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Database: PDB
Entry: 3PXC
LinkDB: 3PXC
Original site: 3PXC 
HEADER    PROTEIN BINDING                         09-DEC-10   3PXC              
TITLE     IMPACT OF BRCA1 BRCT DOMAIN MISSENSE SUBSTITUTIONS ON PHOSPHO-PEPTIDE 
TITLE    2 RECOGNITION: R1699Q                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: X;                                                            
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 3PXC    1       REMARK                                   
REVDAT   2   15-JUN-11 3PXC    1       JRNL                                     
REVDAT   1   20-APR-11 3PXC    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.    2.80 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) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.60                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.2                           
REMARK   3   NUMBER OF REFLECTIONS             : 12034                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.230                           
REMARK   3   R VALUE            (WORKING SET) : 0.228                           
REMARK   3   FREE R VALUE                     : 0.270                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 602                             
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 19.5959 -  4.4318    0.99     2996   158  0.1847 0.2343        
REMARK   3     2  4.4318 -  3.5243    0.99     2848   150  0.2260 0.2598        
REMARK   3     3  3.5243 -  3.0808    0.99     2811   148  0.2957 0.3172        
REMARK   3     4  3.0808 -  2.8000    0.99     2777   146  0.3338 0.3811        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.95                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 57.71                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.390            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.30                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.13780                                             
REMARK   3    B22 (A**2) : -0.13780                                             
REMARK   3    B33 (A**2) : 0.27560                                              
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           1657                                  
REMARK   3   ANGLE     :  1.179           2255                                  
REMARK   3   CHIRALITY :  0.071            257                                  
REMARK   3   PLANARITY :  0.005            284                                  
REMARK   3   DIHEDRAL  : 15.096            582                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN X AND RESID 1649:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A):  39.0750  50.3909  44.6967              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4859 T22:   0.6867                                     
REMARK   3      T33:   0.5070 T12:   0.3228                                     
REMARK   3      T13:   0.0062 T23:   0.1894                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.5793 L22:   6.7018                                     
REMARK   3      L33:   1.1251 L12:  -5.5183                                     
REMARK   3      L13:   1.0930 L23:  -0.6456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.3694 S12:   0.8861 S13:   1.2246                       
REMARK   3      S21:  -0.3939 S22:  -0.6729 S23:  -0.9350                       
REMARK   3      S31:   0.4495 S32:   0.4471 S33:   0.3415                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN X AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.8480  49.0016  34.1396              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.0064 T22:   0.9082                                     
REMARK   3      T33:   0.2821 T12:   0.7097                                     
REMARK   3      T13:   0.0194 T23:   0.0415                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   5.4696 L22:   5.0280                                     
REMARK   3      L33:   0.3076 L12:  -4.8616                                     
REMARK   3      L13:   1.5350 L23:  -0.3985                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.7966 S12:   2.2446 S13:  -0.2381                       
REMARK   3      S21:  -1.7386 S22:  -1.9851 S23:   0.1233                       
REMARK   3      S31:   0.3799 S32:   0.0962 S33:   0.1468                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN X AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.1143  54.0757  26.4029              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   2.0209 T22:   1.6195                                     
REMARK   3      T33:   0.3751 T12:   1.4291                                     
REMARK   3      T13:   0.2017 T23:   0.1776                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.0448 L22:   3.8452                                     
REMARK   3      L33:   2.0799 L12:  -3.7450                                     
REMARK   3      L13:   2.3029 L23:  -2.5653                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   2.2428 S12:   2.3995 S13:   0.0739                       
REMARK   3      S21:  -2.9712 S22:  -2.2789 S23:   0.2266                       
REMARK   3      S31:   2.9104 S32:   1.1842 S33:  -0.0440                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN X AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A):  18.9852  69.3244  38.5316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4512 T22:   0.3269                                     
REMARK   3      T33:   0.5248 T12:   0.1164                                     
REMARK   3      T13:  -0.1078 T23:   0.1239                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.9472 L22:   9.0556                                     
REMARK   3      L33:   6.9945 L12:  -6.3962                                     
REMARK   3      L13:   1.7868 L23:  -2.9488                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0222 S12:   0.1320 S13:   1.2581                       
REMARK   3      S21:   0.4168 S22:  -0.5924 S23:  -0.3983                       
REMARK   3      S31:  -0.6632 S32:   0.2740 S33:   0.5032                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN X AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A):   9.0325  65.3331  34.9755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5574 T22:   0.1796                                     
REMARK   3      T33:   0.6410 T12:   0.2461                                     
REMARK   3      T13:  -0.3414 T23:  -0.1101                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   6.6303 L22:   2.6821                                     
REMARK   3      L33:   6.3596 L12:  -7.1474                                     
REMARK   3      L13:   2.8960 L23:  -1.9965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.5280 S12:   0.9046 S13:  -1.6041                       
REMARK   3      S21:  -1.8101 S22:  -1.7140 S23:   3.1346                       
REMARK   3      S31:   0.6411 S32:  -0.0904 S33:  -0.2376                       
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 3PXC 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_1000062927.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 12.3.1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.11584                            
REMARK 200  MONOCHROMATOR                  : SI(111) DOUBLE CRYSTAL             
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12036                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.8                               
REMARK 200  DATA REDUNDANCY                : 4.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05700                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.85                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.8                               
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   (%): 73.97                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M LI2SO4 100MM TRIS 5MM CACL2 10MM    
REMARK 280  NICL2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K, PH 8        
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: X                                     
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 X   8  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 X  1646                                                      
REMARK 465     ASN X  1647                                                      
REMARK 465     LYS X  1648                                                      
REMARK 465     GLU X  1694                                                      
REMARK 465     GLU X  1817                                                      
REMARK 465     ASP X  1818                                                      
REMARK 465     ASN X  1819                                                      
REMARK 465     GLY X  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 X1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET X1663    CG   SD   CE                                        
REMARK 470     LYS X1671    CG   CD   CE   NZ                                   
REMARK 470     ARG X1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP X1733    CG   OD1  OD2                                       
REMARK 470     ASP X1757    CG   OD1  OD2                                       
REMARK 470     ARG X1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS X1793    CG   CD   CE   NZ                                   
REMARK 470     LEU X1800    CG   CD1  CD2                                       
REMARK 470     GLU X1849    CG   CD   OE1  OE2                                  
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG X 1737   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     TRP X 1815   CD2                                                 
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    HIS X1673       36.02     71.93                                   
REMARK 500    ARG X1726       23.87     48.24                                   
REMARK 500    GLU X1735      158.31    -43.53                                   
REMARK 500    THR X1773      -86.79   -101.64                                   
REMARK 500    ALA X1814       20.98    -75.64                                   
REMARK 500    GLU X1829       63.46   -109.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NI X  21  NI                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X1805   NE2                                                    
REMARK 620 2 HOH X  12   O   128.0                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 20                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI X 21                   
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: 3PXD   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3PXE   RELATED DB: PDB                                   
DBREF  3PXC X 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
SEQADV 3PXC GLN X 1699  UNP  P38398    ARG  1699 ENGINEERED MUTATION            
SEQRES   1 X  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 X  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 X  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 X  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 X  214  GLU GLN THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 X  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 X  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 X  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 X  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 X  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 X  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 X  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 X  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 X  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 X  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 X  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 X  214  LEU ILE PRO GLN ILE PRO                                      
HET    SO4  X  20       5                                                       
HET     NI  X  21       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   NI    NI 2+                                                        
FORMUL   4  HOH   *13(H2 O)                                                     
HELIX    1   1 THR X 1658  HIS X 1673  1                                  16    
HELIX    2   2 THR X 1700  GLY X 1709  1                                  10    
HELIX    3   3 TYR X 1716  GLU X 1725  1                                  10    
HELIX    4   4 ASN X 1730  PHE X 1734  5                                   5    
HELIX    5   5 GLN X 1747  SER X 1755  1                                   9    
HELIX    6   6 PRO X 1776  CYS X 1787  1                                  12    
HELIX    7   7 GLU X 1794  PHE X 1798  5                                   5    
HELIX    8   8 GLN X 1811  TRP X 1815  5                                   5    
HELIX    9   9 ALA X 1823  MET X 1827  5                                   5    
HELIX   10  10 ARG X 1835  TYR X 1845  1                                  11    
HELIX   11  11 GLU X 1849  LEU X 1854  5                                   6    
SHEET    1   A 4 THR X1675  LEU X1676  0                                        
SHEET    2   A 4 SER X1651  SER X1655  1  N  MET X1652   O  THR X1675           
SHEET    3   A 4 HIS X1686  MET X1689  1  O  VAL X1688   N  SER X1655           
SHEET    4   A 4 TRP X1712  SER X1715  1  O  VAL X1714   N  MET X1689           
SHEET    1   B 2 VAL X1696  CYS X1697  0                                        
SHEET    2   B 2 GLY X1738  ASP X1739  1  O  GLY X1738   N  CYS X1697           
SHEET    1   C 4 ALA X1789  VAL X1792  0                                        
SHEET    2   C 4 LEU X1764  CYS X1768  1  N  ILE X1766   O  VAL X1792           
SHEET    3   C 4 HIS X1805  VAL X1810  1  O  ILE X1807   N  CYS X1767           
SHEET    4   C 4 VAL X1832  THR X1834  1  O  VAL X1833   N  VAL X1808           
LINK         NE2 HIS X1805                NI    NI X  21     1555   1555  2.60  
LINK        NI    NI X  21                 O   HOH X  12     1555   1555  2.67  
SITE     1 AC1  4 HOH X   1  SER X1655  GLY X1656  LYS X1702                    
SITE     1 AC2  4 HOH X  10  HOH X  12  HIS X1673  HIS X1805                    
CRYST1  114.620  114.620  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      0.008724  0.005037  0.000000        0.00000                         
SCALE2      0.000000  0.010074  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008189        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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