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Database: PDB
Entry: 4ORH
LinkDB: 4ORH
Original site: 4ORH 
HEADER    PROTEIN BINDING/LIGASE                  11-FEB-14   4ORH              
TITLE     CRYSTAL STRUCTURE OF RNF8 BOUND TO THE UBC13/MMS2 HETERODIMER         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 VARIANT 2;                 
COMPND   3 CHAIN: A, E, I;                                                      
COMPND   4 SYNONYM: DDVIT 1, ENTEROCYTE DIFFERENTIATION-ASSOCIATED FACTOR 1,    
COMPND   5 EDAF-1, ENTEROCYTE DIFFERENTIATION-PROMOTING FACTOR 1, EDPF-1, MMS2  
COMPND   6 HOMOLOG, VITAMIN D3-INDUCIBLE PROTEIN;                               
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: UBIQUITIN-CONJUGATING ENZYME E2 N;                         
COMPND  10 CHAIN: B, F, J;                                                      
COMPND  11 SYNONYM: BENDLESS-LIKE UBIQUITIN-CONJUGATING ENZYME, UBC13, UBCH13,  
COMPND  12 UBIQUITIN CARRIER PROTEIN N, UBIQUITIN-PROTEIN LIGASE N;             
COMPND  13 EC: 6.3.2.19;                                                        
COMPND  14 ENGINEERED: YES;                                                     
COMPND  15 MOL_ID: 3;                                                           
COMPND  16 MOLECULE: E3 UBIQUITIN-PROTEIN LIGASE RNF8;                          
COMPND  17 CHAIN: C, G, H, K, L;                                                
COMPND  18 SYNONYM: HRNF8, RING FINGER PROTEIN 8;                               
COMPND  19 EC: 6.3.2.-;                                                         
COMPND  20 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MMS2, UBE2V2, UEV2;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 GENE: UBE2N, BLU;                                                    
SOURCE  16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  18 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;                                 
SOURCE  19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  20 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1;                                
SOURCE  21 MOL_ID: 3;                                                           
SOURCE  22 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  23 ORGANISM_COMMON: HUMAN;                                              
SOURCE  24 ORGANISM_TAXID: 9606;                                                
SOURCE  25 GENE: RNF8, KIAA0646;                                                
SOURCE  26 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  27 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE  28 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;                                 
SOURCE  29 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  30 EXPRESSION_SYSTEM_PLASMID: PGEX-6P-1                                 
KEYWDS    COILED-COIL, E3 UBIQUITIN LIGASE, UBIQUITIN, PROTEIN BINDING-LIGASE,  
KEYWDS   2 PROTEIN BINDING-LIGASE COMPLEX                                       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.CAMPBELL,R.A.EDWARDS,J.N.M.GLOVER                                 
REVDAT   4   22-NOV-17 4ORH    1       REMARK                                   
REVDAT   3   03-DEC-14 4ORH    1       AUTHOR                                   
REVDAT   2   05-NOV-14 4ORH    1       AUTHOR                                   
REVDAT   1   26-FEB-14 4ORH    0                                                
SPRSDE     26-FEB-14 4ORH      4EPO                                             
JRNL        AUTH   S.J.CAMPBELL,R.A.EDWARDS,C.C.LEUNG,D.NECULAI,C.D.HODGE,      
JRNL        AUTH 2 S.DHE-PAGANON,J.N.GLOVER                                     
JRNL        TITL   MOLECULAR INSIGHTS INTO THE FUNCTION OF RING FINGER          
JRNL        TITL 2 (RNF)-CONTAINING PROTEINS HRNF8 AND HRNF168 IN               
JRNL        TITL 3 UBC13/MMS2-DEPENDENT UBIQUITYLATION.                         
JRNL        REF    J.BIOL.CHEM.                  V. 287 23900 2012              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   22589545                                                     
JRNL        DOI    10.1074/JBC.M112.359653                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.3_1479                                    
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) : 4.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 123.54                         
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.910                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 45858                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.277                           
REMARK   3   R VALUE            (WORKING SET) : 0.276                           
REMARK   3   FREE R VALUE                     : 0.282                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1258                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1123.5808 - 12.3430    0.99     2618   119  0.2357 0.2137        
REMARK   3     2 12.3430 -  9.7983    0.99     2595   146  0.1822 0.1893        
REMARK   3     3  9.7983 -  8.5601    1.00     2615   144  0.2318 0.2340        
REMARK   3     4  8.5601 -  7.7776    1.00     2615   151  0.2536 0.2607        
REMARK   3     5  7.7776 -  7.2202    1.00     2665   108  0.2787 0.2956        
REMARK   3     6  7.2202 -  6.7945    1.00     2618   124  0.3013 0.3661        
REMARK   3     7  6.7945 -  6.4543    0.99     2594   124  0.3269 0.3760        
REMARK   3     8  6.4543 -  6.1733    0.96     2515   176  0.3564 0.3533        
REMARK   3     9  6.1733 -  5.9357    0.97     2543   114  0.3426 0.3246        
REMARK   3    10  5.9357 -  5.7308    0.97     2546   118  0.3412 0.3312        
REMARK   3    11  5.7308 -  5.5517    0.97     2515   180  0.3396 0.3623        
REMARK   3    12  5.5517 -  5.3930    0.97     2525   131  0.3470 0.3622        
REMARK   3    13  5.3930 -  5.2510    0.97     2553   146  0.3610 0.3694        
REMARK   3    14  5.2510 -  5.1229    0.97     2536   147  0.3544 0.3796        
REMARK   3    15  5.1229 -  5.0064    0.97     2532   143  0.3540 0.3101        
REMARK   3    16  5.0064 -  4.8999    0.97     2566   129  0.3572 0.3652        
REMARK   3    17  4.8999 -  4.8018    0.92     2377   130  0.3549 0.3655        
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)     : 0.740            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 175.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 258.4                          
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      :  0.007          11728                                  
REMARK   3   ANGLE     :  1.091          15931                                  
REMARK   3   CHIRALITY :  0.058           1817                                  
REMARK   3   PLANARITY :  0.004           2084                                  
REMARK   3   DIHEDRAL  : 12.361           4352                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 11                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 6 THROUGH 144)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  46.8753  33.1482  17.3940              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9041 T22:   2.7651                                     
REMARK   3      T33:   2.4334 T12:   0.0882                                     
REMARK   3      T13:  -0.4148 T23:  -0.0882                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.8025 L22:  10.4676                                     
REMARK   3      L33:   7.2046 L12:   1.5215                                     
REMARK   3      L13:  -1.0968 L23:  -5.9856                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4646 S12:  -0.1035 S13:   0.5232                       
REMARK   3      S21:  -0.6378 S22:  -0.1910 S23:  -0.3261                       
REMARK   3      S31:  -0.7873 S32:  -0.1020 S33:  -0.0009                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 3 THROUGH 150)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  36.5562   5.3868  31.2266              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1307 T22:   3.1914                                     
REMARK   3      T33:   1.7092 T12:  -0.4525                                     
REMARK   3      T13:  -0.1205 T23:   0.2011                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  14.3881 L22:  15.0554                                     
REMARK   3      L33:   9.6163 L12:  -4.7716                                     
REMARK   3      L13:   2.8746 L23:  -6.7414                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4506 S12:  -0.4020 S13:  -0.2486                       
REMARK   3      S21:  -0.3177 S22:  -0.6173 S23:   0.2458                       
REMARK   3      S31:   0.1400 S32:  -0.5332 S33:   0.0048                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 392 THROUGH 483)                  
REMARK   3    ORIGIN FOR THE GROUP (A):   6.3656   8.3386  30.8612              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.3826 T22:   3.5515                                     
REMARK   3      T33:   3.1570 T12:  -0.0142                                     
REMARK   3      T13:  -0.3525 T23:  -0.2434                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.6764 L22:   4.8112                                     
REMARK   3      L33:   9.6901 L12:  -1.2684                                     
REMARK   3      L13:   1.9324 L23:  -4.0872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0492 S12:  -0.6541 S13:   0.4414                       
REMARK   3      S21:   0.3805 S22:  -0.6924 S23:   0.1681                       
REMARK   3      S31:  -0.6138 S32:  -0.2506 S33:  -0.0002                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'E' AND RESID 7 THROUGH 144)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  93.3840 -18.9786  44.8469              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.4120 T22:   3.3593                                     
REMARK   3      T33:   2.0662 T12:  -0.0524                                     
REMARK   3      T13:   0.0958 T23:   0.6246                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.6165 L22:   8.0628                                     
REMARK   3      L33:   9.3834 L12:  -3.2907                                     
REMARK   3      L13:  -1.9392 L23:  -0.1050                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3416 S12:  -1.9560 S13:  -0.5958                       
REMARK   3      S21:  -0.2920 S22:  -0.0248 S23:   0.6708                       
REMARK   3      S31:   0.4441 S32:   0.4392 S33:   0.0019                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN 'F' AND RESID 3 THROUGH 150)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  67.2221  -1.8946  34.6389              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2792 T22:   2.8140                                     
REMARK   3      T33:   1.8845 T12:   0.0245                                     
REMARK   3      T13:  -0.0148 T23:   0.6316                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   9.4580 L22:  13.1760                                     
REMARK   3      L33:  10.3848 L12:  -1.5730                                     
REMARK   3      L13:   0.7145 L23:  10.9533                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6477 S12:  -1.0270 S13:   0.2226                       
REMARK   3      S21:  -0.0727 S22:  -0.4587 S23:   0.4098                       
REMARK   3      S31:   0.3321 S32:   0.1613 S33:  -0.0003                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN 'G' AND RESID 345 THROUGH 483)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  58.0791 -14.1912   0.8909              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2474 T22:   2.5298                                     
REMARK   3      T33:   2.3608 T12:  -0.1172                                     
REMARK   3      T13:   0.1694 T23:   0.0319                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4507 L22:  -1.2580                                     
REMARK   3      L33:   8.1503 L12:   0.3963                                     
REMARK   3      L13:  -1.9616 L23:  -0.5336                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5719 S12:  -0.3301 S13:  -0.1833                       
REMARK   3      S21:  -0.1356 S22:   0.1764 S23:  -0.1134                       
REMARK   3      S31:  -0.0073 S32:   1.1898 S33:   0.0012                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: (CHAIN 'H' AND RESID 342 THROUGH 483)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  45.1038 -16.1521  -5.3711              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2560 T22:   2.5434                                     
REMARK   3      T33:   2.4203 T12:  -0.3540                                     
REMARK   3      T13:  -0.3135 T23:   0.2938                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -1.0815 L22:   9.3442                                     
REMARK   3      L33:   5.1519 L12:   2.7267                                     
REMARK   3      L13:   0.0972 L23:  -7.3169                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4404 S12:  -1.0275 S13:   0.1033                       
REMARK   3      S21:  -0.8789 S22:  -0.3728 S23:   0.2117                       
REMARK   3      S31:   1.3930 S32:   0.1065 S33:  -0.0241                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: (CHAIN 'I' AND RESID 7 THROUGH 144)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  73.3378  49.2326  71.3638              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   5.0072 T22:   4.5660                                     
REMARK   3      T33:   5.1996 T12:   0.5951                                     
REMARK   3      T13:   0.7317 T23:  -0.9877                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -1.0254 L22:  -0.2201                                     
REMARK   3      L33:  -0.9084 L12:   0.3791                                     
REMARK   3      L13:   0.0780 L23:  -2.7298                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.4348 S12:  -0.1408 S13:   2.4092                       
REMARK   3      S21:   2.9829 S22:   0.2521 S23:   2.5559                       
REMARK   3      S31:  -2.3628 S32:   1.0700 S33:   0.2461                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: (CHAIN 'J' AND RESID 3 THROUGH 150)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  75.0702  20.7311  55.8294              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.5447 T22:   3.5799                                     
REMARK   3      T33:   2.3017 T12:   0.7107                                     
REMARK   3      T13:  -0.0098 T23:  -0.3780                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  10.6003 L22:   7.1057                                     
REMARK   3      L33:  13.6605 L12:   4.0070                                     
REMARK   3      L13:  -4.9763 L23:  -1.8651                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.6813 S12:  -0.5864 S13:   0.7787                       
REMARK   3      S21:   0.2224 S22:   0.3813 S23:  -0.5626                       
REMARK   3      S31:  -0.4983 S32:  -1.6822 S33:  -0.0006                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: (CHAIN 'K' AND RESID 345 THROUGH 483)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  54.4199  -4.0385  75.0794              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.2795 T22:   5.1505                                     
REMARK   3      T33:   2.5161 T12:   0.2642                                     
REMARK   3      T13:   0.3760 T23:   0.3753                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  -0.6745 L22:   6.5504                                     
REMARK   3      L33:   1.3192 L12:   1.8203                                     
REMARK   3      L13:  -1.6447 L23:  -2.2104                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0041 S12:  -0.0832 S13:   0.8183                       
REMARK   3      S21:   2.7237 S22:  -0.2701 S23:  -0.2449                       
REMARK   3      S31:  -0.4586 S32:  -1.3820 S33:  -0.0424                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: (CHAIN 'L' AND RESID 342 THROUGH 483)                  
REMARK   3    ORIGIN FOR THE GROUP (A):  45.9062 -15.2438  70.8316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.7828 T22:   5.1651                                     
REMARK   3      T33:   3.0751 T12:  -0.3380                                     
REMARK   3      T13:   0.4676 T23:   0.6652                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.2624 L22:   4.6303                                     
REMARK   3      L33:  -1.0143 L12:  -1.3823                                     
REMARK   3      L13:   0.3963 L23:  -2.0967                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -1.0282 S12:  -0.9148 S13:  -0.2838                       
REMARK   3      S21:  -0.4893 S22:   1.9770 S23:  -0.0583                       
REMARK   3      S31:   0.9064 S32:  -3.3930 S33:   0.1133                       
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 4ORH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 12-FEB-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000084858.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 105                                
REMARK 200  PH                             : 4.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11435                            
REMARK 200  MONOCHROMATOR                  : UNK.                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 45946                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 4.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 200.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : 0.11400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 4.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 4.97                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57300                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 80.79                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 6.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 75 MM SODIUM ACETATE, 1.0 M AMMONIUM     
REMARK 280  PHOSPHATE, PH 4.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  298K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 42 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z                                                
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000      102.62900            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000      102.62900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      117.68600            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000      102.62900            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000      102.62900            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      117.68600            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000      102.62900            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000      102.62900            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      117.68600            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000      102.62900            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000      102.62900            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      117.68600            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, J, K, L                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F, G, H                            
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: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     GLY A    -7                                                      
REMARK 465     PRO A    -6                                                      
REMARK 465     LEU A    -5                                                      
REMARK 465     GLY A    -4                                                      
REMARK 465     SER A    -3                                                      
REMARK 465     PRO A    -2                                                      
REMARK 465     GLU A    -1                                                      
REMARK 465     PHE A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     PRO B    -6                                                      
REMARK 465     LEU B    -5                                                      
REMARK 465     GLY B    -4                                                      
REMARK 465     SER B    -3                                                      
REMARK 465     PRO B    -2                                                      
REMARK 465     GLU B    -1                                                      
REMARK 465     PHE B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ALA B     2                                                      
REMARK 465     ASN B   151                                                      
REMARK 465     ILE B   152                                                      
REMARK 465     GLY C   337                                                      
REMARK 465     PRO C   338                                                      
REMARK 465     LEU C   339                                                      
REMARK 465     GLY C   340                                                      
REMARK 465     SER C   341                                                      
REMARK 465     PRO C   342                                                      
REMARK 465     GLU C   343                                                      
REMARK 465     PHE C   344                                                      
REMARK 465     GLN C   345                                                      
REMARK 465     GLU C   346                                                      
REMARK 465     HIS C   347                                                      
REMARK 465     TRP C   348                                                      
REMARK 465     ALA C   349                                                      
REMARK 465     LEU C   350                                                      
REMARK 465     MET C   351                                                      
REMARK 465     GLU C   352                                                      
REMARK 465     GLU C   353                                                      
REMARK 465     LEU C   354                                                      
REMARK 465     ASN C   355                                                      
REMARK 465     ARG C   356                                                      
REMARK 465     SER C   357                                                      
REMARK 465     LYS C   358                                                      
REMARK 465     LYS C   359                                                      
REMARK 465     ASP C   360                                                      
REMARK 465     PHE C   361                                                      
REMARK 465     GLU C   362                                                      
REMARK 465     ALA C   363                                                      
REMARK 465     ILE C   364                                                      
REMARK 465     ILE C   365                                                      
REMARK 465     GLN C   366                                                      
REMARK 465     ALA C   367                                                      
REMARK 465     LYS C   368                                                      
REMARK 465     ASN C   369                                                      
REMARK 465     LYS C   370                                                      
REMARK 465     GLU C   371                                                      
REMARK 465     LEU C   372                                                      
REMARK 465     GLU C   373                                                      
REMARK 465     GLN C   374                                                      
REMARK 465     THR C   375                                                      
REMARK 465     LYS C   376                                                      
REMARK 465     GLU C   377                                                      
REMARK 465     GLU C   378                                                      
REMARK 465     LYS C   379                                                      
REMARK 465     GLU C   380                                                      
REMARK 465     LYS C   381                                                      
REMARK 465     MET C   382                                                      
REMARK 465     GLN C   383                                                      
REMARK 465     ALA C   384                                                      
REMARK 465     GLN C   385                                                      
REMARK 465     LYS C   386                                                      
REMARK 465     GLU C   387                                                      
REMARK 465     GLU C   388                                                      
REMARK 465     VAL C   389                                                      
REMARK 465     LEU C   390                                                      
REMARK 465     SER C   391                                                      
REMARK 465     LEU C   484                                                      
REMARK 465     PHE C   485                                                      
REMARK 465     GLY E    -7                                                      
REMARK 465     PRO E    -6                                                      
REMARK 465     LEU E    -5                                                      
REMARK 465     GLY E    -4                                                      
REMARK 465     SER E    -3                                                      
REMARK 465     PRO E    -2                                                      
REMARK 465     GLU E    -1                                                      
REMARK 465     PHE E     0                                                      
REMARK 465     MET E     1                                                      
REMARK 465     ALA E     2                                                      
REMARK 465     VAL E     3                                                      
REMARK 465     SER E     4                                                      
REMARK 465     THR E     5                                                      
REMARK 465     GLY E     6                                                      
REMARK 465     ASN E   145                                                      
REMARK 465     GLY F    -7                                                      
REMARK 465     PRO F    -6                                                      
REMARK 465     LEU F    -5                                                      
REMARK 465     GLY F    -4                                                      
REMARK 465     SER F    -3                                                      
REMARK 465     PRO F    -2                                                      
REMARK 465     GLU F    -1                                                      
REMARK 465     PHE F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     ALA F     2                                                      
REMARK 465     ASN F   151                                                      
REMARK 465     ILE F   152                                                      
REMARK 465     GLY G   337                                                      
REMARK 465     PRO G   338                                                      
REMARK 465     LEU G   339                                                      
REMARK 465     GLY G   340                                                      
REMARK 465     SER G   341                                                      
REMARK 465     PRO G   342                                                      
REMARK 465     GLU G   343                                                      
REMARK 465     PHE G   344                                                      
REMARK 465     LEU G   484                                                      
REMARK 465     PHE G   485                                                      
REMARK 465     GLY H   337                                                      
REMARK 465     PRO H   338                                                      
REMARK 465     LEU H   339                                                      
REMARK 465     GLY H   340                                                      
REMARK 465     SER H   341                                                      
REMARK 465     LEU H   484                                                      
REMARK 465     PHE H   485                                                      
REMARK 465     GLY I    -7                                                      
REMARK 465     PRO I    -6                                                      
REMARK 465     LEU I    -5                                                      
REMARK 465     GLY I    -4                                                      
REMARK 465     SER I    -3                                                      
REMARK 465     PRO I    -2                                                      
REMARK 465     GLU I    -1                                                      
REMARK 465     PHE I     0                                                      
REMARK 465     MET I     1                                                      
REMARK 465     ALA I     2                                                      
REMARK 465     VAL I     3                                                      
REMARK 465     SER I     4                                                      
REMARK 465     THR I     5                                                      
REMARK 465     GLY I     6                                                      
REMARK 465     ASN I   145                                                      
REMARK 465     GLY J    -7                                                      
REMARK 465     PRO J    -6                                                      
REMARK 465     LEU J    -5                                                      
REMARK 465     GLY J    -4                                                      
REMARK 465     SER J    -3                                                      
REMARK 465     PRO J    -2                                                      
REMARK 465     GLU J    -1                                                      
REMARK 465     PHE J     0                                                      
REMARK 465     MET J     1                                                      
REMARK 465     ALA J     2                                                      
REMARK 465     ASN J   151                                                      
REMARK 465     ILE J   152                                                      
REMARK 465     GLY K   337                                                      
REMARK 465     PRO K   338                                                      
REMARK 465     LEU K   339                                                      
REMARK 465     GLY K   340                                                      
REMARK 465     SER K   341                                                      
REMARK 465     PRO K   342                                                      
REMARK 465     GLU K   343                                                      
REMARK 465     PHE K   344                                                      
REMARK 465     LEU K   484                                                      
REMARK 465     PHE K   485                                                      
REMARK 465     GLY L   337                                                      
REMARK 465     PRO L   338                                                      
REMARK 465     LEU L   339                                                      
REMARK 465     GLY L   340                                                      
REMARK 465     SER L   341                                                      
REMARK 465     LEU L   484                                                      
REMARK 465     PHE L   485                                                      
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     HIS C 392    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET C 393    CG   SD   CE                                        
REMARK 470     ASN C 394    CG   OD1  ND2                                       
REMARK 470     ASP C 395    CG   OD1  OD2                                       
REMARK 470     VAL C 396    CG1  CG2                                            
REMARK 470     LEU C 397    CG   CD1  CD2                                       
REMARK 470     LYS C 480    CG   CD   CE   NZ                                   
REMARK 470     LYS C 482    CG   CD   CE   NZ                                   
REMARK 470     ARG C 483    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN G 345    CG   CD   OE1  NE2                                  
REMARK 470     GLU G 346    CG   CD   OE1  OE2                                  
REMARK 470     HIS G 347    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP G 348    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP G 348    CZ3  CH2                                            
REMARK 470     LEU G 350    CG   CD1  CD2                                       
REMARK 470     MET G 351    CG   SD   CE                                        
REMARK 470     GLU G 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 353    CG   CD   OE1  OE2                                  
REMARK 470     LEU G 354    CG   CD1  CD2                                       
REMARK 470     ASN G 355    CG   OD1  ND2                                       
REMARK 470     ARG G 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER G 357    OG                                                  
REMARK 470     LYS G 358    CG   CD   CE   NZ                                   
REMARK 470     LYS G 359    CG   CD   CE   NZ                                   
REMARK 470     ASP G 360    CG   OD1  OD2                                       
REMARK 470     PHE G 361    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU G 362    CG   CD   OE1  OE2                                  
REMARK 470     ILE G 364    CG1  CG2  CD1                                       
REMARK 470     ILE G 365    CG1  CG2  CD1                                       
REMARK 470     GLN G 366    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 368    CG   CD   CE   NZ                                   
REMARK 470     ASN G 369    CG   OD1  ND2                                       
REMARK 470     LYS G 370    CG   CD   CE   NZ                                   
REMARK 470     GLU G 371    CG   CD   OE1  OE2                                  
REMARK 470     LEU G 372    CG   CD1  CD2                                       
REMARK 470     GLU G 373    CG   CD   OE1  OE2                                  
REMARK 470     GLN G 374    CG   CD   OE1  NE2                                  
REMARK 470     THR G 375    OG1  CG2                                            
REMARK 470     LYS G 376    CG   CD   CE   NZ                                   
REMARK 470     GLU G 377    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 378    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 379    CG   CD   CE   NZ                                   
REMARK 470     GLU G 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS G 381    CG   CD   CE   NZ                                   
REMARK 470     MET G 382    CG   SD   CE                                        
REMARK 470     GLN G 383    CG   CD   OE1  NE2                                  
REMARK 470     GLN G 385    CG   CD   OE1  NE2                                  
REMARK 470     LYS G 386    CG   CD   CE   NZ                                   
REMARK 470     GLU G 387    CG   CD   OE1  OE2                                  
REMARK 470     GLU G 388    CG   CD   OE1  OE2                                  
REMARK 470     VAL G 389    CG1  CG2                                            
REMARK 470     LEU G 390    CG   CD1  CD2                                       
REMARK 470     SER G 391    OG                                                  
REMARK 470     HIS G 392    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET G 393    CG   SD   CE                                        
REMARK 470     ASN G 394    CG   OD1  ND2                                       
REMARK 470     ASP G 395    CG   OD1  OD2                                       
REMARK 470     VAL G 396    CG1  CG2                                            
REMARK 470     LEU G 397    CG   CD1  CD2                                       
REMARK 470     LYS G 480    CG   CD   CE   NZ                                   
REMARK 470     LYS G 482    CG   CD   CE   NZ                                   
REMARK 470     ARG G 483    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO H 342    CG   CD                                             
REMARK 470     GLU H 343    CB   CG   CD   OE1  OE2                             
REMARK 470     PHE H 344    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN H 345    CG   CD   OE1  NE2                                  
REMARK 470     GLU H 346    CG   CD   OE1  OE2                                  
REMARK 470     HIS H 347    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP H 348    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP H 348    CZ3  CH2                                            
REMARK 470     LEU H 350    CG   CD1  CD2                                       
REMARK 470     MET H 351    CG   SD   CE                                        
REMARK 470     GLU H 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 353    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 354    CG   CD1  CD2                                       
REMARK 470     ASN H 355    CG   OD1  ND2                                       
REMARK 470     ARG H 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER H 357    OG                                                  
REMARK 470     LYS H 358    CG   CD   CE   NZ                                   
REMARK 470     LYS H 359    CG   CD   CE   NZ                                   
REMARK 470     ASP H 360    CG   OD1  OD2                                       
REMARK 470     PHE H 361    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU H 362    CG   CD   OE1  OE2                                  
REMARK 470     ILE H 364    CG1  CG2  CD1                                       
REMARK 470     ILE H 365    CG1  CG2  CD1                                       
REMARK 470     GLN H 366    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 368    CG   CD   CE   NZ                                   
REMARK 470     ASN H 369    CG   OD1  ND2                                       
REMARK 470     LYS H 370    CG   CD   CE   NZ                                   
REMARK 470     GLU H 371    CG   CD   OE1  OE2                                  
REMARK 470     LEU H 372    CG   CD1  CD2                                       
REMARK 470     GLU H 373    CG   CD   OE1  OE2                                  
REMARK 470     GLN H 374    CG   CD   OE1  NE2                                  
REMARK 470     THR H 375    OG1  CG2                                            
REMARK 470     LYS H 376    CG   CD   CE   NZ                                   
REMARK 470     GLU H 377    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 378    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 379    CG   CD   CE   NZ                                   
REMARK 470     GLU H 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS H 381    CG   CD   CE   NZ                                   
REMARK 470     MET H 382    CG   SD   CE                                        
REMARK 470     GLN H 383    CG   CD   OE1  NE2                                  
REMARK 470     GLN H 385    CG   CD   OE1  NE2                                  
REMARK 470     LYS H 386    CG   CD   CE   NZ                                   
REMARK 470     GLU H 387    CG   CD   OE1  OE2                                  
REMARK 470     GLU H 388    CG   CD   OE1  OE2                                  
REMARK 470     VAL H 389    CG1  CG2                                            
REMARK 470     LEU H 390    CG   CD1  CD2                                       
REMARK 470     SER H 391    OG                                                  
REMARK 470     HIS H 392    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET H 393    CG   SD   CE                                        
REMARK 470     ASN H 394    CG   OD1  ND2                                       
REMARK 470     ASP H 395    CG   OD1  OD2                                       
REMARK 470     VAL H 396    CG1  CG2                                            
REMARK 470     LEU H 397    CG   CD1  CD2                                       
REMARK 470     LYS H 480    CG   CD   CE   NZ                                   
REMARK 470     LYS H 482    CG   CD   CE   NZ                                   
REMARK 470     ARG H 483    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN K 345    CG   CD   OE1  NE2                                  
REMARK 470     GLU K 346    CG   CD   OE1  OE2                                  
REMARK 470     HIS K 347    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP K 348    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP K 348    CZ3  CH2                                            
REMARK 470     LEU K 350    CG   CD1  CD2                                       
REMARK 470     MET K 351    CG   SD   CE                                        
REMARK 470     GLU K 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 353    CG   CD   OE1  OE2                                  
REMARK 470     LEU K 354    CG   CD1  CD2                                       
REMARK 470     ASN K 355    CG   OD1  ND2                                       
REMARK 470     ARG K 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER K 357    OG                                                  
REMARK 470     LYS K 358    CG   CD   CE   NZ                                   
REMARK 470     LYS K 359    CG   CD   CE   NZ                                   
REMARK 470     ASP K 360    CG   OD1  OD2                                       
REMARK 470     PHE K 361    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU K 362    CG   CD   OE1  OE2                                  
REMARK 470     ILE K 364    CG1  CG2  CD1                                       
REMARK 470     ILE K 365    CG1  CG2  CD1                                       
REMARK 470     GLN K 366    CG   CD   OE1  NE2                                  
REMARK 470     LYS K 368    CG   CD   CE   NZ                                   
REMARK 470     ASN K 369    CG   OD1  ND2                                       
REMARK 470     LYS K 370    CG   CD   CE   NZ                                   
REMARK 470     GLU K 371    CG   CD   OE1  OE2                                  
REMARK 470     LEU K 372    CG   CD1  CD2                                       
REMARK 470     GLU K 373    CG   CD   OE1  OE2                                  
REMARK 470     GLN K 374    CG   CD   OE1  NE2                                  
REMARK 470     THR K 375    OG1  CG2                                            
REMARK 470     LYS K 376    CG   CD   CE   NZ                                   
REMARK 470     GLU K 377    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 378    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 379    CG   CD   CE   NZ                                   
REMARK 470     GLU K 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS K 381    CG   CD   CE   NZ                                   
REMARK 470     MET K 382    CG   SD   CE                                        
REMARK 470     GLN K 383    CG   CD   OE1  NE2                                  
REMARK 470     GLN K 385    CG   CD   OE1  NE2                                  
REMARK 470     LYS K 386    CG   CD   CE   NZ                                   
REMARK 470     GLU K 387    CG   CD   OE1  OE2                                  
REMARK 470     GLU K 388    CG   CD   OE1  OE2                                  
REMARK 470     VAL K 389    CG1  CG2                                            
REMARK 470     LEU K 390    CG   CD1  CD2                                       
REMARK 470     SER K 391    OG                                                  
REMARK 470     HIS K 392    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET K 393    CG   SD   CE                                        
REMARK 470     ASN K 394    CG   OD1  ND2                                       
REMARK 470     ASP K 395    CG   OD1  OD2                                       
REMARK 470     VAL K 396    CG1  CG2                                            
REMARK 470     LEU K 397    CG   CD1  CD2                                       
REMARK 470     LYS K 480    CG   CD   CE   NZ                                   
REMARK 470     LYS K 482    CG   CD   CE   NZ                                   
REMARK 470     ARG K 483    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     PRO L 342    CG   CD                                             
REMARK 470     GLU L 343    CB   CG   CD   OE1  OE2                             
REMARK 470     PHE L 344    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLN L 345    CG   CD   OE1  NE2                                  
REMARK 470     GLU L 346    CG   CD   OE1  OE2                                  
REMARK 470     HIS L 347    CG   ND1  CD2  CE1  NE2                             
REMARK 470     TRP L 348    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP L 348    CZ3  CH2                                            
REMARK 470     LEU L 350    CG   CD1  CD2                                       
REMARK 470     MET L 351    CG   SD   CE                                        
REMARK 470     GLU L 352    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 353    CG   CD   OE1  OE2                                  
REMARK 470     LEU L 354    CG   CD1  CD2                                       
REMARK 470     ASN L 355    CG   OD1  ND2                                       
REMARK 470     ARG L 356    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     SER L 357    OG                                                  
REMARK 470     LYS L 358    CG   CD   CE   NZ                                   
REMARK 470     LYS L 359    CG   CD   CE   NZ                                   
REMARK 470     ASP L 360    CG   OD1  OD2                                       
REMARK 470     PHE L 361    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU L 362    CG   CD   OE1  OE2                                  
REMARK 470     ILE L 364    CG1  CG2  CD1                                       
REMARK 470     ILE L 365    CG1  CG2  CD1                                       
REMARK 470     GLN L 366    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 368    CG   CD   CE   NZ                                   
REMARK 470     ASN L 369    CG   OD1  ND2                                       
REMARK 470     LYS L 370    CG   CD   CE   NZ                                   
REMARK 470     GLU L 371    CG   CD   OE1  OE2                                  
REMARK 470     LEU L 372    CG   CD1  CD2                                       
REMARK 470     GLU L 373    CG   CD   OE1  OE2                                  
REMARK 470     GLN L 374    CG   CD   OE1  NE2                                  
REMARK 470     THR L 375    OG1  CG2                                            
REMARK 470     LYS L 376    CG   CD   CE   NZ                                   
REMARK 470     GLU L 377    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 378    CG   CD   OE1  OE2                                  
REMARK 470     LYS L 379    CG   CD   CE   NZ                                   
REMARK 470     GLU L 380    CG   CD   OE1  OE2                                  
REMARK 470     LYS L 381    CG   CD   CE   NZ                                   
REMARK 470     MET L 382    CG   SD   CE                                        
REMARK 470     GLN L 383    CG   CD   OE1  NE2                                  
REMARK 470     GLN L 385    CG   CD   OE1  NE2                                  
REMARK 470     LYS L 386    CG   CD   CE   NZ                                   
REMARK 470     GLU L 387    CG   CD   OE1  OE2                                  
REMARK 470     GLU L 388    CG   CD   OE1  OE2                                  
REMARK 470     VAL L 389    CG1  CG2                                            
REMARK 470     LEU L 390    CG   CD1  CD2                                       
REMARK 470     SER L 391    OG                                                  
REMARK 470     HIS L 392    CG   ND1  CD2  CE1  NE2                             
REMARK 470     MET L 393    CG   SD   CE                                        
REMARK 470     ASN L 394    CG   OD1  ND2                                       
REMARK 470     ASP L 395    CG   OD1  OD2                                       
REMARK 470     VAL L 396    CG1  CG2                                            
REMARK 470     LEU L 397    CG   CD1  CD2                                       
REMARK 470     LYS L 480    CG   CD   CE   NZ                                   
REMARK 470     LYS L 482    CG   CD   CE   NZ                                   
REMARK 470     ARG L 483    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    LEU F    99     OG1  THR F   103              1.91            
REMARK 500   O    MET F    64     NH2  ARG G   433              1.97            
REMARK 500   O    MET J    64     NH2  ARG K   433              2.12            
REMARK 500   NE2  GLN F   135     OG1  THR J   103              2.13            
REMARK 500   O    LEU J    99     OG1  THR J   103              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LYS B  92      -72.94   -145.55                                   
REMARK 500    LYS B  94       40.54    -94.33                                   
REMARK 500    PRO B  97       -7.31    -55.75                                   
REMARK 500    GLN B 100      171.95     79.21                                   
REMARK 500    ASN B 116       78.75   -119.14                                   
REMARK 500    LEU B 121       36.76    -92.56                                   
REMARK 500    ASN B 123     -100.21    -48.56                                   
REMARK 500    ASP B 124      -25.43    177.79                                   
REMARK 500    GLU C 400      -54.85   -137.75                                   
REMARK 500    ALA C 419        1.73     83.75                                   
REMARK 500    LYS F  92      -72.90   -145.52                                   
REMARK 500    LYS F  94       40.53    -94.33                                   
REMARK 500    PRO F  97       -7.31    -55.76                                   
REMARK 500    GLN F 100      172.02     79.20                                   
REMARK 500    ASN F 116       78.70   -119.14                                   
REMARK 500    LEU F 121       36.74    -92.59                                   
REMARK 500    ASN F 123     -100.23    -48.60                                   
REMARK 500    ASP F 124      -25.41    177.87                                   
REMARK 500    LEU G 397      -89.91    -54.90                                   
REMARK 500    GLU G 400      -17.88   -142.26                                   
REMARK 500    ALA G 419        3.75     85.45                                   
REMARK 500    ILE G 435       57.62    -98.49                                   
REMARK 500    GLU H 400      -54.77   -137.79                                   
REMARK 500    ALA H 419        1.88     83.64                                   
REMARK 500    LYS J  92      -72.88   -145.57                                   
REMARK 500    LYS J  94       40.58    -94.36                                   
REMARK 500    PRO J  97       -7.27    -55.81                                   
REMARK 500    GLN J 100      172.00     79.21                                   
REMARK 500    ASN J 116       78.64   -119.10                                   
REMARK 500    LEU J 121       36.78    -92.58                                   
REMARK 500    ASN J 123     -100.18    -48.66                                   
REMARK 500    ASP J 124      -25.31    177.86                                   
REMARK 500    LEU K 397      -77.22    -52.80                                   
REMARK 500    GLU K 400      -33.25   -135.24                                   
REMARK 500    ALA K 419        3.62     85.44                                   
REMARK 500    ILE K 435       57.66    -98.56                                   
REMARK 500    ALA L 419        1.83     83.83                                   
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                              ZN K 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS K 420   ND1                                                    
REMARK 620 2 CYS K 440   SG  113.8                                              
REMARK 620 3 CYS K 418   SG  114.5 108.8                                        
REMARK 620 4 CYS K 437   SG  104.0 109.4 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS G 420   ND1                                                    
REMARK 620 2 CYS G 440   SG  113.8                                              
REMARK 620 3 CYS G 418   SG  114.6 108.8                                        
REMARK 620 4 CYS G 437   SG  104.0 109.4 105.8                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS C 420   ND1                                                    
REMARK 620 2 CYS C 418   SG  112.0                                              
REMARK 620 3 CYS C 440   SG  109.6 107.9                                        
REMARK 620 4 CYS C 437   SG  108.7 109.2 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS L 420   ND1                                                    
REMARK 620 2 CYS L 418   SG  112.0                                              
REMARK 620 3 CYS L 440   SG  109.5 107.9                                        
REMARK 620 4 CYS L 437   SG  108.7 109.2 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 501  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS H 420   ND1                                                    
REMARK 620 2 CYS H 418   SG  112.0                                              
REMARK 620 3 CYS H 440   SG  109.5 107.9                                        
REMARK 620 4 CYS H 437   SG  108.7 109.2 109.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN C 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS C 426   SG                                                     
REMARK 620 2 CYS C 406   SG  106.3                                              
REMARK 620 3 CYS C 403   SG  120.2 110.7                                        
REMARK 620 4 CYS C 423   SG  113.3 101.3 103.5                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN H 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS H 426   SG                                                     
REMARK 620 2 CYS H 406   SG  106.3                                              
REMARK 620 3 CYS H 403   SG  120.2 110.6                                        
REMARK 620 4 CYS H 423   SG  113.4 101.3 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN L 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS L 426   SG                                                     
REMARK 620 2 CYS L 406   SG  106.3                                              
REMARK 620 3 CYS L 403   SG  120.2 110.6                                        
REMARK 620 4 CYS L 423   SG  113.3 101.3 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN K 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS K 426   SG                                                     
REMARK 620 2 CYS K 406   SG  108.6                                              
REMARK 620 3 CYS K 423   SG  111.6 101.8                                        
REMARK 620 4 CYS K 403   SG  117.9 112.1 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN G 502  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 CYS G 426   SG                                                     
REMARK 620 2 CYS G 406   SG  108.6                                              
REMARK 620 3 CYS G 423   SG  111.6 101.9                                        
REMARK 620 4 CYS G 403   SG  117.8 112.1 103.6                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN C 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN G 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN H 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN K 502                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 501                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN L 502                  
DBREF  4ORH A    1   145  UNP    Q15819   UB2V2_HUMAN      1    145             
DBREF  4ORH B    1   152  UNP    P61088   UBE2N_HUMAN      1    152             
DBREF  4ORH C  345   485  UNP    O76064   RNF8_HUMAN     345    485             
DBREF  4ORH E    1   145  UNP    Q15819   UB2V2_HUMAN      1    145             
DBREF  4ORH F    1   152  UNP    P61088   UBE2N_HUMAN      1    152             
DBREF  4ORH G  345   485  UNP    O76064   RNF8_HUMAN     345    485             
DBREF  4ORH H  345   485  UNP    O76064   RNF8_HUMAN     345    485             
DBREF  4ORH I    1   145  UNP    Q15819   UB2V2_HUMAN      1    145             
DBREF  4ORH J    1   152  UNP    P61088   UBE2N_HUMAN      1    152             
DBREF  4ORH K  345   485  UNP    O76064   RNF8_HUMAN     345    485             
DBREF  4ORH L  345   485  UNP    O76064   RNF8_HUMAN     345    485             
SEQADV 4ORH GLY A   -7  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO A   -6  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH LEU A   -5  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY A   -4  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH SER A   -3  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO A   -2  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLU A   -1  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PHE A    0  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY B   -7  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO B   -6  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH LEU B   -5  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY B   -4  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH SER B   -3  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO B   -2  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLU B   -1  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PHE B    0  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY C  337  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO C  338  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH LEU C  339  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY C  340  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH SER C  341  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO C  342  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLU C  343  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PHE C  344  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY E   -7  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO E   -6  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH LEU E   -5  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY E   -4  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH SER E   -3  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO E   -2  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLU E   -1  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PHE E    0  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY F   -7  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO F   -6  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH LEU F   -5  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY F   -4  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH SER F   -3  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO F   -2  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLU F   -1  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PHE F    0  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY G  337  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO G  338  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH LEU G  339  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY G  340  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH SER G  341  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO G  342  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLU G  343  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PHE G  344  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY H  337  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO H  338  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH LEU H  339  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY H  340  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH SER H  341  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO H  342  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLU H  343  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PHE H  344  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY I   -7  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO I   -6  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH LEU I   -5  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY I   -4  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH SER I   -3  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PRO I   -2  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLU I   -1  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH PHE I    0  UNP  Q15819              EXPRESSION TAG                 
SEQADV 4ORH GLY J   -7  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO J   -6  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH LEU J   -5  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY J   -4  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH SER J   -3  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PRO J   -2  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLU J   -1  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH PHE J    0  UNP  P61088              EXPRESSION TAG                 
SEQADV 4ORH GLY K  337  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO K  338  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH LEU K  339  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY K  340  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH SER K  341  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO K  342  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLU K  343  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PHE K  344  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY L  337  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO L  338  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH LEU L  339  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLY L  340  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH SER L  341  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PRO L  342  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH GLU L  343  UNP  O76064              EXPRESSION TAG                 
SEQADV 4ORH PHE L  344  UNP  O76064              EXPRESSION TAG                 
SEQRES   1 A  153  GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR          
SEQRES   2 A  153  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   3 A  153  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   4 A  153  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   5 A  153  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   6 A  153  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   7 A  153  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   8 A  153  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   9 A  153  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES  10 A  153  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  11 A  153  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  12 A  153  GLN PRO PRO GLU GLY GLN THR TYR ASN ASN                      
SEQRES   1 B  160  GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO          
SEQRES   2 B  160  ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU          
SEQRES   3 B  160  PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN          
SEQRES   4 B  160  ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP          
SEQRES   5 B  160  SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE          
SEQRES   6 B  160  LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG          
SEQRES   7 B  160  PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU          
SEQRES   8 B  160  GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER          
SEQRES   9 B  160  PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN          
SEQRES  10 B  160  ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA          
SEQRES  11 B  160  ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN          
SEQRES  12 B  160  ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA          
SEQRES  13 B  160  MET ASN ASN ILE                                              
SEQRES   1 C  149  GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA          
SEQRES   2 C  149  LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU          
SEQRES   3 C  149  ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR          
SEQRES   4 C  149  LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU          
SEQRES   5 C  149  VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU          
SEQRES   6 C  149  GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL          
SEQRES   7 C  149  THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE          
SEQRES   8 C  149  ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS          
SEQRES   9 C  149  ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU          
SEQRES  10 C  149  ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER          
SEQRES  11 C  149  GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG          
SEQRES  12 C  149  LYS ALA LYS ARG LEU PHE                                      
SEQRES   1 E  153  GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR          
SEQRES   2 E  153  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   3 E  153  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   4 E  153  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   5 E  153  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   6 E  153  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   7 E  153  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   8 E  153  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   9 E  153  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES  10 E  153  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  11 E  153  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  12 E  153  GLN PRO PRO GLU GLY GLN THR TYR ASN ASN                      
SEQRES   1 F  160  GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO          
SEQRES   2 F  160  ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU          
SEQRES   3 F  160  PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN          
SEQRES   4 F  160  ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP          
SEQRES   5 F  160  SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE          
SEQRES   6 F  160  LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG          
SEQRES   7 F  160  PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU          
SEQRES   8 F  160  GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER          
SEQRES   9 F  160  PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN          
SEQRES  10 F  160  ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA          
SEQRES  11 F  160  ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN          
SEQRES  12 F  160  ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA          
SEQRES  13 F  160  MET ASN ASN ILE                                              
SEQRES   1 G  149  GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA          
SEQRES   2 G  149  LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU          
SEQRES   3 G  149  ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR          
SEQRES   4 G  149  LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU          
SEQRES   5 G  149  VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU          
SEQRES   6 G  149  GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL          
SEQRES   7 G  149  THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE          
SEQRES   8 G  149  ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS          
SEQRES   9 G  149  ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU          
SEQRES  10 G  149  ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER          
SEQRES  11 G  149  GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG          
SEQRES  12 G  149  LYS ALA LYS ARG LEU PHE                                      
SEQRES   1 H  149  GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA          
SEQRES   2 H  149  LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU          
SEQRES   3 H  149  ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR          
SEQRES   4 H  149  LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU          
SEQRES   5 H  149  VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU          
SEQRES   6 H  149  GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL          
SEQRES   7 H  149  THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE          
SEQRES   8 H  149  ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS          
SEQRES   9 H  149  ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU          
SEQRES  10 H  149  ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER          
SEQRES  11 H  149  GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG          
SEQRES  12 H  149  LYS ALA LYS ARG LEU PHE                                      
SEQRES   1 I  153  GLY PRO LEU GLY SER PRO GLU PHE MET ALA VAL SER THR          
SEQRES   2 I  153  GLY VAL LYS VAL PRO ARG ASN PHE ARG LEU LEU GLU GLU          
SEQRES   3 I  153  LEU GLU GLU GLY GLN LYS GLY VAL GLY ASP GLY THR VAL          
SEQRES   4 I  153  SER TRP GLY LEU GLU ASP ASP GLU ASP MET THR LEU THR          
SEQRES   5 I  153  ARG TRP THR GLY MET ILE ILE GLY PRO PRO ARG THR ASN          
SEQRES   6 I  153  TYR GLU ASN ARG ILE TYR SER LEU LYS VAL GLU CYS GLY          
SEQRES   7 I  153  PRO LYS TYR PRO GLU ALA PRO PRO SER VAL ARG PHE VAL          
SEQRES   8 I  153  THR LYS ILE ASN MET ASN GLY ILE ASN ASN SER SER GLY          
SEQRES   9 I  153  MET VAL ASP ALA ARG SER ILE PRO VAL LEU ALA LYS TRP          
SEQRES  10 I  153  GLN ASN SER TYR SER ILE LYS VAL VAL LEU GLN GLU LEU          
SEQRES  11 I  153  ARG ARG LEU MET MET SER LYS GLU ASN MET LYS LEU PRO          
SEQRES  12 I  153  GLN PRO PRO GLU GLY GLN THR TYR ASN ASN                      
SEQRES   1 J  160  GLY PRO LEU GLY SER PRO GLU PHE MET ALA GLY LEU PRO          
SEQRES   2 J  160  ARG ARG ILE ILE LYS GLU THR GLN ARG LEU LEU ALA GLU          
SEQRES   3 J  160  PRO VAL PRO GLY ILE LYS ALA GLU PRO ASP GLU SER ASN          
SEQRES   4 J  160  ALA ARG TYR PHE HIS VAL VAL ILE ALA GLY PRO GLN ASP          
SEQRES   5 J  160  SER PRO PHE GLU GLY GLY THR PHE LYS LEU GLU LEU PHE          
SEQRES   6 J  160  LEU PRO GLU GLU TYR PRO MET ALA ALA PRO LYS VAL ARG          
SEQRES   7 J  160  PHE MET THR LYS ILE TYR HIS PRO ASN VAL ASP LYS LEU          
SEQRES   8 J  160  GLY ARG ILE CYS LEU ASP ILE LEU LYS ASP LYS TRP SER          
SEQRES   9 J  160  PRO ALA LEU GLN ILE ARG THR VAL LEU LEU SER ILE GLN          
SEQRES  10 J  160  ALA LEU LEU SER ALA PRO ASN PRO ASP ASP PRO LEU ALA          
SEQRES  11 J  160  ASN ASP VAL ALA GLU GLN TRP LYS THR ASN GLU ALA GLN          
SEQRES  12 J  160  ALA ILE GLU THR ALA ARG ALA TRP THR ARG LEU TYR ALA          
SEQRES  13 J  160  MET ASN ASN ILE                                              
SEQRES   1 K  149  GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA          
SEQRES   2 K  149  LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU          
SEQRES   3 K  149  ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR          
SEQRES   4 K  149  LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU          
SEQRES   5 K  149  VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU          
SEQRES   6 K  149  GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL          
SEQRES   7 K  149  THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE          
SEQRES   8 K  149  ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS          
SEQRES   9 K  149  ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU          
SEQRES  10 K  149  ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER          
SEQRES  11 K  149  GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG          
SEQRES  12 K  149  LYS ALA LYS ARG LEU PHE                                      
SEQRES   1 L  149  GLY PRO LEU GLY SER PRO GLU PHE GLN GLU HIS TRP ALA          
SEQRES   2 L  149  LEU MET GLU GLU LEU ASN ARG SER LYS LYS ASP PHE GLU          
SEQRES   3 L  149  ALA ILE ILE GLN ALA LYS ASN LYS GLU LEU GLU GLN THR          
SEQRES   4 L  149  LYS GLU GLU LYS GLU LYS MET GLN ALA GLN LYS GLU GLU          
SEQRES   5 L  149  VAL LEU SER HIS MET ASN ASP VAL LEU GLU ASN GLU LEU          
SEQRES   6 L  149  GLN CYS ILE ILE CYS SER GLU TYR PHE ILE GLU ALA VAL          
SEQRES   7 L  149  THR LEU ASN CYS ALA HIS SER PHE CYS SER TYR CYS ILE          
SEQRES   8 L  149  ASN GLU TRP MET LYS ARG LYS ILE GLU CYS PRO ILE CYS          
SEQRES   9 L  149  ARG LYS ASP ILE LYS SER LYS THR TYR SER LEU VAL LEU          
SEQRES  10 L  149  ASP ASN CYS ILE ASN LYS MET VAL ASN ASN LEU SER SER          
SEQRES  11 L  149  GLU VAL LYS GLU ARG ARG ILE VAL LEU ILE ARG GLU ARG          
SEQRES  12 L  149  LYS ALA LYS ARG LEU PHE                                      
HET     ZN  C 501       1                                                       
HET     ZN  C 502       1                                                       
HET     ZN  G 501       1                                                       
HET     ZN  G 502       1                                                       
HET     ZN  H 501       1                                                       
HET     ZN  H 502       1                                                       
HET     ZN  K 501       1                                                       
HET     ZN  K 502       1                                                       
HET     ZN  L 501       1                                                       
HET     ZN  L 502       1                                                       
HETNAM      ZN ZINC ION                                                         
FORMUL  12   ZN    10(ZN 2+)                                                    
HELIX    1   1 PRO A   10  GLY A   25  1                                  16    
HELIX    2   2 ASP A   99  SER A  102  5                                   4    
HELIX    3   3 ILE A  103  LYS A  108  1                                   6    
HELIX    4   4 SER A  114  MET A  127  1                                  14    
HELIX    5   5 SER A  128  LYS A  133  1                                   6    
HELIX    6   6 PRO B    5  GLU B   18  1                                  14    
HELIX    7   7 LEU B   88  LYS B   92  5                                   5    
HELIX    8   8 GLN B  100  ALA B  114  1                                  15    
HELIX    9   9 ASP B  124  ASN B  132  1                                   9    
HELIX   10  10 ASN B  132  ALA B  148  1                                  17    
HELIX   11  11 MET C  393  LEU C  397  1                                   5    
HELIX   12  12 SER C  424  LYS C  434  1                                  11    
HELIX   13  13 SER C  450  ASN C  462  1                                  13    
HELIX   14  14 SER C  465  ARG C  483  1                                  19    
HELIX   15  15 PRO E   10  GLY E   25  1                                  16    
HELIX   16  16 ASP E   99  SER E  102  5                                   4    
HELIX   17  17 ILE E  103  LYS E  108  1                                   6    
HELIX   18  18 SER E  114  MET E  127  1                                  14    
HELIX   19  19 SER E  128  LYS E  133  1                                   6    
HELIX   20  20 PRO F    5  GLU F   18  1                                  14    
HELIX   21  21 LEU F   88  LYS F   92  5                                   5    
HELIX   22  22 GLN F  100  ALA F  114  1                                  15    
HELIX   23  23 ASP F  124  ASN F  132  1                                   9    
HELIX   24  24 ASN F  132  ALA F  148  1                                  17    
HELIX   25  25 GLU G  346  LEU G  401  1                                  56    
HELIX   26  26 SER G  424  MET G  431  1                                   8    
HELIX   27  27 SER G  450  ASN G  462  1                                  13    
HELIX   28  28 SER G  465  ARG G  483  1                                  19    
HELIX   29  29 GLU H  343  LEU H  397  1                                  55    
HELIX   30  30 SER H  424  LYS H  434  1                                  11    
HELIX   31  31 SER H  450  ASN H  462  1                                  13    
HELIX   32  32 SER H  465  ARG H  483  1                                  19    
HELIX   33  33 PRO I   10  GLY I   25  1                                  16    
HELIX   34  34 ASP I   99  SER I  102  5                                   4    
HELIX   35  35 ILE I  103  LYS I  108  1                                   6    
HELIX   36  36 SER I  114  MET I  127  1                                  14    
HELIX   37  37 SER I  128  LYS I  133  1                                   6    
HELIX   38  38 PRO J    5  GLU J   18  1                                  14    
HELIX   39  39 LEU J   88  LYS J   92  5                                   5    
HELIX   40  40 GLN J  100  ALA J  114  1                                  15    
HELIX   41  41 ASP J  124  ASN J  132  1                                   9    
HELIX   42  42 ASN J  132  ALA J  148  1                                  17    
HELIX   43  43 GLU K  346  LEU K  401  1                                  56    
HELIX   44  44 SER K  424  MET K  431  1                                   8    
HELIX   45  45 SER K  450  ASN K  462  1                                  13    
HELIX   46  46 SER K  465  ARG K  483  1                                  19    
HELIX   47  47 GLU L  343  ASN L  394  1                                  52    
HELIX   48  48 SER L  424  LYS L  434  1                                  11    
HELIX   49  49 SER L  450  ASN L  462  1                                  13    
HELIX   50  50 SER L  465  ARG L  483  1                                  19    
SHEET    1   A 4 VAL A  31  LEU A  35  0                                        
SHEET    2   A 4 ARG A  45  ILE A  51 -1  O  THR A  47   N  GLY A  34           
SHEET    3   A 4 ILE A  62  GLU A  68 -1  O  TYR A  63   N  ILE A  50           
SHEET    4   A 4 SER A  79  PHE A  82 -1  O  SER A  79   N  GLU A  68           
SHEET    1   B 4 ILE B  23  PRO B  27  0                                        
SHEET    2   B 4 TYR B  34  ALA B  40 -1  O  HIS B  36   N  GLU B  26           
SHEET    3   B 4 THR B  51  PHE B  57 -1  O  LEU B  56   N  PHE B  35           
SHEET    4   B 4 LYS B  68  PHE B  71 -1  O  LYS B  68   N  PHE B  57           
SHEET    1   C 3 SER C 421  CYS C 423  0                                        
SHEET    2   C 3 ALA C 413  LEU C 416 -1  N  VAL C 414   O  PHE C 422           
SHEET    3   C 3 LYS C 447  TYR C 449 -1  O  THR C 448   N  THR C 415           
SHEET    1   D 4 VAL E  31  LEU E  35  0                                        
SHEET    2   D 4 ARG E  45  ILE E  51 -1  O  THR E  47   N  GLY E  34           
SHEET    3   D 4 ILE E  62  GLU E  68 -1  O  TYR E  63   N  ILE E  50           
SHEET    4   D 4 SER E  79  PHE E  82 -1  O  SER E  79   N  GLU E  68           
SHEET    1   E 4 ILE F  23  PRO F  27  0                                        
SHEET    2   E 4 TYR F  34  ALA F  40 -1  O  HIS F  36   N  GLU F  26           
SHEET    3   E 4 THR F  51  PHE F  57 -1  O  LEU F  56   N  PHE F  35           
SHEET    4   E 4 LYS F  68  PHE F  71 -1  O  LYS F  68   N  PHE F  57           
SHEET    1   F 3 SER G 421  CYS G 423  0                                        
SHEET    2   F 3 ALA G 413  LEU G 416 -1  N  VAL G 414   O  PHE G 422           
SHEET    3   F 3 LYS G 447  TYR G 449 -1  O  THR G 448   N  THR G 415           
SHEET    1   G 3 SER H 421  CYS H 423  0                                        
SHEET    2   G 3 ALA H 413  LEU H 416 -1  N  VAL H 414   O  PHE H 422           
SHEET    3   G 3 LYS H 447  TYR H 449 -1  O  THR H 448   N  THR H 415           
SHEET    1   H 4 VAL I  31  LEU I  35  0                                        
SHEET    2   H 4 ARG I  45  ILE I  51 -1  O  THR I  47   N  GLY I  34           
SHEET    3   H 4 ILE I  62  GLU I  68 -1  O  TYR I  63   N  ILE I  50           
SHEET    4   H 4 SER I  79  PHE I  82 -1  O  SER I  79   N  GLU I  68           
SHEET    1   I 4 ILE J  23  PRO J  27  0                                        
SHEET    2   I 4 TYR J  34  ALA J  40 -1  O  HIS J  36   N  GLU J  26           
SHEET    3   I 4 THR J  51  PHE J  57 -1  O  LEU J  56   N  PHE J  35           
SHEET    4   I 4 LYS J  68  PHE J  71 -1  O  LYS J  68   N  PHE J  57           
SHEET    1   J 3 SER K 421  CYS K 423  0                                        
SHEET    2   J 3 ALA K 413  LEU K 416 -1  N  VAL K 414   O  PHE K 422           
SHEET    3   J 3 LYS K 447  TYR K 449 -1  O  THR K 448   N  THR K 415           
SHEET    1   K 3 SER L 421  CYS L 423  0                                        
SHEET    2   K 3 ALA L 413  LEU L 416 -1  N  VAL L 414   O  PHE L 422           
SHEET    3   K 3 LYS L 447  TYR L 449 -1  O  THR L 448   N  THR L 415           
LINK         ND1 HIS K 420                ZN    ZN K 501     1555   1555  2.07  
LINK         ND1 HIS G 420                ZN    ZN G 501     1555   1555  2.07  
LINK         ND1 HIS C 420                ZN    ZN C 501     1555   1555  2.22  
LINK         ND1 HIS L 420                ZN    ZN L 501     1555   1555  2.22  
LINK         ND1 HIS H 420                ZN    ZN H 501     1555   1555  2.22  
LINK         SG  CYS H 418                ZN    ZN H 501     1555   1555  2.23  
LINK         SG  CYS C 418                ZN    ZN C 501     1555   1555  2.23  
LINK         SG  CYS L 418                ZN    ZN L 501     1555   1555  2.23  
LINK         SG  CYS L 440                ZN    ZN L 501     1555   1555  2.24  
LINK         SG  CYS C 440                ZN    ZN C 501     1555   1555  2.24  
LINK         SG  CYS H 440                ZN    ZN H 501     1555   1555  2.24  
LINK         SG  CYS C 426                ZN    ZN C 502     1555   1555  2.28  
LINK         SG  CYS H 426                ZN    ZN H 502     1555   1555  2.28  
LINK         SG  CYS L 426                ZN    ZN L 502     1555   1555  2.28  
LINK         SG  CYS K 440                ZN    ZN K 501     1555   1555  2.30  
LINK         SG  CYS G 440                ZN    ZN G 501     1555   1555  2.30  
LINK         SG  CYS G 418                ZN    ZN G 501     1555   1555  2.30  
LINK         SG  CYS K 418                ZN    ZN K 501     1555   1555  2.30  
LINK         SG  CYS C 406                ZN    ZN C 502     1555   1555  2.31  
LINK         SG  CYS H 406                ZN    ZN H 502     1555   1555  2.31  
LINK         SG  CYS L 406                ZN    ZN L 502     1555   1555  2.31  
LINK         SG  CYS G 437                ZN    ZN G 501     1555   1555  2.32  
LINK         SG  CYS K 437                ZN    ZN K 501     1555   1555  2.32  
LINK         SG  CYS L 437                ZN    ZN L 501     1555   1555  2.32  
LINK         SG  CYS H 437                ZN    ZN H 501     1555   1555  2.32  
LINK         SG  CYS C 437                ZN    ZN C 501     1555   1555  2.32  
LINK         SG  CYS K 426                ZN    ZN K 502     1555   1555  2.32  
LINK         SG  CYS G 426                ZN    ZN G 502     1555   1555  2.32  
LINK         SG  CYS K 406                ZN    ZN K 502     1555   1555  2.32  
LINK         SG  CYS G 406                ZN    ZN G 502     1555   1555  2.32  
LINK         SG  CYS L 403                ZN    ZN L 502     1555   1555  2.33  
LINK         SG  CYS H 403                ZN    ZN H 502     1555   1555  2.33  
LINK         SG  CYS C 403                ZN    ZN C 502     1555   1555  2.33  
LINK         SG  CYS H 423                ZN    ZN H 502     1555   1555  2.35  
LINK         SG  CYS L 423                ZN    ZN L 502     1555   1555  2.35  
LINK         SG  CYS C 423                ZN    ZN C 502     1555   1555  2.35  
LINK         SG  CYS G 423                ZN    ZN G 502     1555   1555  2.39  
LINK         SG  CYS K 423                ZN    ZN K 502     1555   1555  2.39  
LINK         SG  CYS K 403                ZN    ZN K 502     1555   1555  2.40  
LINK         SG  CYS G 403                ZN    ZN G 502     1555   1555  2.40  
CISPEP   1 TYR A   73    PRO A   74          0        -0.72                     
CISPEP   2 TYR B   62    PRO B   63          0         9.57                     
CISPEP   3 TYR E   73    PRO E   74          0        -0.72                     
CISPEP   4 TYR F   62    PRO F   63          0         9.51                     
CISPEP   5 TYR I   73    PRO I   74          0        -0.77                     
CISPEP   6 TYR J   62    PRO J   63          0         9.41                     
SITE     1 AC1  4 CYS C 418  HIS C 420  CYS C 437  CYS C 440                    
SITE     1 AC2  4 CYS C 403  CYS C 406  CYS C 423  CYS C 426                    
SITE     1 AC3  4 CYS G 418  HIS G 420  CYS G 437  CYS G 440                    
SITE     1 AC4  4 CYS G 403  CYS G 406  CYS G 423  CYS G 426                    
SITE     1 AC5  4 CYS H 418  HIS H 420  CYS H 437  CYS H 440                    
SITE     1 AC6  4 CYS H 403  CYS H 406  CYS H 423  CYS H 426                    
SITE     1 AC7  4 CYS K 418  HIS K 420  CYS K 437  CYS K 440                    
SITE     1 AC8  4 CYS K 403  CYS K 406  CYS K 423  CYS K 426                    
SITE     1 AC9  4 CYS L 418  HIS L 420  CYS L 437  CYS L 440                    
SITE     1 BC1  4 CYS L 403  CYS L 406  CYS L 423  CYS L 426                    
CRYST1  205.258  205.258  235.372  90.00  90.00  90.00 P 42 21 2    40          
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      0.004872  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.004872  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004249        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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