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Database: PDB
Entry: 6GJ1
LinkDB: 6GJ1
Original site: 6GJ1 
HEADER    STRUCTURAL PROTEIN                      15-MAY-18   6GJ1              
TITLE     THE BASEPLATE COMPLEX FROM THE TYPE VI SECRETION SYSTEM               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PUTATIVE TYPE VI SECRETION PROTEIN;                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TSSG;                                                      
COMPND   7 CHAIN: C;                                                            
COMPND   8 ENGINEERED: YES;                                                     
COMPND   9 MOL_ID: 3;                                                           
COMPND  10 MOLECULE: TSSE;                                                      
COMPND  11 CHAIN: D;                                                            
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 GENE: EC042_4542;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   9 ORGANISM_TAXID: 562;                                                 
SOURCE  10 GENE: EC55989_3321;                                                  
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE  15 ORGANISM_TAXID: 562;                                                 
SOURCE  16 GENE: EC55989_3319;                                                  
SOURCE  17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  18 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    SECRETION, BASEPLATE, COMPLEX, STRUCTURAL PROTEIN                     
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    C.RAPISARDA,R.FRONZES                                                 
REVDAT   5   11-DEC-19 6GJ1    1       SCALE                                    
REVDAT   4   05-DEC-18 6GJ1    1       JRNL                                     
REVDAT   3   21-NOV-18 6GJ1    1       REMARK LINK                              
REVDAT   2   24-OCT-18 6GJ1    1       JRNL                                     
REVDAT   1   17-OCT-18 6GJ1    0                                                
JRNL        AUTH   Y.CHERRAK,C.RAPISARDA,R.PELLARIN,G.BOUVIER,B.BARDIAUX,       
JRNL        AUTH 2 F.ALLAIN,C.MALOSSE,M.REY,J.CHAMOT-ROOKE,E.CASCALES,          
JRNL        AUTH 3 R.FRONZES,E.DURAND                                           
JRNL        TITL   BIOGENESIS AND STRUCTURE OF A TYPE VI SECRETION BASEPLATE.   
JRNL        REF    NAT MICROBIOL                 V.   3  1404 2018              
JRNL        REFN                   ESSN 2058-5276                               
JRNL        PMID   30323254                                                     
JRNL        DOI    10.1038/S41564-018-0260-1                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : GCTF, CRYOSPARC, RELION                   
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
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)  : 4.700                          
REMARK   3   NUMBER OF PARTICLES               : 32504                          
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 6GJ1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-MAY-18.                  
REMARK 100 THE DEPOSITION ID IS D_1200010047.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : TYPE VI SECRETION SYSTEM          
REMARK 245                                    BASEPLATE COMPLEX                 
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
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      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1.50                           
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)         : 300                            
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: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     MET B     1                                                      
REMARK 465     ASP B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     GLY B   587                                                      
REMARK 465     MET C     1                                                      
REMARK 465     HIS C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     VAL C     4                                                      
REMARK 465     GLU C     5                                                      
REMARK 465     ARG C     6                                                      
REMARK 465     LYS C     7                                                      
REMARK 465     THR C   358                                                      
REMARK 465     GLN C   359                                                      
REMARK 465     GLU C   360                                                      
REMARK 465     ASN C   361                                                      
REMARK 465     GLY C   362                                                      
REMARK 465     ASP C   363                                                      
REMARK 465     TYR C   364                                                      
REMARK 465     ARG C   365                                                      
REMARK 465     TRP C   366                                                      
REMARK 465     MET D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     ARG D     3                                                      
REMARK 465     PRO D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     LEU D     6                                                      
REMARK 465     TYR D     7                                                      
REMARK 465     GLU D     8                                                      
REMARK 465     ILE D     9                                                      
REMARK 465     LEU D    10                                                      
REMARK 465     TYR D    11                                                      
REMARK 465     GLY D    12                                                      
REMARK 465     ASN D    13                                                      
REMARK 465     PHE D    14                                                      
REMARK 465     THR D    15                                                      
REMARK 465     GLY D    16                                                      
REMARK 465     GLY D    17                                                      
REMARK 465     LEU D    18                                                      
REMARK 465     GLU D    19                                                      
REMARK 465     LEU D    20                                                      
REMARK 465     ASN D    21                                                      
REMARK 465     GLN D    22                                                      
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     SER C 334    OG                                                  
REMARK 470     ARG C 337    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL C 338    CG1  CG2                                            
REMARK 470     MET C 339    CG   SD   CE                                        
REMARK 470     THR C 340    OG1  CG2                                            
REMARK 470     ILE C 341    CG1  CG2  CD1                                       
REMARK 470     SER C 342    OG                                                  
REMARK 470     LEU C 343    CG   CD1  CD2                                       
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   N    PRO A    44     NE   ARG D    87              0.34            
REMARK 500   N    PRO C    99     NH2  ARG D    39              0.38            
REMARK 500   CG   PRO A    44     NH1  ARG D    87              0.39            
REMARK 500   NH1  ARG A    48     CB   TYR D    84              0.53            
REMARK 500   CZ   ARG A    48     CA   TYR D    84              0.57            
REMARK 500   OE2  GLU D    26     CD1  LEU D   131              0.76            
REMARK 500   OE2  GLU D    26     CG   LEU D   131              0.79            
REMARK 500   CA   PRO A    44     NH2  ARG D    87              0.87            
REMARK 500   N    ASP A    43     CG   ARG D    87              0.90            
REMARK 500   C    PRO A    42     CG   ARG D    87              0.93            
REMARK 500   CZ   ARG A    48     C    TYR D    84              0.93            
REMARK 500   CD   GLU D    26     CD1  LEU D   131              0.98            
REMARK 500   CB   PRO C    99     NE   ARG D    39              0.99            
REMARK 500   N    PRO A    44     CZ   ARG D    87              1.03            
REMARK 500   CA   PRO A    44     CZ   ARG D    87              1.07            
REMARK 500   NH1  ARG A    48     CA   TYR D    84              1.08            
REMARK 500   C    ASP A    43     NE   ARG D    87              1.08            
REMARK 500   CD   PRO A    44     NH1  ARG D    87              1.19            
REMARK 500   CA   ASP A    43     CB   ARG D    87              1.24            
REMARK 500   CG   PRO C    99     NE   ARG D    39              1.26            
REMARK 500   CD   PRO C    99     NH2  ARG D    39              1.28            
REMARK 500   O    THR D    43     O    ARG D    44              1.29            
REMARK 500   NE   ARG A    48     O    TYR D    84              1.29            
REMARK 500   NE   ARG A    48     C    TYR D    84              1.34            
REMARK 500   CB   PRO A    44     NH2  ARG D    87              1.36            
REMARK 500   C    SER C    98     NH2  ARG D    39              1.38            
REMARK 500   N    PRO C    99     CZ   ARG D    39              1.39            
REMARK 500   NH2  ARG A    48     N    GLU D    85              1.43            
REMARK 500   CB   PRO A    44     CZ   ARG D    87              1.44            
REMARK 500   OG1  THR A    41     O    PRO D    86              1.44            
REMARK 500   CD   PRO C    99     CZ   ARG D    39              1.44            
REMARK 500   CD   PRO A    44     CZ   ARG D    87              1.47            
REMARK 500   NH2  ARG A    48     C    TYR D    84              1.47            
REMARK 500   O    PRO A    42     CG   ARG D    87              1.49            
REMARK 500   N    ASP A    43     CD   ARG D    87              1.52            
REMARK 500   CG   PRO A    44     CZ   ARG D    87              1.52            
REMARK 500   CD2  LEU D    34     CD1  LEU D   135              1.52            
REMARK 500   NH2  ARG A    48     N    TYR D    84              1.54            
REMARK 500   CA   ASP A    43     CG   ARG D    87              1.56            
REMARK 500   NH2  ARG A    48     CA   TYR D    84              1.56            
REMARK 500   CB   ALA C   102     CB   SER D    32              1.59            
REMARK 500   CD2  LEU D    34     CG   LEU D   135              1.62            
REMARK 500   NE   ARG A    48     CA   TYR D    84              1.63            
REMARK 500   N    PRO A    44     CD   ARG D    87              1.66            
REMARK 500   CB   PRO A    44     NH1  ARG D    87              1.67            
REMARK 500   CD   PRO A    44     NE   ARG D    87              1.67            
REMARK 500   CA   PRO A    44     NE   ARG D    87              1.68            
REMARK 500   CG   GLU D    26     CD1  LEU D   131              1.69            
REMARK 500   CD   PRO A    44     CD   ARG D    87              1.69            
REMARK 500   CD   GLU D    26     CG   LEU D   131              1.72            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      93 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    LEU A 203   CA  -  CB  -  CG  ANGL. DEV. =  16.3 DEGREES          
REMARK 500    LEU A 317   CA  -  CB  -  CG  ANGL. DEV. =  17.2 DEGREES          
REMARK 500    TYR D  84   CA  -  CB  -  CG  ANGL. DEV. = -13.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ALA A  24      -63.30    -98.29                                   
REMARK 500    PRO A 109       48.96    -89.52                                   
REMARK 500    SER A 154      108.29   -161.97                                   
REMARK 500    CYS A 162       19.29   -141.46                                   
REMARK 500    GLU A 164       39.71    -97.56                                   
REMARK 500    LEU A 176       77.70    -68.49                                   
REMARK 500    TYR A 179     -168.58   -106.87                                   
REMARK 500    ASN A 208       34.30   -141.59                                   
REMARK 500    ARG A 213       -0.81     61.78                                   
REMARK 500    GLU A 226       36.66    -93.55                                   
REMARK 500    PHE A 237     -163.92   -161.86                                   
REMARK 500    TYR A 240       14.28   -143.65                                   
REMARK 500    ASP A 274       41.35   -106.45                                   
REMARK 500    ASP A 291       59.55    -97.86                                   
REMARK 500    ASP A 292       58.11    -90.77                                   
REMARK 500    ALA A 309     -167.69   -161.02                                   
REMARK 500    TYR A 321      -37.40   -133.80                                   
REMARK 500    PRO A 325     -173.11    -69.99                                   
REMARK 500    SER A 357       38.12    -98.19                                   
REMARK 500    ARG A 359       36.40    -97.85                                   
REMARK 500    HIS A 360       66.60     66.42                                   
REMARK 500    PRO A 370     -173.21    -68.48                                   
REMARK 500    TYR A 374       97.83   -160.19                                   
REMARK 500    MET A 385     -167.11   -128.27                                   
REMARK 500    ASP A 387      116.69   -164.98                                   
REMARK 500    GLU A 398       73.58   -100.23                                   
REMARK 500    GLU A 433       20.91    -77.32                                   
REMARK 500    VAL A 435      -76.45   -100.01                                   
REMARK 500    LEU A 436       62.35     28.45                                   
REMARK 500    PRO A 455     -164.53    -73.13                                   
REMARK 500    MET A 475       -3.25   -143.56                                   
REMARK 500    LEU A 476     -152.49    -79.57                                   
REMARK 500    SER A 477      132.52    -38.50                                   
REMARK 500    ASP A 531      128.39    -30.11                                   
REMARK 500    ALA A 536     -158.87   -148.35                                   
REMARK 500    LEU A 554       50.12   -116.65                                   
REMARK 500    PRO A 570       78.94    -66.01                                   
REMARK 500    PRO B  28        3.69    -62.02                                   
REMARK 500    ARG B  59      -65.14    -92.28                                   
REMARK 500    LEU B  68       75.10     52.76                                   
REMARK 500    SER B 100       74.94     55.12                                   
REMARK 500    LEU B 139      142.79   -171.76                                   
REMARK 500    ALA B 161      -62.59    -93.51                                   
REMARK 500    ARG B 175       66.37     61.59                                   
REMARK 500    SER B 187       47.92    -84.41                                   
REMARK 500    ALA B 199       58.19   -140.62                                   
REMARK 500    ARG B 211      -36.53   -130.61                                   
REMARK 500    ASP B 215     -156.87   -140.56                                   
REMARK 500    SER B 238      108.77    -59.46                                   
REMARK 500    MET B 254       78.29     57.87                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     105 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU A  173     HIS A  174                 -148.63                    
REMARK 500 GLU A  276     VAL A  277                 -145.50                    
REMARK 500 HIS A  360     ARG A  361                  143.15                    
REMARK 500 LEU A  390     ILE A  391                 -143.35                    
REMARK 500 VAL A  435     LEU A  436                  120.74                    
REMARK 500 TYR A  453     PRO A  454                  146.19                    
REMARK 500 LEU A  530     ASP A  531                 -125.45                    
REMARK 500 ASN A  562     GLN A  563                 -147.38                    
REMARK 500 TRP B   80     PRO B   81                  141.95                    
REMARK 500 TYR B  240     GLN B  241                 -149.83                    
REMARK 500 PHE B  247     THR B  248                  142.92                    
REMARK 500 HIS B  257     LEU B  258                  147.76                    
REMARK 500 GLY B  363     MET B  364                 -149.10                    
REMARK 500 HIS B  467     LEU B  468                 -145.35                    
REMARK 500 PHE B  515     GLU B  516                  138.28                    
REMARK 500 GLN B  560     PHE B  561                 -149.22                    
REMARK 500 ARG B  576     TRP B  577                 -141.31                    
REMARK 500 LYS B  578     GLU B  579                  142.61                    
REMARK 500 TYR C  142     PRO C  143                 -133.26                    
REMARK 500 ARG C  219     ILE C  220                 -112.59                    
REMARK 500 ILE C  220     PRO C  221                 -116.89                    
REMARK 500 HIS C  231     HIS C  232                  149.88                    
REMARK 500 LYS C  237     SER C  238                 -136.18                    
REMARK 500 VAL C  249     ASN C  250                  141.77                    
REMARK 500 LEU C  308     SER C  309                 -132.23                    
REMARK 500 CYS C  310     ARG C  311                  139.60                    
REMARK 500 TYR C  346     GLN C  347                  139.33                    
REMARK 500 GLN C  347     ARG C  348                 -123.35                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-0009   RELATED DB: EMDB                              
REMARK 900 THE BASEPLATE COMPLEX FROM THE TYPE VI SECRETION SYSTEM              
DBREF  6GJ1 A    1   587  UNP    D3GUX3   D3GUX3_ECO44     1    587             
DBREF  6GJ1 B    1   587  UNP    D3GUX3   D3GUX3_ECO44     1    587             
DBREF  6GJ1 C    1   366  UNP    B7LFT6   B7LFT6_ECO55     1    366             
DBREF  6GJ1 D    1   143  UNP    B7LFT4   B7LFT4_ECO55     2    144             
SEQRES   1 A  587  MET ASP ASP LEU THR LEU ARG TYR PHE ASP ALA GLU MET          
SEQRES   2 A  587  ARG TYR LEU ARG GLU ALA GLY LYS ALA PHE ALA GLN ALA          
SEQRES   3 A  587  HIS PRO ASP ARG ALA ALA MET LEU ASP LEU ASP LYS ALA          
SEQRES   4 A  587  GLY THR PRO ASP PRO CYS VAL GLU ARG LEU PHE GLU GLY          
SEQRES   5 A  587  PHE ALA PHE SER MET GLY ARG LEU ARG GLN LYS ILE ASP          
SEQRES   6 A  587  ASP ASP LEU PRO GLU LEU THR GLU SER LEU VAL SER MET          
SEQRES   7 A  587  LEU TRP PRO HIS TYR LEU ARG THR ILE PRO SER LEU SER          
SEQRES   8 A  587  VAL VAL ALA LEU THR PRO ARG LEU SER VAL MET LYS MET          
SEQRES   9 A  587  ALA GLU THR VAL PRO ALA GLY LEU GLU VAL THR SER ARG          
SEQRES  10 A  587  PRO VAL GLY PRO GLY ASN THR VAL CYS ARG TYR ARG THR          
SEQRES  11 A  587  THR ARG ALA ILE PRO LEU ASN PRO LEU ALA VAL GLU LYS          
SEQRES  12 A  587  VAL VAL MET THR THR GLU PRO ASP GLY ARG SER VAL LEU          
SEQRES  13 A  587  LYS ILE GLY PHE ALA CYS SER GLU LEU ALA ASP TRP SER          
SEQRES  14 A  587  GLN VAL ASP LEU HIS ARG LEU SER LEU TYR LEU ALA ALA          
SEQRES  15 A  587  GLU ALA PRO VAL SER SER THR LEU HIS LEU MET MET THR          
SEQRES  16 A  587  LYS ARG LEU ALA ALA LEU TYR LEU ARG LEU PRO GLY ASN          
SEQRES  17 A  587  ASP GLU ARG ILE ARG ILE ASP GLY TRP PHE SER PRO GLY          
SEQRES  18 A  587  GLY PHE ALA GLU GLU ASP ARG LEU TRP PRO LYS GLY ASP          
SEQRES  19 A  587  SER ALA PHE SER GLY TYR GLN LEU LEU LEU GLU TYR PHE          
SEQRES  20 A  587  THR PHE ARG GLU LYS PHE MET PHE VAL HIS LEU ASN GLY          
SEQRES  21 A  587  LEU GLU ASN VAL SER LEU PRO ALA GLY ILE SER GLY PHE          
SEQRES  22 A  587  ASP LEU GLU VAL VAL LEU SER GLN PRO TRP PRO ALA ASP          
SEQRES  23 A  587  LEU PRO VAL THR ASP ASP ALA LEU CYS LEU HIS CYS VAL          
SEQRES  24 A  587  PRO VAL ILE ASN LEU PHE THR LEU GLU ALA ASP PRO LEU          
SEQRES  25 A  587  ILE ILE ASN GLY LEU GLU SER GLU TYR LEU LEU ARG PRO          
SEQRES  26 A  587  LYS ARG LEU GLN ASP GLY TYR THR GLU ILE TYR SER VAL          
SEQRES  27 A  587  ASP ALA VAL THR GLY SER GLY ARG THR GLY SER ALA GLU          
SEQRES  28 A  587  TYR VAL PRO PHE THR SER PHE ARG HIS ARG GLY GLY MET          
SEQRES  29 A  587  LEU ARG HIS ASP ALA PRO GLU ARG TYR TYR HIS THR ARG          
SEQRES  30 A  587  VAL LYS ARG GLY VAL THR GLY MET TYR ASP THR TRP LEU          
SEQRES  31 A  587  ILE LEU GLY GLY GLN ARG TRP GLU ALA ASP ARG MET PRO          
SEQRES  32 A  587  GLU ARG GLU THR LEU SER LEU ARG ILE THR GLY THR ASN          
SEQRES  33 A  587  GLY GLN LEU PRO ARG ARG ALA LEU GLN SER THR LEU LEU          
SEQRES  34 A  587  ASP ARG CYS GLU GLN VAL LEU GLN ALA PRO VAL SER VAL          
SEQRES  35 A  587  ARG ASN LEU CYS LYS PRO THR LEU PRO VAL TYR PRO PRO          
SEQRES  36 A  587  THR GLU ASP ARG PHE HIS TRP ARG VAL MET SER HIS LEU          
SEQRES  37 A  587  GLY THR GLY PHE LEU ASN MET LEU SER SER ALA GLU VAL          
SEQRES  38 A  587  LEU ARG GLY THR LEU ALA LEU TYR ASN TRP ARG ASP ASP          
SEQRES  39 A  587  GLU LEU ASN HIS ARG ARG LEU ASP ALA ILE LEU ALA VAL          
SEQRES  40 A  587  GLN HIS HIS ARG ILE GLN ARG PHE GLU LYS GLY PHE LEU          
SEQRES  41 A  587  LEU ARG GLY LEU ASP VAL GLU VAL THR LEU ASP GLY ASN          
SEQRES  42 A  587  GLY PHE ALA GLY GLU GLY ASP ILE HIS LEU PHE GLY GLU          
SEQRES  43 A  587  MET LEU ASN ARG PHE LEU ALA LEU TYR ALA ASP MET ASN          
SEQRES  44 A  587  GLN PHE ASN GLN LEU THR LEU ILE VAL GLN PRO GLU GLY          
SEQRES  45 A  587  LYS CYS ILE ARG TRP LYS GLU ASN HIS ASN PRO ARG LEU          
SEQRES  46 A  587  PRO GLY                                                      
SEQRES   1 B  587  MET ASP ASP LEU THR LEU ARG TYR PHE ASP ALA GLU MET          
SEQRES   2 B  587  ARG TYR LEU ARG GLU ALA GLY LYS ALA PHE ALA GLN ALA          
SEQRES   3 B  587  HIS PRO ASP ARG ALA ALA MET LEU ASP LEU ASP LYS ALA          
SEQRES   4 B  587  GLY THR PRO ASP PRO CYS VAL GLU ARG LEU PHE GLU GLY          
SEQRES   5 B  587  PHE ALA PHE SER MET GLY ARG LEU ARG GLN LYS ILE ASP          
SEQRES   6 B  587  ASP ASP LEU PRO GLU LEU THR GLU SER LEU VAL SER MET          
SEQRES   7 B  587  LEU TRP PRO HIS TYR LEU ARG THR ILE PRO SER LEU SER          
SEQRES   8 B  587  VAL VAL ALA LEU THR PRO ARG LEU SER VAL MET LYS MET          
SEQRES   9 B  587  ALA GLU THR VAL PRO ALA GLY LEU GLU VAL THR SER ARG          
SEQRES  10 B  587  PRO VAL GLY PRO GLY ASN THR VAL CYS ARG TYR ARG THR          
SEQRES  11 B  587  THR ARG ALA ILE PRO LEU ASN PRO LEU ALA VAL GLU LYS          
SEQRES  12 B  587  VAL VAL MET THR THR GLU PRO ASP GLY ARG SER VAL LEU          
SEQRES  13 B  587  LYS ILE GLY PHE ALA CYS SER GLU LEU ALA ASP TRP SER          
SEQRES  14 B  587  GLN VAL ASP LEU HIS ARG LEU SER LEU TYR LEU ALA ALA          
SEQRES  15 B  587  GLU ALA PRO VAL SER SER THR LEU HIS LEU MET MET THR          
SEQRES  16 B  587  LYS ARG LEU ALA ALA LEU TYR LEU ARG LEU PRO GLY ASN          
SEQRES  17 B  587  ASP GLU ARG ILE ARG ILE ASP GLY TRP PHE SER PRO GLY          
SEQRES  18 B  587  GLY PHE ALA GLU GLU ASP ARG LEU TRP PRO LYS GLY ASP          
SEQRES  19 B  587  SER ALA PHE SER GLY TYR GLN LEU LEU LEU GLU TYR PHE          
SEQRES  20 B  587  THR PHE ARG GLU LYS PHE MET PHE VAL HIS LEU ASN GLY          
SEQRES  21 B  587  LEU GLU ASN VAL SER LEU PRO ALA GLY ILE SER GLY PHE          
SEQRES  22 B  587  ASP LEU GLU VAL VAL LEU SER GLN PRO TRP PRO ALA ASP          
SEQRES  23 B  587  LEU PRO VAL THR ASP ASP ALA LEU CYS LEU HIS CYS VAL          
SEQRES  24 B  587  PRO VAL ILE ASN LEU PHE THR LEU GLU ALA ASP PRO LEU          
SEQRES  25 B  587  ILE ILE ASN GLY LEU GLU SER GLU TYR LEU LEU ARG PRO          
SEQRES  26 B  587  LYS ARG LEU GLN ASP GLY TYR THR GLU ILE TYR SER VAL          
SEQRES  27 B  587  ASP ALA VAL THR GLY SER GLY ARG THR GLY SER ALA GLU          
SEQRES  28 B  587  TYR VAL PRO PHE THR SER PHE ARG HIS ARG GLY GLY MET          
SEQRES  29 B  587  LEU ARG HIS ASP ALA PRO GLU ARG TYR TYR HIS THR ARG          
SEQRES  30 B  587  VAL LYS ARG GLY VAL THR GLY MET TYR ASP THR TRP LEU          
SEQRES  31 B  587  ILE LEU GLY GLY GLN ARG TRP GLU ALA ASP ARG MET PRO          
SEQRES  32 B  587  GLU ARG GLU THR LEU SER LEU ARG ILE THR GLY THR ASN          
SEQRES  33 B  587  GLY GLN LEU PRO ARG ARG ALA LEU GLN SER THR LEU LEU          
SEQRES  34 B  587  ASP ARG CYS GLU GLN VAL LEU GLN ALA PRO VAL SER VAL          
SEQRES  35 B  587  ARG ASN LEU CYS LYS PRO THR LEU PRO VAL TYR PRO PRO          
SEQRES  36 B  587  THR GLU ASP ARG PHE HIS TRP ARG VAL MET SER HIS LEU          
SEQRES  37 B  587  GLY THR GLY PHE LEU ASN MET LEU SER SER ALA GLU VAL          
SEQRES  38 B  587  LEU ARG GLY THR LEU ALA LEU TYR ASN TRP ARG ASP ASP          
SEQRES  39 B  587  GLU LEU ASN HIS ARG ARG LEU ASP ALA ILE LEU ALA VAL          
SEQRES  40 B  587  GLN HIS HIS ARG ILE GLN ARG PHE GLU LYS GLY PHE LEU          
SEQRES  41 B  587  LEU ARG GLY LEU ASP VAL GLU VAL THR LEU ASP GLY ASN          
SEQRES  42 B  587  GLY PHE ALA GLY GLU GLY ASP ILE HIS LEU PHE GLY GLU          
SEQRES  43 B  587  MET LEU ASN ARG PHE LEU ALA LEU TYR ALA ASP MET ASN          
SEQRES  44 B  587  GLN PHE ASN GLN LEU THR LEU ILE VAL GLN PRO GLU GLY          
SEQRES  45 B  587  LYS CYS ILE ARG TRP LYS GLU ASN HIS ASN PRO ARG LEU          
SEQRES  46 B  587  PRO GLY                                                      
SEQRES   1 C  366  MET HIS PRO VAL GLU ARG LYS SER GLN SER ALA PRO ALA          
SEQRES   2 C  366  ARG LEU ILE THR ARG TYR ARG LYS GLN LEU PRO TYR ILE          
SEQRES   3 C  366  ASN PHE TYR ARG PHE CYS GLN LEU LEU GLU GLN SER GLN          
SEQRES   4 C  366  PRO ASP GLN PRO PRO ILE GLY SER GLY TRP GLN ALA ARG          
SEQRES   5 C  366  GLN GLU ALA VAL ARG PHE CYS PRO TYR PRO GLY MET GLY          
SEQRES   6 C  366  PHE PRO ALA SER GLU ILE LYS ASP ALA VAL ILE PRO GLU          
SEQRES   7 C  366  GLU SER HIS LEU PRO PRO ILE VAL HIS VAL THR PHE MET          
SEQRES   8 C  366  GLY LEU TYR GLY VAL THR SER PRO LEU PRO ALA HIS TYR          
SEQRES   9 C  366  ILE SER ASP ILE ALA GLN GLN ARG GLU GLY HIS GLU ALA          
SEQRES  10 C  366  ALA ALA ASP PHE LEU ASP ILE PHE SER HIS ARG LEU ILE          
SEQRES  11 C  366  THR GLN TYR TYR ARG ILE TRP ARG LYS TYR SER TYR PRO          
SEQRES  12 C  366  ALA THR PHE GLU ALA GLY GLY GLN ASP LYS THR SER GLN          
SEQRES  13 C  366  TYR LEU LEU GLY LEU ALA ARG LEU GLY ILE PRO GLY CYS          
SEQRES  14 C  366  ALA GLN ASN ILE ALA THR PRO VAL SER ARG PHE LEU ALA          
SEQRES  15 C  366  LEU LEU PRO LEU MET LEU LEU PRO GLY ARG THR ALA GLU          
SEQRES  16 C  366  GLY LEU THR SER LEU VAL THR LEU LEU ALA PRO GLY THR          
SEQRES  17 C  366  GLN ALA ARG VAL TRP HIS HIS ASP ARG ARG ARG ILE PRO          
SEQRES  18 C  366  LEU LYS THR PRO LEU THR MET ARG VAL HIS HIS PRO VAL          
SEQRES  19 C  366  SER LEU LYS SER ARG PRO VAL MET GLY ASP HIS ALA THR          
SEQRES  20 C  366  ASP VAL ASN GLY GLN VAL LEU LEU GLN LEU SER THR GLN          
SEQRES  21 C  366  THR GLY SER GLU VAL GLN GLY TRP LEU PRO GLY GLY HIS          
SEQRES  22 C  366  LEU TYR SER ASP LEU LEU ALA LEU LEU HIS VAL TYR LEU          
SEQRES  23 C  366  GLY SER ARG LEU ASP VAL ARG LEU GLN LEU CYS VAL GLU          
SEQRES  24 C  366  ARG SER LEU LEU PRO ASP ALA ARG LEU SER CYS ARG PRO          
SEQRES  25 C  366  ALA ALA GLY SER PRO GLN LEU GLY ARG THR ALA VAL MET          
SEQRES  26 C  366  ARG THR GLN ALA LYS ILE ALA THR SER ALA ALA ARG VAL          
SEQRES  27 C  366  MET THR ILE SER LEU GLY ARG TYR GLN ARG VAL GLN GLU          
SEQRES  28 C  366  HIS TYR GLN ARG LYS GLU THR GLN GLU ASN GLY ASP TYR          
SEQRES  29 C  366  ARG TRP                                                      
SEQRES   1 D  143  MET PRO ARG PRO SER LEU TYR GLU ILE LEU TYR GLY ASN          
SEQRES   2 D  143  PHE THR GLY GLY LEU GLU LEU ASN GLN VAL GLY GLU GLU          
SEQRES   3 D  143  GLU GLN VAL ILE LEU SER VAL LEU ASP ASN MET GLN ARG          
SEQRES   4 D  143  ILE LEU ASN THR ARG ALA GLY SER LEU LYS HIS LEU PRO          
SEQRES   5 D  143  ASP TYR GLY LEU PRO ASP ILE THR THR ILE LEU GLN GLY          
SEQRES   6 D  143  MET PRO GLY THR ALA HIS GLN LEU MET ARG VAL LEU SER          
SEQRES   7 D  143  ASP VAL LEU LEU LYS TYR GLU PRO ARG ILE LYS ARG VAL          
SEQRES   8 D  143  ASP VAL THR MET GLN GLU GLN THR GLN PRO GLY GLU LEU          
SEQRES   9 D  143  HIS TYR VAL ILE ASP ALA GLU LEU LYS ASP ALA GLY LEU          
SEQRES  10 D  143  VAL ARG TYR GLY THR THR PHE ILE PRO GLU GLY ARG VAL          
SEQRES  11 D  143  LEU LEU ARG HIS LEU LYS GLN GLN ARG TYR VAL GLN THR          
HELIX    1 AA1 LEU A    4  LYS A   21  1                                  18    
HELIX    2 AA2 VAL A   46  ASP A   66  1                                  21    
HELIX    3 AA3 ASP A   67  GLU A   70  5                                   4    
HELIX    4 AA4 LEU A   71  SER A   77  1                                   7    
HELIX    5 AA5 ARG A   98  MET A  102  5                                   5    
HELIX    6 AA6 TRP A  168  LEU A  173  1                                   6    
HELIX    7 AA7 VAL A  186  THR A  195  1                                  10    
HELIX    8 AA8 LEU A  229  ASP A  234  1                                   6    
HELIX    9 AA9 ASP A  430  VAL A  435  5                                   6    
HELIX   10 AB1 ASP A  458  GLY A  471  1                                  14    
HELIX   11 AB2 SER A  478  GLY A  484  1                                   7    
HELIX   12 AB3 ALA A  487  ASP A  493  1                                   7    
HELIX   13 AB4 ASP A  494  LEU A  501  1                                   8    
HELIX   14 AB5 GLU A  538  ALA A  553  1                                  16    
HELIX   15 AB6 THR B    5  ALA B   22  1                                  18    
HELIX   16 AB7 HIS B   27  ALA B   32  5                                   6    
HELIX   17 AB8 MET B   33  LYS B   38  1                                   6    
HELIX   18 AB9 VAL B   46  GLY B   58  1                                  13    
HELIX   19 AC1 ARG B   59  LEU B   68  1                                  10    
HELIX   20 AC2 GLU B   70  SER B   74  5                                   5    
HELIX   21 AC3 PRO B   81  THR B   86  5                                   6    
HELIX   22 AC4 SER B  188  ARG B  197  1                                  10    
HELIX   23 AC5 GLY B  222  GLU B  226  5                                   5    
HELIX   24 AC6 LEU B  229  SER B  235  1                                   7    
HELIX   25 AC7 ALA B  236  SER B  238  5                                   3    
HELIX   26 AC8 LEU B  275  SER B  280  1                                   6    
HELIX   27 AC9 GLN B  329  GLU B  334  1                                   6    
HELIX   28 AD1 ASP B  458  GLY B  469  1                                  12    
HELIX   29 AD2 SER B  477  ARG B  483  1                                   7    
HELIX   30 AD3 LEU B  486  ASN B  490  5                                   5    
HELIX   31 AD4 ASP B  494  ASP B  502  1                                   9    
HELIX   32 AD5 GLY B  537  ALA B  553  1                                  17    
HELIX   33 AD6 GLN C    9  LEU C   15  1                                   7    
HELIX   34 AD7 GLN C   22  ILE C   26  5                                   5    
HELIX   35 AD8 ASN C   27  GLN C   39  1                                  13    
HELIX   36 AD9 ILE C   45  ALA C   51  5                                   7    
HELIX   37 AE1 PRO C  101  ALA C  109  1                                   9    
HELIX   38 AE2 ARG C  112  ALA C  117  5                                   6    
HELIX   39 AE3 ALA C  118  ASP C  123  1                                   6    
HELIX   40 AE4 ASP C  123  LYS C  139  1                                  17    
HELIX   41 AE5 THR C  154  ALA C  162  1                                   9    
HELIX   42 AE6 ARG C  179  MET C  187  1                                   9    
HELIX   43 AE7 GLU C  195  ALA C  205  1                                  11    
HELIX   44 AE8 THR C  261  GLN C  266  1                                   6    
HELIX   45 AE9 HIS C  273  HIS C  283  1                                  11    
HELIX   46 AF1 GLY D   24  THR D   43  1                                  20    
HELIX   47 AF2 ILE D   59  GLN D   64  1                                   6    
HELIX   48 AF3 GLY D   68  GLU D   85  1                                  18    
SHEET    1 AA1 2 VAL A  93  LEU A  95  0                                        
SHEET    2 AA1 2 VAL A 442  ASN A 444 -1  O  ARG A 443   N  ALA A  94           
SHEET    1 AA2 2 VAL A 338  THR A 342  0                                        
SHEET    2 AA2 2 SER A 409  ILE A 412 -1  O  SER A 409   N  THR A 342           
SHEET    1 AA3 4 VAL A 507  ARG A 514  0                                        
SHEET    2 AA3 4 LEU A 520  THR A 529 -1  O  ASP A 525   N  HIS A 509           
SHEET    3 AA3 4 THR A 565  ILE A 567  1  O  ILE A 567   N  VAL A 528           
SHEET    4 AA3 4 CYS A 574  ARG A 576 -1  O  ILE A 575   N  LEU A 566           
SHEET    1 AA4 2 VAL B  93  ALA B  94  0                                        
SHEET    2 AA4 2 VAL B 299  PRO B 300 -1  O  VAL B 299   N  ALA B  94           
SHEET    1 AA5 2 LEU B 178  TYR B 179  0                                        
SHEET    2 AA5 2 PRO B 220  GLY B 221  1  O  GLY B 221   N  LEU B 178           
SHEET    1 AA6 2 LEU B 203  ARG B 204  0                                        
SHEET    2 AA6 2 GLY B 272  PHE B 273 -1  O  GLY B 272   N  ARG B 204           
SHEET    1 AA7 3 PHE B 305  LEU B 307  0                                        
SHEET    2 AA7 3 ARG B 411  GLY B 414 -1  O  GLY B 414   N  PHE B 305           
SHEET    3 AA7 3 ALA B 340  THR B 342 -1  N  THR B 342   O  ARG B 411           
SHEET    1 AA8 2 TYR B 374  THR B 376  0                                        
SHEET    2 AA8 2 LEU B 392  GLY B 394 -1  O  GLY B 393   N  HIS B 375           
SHEET    1 AA9 2 GLN B 508  HIS B 510  0                                        
SHEET    2 AA9 2 GLY B 523  ASP B 525 -1  O  GLY B 523   N  HIS B 510           
SHEET    1 AB1 2 THR B 565  LEU B 566  0                                        
SHEET    2 AB1 2 CYS B 574  ILE B 575 -1  O  CYS B 574   N  LEU B 566           
SHEET    1 AB2 2 GLN C 209  TRP C 213  0                                        
SHEET    2 AB2 2 LEU C 254  SER C 258 -1  O  SER C 258   N  GLN C 209           
SHEET    1 AB3 2 LEU C 294  GLN C 295  0                                        
SHEET    2 AB3 2 ALA C 336  ARG C 337 -1  O  ARG C 337   N  LEU C 294           
SHEET    1 AB4 3 ILE D  88  GLU D  97  0                                        
SHEET    2 AB4 3 ILE D 108  GLY D 116 -1  O  ASP D 109   N  GLN D  96           
SHEET    3 AB4 3 ARG D 133  ARG D 139 -1  O  GLN D 137   N  ALA D 110           
CISPEP   1 ILE B  313    ILE B  314          0       -11.42                     
CISPEP   2 GLY B  484    THR B  485          0         0.53                     
CISPEP   3 ALA C  109    GLN C  110          0        16.56                     
CISPEP   4 ARG C  192    THR C  193          0         0.55                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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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