TYR B1428           
SHEET    3  BJ 5 SER B1401  SER B1406 -1  O  SER B1401   N  LEU B1448           
SHEET    4  BJ 5 GLY B1475  ALA B1481 -1  O  ALA B1476   N  SER B1406           
SHEET    5  BJ 5 ASN B1484  TYR B1493 -1  O  ASN B1484   N  ALA B1481           
SHEET    1  BK 7 PHE B1611  TRP B1612  0                                        
SHEET    2  BK 7 SER B1619  ILE B1621 -1  O  SER B1619   N  TRP B1612           
SHEET    3  BK 7 GLN B1581  PRO B1587  1  O  THR B1583   N  TYR B1620           
SHEET    4  BK 7 PHE B1558  LYS B1570 -1  O  ASP B1559   N  SER B1586           
SHEET    5  BK 7 VAL B1541  LEU B1554 -1  O  VAL B1544   N  LYS B1570           
SHEET    6  BK 7 HIS B1601  LEU B1607 -1  O  TYR B1602   N  THR B1547           
SHEET    7  BK 7 TRP B1627  TRP B1631 -1  O  TRP B1627   N  TRP B1605           
SHEET    1  CA 3 GLY C 171  HIS C 173  0                                        
SHEET    2  CA 3 ALA C 186  CYS C 191 -1  O  SER C 190   N  LYS C 172           
SHEET    3  CA 3 THR C 207  TYR C 209 -1  O  ILE C 208   N  VAL C 187           
SHEET    1  CB 2 SER C 201  ILE C 203  0                                        
SHEET    2  CB 2 GLU C 222  LYS C 224 -1  O  GLU C 222   N  ILE C 203           
SHEET    1  CC 4 GLY C 236  SER C 240  0                                        
SHEET    2  CC 4 THR C 251  CYS C 256 -1  O  MET C 253   N  ILE C 239           
SHEET    3  CC 4 THR C 267  CYS C 270 -1  O  ILE C 268   N  VAL C 252           
SHEET    4  CC 4 TRP C 276  ASP C 277 -1  O  ASP C 277   N  VAL C 269           
SHEET    1  CD 2 PHE C 260  ASP C 263  0                                        
SHEET    2  CD 2 LYS C 282  LYS C 285 -1  O  LYS C 282   N  ASP C 263           
SSBOND   1 CYS A  559    CYS B  816                          1555   1555  2.03  
SSBOND   2 CYS A  627    CYS A  662                          1555   1555  2.04  
SSBOND   3 CYS B  873    CYS B 1513                          1555   1555  2.84  
SSBOND   4 CYS B 1101    CYS B 1158                          1555   1555  2.04  
SSBOND   5 CYS B 1358    CYS B 1489                          1555   1555  2.04  
SSBOND   6 CYS B 1389    CYS B 1458                          1555   1555  2.04  
SSBOND   7 CYS B 1506    CYS B 1511                          1555   1555  2.04  
SSBOND   8 CYS B 1518    CYS B 1590                          1555   1555  2.03  
SSBOND   9 CYS B 1537    CYS B 1661                          1555   1555  2.05  
SSBOND  10 CYS B 1637    CYS B 1646                          1555   1555  2.04  
SSBOND  11 CYS C  162    CYS C  210                          1555   1555  2.04  
SSBOND  12 CYS C  191    CYS C  223                          1555   1555  2.05  
SSBOND  13 CYS C  228    CYS C  270                          1555   1555  2.05  
SSBOND  14 CYS C  256    CYS C  283                          1555   1555  2.04  
LINK         ND2 ASN A  85                 C1  NAG D   1     1555   1555  1.44  
LINK         ND2 ASN B 939                 C1  NAG E   1     1555   1555  1.44  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.44  
LINK         O4  NAG E   2                 C1  BMA E   3     1555   1555  1.44  
CISPEP   1 PHE A   62    PRO A   63          0         4.51                     
CISPEP   2 ILE A  526    PRO A  527          0         1.59                     
CISPEP   3 GLY A  539    ALA A  540          0         5.39                     
CISPEP   4 GLN A  569    SER A  570          0        27.99                     
CISPEP   5 ARG A  573    GLN A  574          0         2.87                     
CISPEP   6 ARG B 1507    ASP B 1508          0        -3.26                     
CISPEP   7 LYS B 1615    PRO B 1616          0        -2.49                     
CISPEP   8 ASP C  277    PRO C  278          0        -2.04                     
CRYST1   82.830  130.630  233.830  90.00  90.00  90.00 P 21 2 21     4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012073  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007655  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004277        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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