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Database: PDB
Entry: 3PXA
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Original site: 3PXA 
HEADER    PROTEIN BINDING                         09-DEC-10   3PXA              
TITLE     IMPACT OF BRCA1 BRCT DOMAIN MISSENSE SUBSTITUTIONS ON PHOSPHO-PEPTIDE 
TITLE    2 RECOGNITION: G1656D                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A;                                                            
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                                                        
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                                      
KEYWDS    BRCA1 PROTEIN, MISSENSE, PHOSPHOPEPTIDE RECOGNITION, BRCT TANDEM      
KEYWDS   2 REPEATS, BACH1 CTIP ABRAXAS, NUCLEAR PROTEIN, PROTEIN BINDING        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,R.GREEN,J.N.M.GLOVER                                       
REVDAT   3   08-NOV-17 3PXA    1       REMARK                                   
REVDAT   2   15-JUN-11 3PXA    1       JRNL                                     
REVDAT   1   20-APR-11 3PXA    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.    2.55 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 : ENGH & HUBER                                  
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.55                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.67                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 15760                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.239                           
REMARK   3   R VALUE            (WORKING SET) : 0.238                           
REMARK   3   FREE R VALUE                     : 0.261                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 783                             
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 37.6760 -  4.6312    0.94     2561   137  0.2047 0.2258        
REMARK   3     2  4.6312 -  3.6769    0.98     2506   129  0.2038 0.2154        
REMARK   3     3  3.6769 -  3.2124    0.99     2481   127  0.2712 0.2864        
REMARK   3     4  3.2124 -  2.9188    0.99     2486   134  0.2786 0.3451        
REMARK   3     5  2.9188 -  2.7097    0.99     2468   132  0.3122 0.3535        
REMARK   3     6  2.7097 -  2.5500    1.00     2475   124  0.3413 0.3721        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 61.59                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.350            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 65.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 5.35990                                              
REMARK   3    B22 (A**2) : 5.35990                                              
REMARK   3    B33 (A**2) : -10.71970                                            
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      :  0.008           1672                                  
REMARK   3   ANGLE     :  1.172           2273                                  
REMARK   3   CHIRALITY :  0.078            260                                  
REMARK   3   PLANARITY :  0.006            287                                  
REMARK   3   DIHEDRAL  : 16.143            597                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 6                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1649:1684)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -33.3346  40.4847   3.7892              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2235 T22:   0.5351                                     
REMARK   3      T33:   0.3893 T12:  -0.1214                                     
REMARK   3      T13:   0.0503 T23:  -0.0112                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.1474 L22:   2.4295                                     
REMARK   3      L33:   3.6563 L12:   2.1615                                     
REMARK   3      L13:   0.5070 L23:  -1.1844                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2278 S12:   0.5332 S13:  -0.7933                       
REMARK   3      S21:  -0.2728 S22:  -0.3796 S23:  -0.3805                       
REMARK   3      S31:   0.3501 S32:  -0.4740 S33:   0.0005                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1685:1741)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -32.0200  45.5757  -6.6029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4121 T22:   1.3837                                     
REMARK   3      T33:   0.4614 T12:  -0.2436                                     
REMARK   3      T13:   0.0456 T23:  -0.0270                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.0545 L22:   1.9429                                     
REMARK   3      L33:  -1.5774 L12:   1.8091                                     
REMARK   3      L13:  -0.1121 L23:  -0.4398                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8952 S12:   2.9775 S13:  -0.3453                       
REMARK   3      S21:  -0.7288 S22:   0.7776 S23:   0.1008                       
REMARK   3      S31:   0.1450 S32:  -0.1540 S33:  -0.0004                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1742:1748)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -25.8821  53.4304 -14.7028              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6453 T22:   2.2532                                     
REMARK   3      T33:   0.6907 T12:  -0.2877                                     
REMARK   3      T13:   0.0016 T23:   0.3850                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1879 L22:   0.2029                                     
REMARK   3      L33:   0.0054 L12:  -0.0428                                     
REMARK   3      L13:   0.0859 L23:  -0.0492                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.8550 S12:   1.5218 S13:   0.4161                       
REMARK   3      S21:  -1.5049 S22:   0.8013 S23:   0.8144                       
REMARK   3      S31:   0.4574 S32:   0.0239 S33:  -0.0034                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1749:1753)                          
REMARK   3    ORIGIN FOR THE GROUP (A): -22.2082  43.2582 -13.7406              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.6656 T22:   1.9193                                     
REMARK   3      T33:   0.6879 T12:  -0.6663                                     
REMARK   3      T13:   0.2397 T23:  -0.5245                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1662 L22:   0.0804                                     
REMARK   3      L33:   0.0152 L12:  -0.1701                                     
REMARK   3      L13:  -0.0952 L23:   0.0317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0521 S12:   0.7743 S13:  -0.6922                       
REMARK   3      S21:  -0.8812 S22:   0.2023 S23:  -1.7659                       
REMARK   3      S31:  -0.2605 S32:  -0.3665 S33:   0.0046                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1754:1803)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -6.7318  48.3685  -2.1516              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2836 T22:   0.6614                                     
REMARK   3      T33:   0.6562 T12:   0.0223                                     
REMARK   3      T13:   0.1458 T23:   0.0171                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  11.5505 L22:   5.6903                                     
REMARK   3      L33:   5.3377 L12:   3.4253                                     
REMARK   3      L13:  -2.9696 L23:  -2.8373                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4613 S12:   0.3773 S13:  -1.3588                       
REMARK   3      S21:  -0.0244 S22:  -0.2335 S23:  -0.7047                       
REMARK   3      S31:   0.7135 S32:   0.1584 S33:  -0.0002                       
REMARK   3   TLS GROUP : 6                                                      
REMARK   3    SELECTION: (CHAIN A AND RESID 1804:1859)                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.5714  58.8760  -6.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2088 T22:   0.8875                                     
REMARK   3      T33:   0.6281 T12:  -0.0017                                     
REMARK   3      T13:   0.1236 T23:   0.2800                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  12.2928 L22:   4.9481                                     
REMARK   3      L33:   5.3673 L12:   1.1626                                     
REMARK   3      L13:  -2.4876 L23:  -3.1396                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0889 S12:   2.3414 S13:   2.1419                       
REMARK   3      S21:   0.1300 S22:   0.3843 S23:   0.0469                       
REMARK   3      S31:  -0.1213 S32:  -0.3549 S33:   0.0017                       
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 3PXA 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_1000062925.                                   
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                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
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   : 15761                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.550                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY                : 4.800                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 18.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.60                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
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   (%): 73.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.0M LI2SO4 100MM TRIS 5MM CACL2 10MM    
REMARK 280  NICL2 , PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.70333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.40667            
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       61.05500            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      101.75833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       20.35167            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.70333            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       81.40667            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      101.75833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       61.05500            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       20.35167            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A  25  LIES ON A SPECIAL POSITION.                          
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     ASN A  1647                                                      
REMARK 465     LYS A  1648                                                      
REMARK 465     GLU A  1817                                                      
REMARK 465     ASP A  1818                                                      
REMARK 465     ASN A  1819                                                      
REMARK 465     GLY A  1820                                                      
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 A1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1727    CG   CD   CE   NZ                                   
REMARK 470     ASN A1730    CG   OD1  ND2                                       
REMARK 470     ARG A1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A1815    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A1815    CZ3  CH2                                            
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    ASN A1745       78.42   -150.04                                   
REMARK 500    SER A1755       25.00    -74.54                                   
REMARK 500    MET A1775      119.25   -160.76                                   
REMARK 500    TYR A1845       50.38     30.80                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 100                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 101                 
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: 3PXB   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXC   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXE   RELATED DB: PDB                                   
DBREF  3PXA A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
SEQADV 3PXA ASP A 1656  UNP  P38398    GLY  1656 ENGINEERED MUTATION            
SEQRES   1 A  214  VAL ASN LYS ARG MET SER MET VAL VAL SER ASP 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 GLU 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                                      
HET     NI  A 100       1                                                       
HET    SO4  A 101       5                                                       
HETNAM      NI NICKEL (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   NI    NI 2+                                                        
FORMUL   3  SO4    O4 S 2-                                                      
FORMUL   4  HOH   *29(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 PRO A 1776  CYS A 1787  1                                  12    
HELIX    7   7 GLU A 1794  PHE A 1798  5                                   5    
HELIX    8   8 GLN A 1811  TRP A 1815  5                                   5    
HELIX    9   9 ALA A 1823  MET A 1827  5                                   5    
HELIX   10  10 ARG A 1835  LEU A 1844  1                                  10    
HELIX   11  11 GLU A 1849  TYR A 1853  5                                   5    
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  TRP A1712   N  VAL A1687           
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 ALA A1789  VAL A1791  0                                        
SHEET    2   C 4 LEU A1764  CYS A1768  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 A1808           
LINK         NE2 HIS A1805                NI    NI A 100     1555   1555  2.47  
SITE     1 AC1  3 HOH A  15  HIS A1673  HIS A1805                               
SITE     1 AC2  5 HOH A   4  HOH A   6  SER A1655  ASP A1656                    
SITE     2 AC2  5 LYS A1702                                                     
CRYST1  114.870  114.870  122.110  90.00  90.00 120.00 P 61 2 2     12          
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      0.008705  0.005026  0.000000        0.00000                         
SCALE2      0.000000  0.010052  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008189        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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