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Database: PDB
Entry: 3K0K
LinkDB: 3K0K
Original site: 3K0K 
HEADER    PROTEIN BINDING                         24-SEP-09   3K0K              
TITLE     CRYSTAL STRUCTURE OF BRCA1 BRCT IN COMPLEX WITH A MINIMAL RECOGNITION 
TITLE    2 TETRAPEPTIDE WITH A FREE CARBOXY C-TERMINUS.                         
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 TO 1859);                   
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PHOSPHO PEPTIDE PSPTF-COOH;                                
COMPND   9 CHAIN: B;                                                            
COMPND  10 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: BRCA1, RNF53;                                                  
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21 GOLD;                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PLM1-CD6;                                 
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_TAXID: 9606;                                                
SOURCE  14 OTHER_DETAILS: THIS SEQUENCE OCCURS NATURALLY IN HUMANS IN THE       
SOURCE  15 PROTEIN ABRAXAS/CCDC98. THE PEPTIDE IS CHEMICALLY SYNTHESIZED.       
KEYWDS    BRCA1, BRCT DOMAIN, DNA DAMAGE RESPONSE, PHOSPHO PEPTIDE              
KEYWDS   2 INTERACTIONS, ABRAXAS, ALTERNATIVE INITIATION, CELL CYCLE, DISEASE   
KEYWDS   3 MUTATION, DNA DAMAGE, DNA REPAIR, DNA-BINDING, FATTY ACID            
KEYWDS   4 BIOSYNTHESIS, LIGASE, LIPID SYNTHESIS, METAL-BINDING, NUCLEUS,       
KEYWDS   5 PHOSPHOPROTEIN, TUMOR SUPPRESSOR, UBL CONJUGATION PATHWAY, ZINC-     
KEYWDS   6 FINGER, PROTEIN BINDING                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.J.CAMPBELL,R.A.EDWARDS,J.N.GLOVER                                   
REVDAT   4   01-NOV-17 3K0K    1       REMARK                                   
REVDAT   3   13-JUL-11 3K0K    1       VERSN                                    
REVDAT   2   28-JUL-10 3K0K    1       AUTHOR                                   
REVDAT   1   02-MAR-10 3K0K    0                                                
JRNL        AUTH   S.J.CAMPBELL,R.A.EDWARDS,J.N.GLOVER                          
JRNL        TITL   COMPARISON OF THE STRUCTURES AND PEPTIDE BINDING             
JRNL        TITL 2 SPECIFICITIES OF THE BRCT DOMAINS OF MDC1 AND BRCA1          
JRNL        REF    STRUCTURE                     V.  18   167 2010              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   20159462                                                     
JRNL        DOI    10.1016/J.STR.2009.12.008                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 35.83                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 13512                          
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) : 0.261                           
REMARK   3   R VALUE            (WORKING SET) : 0.259                           
REMARK   3   FREE R VALUE                     : 0.299                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 667                             
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) : 2.70                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.77                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 850                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 92.29                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3300                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 48                           
REMARK   3   BIN FREE R VALUE                    : 0.4350                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1731                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 12                                      
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) : 48.29                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.20000                                             
REMARK   3    B22 (A**2) : -0.20000                                             
REMARK   3    B33 (A**2) : 0.31000                                              
REMARK   3    B12 (A**2) : -0.10000                                             
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): 0.391         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.305         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.262         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 25.623        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.926                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1785 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2424 ; 1.035 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   215 ; 5.867 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    84 ;35.462 ;23.690       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   307 ;16.468 ;15.049       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    12 ;12.654 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   268 ; 0.067 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1349 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
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):  1076 ; 0.343 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1756 ; 0.649 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   709 ; 0.844 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   668 ; 1.409 ; 4.500       
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 :   A  1649        A  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A): -18.7689  48.8396  -3.8906              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0582 T22:   0.4727                                     
REMARK   3      T33:   0.0415 T12:   0.0062                                     
REMARK   3      T13:   0.0255 T23:   0.1043                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  17.2140 L22:   2.8550                                     
REMARK   3      L33:   1.5473 L12:   3.5217                                     
REMARK   3      L13:  -1.9927 L23:  -0.7288                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1937 S12:   1.8444 S13:   0.0670                       
REMARK   3      S21:  -0.3247 S22:   0.1786 S23:  -0.1501                       
REMARK   3      S31:   0.2117 S32:  -0.2722 S33:   0.0151                       
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 U VALUES : RESIDUAL ONLY                                  
REMARK   4                                                                      
REMARK   4 3K0K COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-SEP-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000055393.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 15-JUL-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.3                                
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) : 0.97934                            
REMARK 200  MONOCHROMATOR                  : DCM                                
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, HKL-2000                    
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK, HKL-2000                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13551                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.3                               
REMARK 200  DATA REDUNDANCY                : 19.20                              
REMARK 200  R MERGE                    (I) : 0.06100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 12.5000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 94.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.55700                            
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 2.1.4                                          
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 73.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.64                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: LI2SO4, TRIS-HCL, NICL2, PH 7.3, VAPOR   
REMARK 280  DIFFUSION, TEMPERATURE 298K                                         
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       41.00167            
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       82.00333            
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       61.50250            
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      102.50417            
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       20.50083            
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       41.00167            
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       82.00333            
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      102.50417            
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       61.50250            
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       20.50083            
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 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 960 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11100 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
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     MET A  1645                                                      
REMARK 465     VAL A  1646                                                      
REMARK 465     ASN A  1647                                                      
REMARK 465     LYS A  1648                                                      
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    GLU A1725       37.49   -143.99                                   
REMARK 500    ARG A1726       57.80     17.03                                   
REMARK 500    ASN A1745       65.36   -150.41                                   
REMARK 500    SER A1755       50.33   -176.04                                   
REMARK 500    ARG A1758       88.33   -159.01                                   
REMARK 500    ASN A1774       -9.40     57.54                                   
REMARK 500    THR A1799       99.64    -69.67                                   
REMARK 500    THR A1802      -37.94   -154.54                                   
REMARK 500    ASP A1818      -85.55    -97.28                                   
REMARK 500    ALA A1843      -73.74    -53.78                                   
REMARK 500    GLU A1849      134.80    -38.78                                   
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 CL B 5                    
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NI A 1                    
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3K05   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3K0H   RELATED DB: PDB                                   
DBREF  3K0K A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  3K0K B    1     4  PDB    3K0K     3K0K             1      4             
SEQADV 3K0K MET A 1645  UNP  P38398              EXPRESSION TAG                 
SEQRES   1 A  215  MET VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU          
SEQRES   2 A  215  THR PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG          
SEQRES   3 A  215  LYS HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU          
SEQRES   4 A  215  THR THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL          
SEQRES   5 A  215  CYS GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY          
SEQRES   6 A  215  GLY LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER          
SEQRES   7 A  215  ILE LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU          
SEQRES   8 A  215  VAL ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY          
SEQRES   9 A  215  PRO LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE          
SEQRES  10 A  215  ARG GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN          
SEQRES  11 A  215  MET PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS          
SEQRES  12 A  215  GLY ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU          
SEQRES  13 A  215  GLY THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP          
SEQRES  14 A  215  ALA TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN          
SEQRES  15 A  215  MET CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU          
SEQRES  16 A  215  ASP SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR          
SEQRES  17 A  215  TYR LEU ILE PRO GLN ILE PRO                                  
SEQRES   1 B    4  SEP PRO THR PHE                                              
MODRES 3K0K SEP B    1  SER  PHOSPHOSERINE                                      
HET    SEP  B   1      10                                                       
HET     NI  A   1       1                                                       
HET     CL  B   5       1                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETNAM      NI NICKEL (II) ION                                                  
HETNAM      CL CHLORIDE ION                                                     
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   2  SEP    C3 H8 N O6 P                                                 
FORMUL   3   NI    NI 2+                                                        
FORMUL   4   CL    CL 1-                                                        
FORMUL   5  HOH   *12(H2 O)                                                     
HELIX    1   1 THR A 1658  HIS A 1673  1                                  16    
HELIX    2   2 THR A 1700  GLY A 1709  1                                  10    
HELIX    3   3 TYR A 1716  LYS A 1724  1                                   9    
HELIX    4   4 ASN A 1730  GLU A 1735  5                                   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 ARG A 1835  TYR A 1845  1                                  11    
HELIX   10  10 GLU A 1849  TYR A 1853  5                                   5    
SHEET    1   A 4 THR A1675  LEU A1676  0                                        
SHEET    2   A 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3   A 4 HIS A1686  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    4   A 4 TRP A1712  SER A1715  1  O  TRP A1712   N  VAL A1687           
SHEET    1   B 2 VAL A1696  CYS A1697  0                                        
SHEET    2   B 2 GLY A1738  ASP A1739  1  O  GLY A1738   N  CYS A1697           
SHEET    1   C 4 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 A1810  1  O  ILE A1807   N  CYS A1767           
SHEET    4   C 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1810           
LINK         C   SEP B   1                 N   PRO B   2     1555   1555  1.34  
LINK         NE2 HIS A1805                NI    NI A   1     1555   1555  2.03  
SITE     1 AC1  1 SEP B   1                                                     
SITE     1 AC2  2 HIS A1673  HIS A1805                                          
CRYST1  114.422  114.422  123.005  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      0.008740  0.005046  0.000000        0.00000                         
SCALE2      0.000000  0.010092  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008130        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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