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Database: PDB
Entry: 3A69
LinkDB: 3A69
Original site: 3A69 
HEADER    MOTOR PROTEIN                           26-AUG-09   3A69              
TITLE     ATOMIC MODEL OF THE BACTERIAL FLAGELLAR HOOK BASED ON                 
TITLE    2 DOCKING AN X-RAY DERIVED STRUCTURE AND TERMINAL TWO ALPHA-           
TITLE    3 HELICES INTO AN 7.1 ANGSTROM RESOLUTION CRYOEM MAP                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FLAGELLAR HOOK PROTEIN FLGE;                               
COMPND   3 CHAIN: A                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SALMONELLA ENTERICA SUBSP. ENTERICA             
SOURCE   3 SEROVAR TYPHIMURIUM;                                                 
SOURCE   4 ORGANISM_TAXID: 90371;                                               
SOURCE   5 STRAIN: SJW880                                                       
KEYWDS    THE BACTERIAL FLAGELLAR MOTOR, UNIVERSAL JOINT, BACTERIAL             
KEYWDS   2 FLAGELLUM, MOTOR PROTEIN                                             
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    T.FUJII,T.KATO,K.NAMBA                                                
REVDAT   1   15-DEC-09 3A69    0                                                
JRNL        AUTH   T.FUJII,T.KATO,K.NAMBA                                       
JRNL        TITL   SPECIFIC ARRANGEMENT OF ALPHA-HELICAL COILED COILS           
JRNL        TITL 2 IN THE CORE DOMAIN OF THE BACTERIAL FLAGELLAR HOOK           
JRNL        TITL 3 FOR THE UNIVERSAL JOINT FUNCTION                             
JRNL        REF    STRUCTURE                     V.  17  1485 2009              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   19913483                                                     
JRNL        DOI    10.1016/J.STR.2009.08.017                                    
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    7.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : IHRSR                                     
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)    : 1.680                          
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 7.100                          
REMARK   3   NUMBER OF PARTICLES               : NULL                           
REMARK   3   CTF CORRECTION METHOD             : EACH IMAGES                    
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: TMV IMAGES              
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: A MODIFIED VERSION OF SPIDER PROGRAM WAS USED         
REMARK   3  FOR THE RECONSTRUCTION                                              
REMARK   4                                                                      
REMARK   4 3A69 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-SEP-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB028863.                                      
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : NULL                              
REMARK 245   NAME OF SAMPLE                 : BACTERIAL FLAGELLAR HOOK          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : 20MM TRIS-HCL, 100MM NACL         
REMARK 245   PH                             : 7.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 20-FEB-08                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 50.00                          
REMARK 245   MICROSCOPE MODEL                  : OTHER                          
REMARK 245   DETECTOR TYPE                     : 16 MEGAPIXELS SLOW-SCAN        
REMARK 245                                       CCD CAMERA, TEMCAM-F415MP      
REMARK 245   MINIMUM DEFOCUS (NM)              : 500.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 1.60                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 50000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 89285                          
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 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1                              
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,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                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 HELICAL SYMMETRY WITH THE FOLLOWING PARAMETERS:                      
REMARK 300 ROTATION PER SUBUNIT (TWIST) = 64.79 DEGREES                         
REMARK 300 RISE PER SUBUNIT (HEIGHT) = 4.12 ANGSTROMS                           
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  0.808298 -0.588773  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.588773  0.808298  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000      -20.61500            
REMARK 350   BIOMT1   2 -0.188341 -0.982104  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.982104 -0.188341  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000      -16.49200            
REMARK 350   BIOMT1   3 -0.968765 -0.247980  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.247980 -0.968765  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000      -12.36900            
REMARK 350   BIOMT1   4 -0.637047  0.770825  0.000000        0.00000            
REMARK 350   BIOMT2   4 -0.770825 -0.637047  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000       -8.24600            
REMARK 350   BIOMT1   5  0.426000  0.904723  0.000000        0.00000            
REMARK 350   BIOMT2   5 -0.904723  0.426000  0.000000        0.00000            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000       -4.12300            
REMARK 350   BIOMT1   6  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   6  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   7  0.426000 -0.904723  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.904723  0.426000  0.000000        0.00000            
REMARK 350   BIOMT3   7  0.000000  0.000000  1.000000        4.12300            
REMARK 350   BIOMT1   8 -0.637047 -0.770825  0.000000        0.00000            
REMARK 350   BIOMT2   8  0.770825 -0.637047  0.000000        0.00000            
REMARK 350   BIOMT3   8  0.000000  0.000000  1.000000        8.24600            
REMARK 350   BIOMT1   9 -0.968765  0.247980  0.000000        0.00000            
REMARK 350   BIOMT2   9 -0.247980 -0.968765  0.000000        0.00000            
REMARK 350   BIOMT3   9  0.000000  0.000000  1.000000       12.36900            
REMARK 350   BIOMT1  10 -0.188341  0.982104  0.000000        0.00000            
REMARK 350   BIOMT2  10 -0.982104 -0.188341  0.000000        0.00000            
REMARK 350   BIOMT3  10  0.000000  0.000000  1.000000       16.49200            
REMARK 350   BIOMT1  11  0.808298  0.588773  0.000000        0.00000            
REMARK 350   BIOMT2  11 -0.588773  0.808298  0.000000        0.00000            
REMARK 350   BIOMT3  11  0.000000  0.000000  1.000000       20.61500            
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     ASN A    25                                                      
REMARK 465     SER A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     THR A    28                                                      
REMARK 465     TYR A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     PHE A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     GLY A    34                                                      
REMARK 465     THR A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     SER A    37                                                      
REMARK 465     PHE A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     MET A    41                                                      
REMARK 465     PHE A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     SER A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     LEU A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     VAL A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     VAL A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     GLY A    55                                                      
REMARK 465     ILE A    56                                                      
REMARK 465     THR A    57                                                      
REMARK 465     GLN A    58                                                      
REMARK 465     ASP A    59                                                      
REMARK 465     PHE A    60                                                      
REMARK 465     THR A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     GLY A    63                                                      
REMARK 465     THR A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     THR A    66                                                      
REMARK 465     ASN A    67                                                      
REMARK 465     THR A    68                                                      
REMARK 465     GLY A    69                                                      
REMARK 465     ARG A    70                                                      
REMARK 465     GLY A   358                                                      
REMARK 465     ALA A   359                                                      
REMARK 465     LEU A   360                                                      
REMARK 465     GLU A   361                                                      
REMARK 465     ALA A   362                                                      
REMARK 465     SER A   363                                                      
REMARK 465     ASN A   364                                                      
REMARK 465     VAL A   365                                                      
REMARK 465     ASP A   366                                                      
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    ARG A 105   NE  -  CZ  -  NH1 ANGL. DEV. =   4.4 DEGREES          
REMARK 500    ARG A 105   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 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    ASN A 264       -0.53     80.24                                   
REMARK 500    PRO A 285      160.78    -40.68                                   
REMARK 500    ASP A 330     -143.99     48.78                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-1647   RELATED DB: EMDB                              
REMARK 900 7.1 ANGSTROM REOLUTION CRYOEM MAP OF THE BACTERIAL                   
REMARK 900 FLAGELLAR HOOK                                                       
DBREF  3A69 A    1   402  UNP    P0A1J1   FLGE_SALTY       2    403             
SEQRES   1 A  402  SER PHE SER GLN ALA VAL SER GLY LEU ASN ALA ALA ALA          
SEQRES   2 A  402  THR ASN LEU ASP VAL ILE GLY ASN ASN ILE ALA ASN SER          
SEQRES   3 A  402  ALA THR TYR GLY PHE LYS SER GLY THR ALA SER PHE ALA          
SEQRES   4 A  402  ASP MET PHE ALA GLY SER LYS VAL GLY LEU GLY VAL LYS          
SEQRES   5 A  402  VAL ALA GLY ILE THR GLN ASP PHE THR ASP GLY THR THR          
SEQRES   6 A  402  THR ASN THR GLY ARG GLY LEU ASP VAL ALA ILE SER GLN          
SEQRES   7 A  402  ASN GLY PHE PHE ARG LEU VAL ASP SER ASN GLY SER VAL          
SEQRES   8 A  402  PHE TYR SER ARG ASN GLY GLN PHE LYS LEU ASP GLU ASN          
SEQRES   9 A  402  ARG ASN LEU VAL ASN MET GLN GLY MET GLN LEU THR GLY          
SEQRES  10 A  402  TYR PRO ALA THR GLY THR PRO PRO THR ILE GLN GLN GLY          
SEQRES  11 A  402  ALA ASN PRO ALA PRO ILE THR ILE PRO ASN THR LEU MET          
SEQRES  12 A  402  ALA ALA LYS SER THR THR THR ALA SER MET GLN ILE ASN          
SEQRES  13 A  402  LEU ASN SER THR ASP PRO VAL PRO SER LYS THR PRO PHE          
SEQRES  14 A  402  SER VAL SER ASP ALA ASP SER TYR ASN LYS LYS GLY THR          
SEQRES  15 A  402  VAL THR VAL TYR ASP SER GLN GLY ASN ALA HIS ASP MET          
SEQRES  16 A  402  ASN VAL TYR PHE VAL LYS THR LYS ASP ASN GLU TRP ALA          
SEQRES  17 A  402  VAL TYR THR HIS ASP SER SER ASP PRO ALA ALA THR ALA          
SEQRES  18 A  402  PRO THR THR ALA SER THR THR LEU LYS PHE ASN GLU ASN          
SEQRES  19 A  402  GLY ILE LEU GLU SER GLY GLY THR VAL ASN ILE THR THR          
SEQRES  20 A  402  GLY THR ILE ASN GLY ALA THR ALA ALA THR PHE SER LEU          
SEQRES  21 A  402  SER PHE LEU ASN SER MET GLN GLN ASN THR GLY ALA ASN          
SEQRES  22 A  402  ASN ILE VAL ALA THR ASN GLN ASN GLY TYR LYS PRO GLY          
SEQRES  23 A  402  ASP LEU VAL SER TYR GLN ILE ASN ASN ASP GLY THR VAL          
SEQRES  24 A  402  VAL GLY ASN TYR SER ASN GLU GLN GLU GLN VAL LEU GLY          
SEQRES  25 A  402  GLN ILE VAL LEU ALA ASN PHE ALA ASN ASN GLU GLY LEU          
SEQRES  26 A  402  ALA SER GLN GLY ASP ASN VAL TRP ALA ALA THR GLN ALA          
SEQRES  27 A  402  SER GLY VAL ALA LEU LEU GLY THR ALA GLY SER GLY ASN          
SEQRES  28 A  402  PHE GLY LYS LEU THR ASN GLY ALA LEU GLU ALA SER ASN          
SEQRES  29 A  402  VAL ASP LEU SER LYS GLU LEU VAL ASN MET ILE VAL ALA          
SEQRES  30 A  402  GLN ARG ASN TYR GLN SER ASN ALA GLN THR ILE LYS THR          
SEQRES  31 A  402  GLN ASP GLN ILE LEU ASN THR LEU VAL ASN LEU ARG              
HELIX    1   1 SER A    1  ALA A   24  1                                  24    
HELIX    2   2 ASN A  321  LEU A  325  5                                   5    
HELIX    3   3 LEU A  367  LEU A  401  1                                  35    
SHEET    1   A 3 LEU A  72  ASP A  73  0                                        
SHEET    2   A 3 GLN A  98  LEU A 101 -1  O  PHE A  99   N  LEU A  72           
SHEET    3   A 3 LEU A 107  VAL A 108 -1  O  VAL A 108   N  LYS A 100           
SHEET    1   B 6 VAL A  91  SER A  94  0                                        
SHEET    2   B 6 PHE A  81  VAL A  85 -1  N  LEU A  84   O  PHE A  92           
SHEET    3   B 6 GLN A 114  PRO A 119 -1  O  GLN A 114   N  VAL A  85           
SHEET    4   B 6 GLU A 308  ILE A 314 -1  O  GLN A 313   N  TYR A 118           
SHEET    5   B 6 THR A 298  TYR A 303 -1  N  VAL A 299   O  LEU A 311           
SHEET    6   B 6 LEU A 288  ILE A 293 -1  N  VAL A 289   O  ASN A 302           
SHEET    1   C 5 ALA A 134  PRO A 135  0                                        
SHEET    2   C 5 GLN A 114  PRO A 119 -1  N  GLY A 117   O  ALA A 134           
SHEET    3   C 5 PHE A  81  VAL A  85 -1  N  VAL A  85   O  GLN A 114           
SHEET    4   C 5 LEU A 316  ASN A 318 -1  O  ALA A 317   N  PHE A  81           
SHEET    5   C 5 LEU A 343  GLY A 345 -1  O  GLY A 345   N  LEU A 316           
SHEET    1   D 4 THR A 242  THR A 246  0                                        
SHEET    2   D 4 THR A 257  SER A 261 -1  O  PHE A 258   N  ILE A 245           
SHEET    3   D 4 THR A 150  ASN A 158  1  N  ALA A 151   O  SER A 259           
SHEET    4   D 4 MET A 266  GLN A 268  1  O  MET A 266   N  LEU A 157           
SHEET    1   E 4 THR A 242  THR A 246  0                                        
SHEET    2   E 4 THR A 257  SER A 261 -1  O  PHE A 258   N  ILE A 245           
SHEET    3   E 4 THR A 150  ASN A 158  1  N  ALA A 151   O  SER A 259           
SHEET    4   E 4 ASN A 274  GLN A 280 -1  O  ALA A 277   N  GLN A 154           
SHEET    1   F 5 LYS A 179  TYR A 186  0                                        
SHEET    2   F 5 ALA A 192  LYS A 203 -1  O  HIS A 193   N  VAL A 185           
SHEET    3   F 5 GLU A 206  ASP A 213 -1  O  ALA A 208   N  VAL A 200           
SHEET    4   F 5 THR A 227  PHE A 231 -1  O  LEU A 229   N  TRP A 207           
SHEET    5   F 5 LEU A 237  SER A 239 -1  O  GLU A 238   N  LYS A 230           
SHEET    1   G 2 ALA A 326  SER A 327  0                                        
SHEET    2   G 2 TRP A 333  ALA A 334 -1  O  ALA A 334   N  ALA A 326           
CISPEP   1 THR A  123    PRO A  124          0         3.44                     
CISPEP   2 THR A  167    PRO A  168          0        -8.23                     
CISPEP   3 PRO A  285    GLY A  286          0        -0.02                     
CRYST1  336.000  336.000  336.000  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      0.002976  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.002976  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002976        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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