GenomeNet

Database: PDB
Entry: 4Y18
LinkDB: 4Y18
Original site: 4Y18 
HEADER    ANTITUMOR PROTEIN                       06-FEB-15   4Y18              
TITLE     STRUCTURE OF BRCA1 BRCT DOMAINS IN COMPLEX WITH ABRAXAS DOUBLE        
TITLE    2 PHOSPHORYLATED PEPTIDE                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BREAST CANCER TYPE 1 SUSCEPTIBILITY PROTEIN;               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 FRAGMENT: BRCT DOMAINS, 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: I, J, K, L, M, N, O, P;                                       
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: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    DNA DAMAGE RESPONSE, BRCT, PHOSPHOPEPTIDE, LIGASE-PEPTIDE COMPLEX,    
KEYWDS   2 ANTITUMOR PROTEIN                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Q.WU,T.L.BLUNDELL                                                     
REVDAT   5   10-JAN-24 4Y18    1       REMARK                                   
REVDAT   4   10-JUL-19 4Y18    1       REMARK                                   
REVDAT   3   20-FEB-19 4Y18    1       REMARK LINK                              
REVDAT   2   17-FEB-16 4Y18    1       JRNL                                     
REVDAT   1   27-JAN-16 4Y18    0                                                
JRNL        AUTH   Q.WU,A.PAUL,D.SU,S.MEHMOOD,T.K.FOO,T.OCHI,E.L.BUNTING,B.XIA, 
JRNL        AUTH 2 C.V.ROBINSON,B.WANG,T.L.BLUNDELL                             
JRNL        TITL   STRUCTURE OF BRCA1-BRCT/ABRAXAS COMPLEX REVEALS              
JRNL        TITL 2 PHOSPHORYLATION-DEPENDENT BRCT DIMERIZATION AT DNA DAMAGE    
JRNL        TITL 3 SITES.                                                       
JRNL        REF    MOL.CELL                      V.  61   434 2016              
JRNL        REFN                   ISSN 1097-2765                               
JRNL        PMID   26778126                                                     
JRNL        DOI    10.1016/J.MOLCEL.2015.12.017                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 95.26                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 39160                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.236                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1961                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 95.2902 -  8.4337    1.00     2838   155  0.1969 0.2969        
REMARK   3     2  8.4337 -  6.6946    1.00     2721   147  0.2130 0.2838        
REMARK   3     3  6.6946 -  5.8485    1.00     2694   132  0.2408 0.3126        
REMARK   3     4  5.8485 -  5.3138    1.00     2665   146  0.2184 0.2663        
REMARK   3     5  5.3138 -  4.9330    1.00     2676   139  0.2124 0.2551        
REMARK   3     6  4.9330 -  4.6421    1.00     2627   141  0.2283 0.2649        
REMARK   3     7  4.6421 -  4.4097    1.00     2635   137  0.2384 0.3239        
REMARK   3     8  4.4097 -  4.2177    1.00     2648   140  0.2426 0.3057        
REMARK   3     9  4.2177 -  4.0553    1.00     2638   140  0.2422 0.2933        
REMARK   3    10  4.0553 -  3.9154    1.00     2607   140  0.2661 0.3544        
REMARK   3    11  3.9154 -  3.7930    1.00     2640   136  0.2820 0.2909        
REMARK   3    12  3.7930 -  3.6845    1.00     2620   136  0.2899 0.3440        
REMARK   3    13  3.6845 -  3.5875    1.00     2627   142  0.2937 0.3554        
REMARK   3    14  3.5875 -  3.5000    0.98     2563   130  0.3194 0.3409        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.470            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 29.080           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007          14312                                  
REMARK   3   ANGLE     :  0.900          19493                                  
REMARK   3   CHIRALITY :  0.031           2184                                  
REMARK   3   PLANARITY :  0.003           2478                                  
REMARK   3   DIHEDRAL  : 13.510           5111                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4Y18 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 07-FEB-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000206545.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAR-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : DIAMOND                            
REMARK 200  BEAMLINE                       : I04-1                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9200                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 2M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 39170                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.300                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.400                              
REMARK 200  R MERGE                    (I) : 0.09600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.70100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1T15                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.76                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.49                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HEPES, AMMONIUM SULPHATE, PEG 4000.,     
REMARK 280  PH 7.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 291K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
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       43.40950            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       95.25500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       91.86300            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       95.25500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       43.40950            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       91.86300            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12                   
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 APPLY THE FOLLOWING TO CHAINS: A, I                                  
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22030 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, I, J                            
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 APPLY THE FOLLOWING TO CHAINS: B, J                                  
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: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K                                  
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: 5                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3520 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22040 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -27.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, K                                  
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 APPLY THE FOLLOWING TO CHAINS: E, M                                  
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000      -43.40950            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      -91.86300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 6                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L                                  
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: 7                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3240 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21570 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, L                                  
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 APPLY THE FOLLOWING TO CHAINS: F, N                                  
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -91.86300            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -95.25500            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 8                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, M                                  
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: 9                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, N                                  
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: 10                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, O                                  
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: 11                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3030 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 21370 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -24.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, H, O, P                            
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: 12                                                      
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, P                                  
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  1636                                                      
REMARK 465     SER A  1637                                                      
REMARK 465     HIS A  1638                                                      
REMARK 465     HIS A  1639                                                      
REMARK 465     HIS A  1640                                                      
REMARK 465     HIS A  1641                                                      
REMARK 465     HIS A  1642                                                      
REMARK 465     HIS A  1643                                                      
REMARK 465     SER A  1644                                                      
REMARK 465     MET A  1645                                                      
REMARK 465     MET B  1636                                                      
REMARK 465     SER B  1637                                                      
REMARK 465     HIS B  1638                                                      
REMARK 465     HIS B  1639                                                      
REMARK 465     HIS B  1640                                                      
REMARK 465     HIS B  1641                                                      
REMARK 465     HIS B  1642                                                      
REMARK 465     HIS B  1643                                                      
REMARK 465     SER B  1644                                                      
REMARK 465     MET B  1645                                                      
REMARK 465     MET C  1636                                                      
REMARK 465     SER C  1637                                                      
REMARK 465     HIS C  1638                                                      
REMARK 465     HIS C  1639                                                      
REMARK 465     HIS C  1640                                                      
REMARK 465     HIS C  1641                                                      
REMARK 465     HIS C  1642                                                      
REMARK 465     HIS C  1643                                                      
REMARK 465     SER C  1644                                                      
REMARK 465     MET C  1645                                                      
REMARK 465     MET D  1636                                                      
REMARK 465     SER D  1637                                                      
REMARK 465     HIS D  1638                                                      
REMARK 465     HIS D  1639                                                      
REMARK 465     HIS D  1640                                                      
REMARK 465     HIS D  1641                                                      
REMARK 465     HIS D  1642                                                      
REMARK 465     HIS D  1643                                                      
REMARK 465     SER D  1644                                                      
REMARK 465     MET D  1645                                                      
REMARK 465     PRO D  1859                                                      
REMARK 465     MET E  1636                                                      
REMARK 465     SER E  1637                                                      
REMARK 465     HIS E  1638                                                      
REMARK 465     HIS E  1639                                                      
REMARK 465     HIS E  1640                                                      
REMARK 465     HIS E  1641                                                      
REMARK 465     HIS E  1642                                                      
REMARK 465     HIS E  1643                                                      
REMARK 465     SER E  1644                                                      
REMARK 465     MET E  1645                                                      
REMARK 465     MET F  1636                                                      
REMARK 465     SER F  1637                                                      
REMARK 465     HIS F  1638                                                      
REMARK 465     HIS F  1639                                                      
REMARK 465     HIS F  1640                                                      
REMARK 465     HIS F  1641                                                      
REMARK 465     HIS F  1642                                                      
REMARK 465     HIS F  1643                                                      
REMARK 465     SER F  1644                                                      
REMARK 465     MET F  1645                                                      
REMARK 465     MET G  1636                                                      
REMARK 465     SER G  1637                                                      
REMARK 465     HIS G  1638                                                      
REMARK 465     HIS G  1639                                                      
REMARK 465     HIS G  1640                                                      
REMARK 465     HIS G  1641                                                      
REMARK 465     HIS G  1642                                                      
REMARK 465     HIS G  1643                                                      
REMARK 465     SER G  1644                                                      
REMARK 465     MET G  1645                                                      
REMARK 465     VAL G  1646                                                      
REMARK 465     ASN G  1647                                                      
REMARK 465     LYS G  1648                                                      
REMARK 465     MET H  1636                                                      
REMARK 465     SER H  1637                                                      
REMARK 465     HIS H  1638                                                      
REMARK 465     HIS H  1639                                                      
REMARK 465     HIS H  1640                                                      
REMARK 465     HIS H  1641                                                      
REMARK 465     HIS H  1642                                                      
REMARK 465     HIS H  1643                                                      
REMARK 465     SER H  1644                                                      
REMARK 465     MET H  1645                                                      
REMARK 465     VAL H  1646                                                      
REMARK 465     ASN H  1647                                                      
REMARK 465     LYS H  1648                                                      
REMARK 465     GLY I   399                                                      
REMARK 465     PHE I   400                                                      
REMARK 465     GLY J   399                                                      
REMARK 465     PHE J   400                                                      
REMARK 465     GLY K   399                                                      
REMARK 465     PHE K   400                                                      
REMARK 465     GLY L   399                                                      
REMARK 465     PHE L   400                                                      
REMARK 465     GLY L   401                                                      
REMARK 465     GLY M   399                                                      
REMARK 465     PHE M   400                                                      
REMARK 465     GLY M   401                                                      
REMARK 465     GLY N   399                                                      
REMARK 465     PHE N   400                                                      
REMARK 465     GLY N   401                                                      
REMARK 465     GLU N   402                                                      
REMARK 465     GLY O   399                                                      
REMARK 465     PHE O   400                                                      
REMARK 465     GLY O   401                                                      
REMARK 465     GLU O   402                                                      
REMARK 465     GLY P   399                                                      
REMARK 465     PHE P   400                                                      
REMARK 465     GLY P   401                                                      
REMARK 465     GLU P   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     LYS A1648    CG   CD   CE   NZ                                   
REMARK 470     ARG A1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1667    CG   CD   CE   NZ                                   
REMARK 470     LEU A1800    CG   CD1  CD2                                       
REMARK 470     ASP A1851    CG   OD1  OD2                                       
REMARK 470     LYS B1648    CG   CD   CE   NZ                                   
REMARK 470     ARG B1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS B1671    CG   CD   CE   NZ                                   
REMARK 470     ARG B1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU B1817    CG   CD   OE1  OE2                                  
REMARK 470     LYS C1648    CG   CD   CE   NZ                                   
REMARK 470     ARG C1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU C1664    CG   CD1  CD2                                       
REMARK 470     LYS C1671    CG   CD   CE   NZ                                   
REMARK 470     GLU C1817    CG   CD   OE1  OE2                                  
REMARK 470     ASN C1819    CG   OD1  ND2                                       
REMARK 470     ARG D1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS D1667    CG   CD   CE   NZ                                   
REMARK 470     LYS D1671    CG   CD   CE   NZ                                   
REMARK 470     HIS D1732    CG   ND1  CD2  CE1  NE2                             
REMARK 470     ARG D1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU D1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP D1818    CG   OD1  OD2                                       
REMARK 470     ASN D1819    CG   OD1  ND2                                       
REMARK 470     LYS E1648    CG   CD   CE   NZ                                   
REMARK 470     ARG E1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS E1671    CG   CD   CE   NZ                                   
REMARK 470     LEU E1679    CG   CD1  CD2                                       
REMARK 470     LYS E1724    CG   CD   CE   NZ                                   
REMARK 470     ARG E1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG E1762    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU E1817    CG   CD   OE1  OE2                                  
REMARK 470     LYS F1648    CG   CD   CE   NZ                                   
REMARK 470     ARG F1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F1671    CG   CD   CE   NZ                                   
REMARK 470     ARG F1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS F1727    CG   CD   CE   NZ                                   
REMARK 470     ARG F1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU F1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP F1818    CG   OD1  OD2                                       
REMARK 470     ASN F1819    CG   OD1  ND2                                       
REMARK 470     ARG G1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET G1652    CG   SD   CE                                        
REMARK 470     PHE G1662    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET G1663    CG   SD   CE                                        
REMARK 470     ARG G1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU G1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP G1818    CG   OD1  OD2                                       
REMARK 470     ARG H1649    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     MET H1652    CG   SD   CE                                        
REMARK 470     PHE H1662    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET H1663    CG   SD   CE                                        
REMARK 470     TYR H1666    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS H1667    CG   CD   CE   NZ                                   
REMARK 470     PHE H1668    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     LYS H1671    CG   CD   CE   NZ                                   
REMARK 470     VAL H1688    CG1  CG2                                            
REMARK 470     LYS H1711    CG   CD   CE   NZ                                   
REMARK 470     LYS H1724    CG   CD   CE   NZ                                   
REMARK 470     ARG H1726    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG H1758    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU H1817    CG   CD   OE1  OE2                                  
REMARK 470     ASP H1818    CG   OD1  OD2                                       
REMARK 470     GLN H1857    CG   CD   OE1  NE2                                  
REMARK 470     ARG I 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG J 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG K 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG L 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG N 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR O 403    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG O 405    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG P 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   O    ALA D  1669     O    HIS D  1672              1.88            
REMARK 500   OG   SER B  1722     O    LYS B  1727              2.16            
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   SD   MET C  1663     SD   MET E  1663     4445     1.03            
REMARK 500   SD   MET C  1663     CG   MET E  1663     4445     1.80            
REMARK 500   SD   MET C  1663     CE   MET E  1663     4445     1.91            
REMARK 500   CE   MET C  1663     CG   MET E  1663     4445     1.94            
REMARK 500   NH2  ARG D  1670     O1P  SEP N   406     3544     2.06            
REMARK 500   NH2  ARG D  1670     O    ARG N   405     3544     2.11            
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    ASN A1745       45.93   -152.84                                   
REMARK 500    GLU A1829       76.00   -100.42                                   
REMARK 500    ASN B1745       46.68   -153.08                                   
REMARK 500    MET B1775      109.34   -160.31                                   
REMARK 500    GLU B1817       14.46     59.09                                   
REMARK 500    ASN C1745       46.33   -153.29                                   
REMARK 500    GLU C1817       14.86     58.99                                   
REMARK 500    GLU C1829       78.06   -102.28                                   
REMARK 500    ASN D1745       45.81   -151.64                                   
REMARK 500    GLU D1829       78.22   -103.11                                   
REMARK 500    GLN D1857     -159.15   -108.23                                   
REMARK 500    ASN E1745       47.70   -152.96                                   
REMARK 500    GLU E1817        7.23     58.11                                   
REMARK 500    GLU E1829       78.61   -102.65                                   
REMARK 500    ASN F1745       47.06   -152.21                                   
REMARK 500    GLU F1829       76.00   -102.01                                   
REMARK 500    ASN G1745       46.73   -152.50                                   
REMARK 500    MET G1775      109.16   -160.98                                   
REMARK 500    GLU G1829       78.67   -102.98                                   
REMARK 500    ASN H1745       47.22   -152.93                                   
REMARK 500    GLU H1829       78.82   -101.29                                   
REMARK 500    SEP N 404       -4.75     84.26                                   
REMARK 500    ARG N 405     -134.66     53.55                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  4Y18 A 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 B 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 C 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 D 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 E 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 F 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 G 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 H 1646  1859  UNP    P38398   BRCA1_HUMAN   1646   1859             
DBREF  4Y18 I  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 J  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 K  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 L  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 M  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 N  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 O  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
DBREF  4Y18 P  399   409  UNP    Q6UWZ7   F175A_HUMAN    399    409             
SEQADV 4Y18 MET A 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER A 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS A 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER A 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET A 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET B 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER B 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS B 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER B 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET B 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET C 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER C 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS C 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER C 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET C 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET D 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER D 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS D 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER D 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET D 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET E 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER E 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS E 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER E 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET E 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET F 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER F 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS F 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER F 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET F 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET G 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER G 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS G 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER G 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET G 1645  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET H 1636  UNP  P38398              INITIATING METHIONINE          
SEQADV 4Y18 SER H 1637  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1638  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1639  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1640  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1641  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1642  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 HIS H 1643  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 SER H 1644  UNP  P38398              EXPRESSION TAG                 
SEQADV 4Y18 MET H 1645  UNP  P38398              EXPRESSION TAG                 
SEQRES   1 A  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 A  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 A  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 A  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 A  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 A  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 A  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 A  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 A  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 A  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 A  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 A  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 A  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 A  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 A  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 A  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 A  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 A  224  GLN ILE PRO                                                  
SEQRES   1 B  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 B  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 B  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 B  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 B  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 B  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 B  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 B  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 B  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 B  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 B  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 B  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 B  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 B  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 B  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 B  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 B  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 B  224  GLN ILE PRO                                                  
SEQRES   1 C  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 C  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 C  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 C  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 C  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 C  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 C  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 C  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 C  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 C  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 C  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 C  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 C  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 C  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 C  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 C  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 C  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 C  224  GLN ILE PRO                                                  
SEQRES   1 D  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 D  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 D  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 D  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 D  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 D  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 D  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 D  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 D  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 D  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 D  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 D  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 D  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 D  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 D  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 D  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 D  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 D  224  GLN ILE PRO                                                  
SEQRES   1 E  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 E  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 E  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 E  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 E  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 E  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 E  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 E  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 E  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 E  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 E  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 E  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 E  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 E  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 E  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 E  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 E  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 E  224  GLN ILE PRO                                                  
SEQRES   1 F  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 F  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 F  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 F  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 F  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 F  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 F  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 F  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 F  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 F  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 F  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 F  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 F  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 F  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 F  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 F  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 F  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 F  224  GLN ILE PRO                                                  
SEQRES   1 G  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 G  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 G  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 G  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 G  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 G  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 G  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 G  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 G  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 G  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 G  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 G  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 G  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 G  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 G  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 G  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 G  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 G  224  GLN ILE PRO                                                  
SEQRES   1 H  224  MET SER HIS HIS HIS HIS HIS HIS SER MET VAL ASN LYS          
SEQRES   2 H  224  ARG MET SER MET VAL VAL SER GLY LEU THR PRO GLU GLU          
SEQRES   3 H  224  PHE MET LEU VAL TYR LYS PHE ALA ARG LYS HIS HIS ILE          
SEQRES   4 H  224  THR LEU THR ASN LEU ILE THR GLU GLU THR THR HIS VAL          
SEQRES   5 H  224  VAL MET LYS THR ASP ALA GLU PHE VAL CYS GLU ARG THR          
SEQRES   6 H  224  LEU LYS TYR PHE LEU GLY ILE ALA GLY GLY LYS TRP VAL          
SEQRES   7 H  224  VAL SER TYR PHE TRP VAL THR GLN SER ILE LYS GLU ARG          
SEQRES   8 H  224  LYS MET LEU ASN GLU HIS ASP PHE GLU VAL ARG GLY ASP          
SEQRES   9 H  224  VAL VAL ASN GLY ARG ASN HIS GLN GLY PRO LYS ARG ALA          
SEQRES  10 H  224  ARG GLU SER GLN ASP ARG LYS ILE PHE ARG GLY LEU GLU          
SEQRES  11 H  224  ILE CYS CYS TYR GLY PRO PHE THR ASN MET PRO THR ASP          
SEQRES  12 H  224  GLN LEU GLU TRP MET VAL GLN LEU CYS GLY ALA SER VAL          
SEQRES  13 H  224  VAL LYS GLU LEU SER SER PHE THR LEU GLY THR GLY VAL          
SEQRES  14 H  224  HIS PRO ILE VAL VAL VAL GLN PRO ASP ALA TRP THR GLU          
SEQRES  15 H  224  ASP ASN GLY PHE HIS ALA ILE GLY GLN MET CYS GLU ALA          
SEQRES  16 H  224  PRO VAL VAL THR ARG GLU TRP VAL LEU ASP SER VAL ALA          
SEQRES  17 H  224  LEU TYR GLN CYS GLN GLU LEU ASP THR TYR LEU ILE PRO          
SEQRES  18 H  224  GLN ILE PRO                                                  
SEQRES   1 I   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 J   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 K   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 L   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 M   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 N   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 O   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
SEQRES   1 P   11  GLY PHE GLY GLU TYR SEP ARG SEP PRO THR PHE                  
MODRES 4Y18 SEP I  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP I  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP J  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP J  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP K  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP K  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP L  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP L  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP M  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP M  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP N  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP N  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP O  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP O  406  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP P  404  SER  MODIFIED RESIDUE                                   
MODRES 4Y18 SEP P  406  SER  MODIFIED RESIDUE                                   
HET    SEP  I 404      10                                                       
HET    SEP  I 406      10                                                       
HET    SEP  J 404      10                                                       
HET    SEP  J 406      10                                                       
HET    SEP  K 404      10                                                       
HET    SEP  K 406      10                                                       
HET    SEP  L 404      10                                                       
HET    SEP  L 406      10                                                       
HET    SEP  M 404      10                                                       
HET    SEP  M 406      10                                                       
HET    SEP  N 404      10                                                       
HET    SEP  N 406      10                                                       
HET    SEP  O 404      10                                                       
HET    SEP  O 406      10                                                       
HET    SEP  P 404      10                                                       
HET    SEP  P 406      10                                                       
HETNAM     SEP PHOSPHOSERINE                                                    
HETSYN     SEP PHOSPHONOSERINE                                                  
FORMUL   9  SEP    16(C3 H8 N O6 P)                                             
FORMUL  17  HOH   *(H2 O)                                                       
HELIX    1 AA1 THR A 1658  HIS A 1672  1                                  15    
HELIX    2 AA2 THR A 1700  GLY A 1709  1                                  10    
HELIX    3 AA3 TYR A 1716  ARG A 1726  1                                  11    
HELIX    4 AA4 ASN A 1730  GLU A 1735  5                                   6    
HELIX    5 AA5 GLN A 1747  GLU A 1754  1                                   8    
HELIX    6 AA6 PRO A 1776  CYS A 1787  1                                  12    
HELIX    7 AA7 GLU A 1794  PHE A 1798  5                                   5    
HELIX    8 AA8 GLN A 1811  TRP A 1815  5                                   5    
HELIX    9 AA9 ASN A 1819  MET A 1827  5                                   9    
HELIX   10 AB1 ARG A 1835  TYR A 1845  1                                  11    
HELIX   11 AB2 GLU A 1849  LEU A 1854  5                                   6    
HELIX   12 AB3 THR B 1658  HIS B 1672  1                                  15    
HELIX   13 AB4 THR B 1700  GLY B 1709  1                                  10    
HELIX   14 AB5 TYR B 1716  GLU B 1725  1                                  10    
HELIX   15 AB6 ASN B 1730  GLU B 1735  5                                   6    
HELIX   16 AB7 GLN B 1747  SER B 1755  1                                   9    
HELIX   17 AB8 PRO B 1776  CYS B 1787  1                                  12    
HELIX   18 AB9 GLU B 1794  PHE B 1798  5                                   5    
HELIX   19 AC1 GLN B 1811  TRP B 1815  5                                   5    
HELIX   20 AC2 ASN B 1819  MET B 1827  5                                   9    
HELIX   21 AC3 ARG B 1835  TYR B 1845  1                                  11    
HELIX   22 AC4 GLU B 1849  LEU B 1854  5                                   6    
HELIX   23 AC5 THR C 1658  HIS C 1672  1                                  15    
HELIX   24 AC6 THR C 1700  GLY C 1709  1                                  10    
HELIX   25 AC7 TYR C 1716  ARG C 1726  1                                  11    
HELIX   26 AC8 ASN C 1730  GLU C 1735  5                                   6    
HELIX   27 AC9 GLN C 1747  SER C 1755  1                                   9    
HELIX   28 AD1 PRO C 1776  CYS C 1787  1                                  12    
HELIX   29 AD2 GLU C 1794  PHE C 1798  5                                   5    
HELIX   30 AD3 GLN C 1811  TRP C 1815  5                                   5    
HELIX   31 AD4 ASN C 1819  MET C 1827  5                                   9    
HELIX   32 AD5 ARG C 1835  TYR C 1845  1                                  11    
HELIX   33 AD6 GLU C 1849  LEU C 1854  5                                   6    
HELIX   34 AD7 THR D 1658  HIS D 1672  1                                  15    
HELIX   35 AD8 THR D 1700  GLY D 1709  1                                  10    
HELIX   36 AD9 TYR D 1716  ARG D 1726  1                                  11    
HELIX   37 AE1 ASN D 1730  GLU D 1735  5                                   6    
HELIX   38 AE2 GLN D 1747  SER D 1755  1                                   9    
HELIX   39 AE3 GLN D 1756  LYS D 1759  5                                   4    
HELIX   40 AE4 PRO D 1776  CYS D 1787  1                                  12    
HELIX   41 AE5 GLU D 1794  PHE D 1798  5                                   5    
HELIX   42 AE6 ASN D 1819  MET D 1827  5                                   9    
HELIX   43 AE7 ARG D 1835  TYR D 1845  1                                  11    
HELIX   44 AE8 GLU D 1849  LEU D 1854  5                                   6    
HELIX   45 AE9 THR E 1658  HIS E 1673  1                                  16    
HELIX   46 AF1 THR E 1700  GLY E 1709  1                                  10    
HELIX   47 AF2 TYR E 1716  GLU E 1725  1                                  10    
HELIX   48 AF3 ASN E 1730  GLU E 1735  5                                   6    
HELIX   49 AF4 GLN E 1747  SER E 1755  1                                   9    
HELIX   50 AF5 GLN E 1756  LYS E 1759  5                                   4    
HELIX   51 AF6 PRO E 1776  CYS E 1787  1                                  12    
HELIX   52 AF7 GLU E 1794  PHE E 1798  5                                   5    
HELIX   53 AF8 GLN E 1811  TRP E 1815  5                                   5    
HELIX   54 AF9 ASN E 1819  MET E 1827  5                                   9    
HELIX   55 AG1 ARG E 1835  TYR E 1845  1                                  11    
HELIX   56 AG2 GLU E 1849  LEU E 1854  5                                   6    
HELIX   57 AG3 THR F 1658  HIS F 1672  1                                  15    
HELIX   58 AG4 THR F 1700  GLY F 1709  1                                  10    
HELIX   59 AG5 TYR F 1716  ARG F 1726  1                                  11    
HELIX   60 AG6 ASN F 1730  GLU F 1735  5                                   6    
HELIX   61 AG7 GLN F 1747  SER F 1755  1                                   9    
HELIX   62 AG8 PRO F 1776  CYS F 1787  1                                  12    
HELIX   63 AG9 GLU F 1794  PHE F 1798  5                                   5    
HELIX   64 AH1 ASN F 1819  MET F 1827  5                                   9    
HELIX   65 AH2 ARG F 1835  TYR F 1845  1                                  11    
HELIX   66 AH3 GLU F 1849  LEU F 1854  5                                   6    
HELIX   67 AH4 THR G 1658  HIS G 1672  1                                  15    
HELIX   68 AH5 THR G 1700  GLY G 1709  1                                  10    
HELIX   69 AH6 TYR G 1716  ARG G 1726  1                                  11    
HELIX   70 AH7 ASN G 1730  GLU G 1735  5                                   6    
HELIX   71 AH8 GLN G 1747  SER G 1755  1                                   9    
HELIX   72 AH9 PRO G 1776  CYS G 1787  1                                  12    
HELIX   73 AI1 GLU G 1794  PHE G 1798  5                                   5    
HELIX   74 AI2 GLN G 1811  TRP G 1815  5                                   5    
HELIX   75 AI3 ASN G 1819  HIS G 1822  5                                   4    
HELIX   76 AI4 ALA G 1823  CYS G 1828  1                                   6    
HELIX   77 AI5 ARG G 1835  TYR G 1845  1                                  11    
HELIX   78 AI6 GLU G 1849  LEU G 1854  5                                   6    
HELIX   79 AI7 THR H 1658  HIS H 1672  1                                  15    
HELIX   80 AI8 THR H 1700  GLY H 1709  1                                  10    
HELIX   81 AI9 TYR H 1716  ARG H 1726  1                                  11    
HELIX   82 AJ1 ASN H 1730  GLU H 1735  5                                   6    
HELIX   83 AJ2 GLN H 1747  SER H 1755  1                                   9    
HELIX   84 AJ3 PRO H 1776  CYS H 1787  1                                  12    
HELIX   85 AJ4 GLU H 1794  PHE H 1798  5                                   5    
HELIX   86 AJ5 GLN H 1811  TRP H 1815  5                                   5    
HELIX   87 AJ6 ASN H 1819  MET H 1827  5                                   9    
HELIX   88 AJ7 ARG H 1835  TYR H 1845  1                                  11    
HELIX   89 AJ8 GLU H 1849  LEU H 1854  5                                   6    
SHEET    1 AA1 4 THR A1675  LEU A1676  0                                        
SHEET    2 AA1 4 SER A1651  SER A1655  1  N  MET A1652   O  THR A1675           
SHEET    3 AA1 4 HIS A1686  MET A1689  1  O  VAL A1688   N  SER A1655           
SHEET    4 AA1 4 TRP A1712  SER A1715  1  O  TRP A1712   N  VAL A1687           
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 A1791  0                                        
SHEET    2 AA3 4 LEU A1764  CYS A1768  1  N  LEU A1764   O  SER A1790           
SHEET    3 AA3 4 HIS A1805  VAL A1810  1  O  ILE A1807   N  CYS A1767           
SHEET    4 AA3 4 VAL A1832  THR A1834  1  O  VAL A1833   N  VAL A1808           
SHEET    1 AA4 4 THR B1675  LEU B1676  0                                        
SHEET    2 AA4 4 SER B1651  SER B1655  1  N  MET B1652   O  THR B1675           
SHEET    3 AA4 4 HIS B1686  MET B1689  1  O  VAL B1688   N  SER B1655           
SHEET    4 AA4 4 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 B1791  0                                        
SHEET    2 AA6 4 LEU B1764  CYS B1768  1  N  LEU B1764   O  SER B1790           
SHEET    3 AA6 4 HIS B1805  VAL B1810  1  O  ILE B1807   N  GLU B1765           
SHEET    4 AA6 4 VAL B1832  THR B1834  1  O  VAL B1833   N  VAL B1808           
SHEET    1 AA7 4 THR C1675  LEU C1676  0                                        
SHEET    2 AA7 4 SER C1651  SER C1655  1  N  MET C1652   O  THR C1675           
SHEET    3 AA7 4 HIS C1686  MET C1689  1  O  VAL C1688   N  VAL C1653           
SHEET    4 AA7 4 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 C1791  0                                        
SHEET    2 AA9 4 LEU C1764  CYS C1768  1  N  LEU C1764   O  SER C1790           
SHEET    3 AA9 4 HIS C1805  VAL C1810  1  O  ILE C1807   N  GLU C1765           
SHEET    4 AA9 4 VAL C1832  THR C1834  1  O  VAL C1833   N  VAL C1808           
SHEET    1 AB1 4 THR D1675  LEU D1676  0                                        
SHEET    2 AB1 4 SER D1651  SER D1655  1  N  MET D1652   O  THR D1675           
SHEET    3 AB1 4 HIS D1686  MET D1689  1  O  VAL D1688   N  VAL D1653           
SHEET    4 AB1 4 TRP D1712  SER D1715  1  O  TRP D1712   N  VAL D1687           
SHEET    1 AB2 2 VAL D1696  CYS D1697  0                                        
SHEET    2 AB2 2 GLY D1738  ASP D1739  1  O  GLY D1738   N  CYS D1697           
SHEET    1 AB3 4 SER D1790  VAL D1791  0                                        
SHEET    2 AB3 4 LEU D1764  CYS D1768  1  N  LEU D1764   O  SER D1790           
SHEET    3 AB3 4 HIS D1805  VAL D1810  1  O  HIS D1805   N  GLU D1765           
SHEET    4 AB3 4 VAL D1832  THR D1834  1  O  VAL D1833   N  VAL D1808           
SHEET    1 AB4 4 THR E1675  LEU E1676  0                                        
SHEET    2 AB4 4 SER E1651  SER E1655  1  N  MET E1652   O  THR E1675           
SHEET    3 AB4 4 HIS E1686  MET E1689  1  O  VAL E1688   N  VAL E1653           
SHEET    4 AB4 4 TRP E1712  SER E1715  1  O  VAL E1714   N  MET E1689           
SHEET    1 AB5 2 VAL E1696  CYS E1697  0                                        
SHEET    2 AB5 2 GLY E1738  ASP E1739  1  O  GLY E1738   N  CYS E1697           
SHEET    1 AB6 4 SER E1790  VAL E1791  0                                        
SHEET    2 AB6 4 GLU E1765  CYS E1768  1  N  ILE E1766   O  SER E1790           
SHEET    3 AB6 4 PRO E1806  VAL E1810  1  O  ILE E1807   N  CYS E1767           
SHEET    4 AB6 4 VAL E1832  THR E1834  1  O  VAL E1833   N  VAL E1808           
SHEET    1 AB7 4 THR F1675  LEU F1676  0                                        
SHEET    2 AB7 4 SER F1651  SER F1655  1  N  MET F1652   O  THR F1675           
SHEET    3 AB7 4 HIS F1686  MET F1689  1  O  VAL F1688   N  SER F1655           
SHEET    4 AB7 4 TRP F1712  SER F1715  1  O  VAL F1714   N  MET F1689           
SHEET    1 AB8 2 VAL F1696  CYS F1697  0                                        
SHEET    2 AB8 2 GLY F1738  ASP F1739  1  O  GLY F1738   N  CYS F1697           
SHEET    1 AB9 4 SER F1790  VAL F1792  0                                        
SHEET    2 AB9 4 LEU F1764  TYR F1769  1  N  LEU F1764   O  SER F1790           
SHEET    3 AB9 4 HIS F1805  VAL F1810  1  O  ILE F1807   N  GLU F1765           
SHEET    4 AB9 4 VAL F1832  THR F1834  1  O  VAL F1833   N  VAL F1810           
SHEET    1 AC1 4 THR G1675  THR G1677  0                                        
SHEET    2 AC1 4 SER G1651  SER G1655  1  N  MET G1652   O  THR G1675           
SHEET    3 AC1 4 HIS G1686  MET G1689  1  O  VAL G1688   N  VAL G1653           
SHEET    4 AC1 4 TRP G1712  SER G1715  1  O  TRP G1712   N  VAL G1687           
SHEET    1 AC2 2 VAL G1696  CYS G1697  0                                        
SHEET    2 AC2 2 GLY G1738  ASP G1739  1  O  GLY G1738   N  CYS G1697           
SHEET    1 AC3 4 SER G1790  VAL G1791  0                                        
SHEET    2 AC3 4 LEU G1764  CYS G1768  1  N  LEU G1764   O  SER G1790           
SHEET    3 AC3 4 HIS G1805  VAL G1810  1  O  HIS G1805   N  GLU G1765           
SHEET    4 AC3 4 VAL G1832  THR G1834  1  O  VAL G1833   N  VAL G1808           
SHEET    1 AC4 4 THR H1675  THR H1677  0                                        
SHEET    2 AC4 4 SER H1651  SER H1655  1  N  MET H1652   O  THR H1675           
SHEET    3 AC4 4 HIS H1686  MET H1689  1  O  VAL H1688   N  VAL H1653           
SHEET    4 AC4 4 TRP H1712  SER H1715  1  O  TRP H1712   N  VAL H1687           
SHEET    1 AC5 2 VAL H1696  CYS H1697  0                                        
SHEET    2 AC5 2 GLY H1738  ASP H1739  1  O  GLY H1738   N  CYS H1697           
SHEET    1 AC6 4 SER H1790  VAL H1791  0                                        
SHEET    2 AC6 4 LEU H1764  CYS H1768  1  N  LEU H1764   O  SER H1790           
SHEET    3 AC6 4 HIS H1805  VAL H1810  1  O  HIS H1805   N  GLU H1765           
SHEET    4 AC6 4 VAL H1832  THR H1834  1  O  VAL H1833   N  VAL H1808           
LINK         C   TYR I 403                 N   SEP I 404     1555   1555  1.33  
LINK         C   SEP I 404                 N   ARG I 405     1555   1555  1.32  
LINK         C   ARG I 405                 N   SEP I 406     1555   1555  1.33  
LINK         C   SEP I 406                 N   PRO I 407     1555   1555  1.33  
LINK         C   TYR J 403                 N   SEP J 404     1555   1555  1.33  
LINK         C   SEP J 404                 N   ARG J 405     1555   1555  1.33  
LINK         C   ARG J 405                 N   SEP J 406     1555   1555  1.33  
LINK         C   SEP J 406                 N   PRO J 407     1555   1555  1.33  
LINK         C   TYR K 403                 N   SEP K 404     1555   1555  1.32  
LINK         C   SEP K 404                 N   ARG K 405     1555   1555  1.32  
LINK         C   ARG K 405                 N   SEP K 406     1555   1555  1.33  
LINK         C   SEP K 406                 N   PRO K 407     1555   1555  1.33  
LINK         C   TYR L 403                 N   SEP L 404     1555   1555  1.33  
LINK         C   SEP L 404                 N   ARG L 405     1555   1555  1.33  
LINK         C   ARG L 405                 N   SEP L 406     1555   1555  1.33  
LINK         C   SEP L 406                 N   PRO L 407     1555   1555  1.33  
LINK         C   TYR M 403                 N   SEP M 404     1555   1555  1.32  
LINK         C   SEP M 404                 N   ARG M 405     1555   1555  1.32  
LINK         C   ARG M 405                 N   SEP M 406     1555   1555  1.32  
LINK         C   SEP M 406                 N   PRO M 407     1555   1555  1.32  
LINK         C   TYR N 403                 N   SEP N 404     1555   1555  1.33  
LINK         C   SEP N 404                 N   ARG N 405     1555   1555  1.33  
LINK         C   ARG N 405                 N   SEP N 406     1555   1555  1.33  
LINK         C   SEP N 406                 N   PRO N 407     1555   1555  1.33  
LINK         C   TYR O 403                 N   SEP O 404     1555   1555  1.33  
LINK         C   SEP O 404                 N   ARG O 405     1555   1555  1.33  
LINK         C   ARG O 405                 N   SEP O 406     1555   1555  1.33  
LINK         C   SEP O 406                 N   PRO O 407     1555   1555  1.33  
LINK         C   TYR P 403                 N   SEP P 404     1555   1555  1.33  
LINK         C   SEP P 404                 N   ARG P 405     1555   1555  1.32  
LINK         C   ARG P 405                 N   SEP P 406     1555   1555  1.33  
LINK         C   SEP P 406                 N   PRO P 407     1555   1555  1.34  
CISPEP   1 GLY A 1770    PRO A 1771          0         3.46                     
CISPEP   2 GLY B 1770    PRO B 1771          0         3.28                     
CISPEP   3 GLY C 1770    PRO C 1771          0         2.60                     
CISPEP   4 GLY D 1770    PRO D 1771          0         3.37                     
CISPEP   5 GLY E 1770    PRO E 1771          0         3.68                     
CISPEP   6 GLY F 1770    PRO F 1771          0         2.18                     
CISPEP   7 GLY G 1770    PRO G 1771          0         3.31                     
CISPEP   8 GLY H 1770    PRO H 1771          0         3.77                     
CRYST1   86.819  183.726  190.510  90.00  90.00  90.00 P 21 21 21   32          
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      0.011518  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005443  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005249        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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