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Database: PDB
Entry: 4U4A
LinkDB: 4U4A
Original site: 4U4A 
HEADER    ANTITUMOR PROTEIN/SIGNALING PROTEIN     23-JUL-14   4U4A              
TITLE     COMPLEX STRUCTURE OF BRCA1 BRCT WITH SINGLY PHOSPHO ABRAXAS           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 FRAGMENT: BRCT (UNP RESIDUES 1646-1859);                             
COMPND   5 SYNONYM: RING FINGER PROTEIN 53;                                     
COMPND   6 EC: 6.3.2.-;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: BRCA1-A COMPLEX SUBUNIT ABRAXAS;                           
COMPND  10 CHAIN: D, E, F;                                                      
COMPND  11 FRAGMENT: UNP RESIDUES 399-409;                                      
COMPND  12 SYNONYM: COILED-COIL DOMAIN-CONTAINING PROTEIN 98,PROTEIN FAM175A;   
COMPND  13 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: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: GST;                                      
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606                                                 
KEYWDS    COMPLEX, PHOSPHOSPECIFIC, ANTITUMOR PROTEIN-SIGNALING PROTEIN COMPLEX 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.BADGUJAR,M.V.HOSUR,A.K.VARMA                                        
REVDAT   1   26-AUG-15 4U4A    0                                                
JRNL        AUTH   D.BADGUJAR,M.V.HOSUR,A.K.VARMA                               
JRNL        TITL   COMPLEX STRUCTURE OF BRCA1 BRCT WITH SINGLY PHOSPHO ABRAXAS  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.51 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0029                                      
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) : 3.51                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 59.89                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 75.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 14795                          
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) : 0.304                           
REMARK   3   R VALUE            (WORKING SET) : 0.301                           
REMARK   3   FREE R VALUE                     : 0.362                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 754                             
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) : 3.51                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.60                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 261                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 19.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 17                           
REMARK   3   BIN FREE R VALUE                    : 0.3710                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5332                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 57.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -7.45000                                             
REMARK   3    B22 (A**2) : -7.45000                                             
REMARK   3    B33 (A**2) : 14.90000                                             
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  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.876         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.757         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 105.472       
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.877                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.808                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5475 ; 0.010 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5172 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7424 ; 1.469 ; 1.944       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11883 ; 1.046 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   661 ; 8.074 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   249 ;38.771 ;23.454       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   931 ;17.797 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    36 ;15.194 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   822 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6091 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1299 ; 0.005 ; 0.020       
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):  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  : 4                                          
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  1646        A  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  68.8336 164.8279  16.7168              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.7349 T22:   1.1015                                     
REMARK   3      T33:   0.2528 T12:  -0.0793                                     
REMARK   3      T13:  -0.2337 T23:   0.2967                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.4194 L22:   9.8042                                     
REMARK   3      L33:   4.4813 L12:  -0.4856                                     
REMARK   3      L13:  -0.0030 L23:  -3.1713                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.5471 S12:  -0.3096 S13:  -0.5983                       
REMARK   3      S21:   0.0289 S22:   0.0407 S23:   0.4400                       
REMARK   3      S31:   0.0591 S32:  -0.0898 S33:  -0.5878                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B  1646        B  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  47.0771 191.5531  14.5838              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2755 T22:   1.1299                                     
REMARK   3      T33:   1.0387 T12:   0.1238                                     
REMARK   3      T13:   0.4797 T23:   0.5341                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   8.9681 L22:   7.5430                                     
REMARK   3      L33:   1.9162 L12:   1.8836                                     
REMARK   3      L13:   0.5282 L23:  -0.3342                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0240 S12:  -0.2174 S13:   0.2859                       
REMARK   3      S21:   0.4005 S22:   0.5590 S23:   2.3655                       
REMARK   3      S31:  -0.1959 S32:   0.0546 S33:  -0.5830                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C  1648        C  1859                          
REMARK   3    ORIGIN FOR THE GROUP (A):  66.6048 142.3219 -10.2320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.8234 T22:   1.7871                                     
REMARK   3      T33:   0.8829 T12:  -0.0982                                     
REMARK   3      T13:  -0.4730 T23:  -0.3166                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.4117 L22:   0.3109                                     
REMARK   3      L33:   5.6695 L12:   0.0727                                     
REMARK   3      L13:   0.3801 L23:   0.2197                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.2648 S12:   1.1629 S13:  -1.1609                       
REMARK   3      S21:  -0.4356 S22:   0.1398 S23:  -0.1481                       
REMARK   3      S31:   0.3346 S32:  -0.1781 S33:  -0.4045                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   E   399        E   409                          
REMARK   3    ORIGIN FOR THE GROUP (A):  43.2151 209.5097  16.6616              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   1.2984 T22:   1.2904                                     
REMARK   3      T33:   1.3922 T12:  -0.0527                                     
REMARK   3      T13:   0.2994 T23:  -0.1274                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:  16.1534 L22:   0.4964                                     
REMARK   3      L33:   1.4484 L12:   2.4424                                     
REMARK   3      L13:  -3.1593 L23:  -0.7468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.9117 S12:  -1.0417 S13:   1.0392                       
REMARK   3      S21:  -0.3955 S22:   0.1223 S23:  -0.0859                       
REMARK   3      S31:   0.6308 S32:  -0.1364 S33:   0.7894                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4U4A COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-AUG-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000202383.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 03-FEB-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : BM14                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.900                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15491                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.510                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 59.890                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 6.900                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 9.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 74.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.85                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.01M COBALT CHLORIDE, 0.1 M(MES), PH    
REMARK 280  6.5, 30% PEG MONO METHYL ETHER (MME) 5000, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 295K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       42.67500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       93.75000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       93.75000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       21.33750            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       93.75000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       93.75000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       64.01250            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       93.75000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       93.75000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       21.33750            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       93.75000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       93.75000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       64.01250            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       42.67500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3                                                 
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 700 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11840 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 740 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11970 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E                                  
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: 3                                                       
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: 720 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 11300 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, F                                  
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 C  1646                                                      
REMARK 465     ASN C  1647                                                      
REMARK 465     GLY D   399                                                      
REMARK 465     PHE D   400                                                      
REMARK 465     GLY F   399                                                      
REMARK 465     PHE F   400                                                      
REMARK 465     GLY F   401                                                      
REMARK 465     GLU F   402                                                      
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     GLU A1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP A1818    CG   OD1  OD2                                       
REMARK 470     ASN A1819    CG   OD1  ND2                                       
REMARK 470     GLU B1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP B1818    CG   OD1  OD2                                       
REMARK 470     GLU C1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP C1818    CG   OD1  OD2                                       
REMARK 470     ASN C1819    CG   OD1  ND2                                       
REMARK 470     TYR D 403    O    CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR D 403    OH                                                  
REMARK 470     TYR E 403    O                                                   
REMARK 470     TYR F 403    O                                                   
REMARK 470     ARG F 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE2  GLU B  1765     OG1  THR B  1799              1.55            
REMARK 500   OE2  GLU A  1765     OG1  THR A  1799              1.59            
REMARK 500   OG   SER B  1655     O2P  SEP E   406              1.69            
REMARK 500   OE2  GLU C  1765     OG1  THR C  1799              1.84            
REMARK 500   CD   GLU B  1765     OG1  THR B  1799              1.98            
REMARK 500   O    GLY D   401     N    TYR D   403              2.03            
REMARK 500   CD   GLU A  1765     OG1  THR A  1799              2.03            
REMARK 500   OG   SER B  1651     CA   THR B  1684              2.11            
REMARK 500   OE1  GLU B  1765     OG1  THR B  1799              2.11            
REMARK 500   OE1  GLU A  1765     OG1  THR A  1799              2.13            
REMARK 500   OG   SER C  1655     O2P  SEP F   406              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   NH2  ARG A  1670     O    ARG E   405     3655     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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    TYR D 403   CB  -  CA  -  C   ANGL. DEV. =  14.1 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    GLU A1660      -61.98    -26.81                                   
REMARK 500    HIS A1672       31.66    -97.41                                   
REMARK 500    MET A1728       97.28    -64.30                                   
REMARK 500    ASN A1742       61.06   -102.35                                   
REMARK 500    ASN A1745       41.05   -156.92                                   
REMARK 500    SER A1755       45.89    -82.86                                   
REMARK 500    ARG A1758       70.82   -114.31                                   
REMARK 500    CYS A1768       93.54    -69.04                                   
REMARK 500    SER A1797        7.01    -66.49                                   
REMARK 500    ALA A1814       -1.37    -57.76                                   
REMARK 500    GLU A1817       57.81     26.43                                   
REMARK 500    ASP A1818       99.62   -167.74                                   
REMARK 500    PHE A1821       -9.46    -59.99                                   
REMARK 500    LYS B1648     -137.23   -153.22                                   
REMARK 500    GLU B1660      -61.91    -26.82                                   
REMARK 500    HIS B1672       31.51    -96.85                                   
REMARK 500    GLU B1683      -36.08    -34.39                                   
REMARK 500    MET B1728       97.73    -64.96                                   
REMARK 500    ASN B1742       60.31   -101.77                                   
REMARK 500    ASN B1745       44.02   -157.79                                   
REMARK 500    SER B1755       45.28    -83.30                                   
REMARK 500    ARG B1758       71.94   -114.70                                   
REMARK 500    CYS B1768       91.72    -68.81                                   
REMARK 500    SER B1797        6.44    -66.77                                   
REMARK 500    THR B1802      -53.58     63.55                                   
REMARK 500    ALA B1814       -2.07    -58.50                                   
REMARK 500    GLU B1817       58.91     26.69                                   
REMARK 500    ASP B1818       98.30   -167.34                                   
REMARK 500    PHE B1821       -9.77    -59.48                                   
REMARK 500    TYR B1845       69.00     39.95                                   
REMARK 500    MET C1650     -156.34   -158.52                                   
REMARK 500    GLU C1660      -62.17    -26.44                                   
REMARK 500    HIS C1672       31.20    -96.87                                   
REMARK 500    MET C1728       97.17    -64.02                                   
REMARK 500    ASN C1742       60.72   -101.10                                   
REMARK 500    ASN C1745       43.67   -157.85                                   
REMARK 500    SER C1755       45.68    -82.41                                   
REMARK 500    ARG C1758       71.13   -114.29                                   
REMARK 500    CYS C1768       91.80    -68.79                                   
REMARK 500    SER C1797        6.58    -67.10                                   
REMARK 500    THR C1802      -61.69     73.08                                   
REMARK 500    ALA C1814       -1.40    -58.13                                   
REMARK 500    GLU C1817       58.24     27.08                                   
REMARK 500    ASP C1818      100.81   -169.88                                   
REMARK 500    PHE C1821       -9.44    -59.64                                   
REMARK 500    GLU D 402      -31.94     40.23                                   
REMARK 500    TYR D 403     -166.55     -3.38                                   
REMARK 500    SER D 404      -20.42   -153.41                                   
REMARK 500    ARG D 405      144.34    107.19                                   
REMARK 500    TYR E 403     -176.44     76.13                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      54 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY A 1801     THR A 1802                  -32.03                    
REMARK 500 VAL B 1646     ASN B 1647                 -128.54                    
REMARK 500 ASN B 1647     LYS B 1648                 -142.03                    
REMARK 500 MET C 1650     SER C 1651                 -148.71                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4JLU   RELATED DB: PDB                                   
REMARK 900 DOUBLY PHOSPHO COMPLEX WITH BRCA1 BRCT                               
DBREF  4U4A A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4U4A B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4U4A C 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4U4A D  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4U4A E  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4U4A F  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
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 ARG GLU TRP VAL LEU ASP          
SEQRES  16 A  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 A  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 B  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 B  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 B  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 B  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 B  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 B  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 B  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 B  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 B  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 B  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 B  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 B  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 B  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 B  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 B  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 B  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 B  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 C  214  VAL ASN LYS ARG MET SER MET VAL VAL SER GLY LEU THR          
SEQRES   2 C  214  PRO GLU GLU PHE MET LEU VAL TYR LYS PHE ALA ARG LYS          
SEQRES   3 C  214  HIS HIS ILE THR LEU THR ASN LEU ILE THR GLU GLU THR          
SEQRES   4 C  214  THR HIS VAL VAL MET LYS THR ASP ALA GLU PHE VAL CYS          
SEQRES   5 C  214  GLU ARG THR LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY          
SEQRES   6 C  214  LYS TRP VAL VAL SER TYR PHE TRP VAL THR GLN SER ILE          
SEQRES   7 C  214  LYS GLU ARG LYS MET LEU ASN GLU HIS ASP PHE GLU VAL          
SEQRES   8 C  214  ARG GLY ASP VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO          
SEQRES   9 C  214  LYS ARG ALA ARG GLU SER GLN ASP ARG LYS ILE PHE ARG          
SEQRES  10 C  214  GLY LEU GLU ILE CYS CYS TYR GLY PRO PHE THR ASN MET          
SEQRES  11 C  214  PRO THR ASP GLN LEU GLU TRP MET VAL GLN LEU CYS GLY          
SEQRES  12 C  214  ALA SER VAL VAL LYS GLU LEU SER SER PHE THR LEU GLY          
SEQRES  13 C  214  THR GLY VAL HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA          
SEQRES  14 C  214  TRP THR GLU ASP ASN GLY PHE HIS ALA ILE GLY GLN MET          
SEQRES  15 C  214  CYS GLU ALA PRO VAL VAL THR ARG GLU TRP VAL LEU ASP          
SEQRES  16 C  214  SER VAL ALA LEU TYR GLN CYS GLN GLU LEU ASP THR TYR          
SEQRES  17 C  214  LEU ILE PRO GLN ILE PRO                                      
SEQRES   1 D   11  GLY PHE GLY GLU TYR SER ARG SEP PRO THR PHE                  
SEQRES   1 E   11  GLY PHE GLY GLU TYR SER ARG SEP PRO THR PHE                  
SEQRES   1 F   11  GLY PHE GLY GLU TYR SER ARG SEP PRO THR PHE                  
MODRES 4U4A SEP D  406  SER  MODIFIED RESIDUE                                   
MODRES 4U4A SEP E  406  SER  MODIFIED RESIDUE                                   
MODRES 4U4A SEP F  406  SER  MODIFIED RESIDUE                                   
HET    SEP  D 406      10                                                       
HET    SEP  E 406      10                                                       
HET    SEP  F 406      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   4  SEP    3(C3 H8 N O6 P)                                              
HELIX    1 AA1 THR A 1658  HIS A 1672  1                                  15    
HELIX    2 AA2 THR A 1700  GLY A 1710  1                                  11    
HELIX    3 AA3 TYR A 1716  ARG A 1726  1                                  11    
HELIX    4 AA4 GLN A 1747  SER A 1755  1                                   9    
HELIX    5 AA5 PRO A 1776  LEU A 1786  1                                  11    
HELIX    6 AA6 GLN A 1811  TRP A 1815  5                                   5    
HELIX    7 AA7 ASN A 1819  HIS A 1822  5                                   4    
HELIX    8 AA8 ALA A 1823  CYS A 1828  1                                   6    
HELIX    9 AA9 ARG A 1835  LEU A 1844  1                                  10    
HELIX   10 AB1 GLU A 1849  LEU A 1854  1                                   6    
HELIX   11 AB2 THR B 1658  HIS B 1672  1                                  15    
HELIX   12 AB3 THR B 1700  GLY B 1710  1                                  11    
HELIX   13 AB4 TYR B 1716  ARG B 1726  1                                  11    
HELIX   14 AB5 GLN B 1747  SER B 1755  1                                   9    
HELIX   15 AB6 PRO B 1776  LEU B 1786  1                                  11    
HELIX   16 AB7 GLN B 1811  TRP B 1815  5                                   5    
HELIX   17 AB8 ASN B 1819  HIS B 1822  5                                   4    
HELIX   18 AB9 ALA B 1823  CYS B 1828  1                                   6    
HELIX   19 AC1 ARG B 1835  LEU B 1844  1                                  10    
HELIX   20 AC2 GLU B 1849  LEU B 1854  1                                   6    
HELIX   21 AC3 THR C 1658  HIS C 1672  1                                  15    
HELIX   22 AC4 THR C 1700  GLY C 1710  1                                  11    
HELIX   23 AC5 TYR C 1716  ARG C 1726  1                                  11    
HELIX   24 AC6 GLN C 1747  SER C 1755  1                                   9    
HELIX   25 AC7 PRO C 1776  LEU C 1786  1                                  11    
HELIX   26 AC8 GLN C 1811  TRP C 1815  5                                   5    
HELIX   27 AC9 ASN C 1819  HIS C 1822  5                                   4    
HELIX   28 AD1 ALA C 1823  CYS C 1828  1                                   6    
HELIX   29 AD2 ARG C 1835  LEU C 1844  1                                  10    
HELIX   30 AD3 GLU C 1849  LEU C 1854  1                                   6    
SHEET    1 AA1 3 SER A1651  SER A1655  0                                        
SHEET    2 AA1 3 THR A1684  MET A1689  1  O  VAL A1688   N  VAL A1653           
SHEET    3 AA1 3 TRP A1712  SER A1715  1  O  VAL A1714   N  MET A1689           
SHEET    1 AA2 2 VAL A1696  CYS A1697  0                                        
SHEET    2 AA2 2 GLY A1738  ASP A1739  1  O  GLY A1738   N  CYS A1697           
SHEET    1 AA3 4 SER A1790  VAL A1792  0                                        
SHEET    2 AA3 4 LEU A1764  CYS A1768  1  N  ILE A1766   O  VAL A1792           
SHEET    3 AA3 4 HIS A1805  VAL A1810  1  O  HIS A1805   N  GLU A1765           
SHEET    4 AA3 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1808           
SHEET    1 AA4 3 SER B1651  SER B1655  0                                        
SHEET    2 AA4 3 THR B1684  MET B1689  1  O  VAL B1688   N  VAL B1653           
SHEET    3 AA4 3 TRP B1712  SER B1715  1  O  VAL B1714   N  MET B1689           
SHEET    1 AA5 2 VAL B1696  CYS B1697  0                                        
SHEET    2 AA5 2 GLY B1738  ASP B1739  1  O  GLY B1738   N  CYS B1697           
SHEET    1 AA6 4 SER B1790  VAL B1792  0                                        
SHEET    2 AA6 4 LEU B1764  CYS B1768  1  N  ILE B1766   O  VAL B1792           
SHEET    3 AA6 4 HIS B1805  VAL B1810  1  O  HIS B1805   N  GLU B1765           
SHEET    4 AA6 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SHEET    1 AA7 3 MET C1652  SER C1655  0                                        
SHEET    2 AA7 3 HIS C1686  MET C1689  1  O  VAL C1688   N  VAL C1653           
SHEET    3 AA7 3 TRP C1712  SER C1715  1  O  VAL C1714   N  MET C1689           
SHEET    1 AA8 2 VAL C1696  CYS C1697  0                                        
SHEET    2 AA8 2 GLY C1738  ASP C1739  1  O  GLY C1738   N  CYS C1697           
SHEET    1 AA9 4 SER C1790  VAL C1792  0                                        
SHEET    2 AA9 4 LEU C1764  CYS C1768  1  N  ILE C1766   O  VAL C1792           
SHEET    3 AA9 4 HIS C1805  VAL C1810  1  O  HIS C1805   N  GLU C1765           
SHEET    4 AA9 4 VAL C1832  THR C1834  1  O  VAL C1833   N  VAL C1808           
LINK         C   ARG D 405                 N   SEP D 406     1555   1555  1.33  
LINK         C   SEP D 406                 N   PRO D 407     1555   1555  1.37  
LINK         C   ARG E 405                 N   SEP E 406     1555   1555  1.33  
LINK         C   SEP E 406                 N   PRO E 407     1555   1555  1.35  
LINK         C   ARG F 405                 N   SEP F 406     1555   1555  1.33  
LINK         C   SEP F 406                 N   PRO F 407     1555   1555  1.37  
CISPEP   1 GLY A 1770    PRO A 1771          0        -1.48                     
CISPEP   2 LYS B 1648    ARG B 1649          0       -10.45                     
CISPEP   3 GLY B 1770    PRO B 1771          0        -4.47                     
CISPEP   4 LYS C 1648    ARG C 1649          0        -6.88                     
CISPEP   5 GLY C 1770    PRO C 1771          0        -3.67                     
CISPEP   6 TYR D  403    SER D  404          0        -7.67                     
CISPEP   7 GLY E  399    PHE E  400          0        11.64                     
CISPEP   8 GLY E  401    GLU E  402          0         0.49                     
CISPEP   9 TYR E  403    SER E  404          0         7.46                     
CISPEP  10 TYR F  403    SER F  404          0        -5.92                     
CRYST1  187.500  187.500   85.350  90.00  90.00  90.00 P 41 21 2    24          
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      0.005333  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005333  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011716        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system