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Database: PDB
Entry: 3PXE
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HEADER    PROTEIN BINDING                         09-DEC-10   3PXE              
TITLE     IMPACT OF BRCA1 BRCT DOMAIN MISSENSE SUBSTITUTIONS ON PHOSPHO-PEPTIDE 
TITLE    2 RECOGNITION: E1836K                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: BRCT DOMAIN, UNP RESIDUES 1646-1859;                       
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MUTATION: YES;                                                       
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: PHOSPHO PEPTIDE;                                           
COMPND  11 CHAIN: E, F, G, H;                                                   
COMPND  12 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: BRCA1, RNF53;                                                  
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: PLM1;                                     
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: PEPTIDE DERIVED FROM BRCA1 PARTNER BACH1.             
KEYWDS    BRCA1 PROTEIN, MISSENSE, PROTEIN BINDING, PHOSPHOPEPTIDE RECOGNITION, 
KEYWDS   2 BRCT DOMAIN, PHOSPHO-PEPTIDE BINDING, NUCLEAR PROTEIN                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,R.GREEN,J.N.M.GLOVER                                       
REVDAT   3   08-NOV-17 3PXE    1       REMARK                                   
REVDAT   2   15-JUN-11 3PXE    1       JRNL                                     
REVDAT   1   20-APR-11 3PXE    0                                                
JRNL        AUTH   N.COQUELLE,R.GREEN,J.N.GLOVER                                
JRNL        TITL   IMPACT OF BRCA1 BRCT DOMAIN MISSENSE SUBSTITUTIONS ON        
JRNL        TITL 2 PHOSPHOPEPTIDE RECOGNITION.                                  
JRNL        REF    BIOCHEMISTRY                  V.  50  4579 2011              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   21473589                                                     
JRNL        DOI    10.1021/BI2003795                                            
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.S.LEE,R.GREEN,S.M.MARSILLAC,N.COQUELLE,R.S.WILLIAMS,       
REMARK   1  AUTH 2 T.YEUNG,D.FOO,D.D.HAU,B.HUI,A.N.MONTEIRO,J.N.GLOVER          
REMARK   1  TITL   COMPREHENSIVE ANALYSIS OF MISSENSE VARIATIONS IN THE BRCT    
REMARK   1  TITL 2 DOMAIN OF BRCA1 BY STRUCTURAL AND FUNCTIONAL ASSAYS.         
REMARK   1  REF    CANCER RES.                   V.  70  4880 2010              
REMARK   1  REFN                   ISSN 0008-5472                               
REMARK   1  PMID   20516115                                                     
REMARK   1  DOI    10.1158/0008-5472.CAN-09-4563                                
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   R.S.WILLIAMS,M.S.LEE,D.D.HAU,J.N.GLOVER                      
REMARK   1  TITL   STRUCTURAL BASIS OF PHOSPHOPEPTIDE RECOGNITION BY THE BRCT   
REMARK   1  TITL 2 DOMAIN OF BRCA1.                                             
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  11   519 2004              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1  PMID   15133503                                                     
REMARK   1  DOI    10.1038/NSMB776                                              
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   J.A.CLAPPERTON,I.A.MANKE,D.M.LOWERY,T.HO,L.F.HAIRE,          
REMARK   1  AUTH 2 M.B.YAFFE,S.J.SMERDON                                        
REMARK   1  TITL   STRUCTURE AND MECHANISM OF BRCA1 BRCT DOMAIN RECOGNITION OF  
REMARK   1  TITL 2 PHOSPHORYLATED BACH1 WITH IMPLICATIONS FOR CANCER.           
REMARK   1  REF    NAT.STRUCT.MOL.BIOL.          V.  11   512 2004              
REMARK   1  REFN                   ISSN 1545-9993                               
REMARK   1  PMID   15133502                                                     
REMARK   1  DOI    10.1038/NSMB775                                              
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   R.S.WILLIAMS,J.N.GLOVER                                      
REMARK   1  TITL   STRUCTURAL CONSEQUENCES OF A CANCER-CAUSING BRCA1-BRCT       
REMARK   1  TITL 2 MISSENSE MUTATION.                                           
REMARK   1  REF    J.BIOL.CHEM.                  V. 278  2630 2003              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1  PMID   12427738                                                     
REMARK   1  DOI    10.1074/JBC.M210019200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.85 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.6.3_473)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.85                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.36                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.990                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 31205                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.223                           
REMARK   3   R VALUE            (WORKING SET) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.266                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1561                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 44.3683 -  6.3330    0.97     2861   151  0.2006 0.2307        
REMARK   3     2  6.3330 -  5.0289    0.97     2742   145  0.2015 0.2632        
REMARK   3     3  5.0289 -  4.3939    0.98     2752   144  0.1638 0.2204        
REMARK   3     4  4.3939 -  3.9924    0.98     2729   144  0.1881 0.2393        
REMARK   3     5  3.9924 -  3.7064    0.97     2728   144  0.2121 0.2522        
REMARK   3     6  3.7064 -  3.4880    0.98     2718   143  0.2309 0.2922        
REMARK   3     7  3.4880 -  3.3134    0.97     2708   142  0.2572 0.2524        
REMARK   3     8  3.3134 -  3.1692    0.98     2725   144  0.2846 0.3746        
REMARK   3     9  3.1692 -  3.0472    0.98     2686   141  0.3043 0.3448        
REMARK   3    10  3.0472 -  2.9421    0.97     2702   143  0.3436 0.4058        
REMARK   3    11  2.9421 -  2.8501    0.83     2293   120  0.3577 0.3909        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.00                                          
REMARK   3   SHRINKAGE RADIUS   : 0.72                                          
REMARK   3   K_SOL              : 0.33                                          
REMARK   3   B_SOL              : 52.02                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.440            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.710           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 38.44330                                             
REMARK   3    B22 (A**2) : -16.31900                                            
REMARK   3    B33 (A**2) : -22.12430                                            
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           6979                                  
REMARK   3   ANGLE     :  1.078           9492                                  
REMARK   3   CHIRALITY :  0.068           1074                                  
REMARK   3   PLANARITY :  0.005           1199                                  
REMARK   3   DIHEDRAL  : 14.970           2485                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 20                                         
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1647:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -1.6773 -14.8793 -39.3337              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2634 T22:   0.4515                                     
REMARK   3      T33:   0.2329 T12:  -0.1033                                     
REMARK   3      T13:   0.0403 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3028 L22:   1.3123                                     
REMARK   3      L33:   1.9895 L12:   0.5831                                     
REMARK   3      L13:   1.2694 L23:   0.2541                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1136 S12:   0.3407 S13:  -0.0881                       
REMARK   3      S21:   0.0269 S22:   0.0403 S23:   0.0216                       
REMARK   3      S31:  -0.0745 S32:  -0.1820 S33:  -0.0008                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A):   3.1192 -15.9708 -28.0535              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5367 T22:   0.4897                                     
REMARK   3      T33:   0.4486 T12:  -0.1299                                     
REMARK   3      T13:  -0.0194 T23:   0.0372                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.5662 L22:   2.8368                                     
REMARK   3      L33:   1.2751 L12:  -1.2492                                     
REMARK   3      L13:   0.6214 L23:   0.0361                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0650 S12:  -0.0218 S13:  -0.1038                       
REMARK   3      S21:   0.7496 S22:  -0.1147 S23:   0.0428                       
REMARK   3      S31:   0.3672 S32:   0.0874 S33:   0.0003                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.5752  -9.5731 -20.7660              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7460 T22:   0.7890                                     
REMARK   3      T33:   0.6989 T12:  -0.1058                                     
REMARK   3      T13:  -0.0310 T23:   0.0141                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0348 L22:   0.2588                                     
REMARK   3      L33:   0.2082 L12:   0.0019                                     
REMARK   3      L13:   0.0855 L23:  -0.1511                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1882 S12:  -0.3446 S13:   0.0421                       
REMARK   3      S21:   1.8967 S22:  -0.0054 S23:   0.0925                       
REMARK   3      S31:   0.6444 S32:  -0.1774 S33:  -0.0030                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.4051   2.2735 -35.2009              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4841 T22:   0.4705                                     
REMARK   3      T33:   0.6843 T12:  -0.0388                                     
REMARK   3      T13:  -0.0596 T23:   0.1423                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2656 L22:   2.5597                                     
REMARK   3      L33:   1.5851 L12:   0.0306                                     
REMARK   3      L13:   1.6050 L23:  -0.1421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1953 S12:   0.4214 S13:   0.7953                       
REMARK   3      S21:  -0.3905 S22:  -0.1901 S23:  -0.4249                       
REMARK   3      S31:  -0.4476 S32:   0.1360 S33:   0.0003                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A):  29.5737  -2.0627 -31.1902              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.0746 T22:   0.1113                                     
REMARK   3      T33:   0.3317 T12:  -0.1013                                     
REMARK   3      T13:  -0.3610 T23:   0.1286                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2470 L22:   1.4107                                     
REMARK   3      L33:   1.9685 L12:   1.2537                                     
REMARK   3      L13:   1.7217 L23:   0.4791                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.8477 S12:   0.1861 S13:   0.6863                       
REMARK   3      S21:   0.3193 S22:  -0.4198 S23:  -0.9941                       
REMARK   3      S31:  -0.6063 S32:   0.4225 S33:   0.0121                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1647:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.4145  14.7510   5.4919              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6179 T22:   0.4507                                     
REMARK   3      T33:   0.4295 T12:   0.0610                                     
REMARK   3      T13:  -0.0442 T23:   0.0399                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8679 L22:   1.4259                                     
REMARK   3      L33:   1.9253 L12:   0.7926                                     
REMARK   3      L13:  -0.2478 L23:   0.0961                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0691 S12:  -0.0985 S13:  -0.1608                       
REMARK   3      S21:   0.2146 S22:  -0.1658 S23:   0.1348                       
REMARK   3      S31:   0.0016 S32:  -0.4118 S33:   0.0001                       
REMARK   3   TLS GROUP : 7                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.0935  17.5484  -2.4608              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2621 T22:   0.3177                                     
REMARK   3      T33:   0.3399 T12:  -0.0150                                     
REMARK   3      T13:  -0.0950 T23:  -0.0092                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3985 L22:   1.3906                                     
REMARK   3      L33:   1.5082 L12:  -0.9719                                     
REMARK   3      L13:   0.1659 L23:  -1.2470                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1042 S12:  -0.0838 S13:   0.3499                       
REMARK   3      S21:   0.2348 S22:  -0.2288 S23:  -0.2640                       
REMARK   3      S31:  -0.6188 S32:   0.0435 S33:   0.0002                       
REMARK   3   TLS GROUP : 8                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.0820  19.1308 -14.1841              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6186 T22:   0.7704                                     
REMARK   3      T33:   0.6032 T12:  -0.0264                                     
REMARK   3      T13:   0.0139 T23:   0.0525                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3094 L22:   0.3110                                     
REMARK   3      L33:   0.2886 L12:   0.2923                                     
REMARK   3      L13:  -0.1013 L23:   0.0106                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0269 S12:   0.0171 S13:   0.5525                       
REMARK   3      S21:  -0.4168 S22:  -0.6480 S23:  -0.2143                       
REMARK   3      S31:  -0.2842 S32:   0.7142 S33:  -0.0024                       
REMARK   3   TLS GROUP : 9                                                      
REMARK   3    SELECTION: CHAIN B AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A): -18.8668   7.8969 -20.6256              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4566 T22:   0.6225                                     
REMARK   3      T33:   0.3790 T12:   0.0726                                     
REMARK   3      T13:  -0.1056 T23:  -0.0430                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.3305 L22:   3.0447                                     
REMARK   3      L33:   2.2489 L12:   1.6568                                     
REMARK   3      L13:  -0.1561 L23:   1.1525                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1654 S12:   0.0156 S13:  -0.0032                       
REMARK   3      S21:  -0.3436 S22:  -0.2556 S23:   0.3728                       
REMARK   3      S31:  -0.7081 S32:  -0.7656 S33:   0.0003                       
REMARK   3   TLS GROUP : 10                                                     
REMARK   3    SELECTION: CHAIN B AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A): -11.3718   0.8201 -26.4148              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2716 T22:   0.3757                                     
REMARK   3      T33:   0.1400 T12:  -0.0611                                     
REMARK   3      T13:  -0.1006 T23:  -0.0210                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.2593 L22:   2.2473                                     
REMARK   3      L33:   3.7518 L12:  -0.3806                                     
REMARK   3      L13:  -0.5208 L23:   1.3455                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0146 S12:   0.4318 S13:   0.0550                       
REMARK   3      S21:  -0.1386 S22:  -0.1680 S23:   0.3690                       
REMARK   3      S31:   0.8122 S32:  -0.0163 S33:   0.0004                       
REMARK   3   TLS GROUP : 11                                                     
REMARK   3    SELECTION: CHAIN C AND RESID 1647:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.5352  57.8826 -27.7166              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4891 T22:   0.5573                                     
REMARK   3      T33:   0.8181 T12:   0.0006                                     
REMARK   3      T13:  -0.0491 T23:   0.0823                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.2211 L22:   1.2642                                     
REMARK   3      L33:   1.6844 L12:   0.8349                                     
REMARK   3      L13:   0.8230 L23:  -0.1876                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0610 S12:   0.1680 S13:   0.3413                       
REMARK   3      S21:  -0.0717 S22:  -0.1777 S23:  -0.3963                       
REMARK   3      S31:  -0.0974 S32:   0.4828 S33:   0.0004                       
REMARK   3   TLS GROUP : 12                                                     
REMARK   3    SELECTION: CHAIN C AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A): -12.6060  47.7789 -30.3615              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6371 T22:   0.4366                                     
REMARK   3      T33:   0.4986 T12:   0.1054                                     
REMARK   3      T13:  -0.0551 T23:   0.0803                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.0944 L22:   1.2961                                     
REMARK   3      L33:   0.5891 L12:   0.8202                                     
REMARK   3      L13:  -0.2404 L23:   0.4554                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0434 S12:   0.5702 S13:  -0.0741                       
REMARK   3      S21:  -0.0713 S22:   0.0131 S23:  -0.4803                       
REMARK   3      S31:   0.6330 S32:   0.0656 S33:  -0.0001                       
REMARK   3   TLS GROUP : 13                                                     
REMARK   3    SELECTION: CHAIN C AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A): -20.9111  40.8968 -26.1356              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9442 T22:   0.7491                                     
REMARK   3      T33:   1.0180 T12:  -0.1727                                     
REMARK   3      T13:  -0.2114 T23:   0.0671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4355 L22:   0.2640                                     
REMARK   3      L33:   0.2819 L12:   0.0857                                     
REMARK   3      L13:   0.2502 L23:  -0.1281                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0803 S12:   0.5660 S13:  -0.2949                       
REMARK   3      S21:  -1.7699 S22:   0.0738 S23:   0.5805                       
REMARK   3      S31:   1.4220 S32:  -0.2590 S33:  -0.0026                       
REMARK   3   TLS GROUP : 14                                                     
REMARK   3    SELECTION: CHAIN C AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A): -19.4709  46.2222  -5.7950              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8591 T22:   0.4783                                     
REMARK   3      T33:   0.6544 T12:   0.0990                                     
REMARK   3      T13:  -0.2039 T23:   0.0100                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.0173 L22:   3.4495                                     
REMARK   3      L33:   2.9875 L12:   0.3356                                     
REMARK   3      L13:   0.6301 L23:   0.3575                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4440 S12:  -0.1957 S13:   0.4404                       
REMARK   3      S21:   1.0922 S22:   0.4864 S23:   0.0130                       
REMARK   3      S31:  -0.2797 S32:  -0.2161 S33:  -0.0002                       
REMARK   3   TLS GROUP : 15                                                     
REMARK   3    SELECTION: CHAIN C AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A): -16.7407  34.7513  -3.7858              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9696 T22:   0.4820                                     
REMARK   3      T33:   0.5365 T12:   0.1402                                     
REMARK   3      T13:  -0.1576 T23:  -0.0422                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6411 L22:   4.0776                                     
REMARK   3      L33:   2.6738 L12:   0.8895                                     
REMARK   3      L13:  -1.1841 L23:  -1.0153                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.5225 S12:  -0.5167 S13:   0.0957                       
REMARK   3      S21:   0.8149 S22:   0.2775 S23:  -0.1150                       
REMARK   3      S31:   0.1545 S32:  -0.4199 S33:   0.0008                       
REMARK   3   TLS GROUP : 16                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1649:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A):   2.2541  68.2059  20.7678              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0010 T22:   0.6960                                     
REMARK   3      T33:   1.2792 T12:   0.0372                                     
REMARK   3      T13:   0.1536 T23:   0.2394                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.3390 L22:   1.1757                                     
REMARK   3      L33:   1.1302 L12:  -1.1552                                     
REMARK   3      L13:  -0.9455 L23:   0.4517                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1551 S12:   0.3844 S13:   0.8225                       
REMARK   3      S21:   0.2797 S22:  -0.4164 S23:  -0.8382                       
REMARK   3      S31:  -0.8194 S32:   0.2810 S33:   0.0016                       
REMARK   3   TLS GROUP : 17                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0245  58.3286  18.8782              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4388 T22:   0.7305                                     
REMARK   3      T33:   1.4019 T12:   0.0589                                     
REMARK   3      T13:   0.3669 T23:   0.2504                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5031 L22:   0.3431                                     
REMARK   3      L33:  -0.0310 L12:   0.4981                                     
REMARK   3      L13:  -0.2414 L23:  -0.1076                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2583 S12:   0.2528 S13:   0.4117                       
REMARK   3      S21:  -0.3169 S22:   0.0669 S23:  -0.9138                       
REMARK   3      S31:  -0.6527 S32:   0.6805 S33:  -0.0004                       
REMARK   3   TLS GROUP : 18                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.1666  46.7506  17.5392              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.9681 T22:   0.9860                                     
REMARK   3      T33:   1.3659 T12:   0.1728                                     
REMARK   3      T13:   0.4075 T23:   0.0745                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0689 L22:   0.1318                                     
REMARK   3      L33:   0.1818 L12:  -0.0811                                     
REMARK   3      L13:  -0.1229 L23:   0.1552                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1368 S12:  -0.0486 S13:   0.6133                       
REMARK   3      S21:  -0.7706 S22:   0.0829 S23:  -1.9651                       
REMARK   3      S31:  -0.6983 S32:   0.6950 S33:   0.0047                       
REMARK   3   TLS GROUP : 19                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A): -10.6150  45.0570  24.7639              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4292 T22:   0.5615                                     
REMARK   3      T33:   0.9446 T12:   0.0476                                     
REMARK   3      T13:   0.1588 T23:  -0.1671                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.6277 L22:   2.9636                                     
REMARK   3      L33:   0.8624 L12:  -0.5075                                     
REMARK   3      L13:   1.4524 L23:  -0.4077                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1349 S12:   0.0922 S13:  -0.1284                       
REMARK   3      S21:   0.0376 S22:  -0.5240 S23:   0.8454                       
REMARK   3      S31:  -0.2094 S32:  -0.7218 S33:  -0.0011                       
REMARK   3   TLS GROUP : 20                                                     
REMARK   3    SELECTION: CHAIN D AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.6822  36.8307  32.6916              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8642 T22:   0.5303                                     
REMARK   3      T33:   0.9431 T12:   0.0239                                     
REMARK   3      T13:   0.4737 T23:  -0.0781                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.7695 L22:   1.9470                                     
REMARK   3      L33:   1.3694 L12:  -1.7482                                     
REMARK   3      L13:   1.1836 L23:  -0.7218                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4198 S12:   0.0082 S13:  -0.8157                       
REMARK   3      S21:   1.2075 S22:  -0.2077 S23:   0.7212                       
REMARK   3      S31:   0.5557 S32:  -0.5009 S33:  -0.0009                       
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 3PXE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 14-DEC-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000062929.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : CLSI                               
REMARK 200  BEAMLINE                       : 08ID-1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97949                            
REMARK 200  MONOCHROMATOR                  : SI(111)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 31218                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.850                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.370                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.1                               
REMARK 200  DATA REDUNDANCY                : 4.400                              
REMARK 200  R MERGE                    (I) : 0.05800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 17.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.85                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 73.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1N5O                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 63.09                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.33                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 50MM MES 0.15M (NH4)2SO4 26% PEG 8000,   
REMARK 280  PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.42000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.42000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       57.91000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       65.52500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       57.91000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       65.52500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       90.42000            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       57.91000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       65.52500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       90.42000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       57.91000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       65.52500            
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, 4                                              
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 900 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, E                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 820 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11140 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 750 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -9.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, G                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 780 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 10540 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, 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 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     VAL A  1646                                                      
REMARK 465     THR A  1802                                                      
REMARK 465     GLY A  1803                                                      
REMARK 465     VAL B  1646                                                      
REMARK 465     VAL C  1646                                                      
REMARK 465     GLY C  1803                                                      
REMARK 465     VAL C  1804                                                      
REMARK 465     VAL D  1646                                                      
REMARK 465     ASN D  1647                                                      
REMARK 465     LYS D  1648                                                      
REMARK 465     PHE D  1798                                                      
REMARK 465     THR D  1799                                                      
REMARK 465     LEU D  1800                                                      
REMARK 465     GLY D  1801                                                      
REMARK 465     THR D  1802                                                      
REMARK 465     SER E     1                                                      
REMARK 465     ARG E     2                                                      
REMARK 465     LYS E    10                                                      
REMARK 465     SER F     1                                                      
REMARK 465     ARG F     2                                                      
REMARK 465     SER F     3                                                      
REMARK 465     THR F     4                                                      
REMARK 465     LYS F    10                                                      
REMARK 465     SER G     1                                                      
REMARK 465     ARG G     2                                                      
REMARK 465     SER G     3                                                      
REMARK 465     LYS G    10                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ARG H     2                                                      
REMARK 465     SER H     3                                                      
REMARK 465     LYS H    10                                                      
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     ARG A1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A1817    CG   CD   OE1  OE2                                  
REMARK 470     GLU A1849    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1851    CG   OD1  OD2                                       
REMARK 470     ARG B1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1694    CG   CD   OE1  OE2                                  
REMARK 470     LYS B1727    CG   CD   CE   NZ                                   
REMARK 470     ARG B1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG B1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1793    CG   CD   CE   NZ                                   
REMARK 470     GLU B1849    CG   CD   OE1  OE2                                  
REMARK 470     ARG C1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1724    CG   CD   CE   NZ                                   
REMARK 470     ARG C1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG C1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS C1750    CG   CD   CE   NZ                                   
REMARK 470     ARG C1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP C1851    CG   OD1  OD2                                       
REMARK 470     ARG D1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG D1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1750    CG   CD   CE   NZ                                   
REMARK 470     ARG D1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D1817    CG   CD   OE1  OE2                                  
REMARK 470     GLU D1829    CG   CD   OE1  OE2                                  
REMARK 470     LYS D1836    CG   CD   CE   NZ                                   
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 A1648      141.60    175.61                                   
REMARK 500    HIS A1673       38.09     70.06                                   
REMARK 500    ARG A1726       16.55     54.26                                   
REMARK 500    VAL A1740        4.91    -62.00                                   
REMARK 500    ASN A1745       63.95   -156.30                                   
REMARK 500    MET A1775      108.54   -161.38                                   
REMARK 500    THR A1816      -73.20    -50.12                                   
REMARK 500    CYS A1828      139.17   -178.23                                   
REMARK 500    TYR A1845       54.30     34.41                                   
REMARK 500    MET B1775       99.48   -169.13                                   
REMARK 500    THR B1802     -174.93    -55.83                                   
REMARK 500    ALA B1814        2.55    -66.61                                   
REMARK 500    ASP B1851      -67.48    -26.37                                   
REMARK 500    ASN C1745       40.69   -149.17                                   
REMARK 500    CYS C1828      139.12    178.23                                   
REMARK 500    TYR C1845       42.83     30.29                                   
REMARK 500    ASP C1851      -48.63    -27.37                                   
REMARK 500    ARG D1726       -1.84     59.42                                   
REMARK 500    ASN D1745       53.13   -152.97                                   
REMARK 500    ILE D1760      -42.07    -21.44                                   
REMARK 500    MET D1775       97.65   -170.79                                   
REMARK 500    CYS D1828      142.93   -177.04                                   
REMARK 500    TYR D1845       53.39     29.83                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1T2V   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T15   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1N5O   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 1T2U   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 2ING   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXA   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXD   RELATED DB: PDB                                   
DBREF  3PXE A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3PXE B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3PXE C 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3PXE D 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3PXE E    1    10  PDB    3PXE     3PXE             1     10             
DBREF  3PXE F    1    10  PDB    3PXE     3PXE             1     10             
DBREF  3PXE G    1    10  PDB    3PXE     3PXE             1     10             
DBREF  3PXE H    1    10  PDB    3PXE     3PXE             1     10             
SEQADV 3PXE LYS A 1836  UNP  P38398    GLU  1836 ENGINEERED MUTATION            
SEQADV 3PXE LYS B 1836  UNP  P38398    GLU  1836 ENGINEERED MUTATION            
SEQADV 3PXE LYS C 1836  UNP  P38398    GLU  1836 ENGINEERED MUTATION            
SEQADV 3PXE LYS D 1836  UNP  P38398    GLU  1836 ENGINEERED MUTATION            
SEQRES   1 A  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 A  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 A  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 A  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 A  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 A  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 A  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 A  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 A  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 A  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 A  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 A  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 A  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 A  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 A  214  CYS GLU ALA PRO VAL VAL THR ARG LYS TRP VAL LEU ASP          
SEQRES  16 A  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 A  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 B  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 B  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 B  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 B  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 B  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 B  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 B  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 B  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 B  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 B  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 B  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 B  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 B  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 B  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 B  214  CYS GLU ALA PRO VAL VAL THR ARG LYS TRP VAL LEU ASP          
SEQRES  16 B  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 B  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 C  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 C  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 C  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 C  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 C  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 C  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 C  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 C  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 C  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 C  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 C  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 C  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 C  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 C  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 C  214  CYS GLU ALA PRO VAL VAL THR ARG LYS TRP VAL LEU ASP          
SEQRES  16 C  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 C  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 D  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 D  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 D  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 D  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 D  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 D  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 D  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 D  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 D  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 D  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 D  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 D  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 D  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 D  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 D  214  CYS GLU ALA PRO VAL VAL THR ARG LYS TRP VAL LEU ASP          
SEQRES  16 D  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 D  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 E   10  SER ARG SER THR SEP PRO THR PHE ASN LYS                      
SEQRES   1 F   10  SER ARG SER THR SEP PRO THR PHE ASN LYS                      
SEQRES   1 G   10  SER ARG SER THR SEP PRO THR PHE ASN LYS                      
SEQRES   1 H   10  SER ARG SER THR SEP PRO THR PHE ASN LYS                      
MODRES 3PXE SEP E    5  SER  PHOSPHOSERINE                                      
MODRES 3PXE SEP F    5  SER  PHOSPHOSERINE                                      
MODRES 3PXE SEP G    5  SER  PHOSPHOSERINE                                      
MODRES 3PXE SEP H    5  SER  PHOSPHOSERINE                                      
HET    SEP  E   5      10                                                       
HET    SEP  F   5      10                                                       
HET    SEP  G   5      10                                                       
HET    SEP  H   5      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   5  SEP    4(C3 H8 N O6 P)                                              
FORMUL   9  HOH   *16(H2 O)                                                     
HELIX    1   1 THR A 1658  HIS A 1673  1                                  16    
HELIX    2   2 THR A 1700  GLY A 1709  1                                  10    
HELIX    3   3 TYR A 1716  GLU A 1725  1                                  10    
HELIX    4   4 ASN A 1730  GLU A 1735  5                                   6    
HELIX    5   5 GLN A 1747  SER A 1755  1                                   9    
HELIX    6   6 GLN A 1756  LYS A 1759  5                                   4    
HELIX    7   7 PRO A 1776  CYS A 1787  1                                  12    
HELIX    8   8 GLU A 1794  PHE A 1798  5                                   5    
HELIX    9   9 GLN A 1811  TRP A 1815  5                                   5    
HELIX   10  10 ASN A 1819  CYS A 1828  5                                  10    
HELIX   11  11 ARG A 1835  TYR A 1845  1                                  11    
HELIX   12  12 LEU A 1850  LEU A 1854  5                                   5    
HELIX   13  13 THR B 1658  HIS B 1672  1                                  15    
HELIX   14  14 THR B 1700  GLY B 1709  1                                  10    
HELIX   15  15 TYR B 1716  GLU B 1725  1                                  10    
HELIX   16  16 ASN B 1730  GLU B 1735  5                                   6    
HELIX   17  17 GLN B 1747  SER B 1755  1                                   9    
HELIX   18  18 GLN B 1756  ARG B 1758  5                                   3    
HELIX   19  19 PRO B 1776  CYS B 1787  1                                  12    
HELIX   20  20 GLN B 1811  TRP B 1815  5                                   5    
HELIX   21  21 ASN B 1819  HIS B 1822  5                                   4    
HELIX   22  22 ALA B 1823  CYS B 1828  1                                   6    
HELIX   23  23 ARG B 1835  TYR B 1845  1                                  11    
HELIX   24  24 GLU B 1849  LEU B 1854  5                                   6    
HELIX   25  25 THR C 1658  HIS C 1673  1                                  16    
HELIX   26  26 THR C 1700  GLY C 1709  1                                  10    
HELIX   27  27 TYR C 1716  GLU C 1725  1                                  10    
HELIX   28  28 ASN C 1730  GLU C 1735  5                                   6    
HELIX   29  29 GLN C 1747  GLN C 1756  1                                  10    
HELIX   30  30 PRO C 1776  CYS C 1787  1                                  12    
HELIX   31  31 ASN C 1819  CYS C 1828  5                                  10    
HELIX   32  32 ARG C 1835  LEU C 1844  1                                  10    
HELIX   33  33 LEU C 1850  LEU C 1854  5                                   5    
HELIX   34  34 THR D 1658  HIS D 1673  1                                  16    
HELIX   35  35 THR D 1700  GLY D 1709  1                                  10    
HELIX   36  36 TYR D 1716  GLU D 1725  1                                  10    
HELIX   37  37 GLN D 1747  SER D 1755  1                                   9    
HELIX   38  38 PRO D 1776  CYS D 1787  1                                  12    
HELIX   39  39 GLN D 1811  TRP D 1815  5                                   5    
HELIX   40  40 ASN D 1819  CYS D 1828  5                                  10    
HELIX   41  41 ARG D 1835  TYR D 1845  1                                  11    
HELIX   42  42 GLU D 1849  LEU D 1854  5                                   6    
SHEET    1   A 4 THR A1675  LEU A1676  0                                        
SHEET    2   A 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3   A 4 HIS A1686  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    4   A 4 TRP A1712  SER A1715  1  O  VAL A1714   N  MET A1689           
SHEET    1   B 2 VAL A1696  CYS A1697  0                                        
SHEET    2   B 2 GLY A1738  ASP A1739  1  O  GLY A1738   N  CYS A1697           
SHEET    1   C 4 SER A1790  VAL A1791  0                                        
SHEET    2   C 4 LEU A1764  CYS A1767  1  N  LEU A1764   O  SER A1790           
SHEET    3   C 4 HIS A1805  VAL A1810  1  O  HIS A1805   N  GLU A1765           
SHEET    4   C 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1810           
SHEET    1   D 4 THR B1675  LEU B1676  0                                        
SHEET    2   D 4 SER B1651  SER B1655  1  N  MET B1652   O  THR B1675           
SHEET    3   D 4 HIS B1686  MET B1689  1  O  VAL B1688   N  VAL B1653           
SHEET    4   D 4 TRP B1712  SER B1715  1  O  TRP B1712   N  VAL B1687           
SHEET    1   E 2 VAL B1696  CYS B1697  0                                        
SHEET    2   E 2 GLY B1738  ASP B1739  1  O  GLY B1738   N  CYS B1697           
SHEET    1   F 4 SER B1790  VAL B1791  0                                        
SHEET    2   F 4 LEU B1764  CYS B1768  1  N  LEU B1764   O  SER B1790           
SHEET    3   F 4 HIS B1805  VAL B1810  1  O  HIS B1805   N  GLU B1765           
SHEET    4   F 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SHEET    1   G 4 THR C1675  LEU C1676  0                                        
SHEET    2   G 4 SER C1651  SER C1655  1  N  MET C1652   O  THR C1675           
SHEET    3   G 4 HIS C1686  MET C1689  1  O  VAL C1688   N  VAL C1653           
SHEET    4   G 4 TRP C1712  SER C1715  1  O  TRP C1712   N  VAL C1687           
SHEET    1   H 2 VAL C1696  CYS C1697  0                                        
SHEET    2   H 2 GLY C1738  ASP C1739  1  O  GLY C1738   N  CYS C1697           
SHEET    1   I 4 SER C1790  VAL C1791  0                                        
SHEET    2   I 4 GLU C1765  CYS C1768  1  N  ILE C1766   O  SER C1790           
SHEET    3   I 4 PRO C1806  VAL C1810  1  O  ILE C1807   N  CYS C1767           
SHEET    4   I 4 VAL C1832  THR C1834  1  O  VAL C1833   N  VAL C1808           
SHEET    1   J 4 THR D1675  LEU D1676  0                                        
SHEET    2   J 4 SER D1651  SER D1655  1  N  MET D1652   O  THR D1675           
SHEET    3   J 4 HIS D1686  MET D1689  1  O  VAL D1688   N  VAL D1653           
SHEET    4   J 4 TRP D1712  SER D1715  1  O  VAL D1714   N  MET D1689           
SHEET    1   K 2 VAL D1696  CYS D1697  0                                        
SHEET    2   K 2 GLY D1738  ASP D1739  1  O  GLY D1738   N  CYS D1697           
SHEET    1   L 4 SER D1790  VAL D1791  0                                        
SHEET    2   L 4 LEU D1764  CYS D1768  1  N  ILE D1766   O  SER D1790           
SHEET    3   L 4 HIS D1805  VAL D1810  1  O  HIS D1805   N  GLU D1765           
SHEET    4   L 4 VAL D1832  THR D1834  1  O  VAL D1833   N  VAL D1808           
LINK         C   THR E   4                 N   SEP E   5     1555   1555  1.34  
LINK         C   SEP E   5                 N   PRO E   6     1555   1555  1.34  
LINK         C   SEP F   5                 N   PRO F   6     1555   1555  1.35  
LINK         C   THR G   4                 N   SEP G   5     1555   1555  1.33  
LINK         C   SEP G   5                 N   PRO G   6     1555   1555  1.34  
LINK         C   THR H   4                 N   SEP H   5     1555   1555  1.33  
LINK         C   SEP H   5                 N   PRO H   6     1555   1555  1.35  
CISPEP   1 GLY A 1770    PRO A 1771          0         8.10                     
CISPEP   2 GLY B 1770    PRO B 1771          0         4.03                     
CISPEP   3 GLY C 1770    PRO C 1771          0         8.20                     
CISPEP   4 GLY D 1770    PRO D 1771          0         1.66                     
CRYST1  115.820  131.050  180.840  90.00  90.00  90.00 C 2 2 21     32          
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      0.008634  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007631  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005530        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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