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Database: PDB
Entry: 6BZE
LinkDB: 6BZE
Original site: 6BZE 
HEADER    SIGNALING PROTEIN                       23-DEC-17   6BZE              
TITLE     CRYO-EM STRUCTURE OF BCL10 CARD FILAMENT                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: B-CELL LYMPHOMA/LEUKEMIA 10;                               
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 SYNONYM: B-CELL CLL/LYMPHOMA 10,BCL-10,CARD-CONTAINING MOLECULE      
COMPND   5 ENHANCING NF-KAPPA-B,CARD-LIKE APOPTOTIC PROTEIN,HCLAP,CED-3/ICH-1   
COMPND   6 PRODOMAIN HOMOLOGOUS E10-LIKE REGULATOR,CIPER,CELLULAR HOMOLOG OF    
COMPND   7 VCARMEN,CCARMEN,CELLULAR-E10,C-E10,MAMMALIAN CARD-CONTAINING ADAPTER 
COMPND   8 MOLECULE E10,ME10;                                                   
COMPND   9 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: BCL10, CIPER, CLAP;                                            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    CARD, FILAMENT, SIGNALOSOME, HELICAL RECONSTRUCTION, SIGNALING        
KEYWDS   2 PROTEIN                                                              
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    L.DAVID,Y.LI,J.MA,E.GARNER,X.ZHANG,H.WU                               
REVDAT   3   18-DEC-19 6BZE    1       REMARK                                   
REVDAT   2   28-FEB-18 6BZE    1       JRNL                                     
REVDAT   1   14-FEB-18 6BZE    0                                                
JRNL        AUTH   L.DAVID,Y.LI,J.MA,E.GARNER,X.ZHANG,H.WU                      
JRNL        TITL   ASSEMBLY MECHANISM OF THE CARMA1-BCL10-MALT1-TRAF6           
JRNL        TITL 2 SIGNALOSOME.                                                 
JRNL        REF    PROC. NATL. ACAD. SCI.        V. 115  1499 2018              
JRNL        REF  2 U.S.A.                                                       
JRNL        REFN                   ESSN 1091-6490                               
JRNL        PMID   29382759                                                     
JRNL        DOI    10.1073/PNAS.1721967115                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EMAN2, LEGINON, RELION, PHENIX, PHENIX,   
REMARK   3                            IHRSR, RELION, PHENIX                     
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 2MB9                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 4.000                          
REMARK   3   NUMBER OF PARTICLES               : 39992                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 6BZE COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-JAN-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000231835.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : BCL10 CARD                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : 5 SECOND BLOTTING TIME WITH       
REMARK 245                                    FORCE 3                           
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : 339                            
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI ARCTICA             
REMARK 245   DETECTOR TYPE                     : DIRECT ELECTRON DE-16 (4K X    
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 6000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.70                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 40.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTAMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H                
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 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   OG   SER D    48     NE2  HIS H    37              1.65            
REMARK 500   OD2  ASP A    70     NH2  ARG D    49              1.79            
REMARK 500   OG   SER A    48     NE2  HIS E    37              1.79            
REMARK 500   OG   SER B    48     NE2  HIS F    37              1.88            
REMARK 500   NH1  ARG D    42     OE1  GLU D    84              1.90            
REMARK 500   NH1  ARG F    42     OE1  GLU F    84              1.92            
REMARK 500   NH1  ARG A    42     OE1  GLU A    84              1.92            
REMARK 500   NH1  ARG H    42     OE1  GLU H    84              1.92            
REMARK 500   OG   SER C    48     NE2  HIS G    37              1.92            
REMARK 500   NH1  ARG C    42     OE1  GLU C    84              1.92            
REMARK 500   O    LYS A    98     N    GLU A   102              1.96            
REMARK 500   NH1  ARG E    42     OE1  GLU E    84              1.96            
REMARK 500   NH1  ARG B    42     OE1  GLU B    84              1.96            
REMARK 500   OE2  GLU C    84     NE   ARG C    88              1.97            
REMARK 500   OE2  GLU A    22     NE2  GLN A    73              1.98            
REMARK 500   OE2  GLU H    84     NE   ARG H    88              1.99            
REMARK 500   O    GLN F    97     OG1  THR F   100              1.99            
REMARK 500   OE2  GLU G    84     NE   ARG G    88              2.00            
REMARK 500   O    LYS F    98     N    GLU F   102              2.00            
REMARK 500   O    LYS G    98     N    GLU G   102              2.00            
REMARK 500   O    ILE F    96     CG1  ILE F    99              2.01            
REMARK 500   OE2  GLU D    84     NE   ARG D    88              2.01            
REMARK 500   O    ILE A    55     NZ   LYS A    67              2.01            
REMARK 500   OE2  GLU B    22     NE2  GLN B    73              2.01            
REMARK 500   OE2  GLU A    84     NE   ARG A    88              2.01            
REMARK 500   OE2  GLU E    84     NE   ARG E    88              2.02            
REMARK 500   O    LYS H    98     N    GLU H   102              2.02            
REMARK 500   OE2  GLU A    50     OG   SER B    60              2.02            
REMARK 500   OE2  GLU F    84     NE   ARG F    88              2.02            
REMARK 500   OE2  GLU H    22     NE2  GLN H    73              2.03            
REMARK 500   O    LYS E    98     N    GLU E   102              2.05            
REMARK 500   OE1  GLU B    54     NH1  ARG F    36              2.05            
REMARK 500   O    ILE F    55     NZ   LYS F    67              2.06            
REMARK 500   NH1  ARG G    42     OE1  GLU G    84              2.06            
REMARK 500   O    LYS B    98     N    GLU B   102              2.06            
REMARK 500   O    ILE E    55     NZ   LYS E    67              2.06            
REMARK 500   O    ILE B    55     NZ   LYS B    67              2.06            
REMARK 500   O    ILE A    96     CG1  ILE A    99              2.06            
REMARK 500   O    GLN B    97     OG1  THR B   100              2.07            
REMARK 500   O    ILE G    96     CG1  ILE G    99              2.07            
REMARK 500   O    LYS C    98     N    GLU C   102              2.08            
REMARK 500   OE2  GLU G    22     NE2  GLN G    73              2.09            
REMARK 500   OE2  GLU B    84     NE   ARG B    88              2.09            
REMARK 500   O    ILE B    96     CG1  ILE B    99              2.10            
REMARK 500   O    ILE G    55     NZ   LYS G    67              2.10            
REMARK 500   O    ILE H    55     NZ   LYS H    67              2.12            
REMARK 500   NZ   LYS B    63     O    ARG E    36              2.13            
REMARK 500   O    ASP D    51     N    ILE D    55              2.13            
REMARK 500   OE1  GLU A    54     NH1  ARG E    36              2.13            
REMARK 500   O    ILE H    96     CG1  ILE H    99              2.13            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      71 CLOSE CONTACTS                                
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    PHE A  38      -18.63   -155.64                                   
REMARK 500    SER A  61        8.39     82.81                                   
REMARK 500    LYS A  67      -70.98    -55.28                                   
REMARK 500    GLU A  74      -75.71    -55.31                                   
REMARK 500    LYS A  77      -71.15    -67.83                                   
REMARK 500    GLU A  89     -120.45     57.10                                   
REMARK 500    LYS A  90     -124.86     59.74                                   
REMARK 500    ASN A  93      -66.49   -138.43                                   
REMARK 500    PHE B  38      -17.58   -152.90                                   
REMARK 500    SER B  48      171.88    -58.75                                   
REMARK 500    ARG B  49      -56.11   -123.08                                   
REMARK 500    SER B  61        8.97     84.58                                   
REMARK 500    GLU B  74      -72.25    -54.28                                   
REMARK 500    GLU B  89     -124.37     55.56                                   
REMARK 500    LYS B  90     -124.05     58.90                                   
REMARK 500    GLN B  92       11.25   -142.67                                   
REMARK 500    ASN B  93      -59.97   -135.11                                   
REMARK 500    PHE C  38      -12.60   -155.56                                   
REMARK 500    SER C  48      171.37    -58.12                                   
REMARK 500    ARG C  49      -56.57   -122.86                                   
REMARK 500    SER C  61        8.54     85.22                                   
REMARK 500    GLU C  74      -74.78    -54.84                                   
REMARK 500    GLU C  89     -121.37     53.29                                   
REMARK 500    LYS C  90     -124.42     60.06                                   
REMARK 500    ASN C  93      -61.16   -134.34                                   
REMARK 500    LEU C 106      -70.93    -61.94                                   
REMARK 500    PHE D  38       -6.36   -157.59                                   
REMARK 500    SER D  61        8.42     84.61                                   
REMARK 500    GLU D  89     -121.07     60.90                                   
REMARK 500    LYS D  90     -114.89     52.91                                   
REMARK 500    ASN D  93      -61.50   -133.72                                   
REMARK 500    LEU D 106      -72.22    -60.97                                   
REMARK 500    HIS E  37      -70.13    -90.48                                   
REMARK 500    ARG E  49      -55.22   -124.14                                   
REMARK 500    SER E  61        7.31     85.59                                   
REMARK 500    GLU E  89     -114.84     53.81                                   
REMARK 500    LYS E  90     -125.85     58.51                                   
REMARK 500    ASN E  93      -67.73   -138.31                                   
REMARK 500    ARG F  49      -53.77   -125.17                                   
REMARK 500    SER F  61        7.25     85.51                                   
REMARK 500    GLU F  89     -116.58     57.37                                   
REMARK 500    LYS F  90     -121.11     48.26                                   
REMARK 500    ASN F  93      -64.33   -134.27                                   
REMARK 500    PHE G  38       -7.77   -144.00                                   
REMARK 500    ARG G  49      -59.17   -134.05                                   
REMARK 500    SER G  61        7.41     85.00                                   
REMARK 500    GLU G  89     -119.66     56.43                                   
REMARK 500    LYS G  90     -115.94     50.42                                   
REMARK 500    ASN G  93      -69.51   -135.98                                   
REMARK 500    HIS H  37      -80.72    -93.95                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      56 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-7314   RELATED DB: EMDB                              
REMARK 900 CRYO-EM STRUCTURE OF BCL10 CARD FILAMENT                             
DBREF  6BZE A   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE B   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE C   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE D   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE E   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE F   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE G   10   115  UNP    O95999   BCL10_HUMAN     10    115             
DBREF  6BZE H   10   115  UNP    O95999   BCL10_HUMAN     10    115             
SEQRES   1 A  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 A  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 A  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 A  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 A  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 A  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 A  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 A  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 A  106  LEU LYS                                                      
SEQRES   1 B  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 B  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 B  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 B  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 B  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 B  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 B  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 B  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 B  106  LEU LYS                                                      
SEQRES   1 C  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 C  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 C  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 C  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 C  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 C  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 C  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 C  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 C  106  LEU LYS                                                      
SEQRES   1 D  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 D  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 D  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 D  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 D  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 D  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 D  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 D  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 D  106  LEU LYS                                                      
SEQRES   1 E  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 E  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 E  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 E  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 E  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 E  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 E  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 E  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 E  106  LEU LYS                                                      
SEQRES   1 F  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 F  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 F  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 F  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 F  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 F  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 F  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 F  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 F  106  LEU LYS                                                      
SEQRES   1 G  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 G  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 G  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 G  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 G  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 G  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 G  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 G  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 G  106  LEU LYS                                                      
SEQRES   1 H  106  GLU GLU ASP LEU THR GLU VAL LYS LYS ASP ALA LEU GLU          
SEQRES   2 H  106  ASN LEU ARG VAL TYR LEU CYS GLU LYS ILE ILE ALA GLU          
SEQRES   3 H  106  ARG HIS PHE ASP HIS LEU ARG ALA LYS LYS ILE LEU SER          
SEQRES   4 H  106  ARG GLU ASP THR GLU GLU ILE SER CYS ARG THR SER SER          
SEQRES   5 H  106  ARG LYS ARG ALA GLY LYS LEU LEU ASP TYR LEU GLN GLU          
SEQRES   6 H  106  ASN PRO LYS GLY LEU ASP THR LEU VAL GLU SER ILE ARG          
SEQRES   7 H  106  ARG GLU LYS THR GLN ASN PHE LEU ILE GLN LYS ILE THR          
SEQRES   8 H  106  ASP GLU VAL LEU LYS LEU ARG ASN ILE LYS LEU GLU HIS          
SEQRES   9 H  106  LEU LYS                                                      
HELIX    1 AA1 ASP A   12  ARG A   25  1                                  14    
HELIX    2 AA2 ILE A   33  PHE A   38  1                                   6    
HELIX    3 AA3 PHE A   38  LYS A   44  1                                   7    
HELIX    4 AA4 ARG A   49  ARG A   58  1                                  10    
HELIX    5 AA5 ARG A   62  GLN A   73  1                                  12    
HELIX    6 AA6 LEU A   79  ARG A   87  1                                   9    
HELIX    7 AA7 LEU A   95  LYS A  115  1                                  21    
HELIX    8 AA8 ASP B   12  ARG B   25  1                                  14    
HELIX    9 AA9 ILE B   33  PHE B   38  1                                   6    
HELIX   10 AB1 PHE B   38  LYS B   44  1                                   7    
HELIX   11 AB2 ARG B   49  ARG B   58  1                                  10    
HELIX   12 AB3 ARG B   62  GLN B   73  1                                  12    
HELIX   13 AB4 LEU B   79  ARG B   87  1                                   9    
HELIX   14 AB5 LEU B   95  LYS B  115  1                                  21    
HELIX   15 AB6 ASP C   12  ARG C   25  1                                  14    
HELIX   16 AB7 ILE C   33  PHE C   38  1                                   6    
HELIX   17 AB8 PHE C   38  LYS C   44  1                                   7    
HELIX   18 AB9 ARG C   49  ARG C   58  1                                  10    
HELIX   19 AC1 ARG C   62  GLN C   73  1                                  12    
HELIX   20 AC2 LEU C   79  ARG C   87  1                                   9    
HELIX   21 AC3 LEU C   95  LYS C  115  1                                  21    
HELIX   22 AC4 ASP D   12  ARG D   25  1                                  14    
HELIX   23 AC5 ILE D   33  PHE D   38  1                                   6    
HELIX   24 AC6 PHE D   38  LYS D   44  1                                   7    
HELIX   25 AC7 ARG D   49  ARG D   58  1                                  10    
HELIX   26 AC8 ARG D   62  ASN D   75  1                                  14    
HELIX   27 AC9 LEU D   79  ARG D   87  1                                   9    
HELIX   28 AD1 LEU D   95  LYS D  115  1                                  21    
HELIX   29 AD2 ASP E   12  ARG E   25  1                                  14    
HELIX   30 AD3 ILE E   33  PHE E   38  1                                   6    
HELIX   31 AD4 PHE E   38  LYS E   44  1                                   7    
HELIX   32 AD5 ARG E   49  ARG E   58  1                                  10    
HELIX   33 AD6 ARG E   62  LEU E   72  1                                  11    
HELIX   34 AD7 LEU E   79  ARG E   87  1                                   9    
HELIX   35 AD8 LEU E   95  LYS E  115  1                                  21    
HELIX   36 AD9 ASP F   12  ARG F   25  1                                  14    
HELIX   37 AE1 ILE F   33  PHE F   38  1                                   6    
HELIX   38 AE2 PHE F   38  LYS F   44  1                                   7    
HELIX   39 AE3 ARG F   49  ARG F   58  1                                  10    
HELIX   40 AE4 ARG F   62  LEU F   72  1                                  11    
HELIX   41 AE5 LEU F   79  ARG F   87  1                                   9    
HELIX   42 AE6 LEU F   95  LYS F  115  1                                  21    
HELIX   43 AE7 ASP G   12  ARG G   25  1                                  14    
HELIX   44 AE8 ILE G   33  PHE G   38  1                                   6    
HELIX   45 AE9 PHE G   38  LYS G   44  1                                   7    
HELIX   46 AF1 ARG G   49  ARG G   58  1                                  10    
HELIX   47 AF2 ARG G   62  LEU G   72  1                                  11    
HELIX   48 AF3 LEU G   79  ARG G   87  1                                   9    
HELIX   49 AF4 LEU G   95  LYS G  115  1                                  21    
HELIX   50 AF5 ASP H   12  ARG H   25  1                                  14    
HELIX   51 AF6 ILE H   32  ARG H   36  5                                   5    
HELIX   52 AF7 PHE H   38  LYS H   44  1                                   7    
HELIX   53 AF8 ARG H   49  ARG H   58  1                                  10    
HELIX   54 AF9 ARG H   62  LEU H   72  1                                  11    
HELIX   55 AG1 LEU H   79  ARG H   87  1                                   9    
HELIX   56 AG2 LEU H   95  LYS H  115  1                                  21    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
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      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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