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Database: PDB
Entry: 3PXD
LinkDB: 3PXD
Original site: 3PXD 
HEADER    PROTEIN BINDING                         09-DEC-10   3PXD              
TITLE     IMPACT OF BRCA1 BRCT DOMAIN MISSENSE SUBSTITUTIONS ON PHOSPHO-PEPTIDE 
TITLE    2 RECOGNITION: R1835P                                                  
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, PHOSPHO-PEPTIDE BINDING, NUCLEAR PROTEIN, PROTEIN BINDING   
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.COQUELLE,R.GREEN,J.N.M.GLOVER                                       
REVDAT   3   08-NOV-17 3PXD    1       REMARK                                   
REVDAT   2   15-JUN-11 3PXD    1       JRNL                                     
REVDAT   1   20-APR-11 3PXD    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) : 40.00                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 11932                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 597                             
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 46.0902 -  4.4439    0.95     2919   154  0.2032 0.2469        
REMARK   3     2  4.4439 -  3.5276    0.98     2844   150  0.2225 0.2763        
REMARK   3     3  3.5276 -  3.0818    0.99     2808   148  0.2868 0.3410        
REMARK   3     4  3.0818 -  2.8001    0.98     2764   145  0.3253 0.3464        
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              : 0.35                                          
REMARK   3   B_SOL              : 74.86                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.340            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.40                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.73710                                              
REMARK   3    B22 (A**2) : 1.73710                                              
REMARK   3    B33 (A**2) : -3.47420                                             
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           1729                                  
REMARK   3   ANGLE     :  1.118           2289                                  
REMARK   3   CHIRALITY :  0.062            260                                  
REMARK   3   PLANARITY :  0.005            289                                  
REMARK   3   DIHEDRAL  : 15.486            593                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 5                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1649:1684                            
REMARK   3    ORIGIN FOR THE GROUP (A):  38.8243  50.9117  44.5334              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.5981 T22:   0.8753                                     
REMARK   3      T33:   0.7395 T12:   0.3944                                     
REMARK   3      T13:   0.1239 T23:   0.2188                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.3625 L22:   1.0210                                     
REMARK   3      L33:   2.4086 L12:  -0.6347                                     
REMARK   3      L13:   0.7386 L23:   1.0973                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0997 S12:   0.4027 S13:   0.6852                       
REMARK   3      S21:  -0.3493 S22:  -0.1464 S23:  -1.0350                       
REMARK   3      S31:   0.5286 S32:   1.3660 S33:   0.0006                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1685:1741                            
REMARK   3    ORIGIN FOR THE GROUP (A):  33.4972  49.6272  33.9986              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.1047 T22:   1.0885                                     
REMARK   3      T33:   0.4867 T12:   0.8631                                     
REMARK   3      T13:   0.1183 T23:   0.0427                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.0283 L22:   5.2854                                     
REMARK   3      L33:   1.0056 L12:  -4.0402                                     
REMARK   3      L13:  -0.4048 L23:   1.2421                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.3030 S12:   1.8675 S13:  -0.2952                       
REMARK   3      S21:  -2.0595 S22:  -1.7020 S23:  -0.4244                       
REMARK   3      S31:   0.0568 S32:   0.4325 S33:   0.0036                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1742:1753                            
REMARK   3    ORIGIN FOR THE GROUP (A):  27.0544  54.6244  26.3220              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.9688 T22:   1.8089                                     
REMARK   3      T33:   0.5167 T12:   1.3615                                     
REMARK   3      T13:   0.2525 T23:   0.4716                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1991 L22:   0.4370                                     
REMARK   3      L33:   0.2541 L12:  -0.2966                                     
REMARK   3      L13:   0.2623 L23:  -0.3456                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.1961 S12:   2.0634 S13:   0.1597                       
REMARK   3      S21:  -1.2896 S22:  -0.9386 S23:   0.3719                       
REMARK   3      S31:   1.3091 S32:   0.0480 S33:  -0.0035                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1754:1803                            
REMARK   3    ORIGIN FOR THE GROUP (A):  19.0649  70.2527  38.3797              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4523 T22:   0.3500                                     
REMARK   3      T33:   0.5930 T12:   0.1872                                     
REMARK   3      T13:  -0.0622 T23:   0.0832                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   7.5256 L22:   8.7574                                     
REMARK   3      L33:   6.5051 L12:  -4.4055                                     
REMARK   3      L13:   2.3184 L23:  -0.3679                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.1891 S12:   0.6361 S13:   1.1076                       
REMARK   3      S21:  -0.7296 S22:  -0.8411 S23:  -0.1647                       
REMARK   3      S31:  -0.1607 S32:   0.7387 S33:   0.0032                       
REMARK   3   TLS GROUP : 5                                                      
REMARK   3    SELECTION: CHAIN A AND RESID 1804:1859                            
REMARK   3    ORIGIN FOR THE GROUP (A):   8.6337  66.1427  35.1658              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8419 T22:   0.3380                                     
REMARK   3      T33:   0.9625 T12:   0.3762                                     
REMARK   3      T13:  -0.4716 T23:  -0.2801                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   4.8464 L22:   2.4127                                     
REMARK   3      L33:   6.1631 L12:  -2.5225                                     
REMARK   3      L13:   4.0331 L23:  -1.9358                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   1.0670 S12:   0.6031 S13:  -1.1429                       
REMARK   3      S21:  -1.6581 S22:  -1.1416 S23:   2.9709                       
REMARK   3      S31:   0.8085 S32:  -0.0134 S33:   0.0007                       
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 3PXD 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_1000062928.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-10                          
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               : 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   : 11935                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
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     (%) : 97.5                               
REMARK 200  DATA REDUNDANCY                : 3.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.05900                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 13.9600                            
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     (%) : 97.6                               
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   (%): 74.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.8M LI2SO4 100 MM 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       40.64667            
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       81.29333            
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       60.97000            
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      101.61667            
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       20.32333            
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       40.64667            
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       81.29333            
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      101.61667            
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       60.97000            
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       20.32333            
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 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 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     MET A1663    CG   SD   CE                                        
REMARK 470     ARG A1670    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1727    CG   CD   CE   NZ                                   
REMARK 470     ARG A1737    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASN A1819    CG   OD1  ND2                                       
REMARK 470     GLU A1849    CG   CD   OE1  OE2                                  
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    MET A1650      119.77   -165.90                                   
REMARK 500    HIS A1673       39.29     71.36                                   
REMARK 500    THR A1684      121.66    -37.39                                   
REMARK 500    LYS A1724        1.98    -61.92                                   
REMARK 500    GLU A1725       21.12   -147.63                                   
REMARK 500    ARG A1726       41.58     37.91                                   
REMARK 500    GLU A1735      173.77    -50.22                                   
REMARK 500    ASN A1774      -26.22     77.32                                   
REMARK 500    MET A1775      128.72   -170.31                                   
REMARK 500    SER A1796        3.48    -67.91                                   
REMARK 500    THR A1802     -148.02    -78.39                                   
REMARK 500    ASP A1813       -8.23    -59.73                                   
REMARK 500    GLU A1829       67.43   -103.82                                   
REMARK 500    GLN A1846      119.91   -162.45                                   
REMARK 500    ILE A1858       99.50    -66.04                                   
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 SO4 A 10                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 11                   
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: 3PXE   RELATED DB: PDB                                   
DBREF  3PXD A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
SEQADV 3PXD PRO A 1835  UNP  P38398    ARG  1835 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 PRO 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    SO4  A  10       5                                                       
HET     NI  A  11       1                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM      NI NICKEL (II) ION                                                  
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3   NI    NI 2+                                                        
FORMUL   4  HOH   *8(H2 O)                                                      
HELIX    1   1 THR A 1658  HIS A 1673  1                                  16    
HELIX    2   2 THR A 1700  GLY A 1710  1                                  11    
HELIX    3   3 TYR A 1716  LYS A 1724  1                                   9    
HELIX    4   4 ASN A 1730  GLU A 1735  1                                   6    
HELIX    5   5 GLN A 1747  GLU A 1754  1                                   8    
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  CYS A 1828  1                                   6    
HELIX   10  10 PRO A 1835  LEU A 1844  1                                  10    
HELIX   11  11 GLU A 1849  LEU A 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  HIS A1686   N  SER A1651           
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 A1768  1  N  ILE A1766   O  SER A1790           
SHEET    3   C 4 HIS A1805  VAL A1809  1  O  ILE A1807   N  CYS A1767           
SHEET    4   C 4 VAL A1832  VAL A1833  1  O  VAL A1833   N  VAL A1808           
LINK         NE2 HIS A1805                NI    NI A  11     1555   1555  2.51  
SITE     1 AC1  5 HOH A   1  VAL A1654  SER A1655  GLY A1656                    
SITE     2 AC1  5 LYS A1702                                                     
SITE     1 AC2  4 HOH A   8  LYS A1671  HIS A1673  HIS A1805                    
CRYST1  114.950  114.950  121.940  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      0.008699  0.005023  0.000000        0.00000                         
SCALE2      0.000000  0.010045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008200        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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