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Database: PDB
Entry: 2ING
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Original site: 2ING 
HEADER    DNA BINDING PROTEIN                     07-OCT-06   2ING              
TITLE     X-RAY STRUCTURE OF THE BRCA1 BRCT MUTANT M1775K                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: X;                                                            
COMPND   4 FRAGMENT: BRCT1, BRCT2;                                              
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 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 BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMAL-C2X                                  
KEYWDS    ZINC-FINGER, DNA-BINDING, DNA REPAIR, DISEASE MUTATION,               
KEYWDS   2 PHOSPHORYLATION, DNA BINDING PROTEIN                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.BIRRANE,A.SONI,J.A.A.LADIAS                                         
REVDAT   6   18-OCT-17 2ING    1       REMARK                                   
REVDAT   5   13-JUL-11 2ING    1       VERSN                                    
REVDAT   4   24-FEB-09 2ING    1       VERSN                                    
REVDAT   3   01-JUL-08 2ING    1       JRNL                                     
REVDAT   2   26-FEB-08 2ING    1       JRNL                                     
REVDAT   1   04-SEP-07 2ING    0                                                
JRNL        AUTH   M.TISCHKOWITZ,N.HAMEL,M.A.CARVALHO,G.BIRRANE,A.SONI,         
JRNL        AUTH 2 E.H.VAN BEERS,S.A.JOOSSE,N.WONG,D.NOVAK,L.A.QUENNEVILLE,     
JRNL        AUTH 3 S.A.GRIST,P.M.NEDERLOF,D.E.GOLDGAR,S.V.TAVTIGIAN,            
JRNL        AUTH 4 A.N.MONTEIRO,J.A.LADIAS,W.D.FOULKES                          
JRNL        TITL   PATHOGENICITY OF THE BRCA1 MISSENSE VARIANT M1775K IS        
JRNL        TITL 2 DETERMINED BY THE DISRUPTION OF THE BRCT                     
JRNL        TITL 3 PHOSPHOPEPTIDE-BINDING POCKET: A MULTI-MODAL APPROACH.       
JRNL        REF    EUR.J.HUM.GENET.              V.  16   820 2008              
JRNL        REFN                   ISSN 1018-4813                               
JRNL        PMID   18285836                                                     
JRNL        DOI    10.1038/EJHG.2008.13                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 5678                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.251                           
REMARK   3   R VALUE            (WORKING SET) : 0.247                           
REMARK   3   FREE R VALUE                     : 0.302                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 8.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 501                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.69                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 374                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.76                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3920                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 36                           
REMARK   3   BIN FREE R VALUE                    : 0.3780                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1671                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 11                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 148.1                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.10000                                             
REMARK   3    B22 (A**2) : -1.10000                                             
REMARK   3    B33 (A**2) : 1.64000                                              
REMARK   3    B12 (A**2) : -0.55000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 3.292         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.642         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.682         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 103.603       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.939                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.908                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1718 ; 0.014 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  1160 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2329 ; 1.635 ; 1.946       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2820 ; 0.955 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   205 ; 9.369 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    78 ;38.721 ;23.590       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   296 ;23.696 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;11.464 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   259 ; 0.083 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1869 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   353 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   570 ; 0.283 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  1355 ; 0.218 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   865 ; 0.207 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):   955 ; 0.096 ; 0.200       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    86 ; 0.201 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):     1 ; 0.009 ; 0.200       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    21 ; 0.236 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):    35 ; 0.203 ; 0.200       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   X  1649        X  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  18.6470  48.2260   3.8670              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.9717 T22:   0.1110                                     
REMARK   3      T33:  -0.6903 T12:  -0.1477                                     
REMARK   3      T13:  -0.0631 T23:  -0.7346                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  23.2434 L22:   5.6322                                     
REMARK   3      L33:   5.6025 L12:  -4.0678                                     
REMARK   3      L13:  -2.2069 L23:   2.0872                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5766 S12:  -2.9547 S13:   0.3596                       
REMARK   3      S21:   0.9229 S22:  -0.4543 S23:   0.7603                       
REMARK   3      S31:   0.2200 S32:   1.2426 S33:  -0.1224                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2ING COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-OCT-06.                  
REMARK 100 THE DEPOSITION ID IS D_1000039784.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-SEP-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.7                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X12B                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 5744                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 27.50                              
REMARK 200  R MERGE                    (I) : 0.09300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.73                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 28.90                              
REMARK 200  R MERGE FOR SHELL          (I) : 0.53000                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1N5O                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.69                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.67                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 1.4M AMMONIUM SULFATE, 20MM COBALT       
REMARK 280  CHLORIDE, 100MM 2-(N-MORPHOLINO) ETHANESULFONIC ACID, PH 6.7,       
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 291K                     
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       39.95933            
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       79.91867            
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       59.93900            
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       99.89833            
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       19.97967            
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       39.95933            
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       79.91867            
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       99.89833            
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       59.93900            
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       19.97967            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: PQS                                                   
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2470 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -81.0 KCAL/MOL                        
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 350   BIOMT1   2  0.500000 -0.866025  0.000000       57.17000            
REMARK 350   BIOMT2   2 -0.866025 -0.500000  0.000000       99.02134            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -19.97967            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY X  1647                                                      
REMARK 465     PRO X  1648                                                      
REMARK 465     GLU X  1694                                                      
REMARK 465     GLU X  1817                                                      
REMARK 465     ASP X  1818                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    PRO X1771   C   -  N   -  CA  ANGL. DEV. =   9.4 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    MET X1663      -71.98    -22.92                                   
REMARK 500    ALA X1669      -70.80    -66.49                                   
REMARK 500    ARG X1670      -67.71    -24.01                                   
REMARK 500    ILE X1680      128.98    -35.21                                   
REMARK 500    THR X1691     -121.81   -151.41                                   
REMARK 500    ASP X1692      -38.20   -178.54                                   
REMARK 500    ARG X1699       73.43   -101.07                                   
REMARK 500    TRP X1718      -34.83    -35.38                                   
REMARK 500    GLU X1725       52.45   -101.43                                   
REMARK 500    ARG X1726       35.49     24.09                                   
REMARK 500    HIS X1732       -2.03    -54.23                                   
REMARK 500    PHE X1734       22.60   -160.99                                   
REMARK 500    ARG X1737       32.74   -141.17                                   
REMARK 500    ASP X1739      -47.04    177.96                                   
REMARK 500    VAL X1740      -53.96    165.56                                   
REMARK 500    ASN X1745      -82.86    -37.83                                   
REMARK 500    PRO X1749      -32.86    -38.39                                   
REMARK 500    LYS X1750      -84.32    -33.36                                   
REMARK 500    SER X1755     -105.03    -81.84                                   
REMARK 500    GLN X1756      -52.88     67.18                                   
REMARK 500    ARG X1762      -91.21     42.08                                   
REMARK 500    PRO X1771      131.54    -11.98                                   
REMARK 500    THR X1773      -66.93   -160.17                                   
REMARK 500    MET X1783      -71.93    -62.54                                   
REMARK 500    SER X1796       48.93    -67.60                                   
REMARK 500    SER X1797       22.55   -160.99                                   
REMARK 500    THR X1802      -50.89     31.68                                   
REMARK 500    PHE X1821        9.37    -60.38                                   
REMARK 500    ALA X1823       39.26    -97.37                                   
REMARK 500    GLN X1826        6.63    -68.44                                   
REMARK 500    ARG X1835      -52.99    -29.12                                   
REMARK 500    ALA X1843      -70.42    -52.09                                   
REMARK 500    TYR X1845       22.03     49.96                                   
REMARK 500    ASP X1851      -66.29    -26.75                                   
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                              CO X 101  CO                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS X1805   NE2                                                    
REMARK 620 2 HIS X1673   NE2  75.3                                              
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 CO X 101                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 1                   
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 X 2                   
DBREF  2ING X 1649  1859  UNP    P38398   BRCA1_HUMAN   1649   1859             
SEQADV 2ING GLY X 1647  UNP  P38398              EXPRESSION TAG                 
SEQADV 2ING PRO X 1648  UNP  P38398              EXPRESSION TAG                 
SEQADV 2ING LYS X 1775  UNP  P38398    MET  1775 ENGINEERED                     
SEQRES   1 X  213  GLY PRO ARG MET SER MET VAL VAL SER GLY LEU THR PRO          
SEQRES   2 X  213  GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS          
SEQRES   3 X  213  HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR THR          
SEQRES   4 X  213  HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU          
SEQRES   5 X  213  ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS          
SEQRES   6 X  213  TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS          
SEQRES   7 X  213  GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG          
SEQRES   8 X  213  GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS          
SEQRES   9 X  213  ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY          
SEQRES  10 X  213  LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN LYS PRO          
SEQRES  11 X  213  THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA          
SEQRES  12 X  213  SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY THR          
SEQRES  13 X  213  GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP          
SEQRES  14 X  213  THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS          
SEQRES  15 X  213  GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER          
SEQRES  16 X  213  VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU          
SEQRES  17 X  213  ILE PRO GLN ILE PRO                                          
HET     CO  X 101       1                                                       
HET    SO4  X   1       5                                                       
HET    SO4  X   2       5                                                       
HETNAM      CO COBALT (II) ION                                                  
HETNAM     SO4 SULFATE ION                                                      
FORMUL   2   CO    CO 2+                                                        
FORMUL   3  SO4    2(O4 S 2-)                                                   
HELIX    1   1 THR X 1658  HIS X 1672  1                                  15    
HELIX    2   2 THR X 1700  GLY X 1710  1                                  11    
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 GLY X 1748  SER X 1755  1                                   8    
HELIX    6   6 PRO X 1776  CYS X 1787  1                                  12    
HELIX    7   7 ARG X 1835  TYR X 1845  1                                  11    
HELIX    8   8 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  TRP X1712   N  VAL X1687           
SHEET    1   B 4 ALA X1789  VAL X1792  0                                        
SHEET    2   B 4 LEU X1764  CYS X1768  1  N  ILE X1766   O  SER X1790           
SHEET    3   B 4 HIS X1805  VAL X1810  1  O  ILE X1807   N  GLU X1765           
SHEET    4   B 4 VAL X1832  THR X1834  1  O  VAL X1833   N  VAL X1808           
LINK         NE2 HIS X1805                CO    CO X 101     1555   1555  2.03  
LINK        CO    CO X 101                 NE2 HIS X1673     1555   6555  2.44  
SITE     1 AC1  2 HIS X1673  HIS X1805                                          
SITE     1 AC2  4 SER X1655  GLY X1656  THR X1700  LYS X1702                    
SITE     1 AC3  3 THR X1677  ASN X1678  LEU X1679                               
CRYST1  114.340  114.340  119.878  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      0.008746  0.005049  0.000000        0.00000                         
SCALE2      0.000000  0.010099  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008342        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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