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Entry: 4ZFO
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HEADER    IMMUNE SYSTEM                           21-APR-15   4ZFO              
TITLE     J22.9-XI: CHIMERIC MOUSE/HUMAN ANTIBODY AGAINST HUMAN BCMA (CD269)    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TUMOR NECROSIS FACTOR RECEPTOR SUPERFAMILY MEMBER 17;      
COMPND   3 CHAIN: F, K;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR (N-TERMINAL) DOMAIN, UNP RESIDUES 1-54;      
COMPND   5 SYNONYM: B-CELL MATURATION PROTEIN, BCMA, CD269;                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: J22.9-XI FAB, LIGHT CHAIN;                                 
COMPND   9 CHAIN: L;                                                            
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 OTHER_DETAILS: FAB LIGHT CHAIN FRAGMENT OF ANTI-BCMA ANTIBODY J22.9- 
COMPND  12 XI;                                                                  
COMPND  13 MOL_ID: 3;                                                           
COMPND  14 MOLECULE: J22.9-XI FAB, HEAVY CHAIN;                                 
COMPND  15 CHAIN: H, A;                                                         
COMPND  16 ENGINEERED: YES;                                                     
COMPND  17 OTHER_DETAILS: FAB HEAVY CHAIN FRAGMENT OF ANTI-BCMA ANTIBODY J22.9- 
COMPND  18 XI;                                                                  
COMPND  19 MOL_ID: 4;                                                           
COMPND  20 MOLECULE: J22.9-XI FAB, LIGHT CHAIN;                                 
COMPND  21 CHAIN: B;                                                            
COMPND  22 ENGINEERED: YES;                                                     
COMPND  23 OTHER_DETAILS: FAB LIGHT CHAIN FRAGMENT OF ANTI-BCMA ANTIBODY J22.9- 
COMPND  24 XI                                                                   
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: TNFRSF17, BCM, BCMA;                                           
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VARIANT: ROSETTA2;                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PGEX6P-1;                                 
SOURCE  12 MOL_ID: 2;                                                           
SOURCE  13 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  14 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  15 ORGANISM_TAXID: 10090;                                               
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  18 EXPRESSION_SYSTEM_CELL_LINE: HEK293_6E;                              
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PTT5;                                     
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  23 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  24 ORGANISM_TAXID: 10090;                                               
SOURCE  25 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  26 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  27 EXPRESSION_SYSTEM_CELL_LINE: HEK293_6E;                              
SOURCE  28 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  29 EXPRESSION_SYSTEM_PLASMID: PTT5;                                     
SOURCE  30 MOL_ID: 4;                                                           
SOURCE  31 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE  32 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE  33 ORGANISM_TAXID: 10090;                                               
SOURCE  34 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  35 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  36 EXPRESSION_SYSTEM_CELL_LINE: HEK293_6E;                              
SOURCE  37 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  38 EXPRESSION_SYSTEM_PLASMID: PTT5                                      
KEYWDS    ANTIBODY FAB-LIGAND COMPLEX ANTI-BCMA ANTI-TUMOR, IMMUNE SYSTEM       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.F.MARINO,O.DAUMKE,D.OLAL                                            
REVDAT   2   12-AUG-15 4ZFO    1       JRNL                                     
REVDAT   1   20-MAY-15 4ZFO    0                                                
JRNL        AUTH   F.ODEN,S.F.MARINO,J.BRAND,S.SCHEU,C.KRIEGEL,D.OLAL,          
JRNL        AUTH 2 A.TAKVORIAN,J.WESTERMANN,B.YILMAZ,M.HINZ,O.DAUMKE,           
JRNL        AUTH 3 U.E.HOPKEN,G.MULLER,M.LIPP                                   
JRNL        TITL   POTENT ANTI-TUMOR RESPONSE BY TARGETING B CELL MATURATION    
JRNL        TITL 2 ANTIGEN (BCMA) IN A MOUSE MODEL OF MULTIPLE MYELOMA.         
JRNL        REF    MOL ONCOL                     V.   9  1348 2015              
JRNL        REFN                   ISSN 1878-0261                               
JRNL        PMID   25953704                                                     
JRNL        DOI    10.1016/J.MOLONC.2015.03.010                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.9_1692                                      
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) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 87918                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.176                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4396                            
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 42.2681 -  5.8846    1.00     3021   159  0.1656 0.1558        
REMARK   3     2  5.8846 -  4.6727    1.00     2883   151  0.1359 0.1718        
REMARK   3     3  4.6727 -  4.0826    1.00     2840   150  0.1291 0.1477        
REMARK   3     4  4.0826 -  3.7096    1.00     2844   149  0.1520 0.1753        
REMARK   3     5  3.7096 -  3.4438    1.00     2820   149  0.1625 0.1921        
REMARK   3     6  3.4438 -  3.2408    1.00     2819   148  0.1717 0.2127        
REMARK   3     7  3.2408 -  3.0786    1.00     2803   148  0.1744 0.2208        
REMARK   3     8  3.0786 -  2.9446    1.00     2791   147  0.1818 0.2006        
REMARK   3     9  2.9446 -  2.8313    1.00     2804   147  0.1738 0.1989        
REMARK   3    10  2.8313 -  2.7336    1.00     2801   148  0.1851 0.2283        
REMARK   3    11  2.7336 -  2.6481    1.00     2774   146  0.1824 0.2304        
REMARK   3    12  2.6481 -  2.5724    1.00     2786   146  0.1849 0.2052        
REMARK   3    13  2.5724 -  2.5047    1.00     2751   145  0.1798 0.2259        
REMARK   3    14  2.5047 -  2.4436    1.00     2789   147  0.1815 0.2319        
REMARK   3    15  2.4436 -  2.3881    1.00     2809   148  0.1749 0.2087        
REMARK   3    16  2.3881 -  2.3373    1.00     2765   145  0.1789 0.2085        
REMARK   3    17  2.3373 -  2.2905    1.00     2762   146  0.1769 0.2018        
REMARK   3    18  2.2905 -  2.2473    1.00     2783   146  0.1877 0.2287        
REMARK   3    19  2.2473 -  2.2072    1.00     2745   145  0.1887 0.2254        
REMARK   3    20  2.2072 -  2.1698    1.00     2797   147  0.1860 0.2658        
REMARK   3    21  2.1698 -  2.1348    1.00     2763   145  0.1880 0.2683        
REMARK   3    22  2.1348 -  2.1019    1.00     2752   145  0.1893 0.2099        
REMARK   3    23  2.1019 -  2.0710    1.00     2752   145  0.1899 0.2365        
REMARK   3    24  2.0710 -  2.0418    1.00     2752   145  0.2037 0.2666        
REMARK   3    25  2.0418 -  2.0142    1.00     2789   147  0.2171 0.2426        
REMARK   3    26  2.0142 -  1.9881    1.00     2764   145  0.2144 0.2296        
REMARK   3    27  1.9881 -  1.9632    1.00     2705   143  0.2213 0.2781        
REMARK   3    28  1.9632 -  1.9396    1.00     2785   146  0.2384 0.2755        
REMARK   3    29  1.9396 -  1.9170    1.00     2765   146  0.2550 0.2882        
REMARK   3    30  1.9170 -  1.8955    0.90     2508   132  0.2951 0.3513        
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)     : 0.200            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 19.750           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 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      :  0.010           7365                                  
REMARK   3   ANGLE     :  1.202           9999                                  
REMARK   3   CHIRALITY :  0.048           1120                                  
REMARK   3   PLANARITY :  0.006           1287                                  
REMARK   3   DIHEDRAL  : 14.127           2653                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 29                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 6 THROUGH 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -56.2243   3.7372 -55.0693              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5118 T22:   0.3570                                     
REMARK   3      T33:   0.4601 T12:   0.0593                                     
REMARK   3      T13:  -0.1391 T23:   0.1843                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9061 L22:   7.3758                                     
REMARK   3      L33:   4.3184 L12:   0.7299                                     
REMARK   3      L13:  -2.0530 L23:  -5.4492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4773 S12:   0.5155 S13:   1.0882                       
REMARK   3      S21:  -0.6570 S22:   0.3325 S23:   0.1841                       
REMARK   3      S31:  -1.0118 S32:  -0.6456 S33:   0.1299                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 12 THROUGH 19 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -52.7153  -1.3948 -46.9005              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1162 T22:   0.1138                                     
REMARK   3      T33:   0.2030 T12:  -0.0252                                     
REMARK   3      T13:  -0.0428 T23:   0.0310                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5783 L22:   3.9365                                     
REMARK   3      L33:   8.7554 L12:  -2.1447                                     
REMARK   3      L13:   5.0497 L23:  -1.6898                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0917 S12:   0.2092 S13:   0.5536                       
REMARK   3      S21:  -0.1020 S22:   0.0069 S23:   0.1725                       
REMARK   3      S31:  -0.3584 S32:   0.2760 S33:   0.1629                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 20 THROUGH 27 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -52.7150  -5.4574 -54.4699              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3381 T22:   0.2010                                     
REMARK   3      T33:   0.1860 T12:  -0.0209                                     
REMARK   3      T13:  -0.0563 T23:   0.0124                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.7565 L22:   5.7378                                     
REMARK   3      L33:   8.1854 L12:   3.2538                                     
REMARK   3      L13:   2.9255 L23:   1.7449                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0312 S12:   0.5478 S13:   0.1310                       
REMARK   3      S21:  -0.5631 S22:   0.0745 S23:   0.4729                       
REMARK   3      S31:   0.8937 S32:  -0.0726 S33:   0.0077                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 28 THROUGH 34 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -58.9223 -12.6131 -54.8218              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5820 T22:   0.4625                                     
REMARK   3      T33:   0.3919 T12:  -0.2012                                     
REMARK   3      T13:  -0.1341 T23:  -0.0921                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.2272 L22:   1.2111                                     
REMARK   3      L33:   2.0873 L12:  -1.8725                                     
REMARK   3      L13:  -2.6275 L23:   0.2977                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4066 S12:   0.9402 S13:  -0.5040                       
REMARK   3      S21:  -0.9124 S22:  -0.2063 S23:   0.7922                       
REMARK   3      S31:   0.1711 S32:  -0.5060 S33:   0.5586                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN 'F' AND (RESID 35 THROUGH 41 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -60.3512  -5.4566 -59.1391              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5785 T22:   0.6360                                     
REMARK   3      T33:   0.6719 T12:  -0.1353                                     
REMARK   3      T13:  -0.3243 T23:   0.1757                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3927 L22:   2.4129                                     
REMARK   3      L33:   4.4402 L12:  -1.8328                                     
REMARK   3      L13:  -1.0956 L23:  -0.0758                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0617 S12:   1.6049 S13:   0.2216                       
REMARK   3      S21:  -1.1609 S22:   0.1491 S23:   1.3078                       
REMARK   3      S31:  -0.0001 S32:  -1.1762 S33:  -0.1347                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 32 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.4859  15.4441 -27.9193              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1219 T22:   0.1584                                     
REMARK   3      T33:   0.2575 T12:  -0.0059                                     
REMARK   3      T13:  -0.0425 T23:   0.0028                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9469 L22:   5.7450                                     
REMARK   3      L33:   1.3351 L12:  -3.5375                                     
REMARK   3      L13:  -0.7761 L23:   1.3461                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0116 S12:   0.0231 S13:   0.2534                       
REMARK   3      S21:   0.1440 S22:   0.1155 S23:  -0.7609                       
REMARK   3      S31:  -0.0418 S32:   0.1490 S33:  -0.0957                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 33 THROUGH 90 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9864  15.4461 -33.2842              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0703 T22:   0.1417                                     
REMARK   3      T33:   0.1482 T12:   0.0379                                     
REMARK   3      T13:   0.0204 T23:   0.0236                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2673 L22:   2.2058                                     
REMARK   3      L33:   1.4292 L12:   0.6144                                     
REMARK   3      L13:   0.5012 L23:   0.5234                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0126 S12:   0.0858 S13:   0.0396                       
REMARK   3      S21:   0.0799 S22:  -0.0138 S23:  -0.1042                       
REMARK   3      S31:  -0.0507 S32:  -0.0332 S33:   0.0093                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 91 THROUGH 113 )                  
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.2514  14.3784 -23.3513              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0875 T22:   0.1286                                     
REMARK   3      T33:   0.1554 T12:   0.0250                                     
REMARK   3      T13:  -0.0453 T23:   0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2508 L22:   2.4890                                     
REMARK   3      L33:   3.6908 L12:  -1.1448                                     
REMARK   3      L13:  -1.7982 L23:   2.5281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1155 S12:   0.0526 S13:   0.0244                       
REMARK   3      S21:   0.0446 S22:  -0.0323 S23:  -0.2247                       
REMARK   3      S31:  -0.1512 S32:   0.0285 S33:  -0.0722                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 114 THROUGH 150 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -12.9531  13.3502   3.4360              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1732 T22:   0.1329                                     
REMARK   3      T33:   0.0837 T12:  -0.0061                                     
REMARK   3      T13:  -0.0169 T23:  -0.0353                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7863 L22:   4.6383                                     
REMARK   3      L33:   5.3591 L12:   0.6847                                     
REMARK   3      L13:  -0.7235 L23:  -3.9460                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0613 S12:  -0.0534 S13:   0.0825                       
REMARK   3      S21:  -0.1597 S22:   0.0198 S23:   0.0621                       
REMARK   3      S31:   0.0470 S32:  -0.0494 S33:   0.0858                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 151 THROUGH 174 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -10.1416  15.1178  -4.1131              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1005 T22:   0.1780                                     
REMARK   3      T33:   0.1054 T12:  -0.0234                                     
REMARK   3      T13:   0.0062 T23:  -0.0275                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3828 L22:   3.5592                                     
REMARK   3      L33:   3.7986 L12:  -0.2876                                     
REMARK   3      L13:   0.1328 L23:  -1.8501                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1037 S12:  -0.0607 S13:   0.0060                       
REMARK   3      S21:  -0.2097 S22:  -0.0177 S23:  -0.0734                       
REMARK   3      S31:  -0.0289 S32:   0.2920 S33:  -0.0693                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN 'L' AND (RESID 175 THROUGH 214 )                 
REMARK   3    ORIGIN FOR THE GROUP (A):  -9.3549  13.5691   9.2893              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1640 T22:   0.2039                                     
REMARK   3      T33:   0.1060 T12:  -0.0281                                     
REMARK   3      T13:  -0.0206 T23:  -0.0097                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3812 L22:   4.6455                                     
REMARK   3      L33:   3.9495 L12:   1.3019                                     
REMARK   3      L13:  -0.7155 L23:  -2.6926                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0615 S12:  -0.1680 S13:   0.0386                       
REMARK   3      S21:   0.2349 S22:  -0.1527 S23:  -0.0347                       
REMARK   3      S31:  -0.2901 S32:   0.3305 S33:   0.0657                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 17 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -19.2782  -6.0886 -26.4897              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1012 T22:   0.1587                                     
REMARK   3      T33:   0.1590 T12:  -0.0355                                     
REMARK   3      T13:  -0.0051 T23:  -0.0189                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4614 L22:   3.3625                                     
REMARK   3      L33:   9.1313 L12:   0.7155                                     
REMARK   3      L13:  -0.3913 L23:  -3.5338                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0068 S12:  -0.0575 S13:   0.0033                       
REMARK   3      S21:  -0.0798 S22:   0.3070 S23:   0.3382                       
REMARK   3      S31:   0.0614 S32:  -0.6872 S33:  -0.3474                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 18 THROUGH 57 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -10.8837  -3.8028 -35.0506              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1076 T22:   0.1338                                     
REMARK   3      T33:   0.0844 T12:   0.0226                                     
REMARK   3      T13:  -0.0070 T23:  -0.0064                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3307 L22:   2.6185                                     
REMARK   3      L33:   2.1779 L12:   0.3222                                     
REMARK   3      L13:  -0.0271 L23:   0.3308                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0974 S12:   0.1139 S13:  -0.1007                       
REMARK   3      S21:   0.0159 S22:   0.0370 S23:  -0.1462                       
REMARK   3      S31:   0.3177 S32:   0.0459 S33:  -0.1391                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 58 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -7.5085 -10.8779 -33.3009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2352 T22:   0.1303                                     
REMARK   3      T33:   0.1466 T12:   0.0733                                     
REMARK   3      T13:  -0.0209 T23:  -0.0162                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6827 L22:   2.3571                                     
REMARK   3      L33:   3.4549 L12:   1.3313                                     
REMARK   3      L13:   1.2133 L23:   0.4841                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1339 S12:  -0.1650 S13:  -0.4678                       
REMARK   3      S21:   0.2034 S22:  -0.0028 S23:  -0.3398                       
REMARK   3      S31:   0.5955 S32:   0.2423 S33:  -0.1320                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 77 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -12.8900  -2.0357 -31.4705              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0743 T22:   0.1179                                     
REMARK   3      T33:   0.0881 T12:   0.0066                                     
REMARK   3      T13:  -0.0146 T23:  -0.0281                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3050 L22:   3.1320                                     
REMARK   3      L33:   3.8657 L12:   0.2328                                     
REMARK   3      L13:  -0.7372 L23:  -1.2356                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0286 S12:   0.0649 S13:  -0.0679                       
REMARK   3      S21:   0.0600 S22:  -0.0091 S23:  -0.0308                       
REMARK   3      S31:   0.1857 S32:   0.0429 S33:   0.0148                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 119 THROUGH 210 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -24.0782   9.0741  -2.6603              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1316 T22:   0.1564                                     
REMARK   3      T33:   0.1128 T12:   0.0223                                     
REMARK   3      T13:  -0.0522 T23:  -0.0182                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9583 L22:   2.9301                                     
REMARK   3      L33:   2.1612 L12:  -0.4828                                     
REMARK   3      L13:  -0.3436 L23:   0.2097                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0330 S12:  -0.0509 S13:   0.1264                       
REMARK   3      S21:  -0.0531 S22:  -0.0128 S23:   0.1673                       
REMARK   3      S31:  -0.1824 S32:  -0.1778 S33:   0.0480                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN 'H' AND (RESID 211 THROUGH 221 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -31.7328   7.8164   2.3710              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2611 T22:   0.2253                                     
REMARK   3      T33:   0.2111 T12:   0.0261                                     
REMARK   3      T13:   0.0244 T23:  -0.0378                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.7622 L22:   1.7709                                     
REMARK   3      L33:   1.8642 L12:   2.7804                                     
REMARK   3      L13:   2.9048 L23:   1.7555                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0446 S12:  -0.4183 S13:   0.6180                       
REMARK   3      S21:   0.3952 S22:  -0.5621 S23:   0.8415                       
REMARK   3      S31:   0.0913 S32:  -0.7265 S33:   0.4999                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 1 THROUGH 75 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -51.3488 -18.2294 -39.5295              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0798 T22:   0.1019                                     
REMARK   3      T33:   0.1382 T12:  -0.0033                                     
REMARK   3      T13:  -0.0443 T23:  -0.0107                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3328 L22:   2.7687                                     
REMARK   3      L33:   1.3990 L12:   0.3432                                     
REMARK   3      L13:  -0.4576 L23:  -0.1271                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0032 S12:   0.0476 S13:  -0.0455                       
REMARK   3      S21:  -0.1060 S22:  -0.0125 S23:   0.0345                       
REMARK   3      S31:   0.0575 S32:  -0.0116 S33:  -0.0018                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 76 THROUGH 113 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -48.1864 -22.2062 -34.7572              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0904 T22:   0.1235                                     
REMARK   3      T33:   0.1515 T12:  -0.0076                                     
REMARK   3      T13:  -0.0231 T23:  -0.0294                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.6452 L22:   4.2516                                     
REMARK   3      L33:   0.9862 L12:  -1.0896                                     
REMARK   3      L13:   0.4605 L23:  -1.5494                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0778 S12:   0.0804 S13:   0.0313                       
REMARK   3      S21:  -0.2883 S22:  -0.0828 S23:  -0.0458                       
REMARK   3      S31:   0.1501 S32:   0.0633 S33:   0.0122                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN 'B' AND (RESID 114 THROUGH 213 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -42.1764 -35.8016  -8.6019              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2842 T22:   0.1826                                     
REMARK   3      T33:   0.1902 T12:  -0.0608                                     
REMARK   3      T13:   0.0242 T23:   0.0161                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6309 L22:   1.5952                                     
REMARK   3      L33:   3.4509 L12:  -0.1868                                     
REMARK   3      L13:   0.6016 L23:   0.3878                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0849 S12:  -0.3281 S13:  -0.1668                       
REMARK   3      S21:   0.5134 S22:  -0.1003 S23:   0.1220                       
REMARK   3      S31:   0.0862 S32:  -0.3605 S33:   0.0039                       
REMARK   3   TLS GROUP : 21                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 1 THROUGH 57 )                    
REMARK   3    ORIGIN FOR THE GROUP (A): -40.8658  -0.6672 -30.1204              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0915 T22:   0.1163                                     
REMARK   3      T33:   0.1353 T12:  -0.0220                                     
REMARK   3      T13:   0.0026 T23:  -0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3873 L22:   1.9968                                     
REMARK   3      L33:   2.6329 L12:   0.1131                                     
REMARK   3      L13:   1.1153 L23:   0.2909                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0165 S12:   0.0542 S13:   0.1260                       
REMARK   3      S21:  -0.1469 S22:   0.0211 S23:  -0.0667                       
REMARK   3      S31:  -0.1561 S32:   0.1836 S33:   0.0110                       
REMARK   3   TLS GROUP : 22                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 58 THROUGH 76 )                   
REMARK   3    ORIGIN FOR THE GROUP (A): -46.9461   4.7836 -27.1635              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1230 T22:   0.0822                                     
REMARK   3      T33:   0.1507 T12:   0.0283                                     
REMARK   3      T13:  -0.0164 T23:  -0.0406                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.2731 L22:   6.0553                                     
REMARK   3      L33:   4.1880 L12:   2.8718                                     
REMARK   3      L13:  -1.0881 L23:  -1.0592                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2597 S12:  -0.3951 S13:   0.1999                       
REMARK   3      S21:  -0.0560 S22:  -0.0850 S23:   0.4230                       
REMARK   3      S31:  -0.0486 S32:  -0.1386 S33:   0.2842                       
REMARK   3   TLS GROUP : 23                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 77 THROUGH 118 )                  
REMARK   3    ORIGIN FOR THE GROUP (A): -41.0535  -3.3663 -30.3715              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0421 T22:   0.1144                                     
REMARK   3      T33:   0.1328 T12:  -0.0217                                     
REMARK   3      T13:   0.0163 T23:  -0.0066                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5849 L22:   1.6231                                     
REMARK   3      L33:   4.9482 L12:  -0.0594                                     
REMARK   3      L13:   0.7595 L23:  -0.3585                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0336 S12:   0.0561 S13:   0.0961                       
REMARK   3      S21:   0.0235 S22:   0.0679 S23:  -0.0007                       
REMARK   3      S31:  -0.0700 S32:   0.0265 S33:  -0.0873                       
REMARK   3   TLS GROUP : 24                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 119 THROUGH 195 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -30.8797 -27.2335 -12.3666              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1486 T22:   0.1536                                     
REMARK   3      T33:   0.1412 T12:  -0.0204                                     
REMARK   3      T13:  -0.0100 T23:  -0.0087                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9718 L22:   5.9927                                     
REMARK   3      L33:   1.1057 L12:  -1.1311                                     
REMARK   3      L13:   0.0659 L23:   1.4279                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0395 S12:   0.0280 S13:  -0.1487                       
REMARK   3      S21:   0.3806 S22:   0.0440 S23:  -0.0559                       
REMARK   3      S31:   0.1361 S32:   0.0575 S33:  -0.0269                       
REMARK   3   TLS GROUP : 25                                                     
REMARK   3    SELECTION: CHAIN 'A' AND (RESID 196 THROUGH 220 )                 
REMARK   3    ORIGIN FOR THE GROUP (A): -21.6415 -28.4105 -10.9414              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1727 T22:   0.1927                                     
REMARK   3      T33:   0.3023 T12:   0.0071                                     
REMARK   3      T13:  -0.0710 T23:  -0.0390                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8368 L22:   6.1891                                     
REMARK   3      L33:   1.5374 L12:  -0.2532                                     
REMARK   3      L13:   0.1652 L23:   1.0860                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0438 S12:   0.0241 S13:  -0.2149                       
REMARK   3      S21:   0.4547 S22:   0.0967 S23:  -1.1290                       
REMARK   3      S31:   0.1489 S32:   0.2116 S33:  -0.1221                       
REMARK   3   TLS GROUP : 26                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 7 THROUGH 11 )                    
REMARK   3    ORIGIN FOR THE GROUP (A):   2.5238   4.1083 -56.0743              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4293 T22:   0.7092                                     
REMARK   3      T33:   0.4426 T12:   0.1758                                     
REMARK   3      T13:   0.1818 T23:  -0.0098                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0483 L22:   3.7112                                     
REMARK   3      L33:   4.0537 L12:   1.6777                                     
REMARK   3      L13:   2.2934 L23:   3.7419                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4262 S12:   0.2617 S13:  -0.8915                       
REMARK   3      S21:  -1.2836 S22:  -0.4353 S23:  -0.2334                       
REMARK   3      S31:   0.3066 S32:   0.1455 S33:   0.8028                       
REMARK   3   TLS GROUP : 27                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 12 THROUGH 27 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):  -0.6759   7.4965 -48.6769              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2119 T22:   0.3444                                     
REMARK   3      T33:   0.2025 T12:   0.0386                                     
REMARK   3      T13:   0.0544 T23:   0.0317                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.1148 L22:   5.0815                                     
REMARK   3      L33:   9.6503 L12:   2.3189                                     
REMARK   3      L13:  -1.4775 L23:  -0.0921                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0430 S12:   0.7677 S13:   0.2841                       
REMARK   3      S21:  -0.6633 S22:   0.0738 S23:  -0.3844                       
REMARK   3      S31:   0.0677 S32:   0.5531 S33:   0.0606                       
REMARK   3   TLS GROUP : 28                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 28 THROUGH 34 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   5.8074  17.7762 -47.5200              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7309 T22:   0.6696                                     
REMARK   3      T33:   0.6883 T12:  -0.0951                                     
REMARK   3      T13:   0.0827 T23:   0.2788                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7928 L22:   2.5480                                     
REMARK   3      L33:   3.1150 L12:  -2.6653                                     
REMARK   3      L13:   2.9495 L23:  -2.8149                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4103 S12:   0.3627 S13:   0.1776                       
REMARK   3      S21:  -0.5263 S22:  -0.1545 S23:  -0.5655                       
REMARK   3      S31:  -0.4285 S32:   0.4666 S33:   0.5402                       
REMARK   3   TLS GROUP : 29                                                     
REMARK   3    SELECTION: CHAIN 'K' AND (RESID 35 THROUGH 41 )                   
REMARK   3    ORIGIN FOR THE GROUP (A):   7.3702  13.6122 -54.8035              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6662 T22:   1.1589                                     
REMARK   3      T33:   0.7755 T12:  -0.0696                                     
REMARK   3      T13:   0.2380 T23:   0.0802                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.1614 L22:   3.0805                                     
REMARK   3      L33:   3.8436 L12:  -2.0292                                     
REMARK   3      L13:   0.6996 L23:   0.1970                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2466 S12:   2.2934 S13:   0.9765                       
REMARK   3      S21:  -1.7049 S22:   0.4630 S23:  -1.2034                       
REMARK   3      S31:  -0.2235 S32:   1.3123 S33:  -0.1977                       
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 4ZFO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 21-APR-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000208798.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-JUL-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JULY 4, 2012                   
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 87925                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.895                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.268                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.18000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.4600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.01                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.30                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER CCP4INTERFACE 2.1.0                            
REMARK 200 STARTING MODEL: 3EO9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1 MICROLITER OF THE COMPLEX AT 8 MG/ML   
REMARK 280  WITH 2 MICROLITERS OF 21% PEG 3350, 0.1 M BISTRIS PH 6.5 AND 5      
REMARK 280  MM CUCL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293.15K        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       36.40050            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.63950            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       55.06950            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.63950            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       36.40050            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       55.06950            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20980 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -44.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, B, A                               
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5160 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21290 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -45.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: L, H, K                               
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     MET F     1                                                      
REMARK 465     LEU F     2                                                      
REMARK 465     GLN F     3                                                      
REMARK 465     MET F     4                                                      
REMARK 465     ALA F     5                                                      
REMARK 465     ASN F    42                                                      
REMARK 465     ALA F    43                                                      
REMARK 465     SER F    44                                                      
REMARK 465     VAL F    45                                                      
REMARK 465     THR F    46                                                      
REMARK 465     ASN F    47                                                      
REMARK 465     SER F    48                                                      
REMARK 465     VAL F    49                                                      
REMARK 465     LYS F    50                                                      
REMARK 465     GLY F    51                                                      
REMARK 465     THR F    52                                                      
REMARK 465     ASN F    53                                                      
REMARK 465     ALA F    54                                                      
REMARK 465     LYS H   136                                                      
REMARK 465     SER H   137                                                      
REMARK 465     THR H   138                                                      
REMARK 465     SER H   139                                                      
REMARK 465     GLY H   140                                                      
REMARK 465     SER A   134                                                      
REMARK 465     SER A   135                                                      
REMARK 465     LYS A   136                                                      
REMARK 465     SER A   137                                                      
REMARK 465     THR A   138                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     MET K     1                                                      
REMARK 465     LEU K     2                                                      
REMARK 465     GLN K     3                                                      
REMARK 465     MET K     4                                                      
REMARK 465     ALA K     5                                                      
REMARK 465     GLY K     6                                                      
REMARK 465     ASN K    42                                                      
REMARK 465     ALA K    43                                                      
REMARK 465     SER K    44                                                      
REMARK 465     VAL K    45                                                      
REMARK 465     THR K    46                                                      
REMARK 465     ASN K    47                                                      
REMARK 465     SER K    48                                                      
REMARK 465     VAL K    49                                                      
REMARK 465     LYS K    50                                                      
REMARK 465     GLY K    51                                                      
REMARK 465     THR K    52                                                      
REMARK 465     ASN K    53                                                      
REMARK 465     ALA K    54                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLN F  10    CG   CD   OE1  NE2                                  
REMARK 470     ASN F  31    CG   OD1  ND2                                       
REMARK 470     LEU F  35    CG   CD1  CD2                                       
REMARK 470     GLN F  38    CG   CD   OE1  NE2                                  
REMARK 470     ARG F  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K  10    CG   CD   OE1  NE2                                  
REMARK 470     ASN K  31    CG   OD1  ND2                                       
REMARK 470     LEU K  35    CG   CD1  CD2                                       
REMARK 470     GLN K  38    CG   CD   OE1  NE2                                  
REMARK 470     ARG K  39    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   320     O    HOH A   451              2.09            
REMARK 500   O1   BTB B   302     O    HOH B   401              2.13            
REMARK 500   OD1  ASP H   105     O    HOH H   301              2.16            
REMARK 500   O    HOH H   441     O    HOH H   478              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP L  30     -128.07     56.27                                   
REMARK 500    ALA L  51      -34.75     69.37                                   
REMARK 500    ALA L  84     -176.13   -171.65                                   
REMARK 500    ASN L 152        9.06     57.48                                   
REMARK 500    ASP B  30     -125.45     46.87                                   
REMARK 500    ALA B  51      -33.84     68.88                                   
REMARK 500    ALA B  84     -172.38   -171.46                                   
REMARK 500    ASN K  31       -9.67     75.21                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP L   1   N                                                      
REMARK 620 2 ASP L   1   OD1  89.8                                              
REMARK 620 3 ASP B   1   N    94.8   5.5                                        
REMARK 620 4 ASP B   1   OD1  93.3   3.9   1.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU L 302  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 189   NE2                                                    
REMARK 620 2 BTB L 303   O4  109.4                                              
REMARK 620 3 BTB L 303   N   162.2  88.3                                        
REMARK 620 4 BTB L 303   O6   87.2 145.6  79.0                                  
REMARK 620 5 BTB L 303   O8   96.4  91.5  80.2 117.1                            
REMARK 620 6 BTB L 303   O3   99.7  77.8  86.1  69.6 163.0                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CU B 301  CU                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B 189   NE2                                                    
REMARK 620 2 BTB B 302   O3  101.4                                              
REMARK 620 3 BTB B 302   N   157.1  84.1                                        
REMARK 620 4 BTB B 302   O6   83.2  87.0  74.9                                  
REMARK 620 5 BTB B 302   O8  102.6 154.7  76.8 103.6                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU L 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU L 302                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB L 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CU B 301                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue BTB B 302                 
DBREF  4ZFO F    1    54  UNP    Q02223   TNR17_HUMAN      1     54             
DBREF  4ZFO L    1   214  PDB    4ZFO     4ZFO             1    214             
DBREF  4ZFO H    1   221  PDB    4ZFO     4ZFO             1    221             
DBREF  4ZFO B    1   213  PDB    4ZFO     4ZFO             1    213             
DBREF  4ZFO A    1   221  PDB    4ZFO     4ZFO             1    221             
DBREF  4ZFO K    1    54  UNP    Q02223   TNR17_HUMAN      1     54             
SEQRES   1 F   54  MET LEU GLN MET ALA GLY GLN CYS SER GLN ASN GLU TYR          
SEQRES   2 F   54  PHE ASP SER LEU LEU HIS ALA CYS ILE PRO CYS GLN LEU          
SEQRES   3 F   54  ARG CYS SER SER ASN THR PRO PRO LEU THR CYS GLN ARG          
SEQRES   4 F   54  TYR CYS ASN ALA SER VAL THR ASN SER VAL LYS GLY THR          
SEQRES   5 F   54  ASN ALA                                                      
SEQRES   1 L  214  ASP ILE VAL MET THR GLN SER GLN ARG PHE MET THR THR          
SEQRES   2 L  214  SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS ALA SER          
SEQRES   3 L  214  GLN SER VAL ASP SER ASN VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  214  PRO ARG GLN SER PRO LYS ALA LEU ILE PHE SER ALA SER          
SEQRES   5 L  214  LEU ARG PHE SER GLY VAL PRO ALA ARG PHE THR GLY SER          
SEQRES   6 L  214  GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN LEU          
SEQRES   7 L  214  GLN SER GLU ASP LEU ALA GLU TYR PHE CYS GLN GLN TYR          
SEQRES   8 L  214  ASN ASN TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU          
SEQRES   9 L  214  GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 L  214  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 L  214  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 L  214  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 L  214  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 L  214  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 L  214  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 L  214  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 L  214  PHE ASN ARG GLY GLU ALA                                      
SEQRES   1 H  221  GLN VAL GLN LEU GLN GLN SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 H  221  PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 H  221  ILE ASP PHE SER ARG TYR TRP MET SER TRP VAL ARG ARG          
SEQRES   4 H  221  ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN          
SEQRES   5 H  221  PRO ASP SER SER THR ILE ASN TYR ALA PRO SER LEU LYS          
SEQRES   6 H  221  ASP LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASN THR          
SEQRES   7 H  221  LEU TYR LEU GLN MET SER LYS VAL ARG SER GLU ASP THR          
SEQRES   8 H  221  ALA LEU TYR TYR CYS ALA SER LEU TYR TYR ASP TYR GLY          
SEQRES   9 H  221  ASP ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 H  221  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 H  221  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 H  221  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 H  221  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 H  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 H  221  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 H  221  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 H  221  PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO ALA          
SEQRES   1 B  213  ASP ILE VAL MET THR GLN SER GLN ARG PHE MET THR THR          
SEQRES   2 B  213  SER VAL GLY ASP ARG VAL SER VAL THR CYS LYS ALA SER          
SEQRES   3 B  213  GLN SER VAL ASP SER ASN VAL ALA TRP TYR GLN GLN LYS          
SEQRES   4 B  213  PRO ARG GLN SER PRO LYS ALA LEU ILE PHE SER ALA SER          
SEQRES   5 B  213  LEU ARG PHE SER GLY VAL PRO ALA ARG PHE THR GLY SER          
SEQRES   6 B  213  GLY SER GLY THR ASP PHE THR LEU THR ILE SER ASN LEU          
SEQRES   7 B  213  GLN SER GLU ASP LEU ALA GLU TYR PHE CYS GLN GLN TYR          
SEQRES   8 B  213  ASN ASN TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU          
SEQRES   9 B  213  GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE          
SEQRES  10 B  213  PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA          
SEQRES  11 B  213  SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU          
SEQRES  12 B  213  ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER          
SEQRES  13 B  213  GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS          
SEQRES  14 B  213  ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER          
SEQRES  15 B  213  LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU          
SEQRES  16 B  213  VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER          
SEQRES  17 B  213  PHE ASN ARG GLY GLU                                          
SEQRES   1 A  221  GLN VAL GLN LEU GLN GLN SER GLY GLY GLY LEU VAL GLN          
SEQRES   2 A  221  PRO GLY GLY SER LEU LYS LEU SER CYS ALA ALA SER GLY          
SEQRES   3 A  221  ILE ASP PHE SER ARG TYR TRP MET SER TRP VAL ARG ARG          
SEQRES   4 A  221  ALA PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASN          
SEQRES   5 A  221  PRO ASP SER SER THR ILE ASN TYR ALA PRO SER LEU LYS          
SEQRES   6 A  221  ASP LYS PHE ILE ILE SER ARG ASP ASN ALA LYS ASN THR          
SEQRES   7 A  221  LEU TYR LEU GLN MET SER LYS VAL ARG SER GLU ASP THR          
SEQRES   8 A  221  ALA LEU TYR TYR CYS ALA SER LEU TYR TYR ASP TYR GLY          
SEQRES   9 A  221  ASP ALA MET ASP TYR TRP GLY GLN GLY THR SER VAL THR          
SEQRES  10 A  221  VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO          
SEQRES  11 A  221  LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA          
SEQRES  12 A  221  ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO          
SEQRES  13 A  221  VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY          
SEQRES  14 A  221  VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU          
SEQRES  15 A  221  TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER          
SEQRES  16 A  221  LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS          
SEQRES  17 A  221  PRO SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO ALA          
SEQRES   1 K   54  MET LEU GLN MET ALA GLY GLN CYS SER GLN ASN GLU TYR          
SEQRES   2 K   54  PHE ASP SER LEU LEU HIS ALA CYS ILE PRO CYS GLN LEU          
SEQRES   3 K   54  ARG CYS SER SER ASN THR PRO PRO LEU THR CYS GLN ARG          
SEQRES   4 K   54  TYR CYS ASN ALA SER VAL THR ASN SER VAL LYS GLY THR          
SEQRES   5 K   54  ASN ALA                                                      
HET     CU  L 301       1                                                       
HET     CU  L 302       1                                                       
HET    BTB  L 303      14                                                       
HET     CU  B 301       1                                                       
HET    BTB  B 302      14                                                       
HETNAM      CU COPPER (II) ION                                                  
HETNAM     BTB 2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-                 
HETNAM   2 BTB  PROPANE-1,3-DIOL                                                
HETSYN     BTB BIS-TRIS BUFFER                                                  
FORMUL   7   CU    3(CU 2+)                                                     
FORMUL   9  BTB    2(C8 H19 N O5)                                               
FORMUL  12  HOH   *769(H2 O)                                                    
HELIX    1 AA1 GLN F   25  CYS F   28  5                                   4    
HELIX    2 AA2 PRO F   34  GLN F   38  5                                   5    
HELIX    3 AA3 GLN L   79  LEU L   83  5                                   5    
HELIX    4 AA4 SER L  121  LYS L  126  1                                   6    
HELIX    5 AA5 LYS L  183  GLU L  187  1                                   5    
HELIX    6 AA6 ASN H   74  LYS H   76  5                                   3    
HELIX    7 AA7 ARG H   87  THR H   91  5                                   5    
HELIX    8 AA8 SER H  163  ALA H  165  5                                   3    
HELIX    9 AA9 SER H  194  LEU H  196  5                                   3    
HELIX   10 AB1 LYS H  208  ASN H  211  5                                   4    
HELIX   11 AB2 GLN B   79  LEU B   83  5                                   5    
HELIX   12 AB3 SER B  121  SER B  127  1                                   7    
HELIX   13 AB4 LYS B  183  GLU B  187  1                                   5    
HELIX   14 AB5 ASP A   28  TYR A   32  5                                   5    
HELIX   15 AB6 PRO A   62  LYS A   65  5                                   4    
HELIX   16 AB7 ASN A   74  LYS A   76  5                                   3    
HELIX   17 AB8 ARG A   87  THR A   91  5                                   5    
HELIX   18 AB9 SER A  163  ALA A  165  5                                   3    
HELIX   19 AC1 SER A  194  LEU A  196  5                                   3    
HELIX   20 AC2 LYS A  208  ASN A  211  5                                   4    
HELIX   21 AC3 GLN K   25  CYS K   28  5                                   4    
HELIX   22 AC4 PRO K   34  GLN K   38  5                                   5    
SHEET    1 AA1 2 GLU F  12  ASP F  15  0                                        
SHEET    2 AA1 2 ALA F  20  PRO F  23 -1  O  ILE F  22   N  TYR F  13           
SHEET    1 AA2 4 MET L   4  THR L   5  0                                        
SHEET    2 AA2 4 VAL L  19  ALA L  25 -1  O  LYS L  24   N  THR L   5           
SHEET    3 AA2 4 ASP L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    4 AA2 4 PHE L  62  SER L  65 -1  N  THR L  63   O  THR L  74           
SHEET    1 AA3 6 PHE L  10  THR L  13  0                                        
SHEET    2 AA3 6 THR L 102  LEU L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3 AA3 6 GLU L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AA3 6 VAL L  33  GLN L  38 -1  N  GLN L  38   O  GLU L  85           
SHEET    5 AA3 6 LYS L  45  PHE L  49 -1  O  LEU L  47   N  TRP L  35           
SHEET    6 AA3 6 LEU L  53  ARG L  54 -1  O  LEU L  53   N  PHE L  49           
SHEET    1 AA4 4 PHE L  10  THR L  13  0                                        
SHEET    2 AA4 4 THR L 102  LEU L 106  1  O  LYS L 103   N  MET L  11           
SHEET    3 AA4 4 GLU L  85  GLN L  90 -1  N  TYR L  86   O  THR L 102           
SHEET    4 AA4 4 THR L  97  PHE L  98 -1  O  THR L  97   N  GLN L  90           
SHEET    1 AA5 4 SER L 114  PHE L 118  0                                        
SHEET    2 AA5 4 THR L 129  PHE L 139 -1  O  ASN L 137   N  SER L 114           
SHEET    3 AA5 4 TYR L 173  SER L 182 -1  O  LEU L 175   N  LEU L 136           
SHEET    4 AA5 4 SER L 159  VAL L 163 -1  N  GLN L 160   O  THR L 178           
SHEET    1 AA6 4 ALA L 153  LEU L 154  0                                        
SHEET    2 AA6 4 LYS L 145  VAL L 150 -1  N  VAL L 150   O  ALA L 153           
SHEET    3 AA6 4 VAL L 191  THR L 197 -1  O  GLU L 195   N  GLN L 147           
SHEET    4 AA6 4 VAL L 205  ASN L 210 -1  O  VAL L 205   N  VAL L 196           
SHEET    1 AA7 4 GLN H   3  SER H   7  0                                        
SHEET    2 AA7 4 LEU H  18  SER H  25 -1  O  ALA H  23   N  GLN H   5           
SHEET    3 AA7 4 THR H  78  MET H  83 -1  O  MET H  83   N  LEU H  18           
SHEET    4 AA7 4 PHE H  68  ASP H  73 -1  N  ASP H  73   O  THR H  78           
SHEET    1 AA8 6 GLY H  10  VAL H  12  0                                        
SHEET    2 AA8 6 THR H 114  VAL H 118  1  O  SER H 115   N  GLY H  10           
SHEET    3 AA8 6 ALA H  92  ASP H 102 -1  N  TYR H  94   O  THR H 114           
SHEET    4 AA8 6 MET H  34  ARG H  39 -1  N  VAL H  37   O  TYR H  95           
SHEET    5 AA8 6 LEU H  45  ILE H  51 -1  O  GLY H  49   N  TRP H  36           
SHEET    6 AA8 6 ILE H  58  TYR H  60 -1  O  ASN H  59   N  GLU H  50           
SHEET    1 AA9 4 GLY H  10  VAL H  12  0                                        
SHEET    2 AA9 4 THR H 114  VAL H 118  1  O  SER H 115   N  GLY H  10           
SHEET    3 AA9 4 ALA H  92  ASP H 102 -1  N  TYR H  94   O  THR H 114           
SHEET    4 AA9 4 ASP H 105  TRP H 110 -1  O  MET H 107   N  TYR H 100           
SHEET    1 AB1 4 SER H 127  LEU H 131  0                                        
SHEET    2 AB1 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3 AB1 4 TYR H 183  PRO H 192 -1  O  LEU H 185   N  VAL H 149           
SHEET    4 AB1 4 VAL H 170  THR H 172 -1  N  HIS H 171   O  VAL H 188           
SHEET    1 AB2 4 SER H 127  LEU H 131  0                                        
SHEET    2 AB2 4 THR H 142  TYR H 152 -1  O  GLY H 146   N  LEU H 131           
SHEET    3 AB2 4 TYR H 183  PRO H 192 -1  O  LEU H 185   N  VAL H 149           
SHEET    4 AB2 4 VAL H 176  LEU H 177 -1  N  VAL H 176   O  SER H 184           
SHEET    1 AB3 3 THR H 158  TRP H 161  0                                        
SHEET    2 AB3 3 ILE H 202  HIS H 207 -1  O  ASN H 204   N  SER H 160           
SHEET    3 AB3 3 THR H 212  ARG H 217 -1  O  VAL H 214   N  VAL H 205           
SHEET    1 AB4 4 MET B   4  THR B   5  0                                        
SHEET    2 AB4 4 VAL B  19  ALA B  25 -1  O  LYS B  24   N  THR B   5           
SHEET    3 AB4 4 ASP B  70  ILE B  75 -1  O  LEU B  73   N  VAL B  21           
SHEET    4 AB4 4 PHE B  62  GLY B  66 -1  N  THR B  63   O  THR B  74           
SHEET    1 AB5 6 PHE B  10  THR B  13  0                                        
SHEET    2 AB5 6 THR B 102  LEU B 106  1  O  GLU B 105   N  THR B  13           
SHEET    3 AB5 6 GLU B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4 AB5 6 VAL B  33  GLN B  38 -1  N  GLN B  38   O  GLU B  85           
SHEET    5 AB5 6 LYS B  45  PHE B  49 -1  O  LEU B  47   N  TRP B  35           
SHEET    6 AB5 6 LEU B  53  ARG B  54 -1  O  LEU B  53   N  PHE B  49           
SHEET    1 AB6 4 PHE B  10  THR B  13  0                                        
SHEET    2 AB6 4 THR B 102  LEU B 106  1  O  GLU B 105   N  THR B  13           
SHEET    3 AB6 4 GLU B  85  GLN B  90 -1  N  TYR B  86   O  THR B 102           
SHEET    4 AB6 4 THR B  97  PHE B  98 -1  O  THR B  97   N  GLN B  90           
SHEET    1 AB7 4 SER B 114  PHE B 118  0                                        
SHEET    2 AB7 4 THR B 129  PHE B 139 -1  O  LEU B 135   N  PHE B 116           
SHEET    3 AB7 4 TYR B 173  SER B 182 -1  O  LEU B 181   N  ALA B 130           
SHEET    4 AB7 4 SER B 159  VAL B 163 -1  N  GLN B 160   O  THR B 178           
SHEET    1 AB8 4 ALA B 153  LEU B 154  0                                        
SHEET    2 AB8 4 LYS B 145  VAL B 150 -1  N  VAL B 150   O  ALA B 153           
SHEET    3 AB8 4 VAL B 191  THR B 197 -1  O  GLU B 195   N  GLN B 147           
SHEET    4 AB8 4 VAL B 205  ASN B 210 -1  O  VAL B 205   N  VAL B 196           
SHEET    1 AB9 4 GLN A   3  SER A   7  0                                        
SHEET    2 AB9 4 LEU A  18  SER A  25 -1  O  ALA A  23   N  GLN A   5           
SHEET    3 AB9 4 THR A  78  MET A  83 -1  O  MET A  83   N  LEU A  18           
SHEET    4 AB9 4 PHE A  68  ASP A  73 -1  N  SER A  71   O  TYR A  80           
SHEET    1 AC1 6 GLY A  10  VAL A  12  0                                        
SHEET    2 AC1 6 THR A 114  VAL A 118  1  O  SER A 115   N  GLY A  10           
SHEET    3 AC1 6 ALA A  92  ASP A 102 -1  N  TYR A  94   O  THR A 114           
SHEET    4 AC1 6 MET A  34  ARG A  39 -1  N  VAL A  37   O  TYR A  95           
SHEET    5 AC1 6 LEU A  45  ILE A  51 -1  O  GLU A  46   N  ARG A  38           
SHEET    6 AC1 6 ILE A  58  TYR A  60 -1  O  ASN A  59   N  GLU A  50           
SHEET    1 AC2 4 GLY A  10  VAL A  12  0                                        
SHEET    2 AC2 4 THR A 114  VAL A 118  1  O  SER A 115   N  GLY A  10           
SHEET    3 AC2 4 ALA A  92  ASP A 102 -1  N  TYR A  94   O  THR A 114           
SHEET    4 AC2 4 ASP A 105  TRP A 110 -1  O  MET A 107   N  TYR A 100           
SHEET    1 AC3 4 SER A 127  LEU A 131  0                                        
SHEET    2 AC3 4 THR A 142  TYR A 152 -1  O  LYS A 150   N  SER A 127           
SHEET    3 AC3 4 TYR A 183  PRO A 192 -1  O  LEU A 185   N  VAL A 149           
SHEET    4 AC3 4 VAL A 170  THR A 172 -1  N  HIS A 171   O  VAL A 188           
SHEET    1 AC4 4 SER A 127  LEU A 131  0                                        
SHEET    2 AC4 4 THR A 142  TYR A 152 -1  O  LYS A 150   N  SER A 127           
SHEET    3 AC4 4 TYR A 183  PRO A 192 -1  O  LEU A 185   N  VAL A 149           
SHEET    4 AC4 4 VAL A 176  LEU A 177 -1  N  VAL A 176   O  SER A 184           
SHEET    1 AC5 3 THR A 158  TRP A 161  0                                        
SHEET    2 AC5 3 ILE A 202  HIS A 207 -1  O  ASN A 204   N  SER A 160           
SHEET    3 AC5 3 THR A 212  ARG A 217 -1  O  VAL A 214   N  VAL A 205           
SHEET    1 AC6 2 GLU K  12  ASP K  15  0                                        
SHEET    2 AC6 2 ALA K  20  PRO K  23 -1  O  ILE K  22   N  TYR K  13           
SSBOND   1 CYS F    8    CYS F   21                          1555   1555  2.05  
SSBOND   2 CYS F   24    CYS F   37                          1555   1555  2.03  
SSBOND   3 CYS F   28    CYS F   41                          1555   1555  2.04  
SSBOND   4 CYS L   23    CYS L   88                          1555   1555  2.05  
SSBOND   5 CYS L  134    CYS L  194                          1555   1555  2.01  
SSBOND   6 CYS H   22    CYS H   96                          1555   1555  2.06  
SSBOND   7 CYS H  147    CYS H  203                          1555   1555  2.04  
SSBOND   8 CYS B   23    CYS B   88                          1555   1555  2.05  
SSBOND   9 CYS B  134    CYS B  194                          1555   1555  2.02  
SSBOND  10 CYS A   22    CYS A   96                          1555   1555  2.09  
SSBOND  11 CYS A  147    CYS A  203                          1555   1555  2.03  
SSBOND  12 CYS K    8    CYS K   21                          1555   1555  2.03  
SSBOND  13 CYS K   24    CYS K   37                          1555   1555  2.04  
SSBOND  14 CYS K   28    CYS K   41                          1555   1555  2.04  
LINK         N   ASP L   1                CU    CU L 301     1555   1555  1.98  
LINK         OD1 ASP L   1                CU    CU L 301     1555   1555  2.05  
LINK         NE2 HIS L 189                CU    CU L 302     1555   1555  1.95  
LINK         NE2 HIS B 189                CU    CU B 301     1555   1555  2.09  
LINK        CU    CU L 302                 O4  BTB L 303     1555   1555  1.94  
LINK        CU    CU L 302                 N   BTB L 303     1555   1555  2.03  
LINK        CU    CU L 302                 O6  BTB L 303     1555   1555  2.20  
LINK        CU    CU L 302                 O8  BTB L 303     1555   1555  2.30  
LINK        CU    CU L 302                 O3  BTB L 303     1555   1555  2.16  
LINK        CU    CU B 301                 O3  BTB B 302     1555   1555  2.24  
LINK        CU    CU B 301                 N   BTB B 302     1555   1555  2.00  
LINK        CU    CU B 301                 O6  BTB B 302     1555   1555  2.44  
LINK        CU    CU B 301                 O8  BTB B 302     1555   1555  2.28  
LINK         N   ASP B   1                CU    CU L 301     1555   1455  1.98  
LINK         OD1 ASP B   1                CU    CU L 301     1555   1455  2.29  
CISPEP   1 TYR L   94    PRO L   95          0         1.06                     
CISPEP   2 TYR L  140    PRO L  141          0         3.48                     
CISPEP   3 PHE H  153    PRO H  154          0        -8.54                     
CISPEP   4 GLU H  155    PRO H  156          0        -1.55                     
CISPEP   5 TYR B   94    PRO B   95          0        -0.68                     
CISPEP   6 TYR B  140    PRO B  141          0         3.72                     
CISPEP   7 PHE A  153    PRO A  154          0        -6.99                     
CISPEP   8 GLU A  155    PRO A  156          0         0.51                     
SITE     1 AC1  4 ASP B   1  HOH B 553  ASP L   1  HOH L 563                    
SITE     1 AC2  2 HIS L 189  BTB L 303                                          
SITE     1 AC3  5 TYR A 103  ASP L 185  HIS L 189   CU L 302                    
SITE     2 AC3  5 HOH L 461                                                     
SITE     1 AC4  2 HIS B 189  BTB B 302                                          
SITE     1 AC5  8 LYS A 213  VAL A 214  ASP A 215  ASP B 185                    
SITE     2 AC5  8 LYS B 188  HIS B 189   CU B 301  HOH B 401                    
CRYST1   72.801  110.139  137.279  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.013736  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009079  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007284        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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