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Database: PDB
Entry: 5MYU
LinkDB: 5MYU
Original site: 5MYU 
HEADER    PROTEIN TRANSPORT                       27-JAN-17   5MYU              
TITLE     VIPA-N2/VIPB CONTRACTED SHEATH OF TYPE VI SECRETION SYSTEM            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UNCHARACTERIZED PROTEIN;                                   
COMPND   3 CHAIN: a, b, c, d, e, f;                                             
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: TYPE VI SECRETION SYSTEM PROTEIN IMPC;                     
COMPND   7 CHAIN: A, B, C, D, E, F;                                             
COMPND   8 SYNONYM: UNCHARACTERIZED PROTEIN IMPC;                               
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   3 ORGANISM_TAXID: 666;                                                 
SOURCE   4 EXPRESSION_SYSTEM: VIBRIO CHOLERAE;                                  
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 666;                                        
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: VIBRIO CHOLERAE;                                
SOURCE   8 ORGANISM_TAXID: 666;                                                 
SOURCE   9 GENE: ERS013138_01484, ERS013140_01660, ERS013165_01090,             
SOURCE  10 ERS013186_01572, ERS013198_01471, ERS013199_00294, ERS013200_00406,  
SOURCE  11 ERS013201_01395, ERS013202_00755, ERS013206_01101, ERS013207_02465;  
SOURCE  12 EXPRESSION_SYSTEM: VIBRIO CHOLERAE;                                  
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 666                                         
KEYWDS    BACTERIAL TYPE VI SECRETION SYSTEM, PROTEIN EXPORT, PROTEIN TRANSPORT 
EXPDTA    ELECTRON MICROSCOPY                                                   
NUMMDL    3                                                                     
AUTHOR    J.WANG,B.BRACKMANN,D.CASTANO-DIEZ,M.KUDRYASHEV,D.GOLDIE,T.MAIER,      
AUTHOR   2 H.STAHLBERG,M.BASLER                                                 
REVDAT   4   24-OCT-18 5MYU    1       REMARK LINK                              
REVDAT   3   08-NOV-17 5MYU    1       JRNL                                     
REVDAT   2   11-OCT-17 5MYU    1       JRNL                                     
REVDAT   1   02-AUG-17 5MYU    0                                                
JRNL        AUTH   J.WANG,M.BRACKMANN,D.CASTANO-DIEZ,M.KUDRYASHEV,K.N.GOLDIE,   
JRNL        AUTH 2 T.MAIER,H.STAHLBERG,M.BASLER                                 
JRNL        TITL   CRYO-EM STRUCTURE OF THE EXTENDED TYPE VI SECRETION SYSTEM   
JRNL        TITL 2 SHEATH-TUBE COMPLEX.                                         
JRNL        REF    NAT MICROBIOL                 V.   2  1507 2017              
JRNL        REFN                   ESSN 2058-5276                               
JRNL        PMID   28947741                                                     
JRNL        DOI    10.1038/S41564-017-0020-7                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    4.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
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          : 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               : 7000                           
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 5MYU COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 30-JAN-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003217.                                   
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                    : HELICAL ARRAY                     
REMARK 245   PARTICLE TYPE                  : HELICAL                           
REMARK 245   NAME OF SAMPLE                 : TYPE IV SECRETION SYSTEM SHEATH   
REMARK 245                                    -TUBE                             
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)  : 30.00                          
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)         : 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: DODECAMERIC                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC                
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 52000 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 174120 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -348.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: a, A, b, B, c, C, d, D, e, E,         
REMARK 350                    AND CHAINS: f, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   CB   SER C   484     CB   ALA d    20              1.30            
REMARK 500   CB   SER D   484     CB   ALA e    20              1.30            
REMARK 500   CB   SER E   484     CB   ALA f    20              1.32            
REMARK 500   CB   SER B   484     CB   ALA c    20              1.33            
REMARK 500   CB   ALA a    20     CB   SER F   484              1.35            
REMARK 500   CB   SER A   484     CB   ALA b    20              1.35            
REMARK 500   OG   SER D   484     CB   ALA e    20              1.59            
REMARK 500   OG   SER C   484     CB   ALA d    20              1.60            
REMARK 500   CB   ALA a    20     OG   SER F   484              1.61            
REMARK 500   OG   SER E   484     CB   ALA f    20              1.61            
REMARK 500   OG   SER B   484     CB   ALA c    20              1.62            
REMARK 500   OG   SER A   484     CB   ALA b    20              1.66            
REMARK 500   OD1  ASN A   480     ND2  ASN b    14              2.13            
REMARK 500   OD1  ASN B   480     ND2  ASN c    14              2.13            
REMARK 500   ND2  ASN a    14     OD1  ASN F   480              2.14            
REMARK 500   OD1  ASN E   480     ND2  ASN f    14              2.14            
REMARK 500   OD1  ASN D   480     ND2  ASN e    14              2.16            
REMARK 500   O    LEU A   483     CD1  TYR b    17              2.16            
REMARK 500   OD1  ASN C   480     ND2  ASN d    14              2.19            
REMARK 500   O    LEU B   483     CD1  TYR c    17              2.19            
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  1 GLU a  11     -169.85   -120.22                                   
REMARK 500  1 ASN A 111       63.21     60.66                                   
REMARK 500  1 SER A 266     -165.45    -79.19                                   
REMARK 500  1 ASN A 297       77.28   -104.59                                   
REMARK 500  1 ASP A 309       68.22     60.34                                   
REMARK 500  1 ASN A 436       82.40   -153.98                                   
REMARK 500  1 ARG A 488       -2.34     66.89                                   
REMARK 500  1 GLU b  11     -169.96   -120.19                                   
REMARK 500  1 ASN B 111       63.23     60.59                                   
REMARK 500  1 SER B 266     -165.47    -79.05                                   
REMARK 500  1 ASN B 297       77.32   -104.62                                   
REMARK 500  1 ASP B 309       68.28     60.38                                   
REMARK 500  1 ASN B 436       82.36   -154.04                                   
REMARK 500  1 ARG B 488       -2.33     66.86                                   
REMARK 500  1 ASN C 111       63.25     60.64                                   
REMARK 500  1 SER C 266     -165.44    -79.16                                   
REMARK 500  1 ASN C 297       77.37   -104.60                                   
REMARK 500  1 ASP C 309       68.31     60.36                                   
REMARK 500  1 ASN C 436       82.39   -153.95                                   
REMARK 500  1 ARG C 488       -2.42     67.06                                   
REMARK 500  1 GLU d  11     -169.96   -120.22                                   
REMARK 500  1 ASN D 111       63.25     60.65                                   
REMARK 500  1 SER D 266     -165.42    -79.18                                   
REMARK 500  1 ASN D 297       77.33   -104.57                                   
REMARK 500  1 ASP D 309       68.30     60.26                                   
REMARK 500  1 ASN D 436       82.44   -154.02                                   
REMARK 500  1 ARG D 488       -2.39     66.98                                   
REMARK 500  1 GLU e  11     -169.98   -120.24                                   
REMARK 500  1 ASN E 111       63.28     60.62                                   
REMARK 500  1 SER E 266     -165.47    -79.16                                   
REMARK 500  1 ASN E 297       77.36   -104.65                                   
REMARK 500  1 ASP E 309       68.31     60.27                                   
REMARK 500  1 ASN E 436       82.39   -154.00                                   
REMARK 500  1 ARG E 488       -2.37     66.92                                   
REMARK 500  1 GLU f  11     -169.92   -120.23                                   
REMARK 500  1 ASN F 111       63.16     60.68                                   
REMARK 500  1 SER F 266     -165.48    -79.15                                   
REMARK 500  1 ASN F 297       77.38   -104.66                                   
REMARK 500  1 ASP F 309       68.24     60.41                                   
REMARK 500  1 ASN F 436       82.42   -154.01                                   
REMARK 500  1 ARG F 488       -2.33     66.90                                   
REMARK 500  2 ASN A 111       63.21     60.73                                   
REMARK 500  2 SER A 266     -165.45    -79.13                                   
REMARK 500  2 ASN A 297       77.28   -104.61                                   
REMARK 500  2 ASP A 309       68.29     60.32                                   
REMARK 500  2 ASN A 436       82.42   -153.96                                   
REMARK 500  2 ARG A 488       -2.35     66.92                                   
REMARK 500  2 GLU b  11     -169.97   -120.26                                   
REMARK 500  2 ASN B 111       63.24     60.62                                   
REMARK 500  2 SER B 266     -165.45    -79.22                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     124 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 ALA A  240     PRO A  241          1      -122.62                    
REMARK 500 ALA B  240     PRO B  241          1      -122.61                    
REMARK 500 ALA C  240     PRO C  241          1      -122.62                    
REMARK 500 ALA D  240     PRO D  241          1      -122.64                    
REMARK 500 ALA E  240     PRO E  241          1      -122.63                    
REMARK 500 ALA F  240     PRO F  241          1      -122.67                    
REMARK 500 ALA A  240     PRO A  241          2      -122.64                    
REMARK 500 ALA B  240     PRO B  241          2      -122.56                    
REMARK 500 ALA C  240     PRO C  241          2      -122.63                    
REMARK 500 ALA D  240     PRO D  241          2      -122.71                    
REMARK 500 ALA E  240     PRO E  241          2      -122.60                    
REMARK 500 ALA F  240     PRO F  241          2      -122.65                    
REMARK 500 ALA A  240     PRO A  241          3      -122.67                    
REMARK 500 ALA B  240     PRO B  241          3      -122.65                    
REMARK 500 ALA C  240     PRO C  241          3      -122.63                    
REMARK 500 ALA D  240     PRO D  241          3      -122.60                    
REMARK 500 ALA E  240     PRO E  241          3      -122.59                    
REMARK 500 ALA F  240     PRO F  241          3      -122.60                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-3567   RELATED DB: EMDB                              
DBREF1 5MYU a    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU a     A0A023PRF3                         21         145             
DBREF1 5MYU A   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU A     A0A023PTI7                         61         490             
DBREF1 5MYU b    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU b     A0A023PRF3                         21         145             
DBREF1 5MYU B   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU B     A0A023PTI7                         61         490             
DBREF1 5MYU c    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU c     A0A023PRF3                         21         145             
DBREF1 5MYU C   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU C     A0A023PTI7                         61         490             
DBREF1 5MYU d    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU d     A0A023PRF3                         21         145             
DBREF1 5MYU D   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU D     A0A023PTI7                         61         490             
DBREF1 5MYU e    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU e     A0A023PRF3                         21         145             
DBREF1 5MYU E   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU E     A0A023PTI7                         61         490             
DBREF1 5MYU f    2   128  UNP                  A0A023PRF3_VIBCL                 
DBREF2 5MYU f     A0A023PRF3                         21         145             
DBREF1 5MYU F   61   490  UNP                  A0A023PTI7_VIBCL                 
DBREF2 5MYU F     A0A023PTI7                         61         490             
SEQADV 5MYU ALA a   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU a   27  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU ALA b   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU b   27  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU ALA c   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU c   27  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU ALA d   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU d   27  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU ALA e   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU e   27  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU ALA f   26  UNP  A0A023PRF           INSERTION                      
SEQADV 5MYU GLU f   27  UNP  A0A023PRF           INSERTION                      
SEQRES   1 a  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 a  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 a  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 a  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 a  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 a  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 a  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 a  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 a  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 a  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 A  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 A  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 A  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 A  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 A  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 A  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 A  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 A  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 A  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 A  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 A  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 A  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 A  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 A  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 A  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 A  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 A  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 A  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 A  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 A  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 A  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 A  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 A  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 A  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 A  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 A  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 A  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 A  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 A  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 A  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 A  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 A  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 A  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 A  430  ASP                                                          
SEQRES   1 b  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 b  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 b  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 b  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 b  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 b  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 b  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 b  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 b  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 b  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 B  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 B  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 B  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 B  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 B  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 B  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 B  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 B  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 B  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 B  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 B  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 B  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 B  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 B  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 B  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 B  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 B  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 B  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 B  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 B  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 B  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 B  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 B  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 B  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 B  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 B  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 B  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 B  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 B  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 B  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 B  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 B  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 B  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 B  430  ASP                                                          
SEQRES   1 c  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 c  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 c  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 c  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 c  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 c  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 c  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 c  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 c  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 c  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 C  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 C  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 C  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 C  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 C  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 C  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 C  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 C  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 C  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 C  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 C  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 C  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 C  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 C  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 C  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 C  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 C  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 C  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 C  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 C  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 C  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 C  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 C  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 C  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 C  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 C  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 C  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 C  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 C  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 C  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 C  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 C  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 C  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 C  430  ASP                                                          
SEQRES   1 d  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 d  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 d  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 d  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 d  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 d  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 d  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 d  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 d  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 d  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 D  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 D  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 D  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 D  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 D  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 D  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 D  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 D  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 D  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 D  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 D  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 D  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 D  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 D  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 D  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 D  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 D  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 D  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 D  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 D  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 D  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 D  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 D  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 D  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 D  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 D  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 D  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 D  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 D  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 D  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 D  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 D  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 D  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 D  430  ASP                                                          
SEQRES   1 e  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 e  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 e  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 e  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 e  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 e  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 e  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 e  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 e  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 e  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 E  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 E  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 E  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 E  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 E  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 E  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 E  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 E  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 E  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 E  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 E  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 E  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 E  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 E  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 E  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 E  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 E  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 E  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 E  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 E  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 E  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 E  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 E  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 E  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 E  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 E  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 E  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 E  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 E  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 E  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 E  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 E  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 E  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 E  430  ASP                                                          
SEQRES   1 f  127  SER LYS GLU GLY SER VAL ALA PRO LYS GLU ARG ILE ASN          
SEQRES   2 f  127  ILE LYS TYR ILE PRO ALA THR GLY ASP ALA GLN ALA GLU          
SEQRES   3 f  127  ALA GLU VAL GLU LEU PRO LEU LYS THR LEU VAL VAL GLY          
SEQRES   4 f  127  ASP PHE LYS GLY HIS ALA GLU GLN THR PRO LEU GLU GLU          
SEQRES   5 f  127  ARG ALA THR VAL THR VAL ASP LYS ASN ASN PHE GLU ALA          
SEQRES   6 f  127  VAL MET ARG GLU SER GLU LEU LYS ILE THR ALA THR VAL          
SEQRES   7 f  127  LYS ASN LYS LEU THR ASP ASP GLU ASN ALA GLU LEU PRO          
SEQRES   8 f  127  VAL GLU LEU ASN PHE LYS SER LEU ALA ASP PHE ALA PRO          
SEQRES   9 f  127  ASP ALA VAL ALA SER GLN VAL PRO GLU LEU LYS LYS LEU          
SEQRES  10 f  127  ILE GLU LEU ARG GLU ALA LEU VAL ALA LEU                      
SEQRES   1 F  430  ASN LYS SER LEU VAL ASP GLN MET LEU VAL GLU LEU ASP          
SEQRES   2 F  430  LYS LYS ILE SER ALA GLN MET ASP GLU ILE LEU HIS ASN          
SEQRES   3 F  430  SER GLN PHE GLN ALA MET GLU SER ALA TRP ARG GLY LEU          
SEQRES   4 F  430  LYS LEU PHE VAL ASP ARG THR ASP PHE ARG GLU ASN ASN          
SEQRES   5 F  430  LYS VAL GLU ILE LEU HIS VAL THR LYS ASP GLU LEU LEU          
SEQRES   6 F  430  GLU ASP PHE GLU PHE ALA PRO GLU THR ALA GLN SER GLY          
SEQRES   7 F  430  LEU TYR LYS HIS VAL TYR SER ALA GLY TYR GLY GLN PHE          
SEQRES   8 F  430  GLY GLY GLU PRO VAL GLY ALA ILE ILE GLY ASN TYR ALA          
SEQRES   9 F  430  PHE THR PRO SER THR PRO ASP MET LYS LEU LEU GLN TYR          
SEQRES  10 F  430  MET GLY ALA LEU GLY ALA MET ALA HIS ALA PRO PHE ILE          
SEQRES  11 F  430  SER SER VAL GLY PRO GLU PHE PHE GLY ILE ASP SER PHE          
SEQRES  12 F  430  GLU GLU LEU PRO ASN ILE LYS ASP LEU LYS SER THR PHE          
SEQRES  13 F  430  GLU SER PRO LYS TYR THR LYS TRP ARG SER LEU ARG GLU          
SEQRES  14 F  430  SER GLU ASP ALA ARG TYR LEU GLY LEU THR ALA PRO ARG          
SEQRES  15 F  430  PHE LEU LEU ARG VAL PRO TYR ASP PRO ILE GLU ASN PRO          
SEQRES  16 F  430  VAL LYS SER PHE ASN TYR ALA GLU ASN VAL SER ALA SER          
SEQRES  17 F  430  HIS GLU HIS TYR LEU TRP GLY ASN THR ALA PHE ALA PHE          
SEQRES  18 F  430  ALA THR ARG LEU THR ASP SER PHE ALA LYS TYR ARG TRP          
SEQRES  19 F  430  CYS PRO ASN ILE ILE GLY PRO GLN SER GLY GLY ALA VAL          
SEQRES  20 F  430  GLU ASP LEU PRO VAL HIS VAL PHE GLU SER MET GLY ALA          
SEQRES  21 F  430  LEU GLN SER LYS ILE PRO THR GLU VAL LEU ILE THR ASP          
SEQRES  22 F  430  ARG LYS GLU PHE GLU LEU ALA GLU GLU GLY PHE ILE ALA          
SEQRES  23 F  430  LEU THR MET ARG LYS GLY SER ASP ASN ALA ALA PHE PHE          
SEQRES  24 F  430  SER ALA ASN SER ILE GLN LYS PRO LYS VAL PHE PRO ASN          
SEQRES  25 F  430  THR LYS GLU GLY LYS GLU ALA GLU THR ASN TYR LYS LEU          
SEQRES  26 F  430  GLY THR GLN LEU PRO TYR MET MET ILE ILE ASN ARG LEU          
SEQRES  27 F  430  ALA HIS TYR VAL LYS VAL LEU GLN ARG GLU GLN ILE GLY          
SEQRES  28 F  430  ALA TRP LYS GLU ARG GLN ASP LEU GLU ARG GLU LEU ASN          
SEQRES  29 F  430  SER TRP ILE LYS GLN TYR VAL ALA ASP GLN GLU ASN PRO          
SEQRES  30 F  430  PRO ALA ASP VAL ARG SER ARG ARG PRO LEU ARG ALA ALA          
SEQRES  31 F  430  ARG ILE GLU VAL MET ASP VAL GLU GLY ASN PRO GLY TRP          
SEQRES  32 F  430  TYR GLN VAL SER LEU SER VAL ARG PRO HIS PHE LYS TYR          
SEQRES  33 F  430  MET GLY ALA ASN PHE GLU LEU SER LEU VAL GLY ARG LEU          
SEQRES  34 F  430  ASP                                                          
HELIX    1 AA1 ASN a   63  GLU a   72  1                                  10    
HELIX    2 AA2 SER a   99  PHE a  103  5                                   5    
HELIX    3 AA3 ALA a  104  VAL a  112  1                                   9    
HELIX    4 AA4 VAL a  112  LEU a  128  1                                  17    
HELIX    5 AA5 LYS A   62  HIS A   85  1                                  24    
HELIX    6 AA6 ASN A   86  ASP A  104  1                                  19    
HELIX    7 AA7 ASP A  107  ASN A  111  5                                   5    
HELIX    8 AA8 THR A  120  ALA A  131  1                                  12    
HELIX    9 AA9 SER A  137  TYR A  144  1                                   8    
HELIX   10 AB1 SER A  168  HIS A  186  1                                  19    
HELIX   11 AB2 GLY A  194  PHE A  198  5                                   5    
HELIX   12 AB3 SER A  202  LEU A  206  5                                   5    
HELIX   13 AB4 SER A  214  LYS A  220  5                                   7    
HELIX   14 AB5 TYR A  221  GLU A  229  1                                   9    
HELIX   15 AB6 SER A  268  TYR A  272  5                                   5    
HELIX   16 AB7 ASN A  276  ARG A  293  1                                  18    
HELIX   17 AB8 THR A  332  GLU A  342  1                                  11    
HELIX   18 AB9 THR A  373  THR A  387  1                                  15    
HELIX   19 AC1 GLN A  388  GLN A  406  1                                  19    
HELIX   20 AC2 GLU A  415  LYS A  428  1                                  14    
HELIX   21 AC3 PRO A  438  ARG A  445  1                                   8    
HELIX   22 AC4 ASN b   63  GLU b   72  1                                  10    
HELIX   23 AC5 SER b   99  PHE b  103  5                                   5    
HELIX   24 AC6 ALA b  104  VAL b  112  1                                   9    
HELIX   25 AC7 VAL b  112  LEU b  128  1                                  17    
HELIX   26 AC8 LYS B   62  HIS B   85  1                                  24    
HELIX   27 AC9 ASN B   86  ASP B  104  1                                  19    
HELIX   28 AD1 ASP B  107  ASN B  111  5                                   5    
HELIX   29 AD2 THR B  120  ALA B  131  1                                  12    
HELIX   30 AD3 SER B  137  TYR B  144  1                                   8    
HELIX   31 AD4 SER B  168  HIS B  186  1                                  19    
HELIX   32 AD5 GLY B  194  PHE B  198  5                                   5    
HELIX   33 AD6 SER B  202  LEU B  206  5                                   5    
HELIX   34 AD7 SER B  214  LYS B  220  5                                   7    
HELIX   35 AD8 TYR B  221  GLU B  229  1                                   9    
HELIX   36 AD9 SER B  268  TYR B  272  5                                   5    
HELIX   37 AE1 ASN B  276  ARG B  293  1                                  18    
HELIX   38 AE2 THR B  332  GLU B  342  1                                  11    
HELIX   39 AE3 THR B  373  THR B  387  1                                  15    
HELIX   40 AE4 GLN B  388  GLN B  406  1                                  19    
HELIX   41 AE5 GLU B  415  LYS B  428  1                                  14    
HELIX   42 AE6 PRO B  438  ARG B  445  1                                   8    
HELIX   43 AE7 ASN c   63  GLU c   72  1                                  10    
HELIX   44 AE8 SER c   99  PHE c  103  5                                   5    
HELIX   45 AE9 ALA c  104  VAL c  112  1                                   9    
HELIX   46 AF1 VAL c  112  LEU c  128  1                                  17    
HELIX   47 AF2 LYS C   62  HIS C   85  1                                  24    
HELIX   48 AF3 ASN C   86  ASP C  104  1                                  19    
HELIX   49 AF4 ASP C  107  ASN C  111  5                                   5    
HELIX   50 AF5 THR C  120  ALA C  131  1                                  12    
HELIX   51 AF6 SER C  137  TYR C  144  1                                   8    
HELIX   52 AF7 SER C  168  HIS C  186  1                                  19    
HELIX   53 AF8 GLY C  194  PHE C  198  5                                   5    
HELIX   54 AF9 SER C  202  LEU C  206  5                                   5    
HELIX   55 AG1 SER C  214  LYS C  220  5                                   7    
HELIX   56 AG2 TYR C  221  GLU C  229  1                                   9    
HELIX   57 AG3 SER C  268  TYR C  272  5                                   5    
HELIX   58 AG4 ASN C  276  ARG C  293  1                                  18    
HELIX   59 AG5 THR C  332  GLU C  342  1                                  11    
HELIX   60 AG6 THR C  373  THR C  387  1                                  15    
HELIX   61 AG7 GLN C  388  GLN C  406  1                                  19    
HELIX   62 AG8 GLU C  415  LYS C  428  1                                  14    
HELIX   63 AG9 PRO C  438  ARG C  445  1                                   8    
HELIX   64 AH1 ASN d   63  GLU d   72  1                                  10    
HELIX   65 AH2 SER d   99  PHE d  103  5                                   5    
HELIX   66 AH3 ALA d  104  VAL d  112  1                                   9    
HELIX   67 AH4 VAL d  112  LEU d  128  1                                  17    
HELIX   68 AH5 LYS D   62  HIS D   85  1                                  24    
HELIX   69 AH6 ASN D   86  ASP D  104  1                                  19    
HELIX   70 AH7 ASP D  107  ASN D  111  5                                   5    
HELIX   71 AH8 THR D  120  ALA D  131  1                                  12    
HELIX   72 AH9 SER D  137  TYR D  144  1                                   8    
HELIX   73 AI1 SER D  168  HIS D  186  1                                  19    
HELIX   74 AI2 GLY D  194  PHE D  198  5                                   5    
HELIX   75 AI3 SER D  202  LEU D  206  5                                   5    
HELIX   76 AI4 SER D  214  LYS D  220  5                                   7    
HELIX   77 AI5 TYR D  221  GLU D  229  1                                   9    
HELIX   78 AI6 SER D  268  TYR D  272  5                                   5    
HELIX   79 AI7 ASN D  276  ARG D  293  1                                  18    
HELIX   80 AI8 THR D  332  GLU D  342  1                                  11    
HELIX   81 AI9 THR D  373  THR D  387  1                                  15    
HELIX   82 AJ1 GLN D  388  GLN D  406  1                                  19    
HELIX   83 AJ2 GLU D  415  LYS D  428  1                                  14    
HELIX   84 AJ3 PRO D  438  ARG D  445  1                                   8    
HELIX   85 AJ4 ASN e   63  GLU e   72  1                                  10    
HELIX   86 AJ5 SER e   99  PHE e  103  5                                   5    
HELIX   87 AJ6 ALA e  104  VAL e  112  1                                   9    
HELIX   88 AJ7 VAL e  112  LEU e  128  1                                  17    
HELIX   89 AJ8 LYS E   62  HIS E   85  1                                  24    
HELIX   90 AJ9 ASN E   86  ASP E  104  1                                  19    
HELIX   91 AK1 ASP E  107  ASN E  111  5                                   5    
HELIX   92 AK2 THR E  120  ALA E  131  1                                  12    
HELIX   93 AK3 SER E  137  TYR E  144  1                                   8    
HELIX   94 AK4 SER E  168  HIS E  186  1                                  19    
HELIX   95 AK5 GLY E  194  PHE E  198  5                                   5    
HELIX   96 AK6 SER E  202  LEU E  206  5                                   5    
HELIX   97 AK7 SER E  214  LYS E  220  5                                   7    
HELIX   98 AK8 TYR E  221  GLU E  229  1                                   9    
HELIX   99 AK9 SER E  268  TYR E  272  5                                   5    
HELIX  100 AL1 ASN E  276  ARG E  293  1                                  18    
HELIX  101 AL2 THR E  332  GLU E  342  1                                  11    
HELIX  102 AL3 THR E  373  THR E  387  1                                  15    
HELIX  103 AL4 GLN E  388  GLN E  406  1                                  19    
HELIX  104 AL5 GLU E  415  LYS E  428  1                                  14    
HELIX  105 AL6 PRO E  438  ARG E  445  1                                   8    
HELIX  106 AL7 ASN f   63  GLU f   72  1                                  10    
HELIX  107 AL8 SER f   99  PHE f  103  5                                   5    
HELIX  108 AL9 ALA f  104  VAL f  112  1                                   9    
HELIX  109 AM1 VAL f  112  LEU f  128  1                                  17    
HELIX  110 AM2 LYS F   62  HIS F   85  1                                  24    
HELIX  111 AM3 ASN F   86  ASP F  104  1                                  19    
HELIX  112 AM4 ASP F  107  ASN F  111  5                                   5    
HELIX  113 AM5 THR F  120  ALA F  131  1                                  12    
HELIX  114 AM6 SER F  137  TYR F  144  1                                   8    
HELIX  115 AM7 SER F  168  HIS F  186  1                                  19    
HELIX  116 AM8 GLY F  194  PHE F  198  5                                   5    
HELIX  117 AM9 SER F  202  LEU F  206  5                                   5    
HELIX  118 AN1 SER F  214  LYS F  220  5                                   7    
HELIX  119 AN2 TYR F  221  GLU F  229  1                                   9    
HELIX  120 AN3 SER F  268  TYR F  272  5                                   5    
HELIX  121 AN4 ASN F  276  ARG F  293  1                                  18    
HELIX  122 AN5 THR F  332  GLU F  342  1                                  11    
HELIX  123 AN6 THR F  373  THR F  387  1                                  15    
HELIX  124 AN7 GLN F  388  GLN F  406  1                                  19    
HELIX  125 AN8 GLU F  415  LYS F  428  1                                  14    
HELIX  126 AN9 PRO F  438  ARG F  445  1                                   8    
SHEET    1 AA1 2 ILE a  13  TYR a  17  0                                        
SHEET    2 AA1 2 ALA F 479  LEU F 483  1  O  PHE F 481   N  ASN a  14           
SHEET    1 AA2 7 VAL a  57  VAL a  59  0                                        
SHEET    2 AA2 7 VAL A 114  HIS A 118 -1  O  VAL A 114   N  VAL a  59           
SHEET    3 AA2 7 LYS a  35  GLY a  40  1  N  THR a  36   O  GLU A 115           
SHEET    4 AA2 7 VAL A 156  ASN A 162  1  O  ILE A 160   N  VAL a  39           
SHEET    5 AA2 7 PHE A 189  SER A 192  1  O  ILE A 190   N  GLY A 161           
SHEET    6 AA2 7 LEU A 236  THR A 239  1  O  THR A 239   N  SER A 191           
SHEET    7 AA2 7 PHE A 344  ILE A 345  1  O  ILE A 345   N  LEU A 238           
SHEET    1 AA3 2 LEU a  73  LYS a  80  0                                        
SHEET    2 AA3 2 GLU a  90  PHE a  97 -1  O  LEU a  91   N  VAL a  79           
SHEET    1 AA4 2 PHE A 243  LEU A 244  0                                        
SHEET    2 AA4 2 TRP A 274  GLY A 275 -1  O  GLY A 275   N  PHE A 243           
SHEET    1 AA5 3 ALA A 306  VAL A 307  0                                        
SHEET    2 AA5 3 ALA A 356  PHE A 358 -1  O  ALA A 356   N  VAL A 307           
SHEET    3 AA5 3 LEU A 347  MET A 349 -1  N  THR A 348   O  ALA A 357           
SHEET    1 AA6 2 HIS A 313  GLU A 316  0                                        
SHEET    2 AA6 2 LEU A 321  LYS A 324 -1  O  GLN A 322   N  PHE A 315           
SHEET    1 AA7 2 LEU A 447  ASP A 456  0                                        
SHEET    2 AA7 2 TYR A 464  PRO A 472 -1  O  GLN A 465   N  MET A 455           
SHEET    1 AA8 2 ALA A 479  LEU A 483  0                                        
SHEET    2 AA8 2 ILE b  13  TYR b  17  1  O  ASN b  14   N  PHE A 481           
SHEET    1 AA9 7 VAL b  57  VAL b  59  0                                        
SHEET    2 AA9 7 VAL B 114  HIS B 118 -1  O  VAL B 114   N  VAL b  59           
SHEET    3 AA9 7 LYS b  35  GLY b  40  1  N  THR b  36   O  GLU B 115           
SHEET    4 AA9 7 VAL B 156  ASN B 162  1  O  ILE B 160   N  VAL b  39           
SHEET    5 AA9 7 PHE B 189  SER B 192  1  O  ILE B 190   N  GLY B 161           
SHEET    6 AA9 7 LEU B 236  THR B 239  1  O  THR B 239   N  SER B 191           
SHEET    7 AA9 7 PHE B 344  ILE B 345  1  O  ILE B 345   N  LEU B 238           
SHEET    1 AB1 2 LEU b  73  LYS b  80  0                                        
SHEET    2 AB1 2 GLU b  90  PHE b  97 -1  O  LEU b  91   N  VAL b  79           
SHEET    1 AB2 2 PHE B 243  LEU B 244  0                                        
SHEET    2 AB2 2 TRP B 274  GLY B 275 -1  O  GLY B 275   N  PHE B 243           
SHEET    1 AB3 3 ALA B 306  VAL B 307  0                                        
SHEET    2 AB3 3 ALA B 356  PHE B 358 -1  O  ALA B 356   N  VAL B 307           
SHEET    3 AB3 3 LEU B 347  MET B 349 -1  N  THR B 348   O  ALA B 357           
SHEET    1 AB4 2 HIS B 313  GLU B 316  0                                        
SHEET    2 AB4 2 LEU B 321  LYS B 324 -1  O  GLN B 322   N  PHE B 315           
SHEET    1 AB5 2 LEU B 447  ASP B 456  0                                        
SHEET    2 AB5 2 TYR B 464  PRO B 472 -1  O  GLN B 465   N  MET B 455           
SHEET    1 AB6 2 ALA B 479  LEU B 483  0                                        
SHEET    2 AB6 2 ILE c  13  TYR c  17  1  O  ASN c  14   N  PHE B 481           
SHEET    1 AB7 7 VAL c  57  VAL c  59  0                                        
SHEET    2 AB7 7 VAL C 114  HIS C 118 -1  O  VAL C 114   N  VAL c  59           
SHEET    3 AB7 7 LYS c  35  GLY c  40  1  N  THR c  36   O  GLU C 115           
SHEET    4 AB7 7 VAL C 156  ASN C 162  1  O  ILE C 160   N  VAL c  39           
SHEET    5 AB7 7 PHE C 189  SER C 192  1  O  ILE C 190   N  GLY C 161           
SHEET    6 AB7 7 LEU C 236  THR C 239  1  O  THR C 239   N  SER C 191           
SHEET    7 AB7 7 PHE C 344  ILE C 345  1  O  ILE C 345   N  LEU C 238           
SHEET    1 AB8 2 LEU c  73  LYS c  80  0                                        
SHEET    2 AB8 2 GLU c  90  PHE c  97 -1  O  LEU c  91   N  VAL c  79           
SHEET    1 AB9 2 PHE C 243  LEU C 244  0                                        
SHEET    2 AB9 2 TRP C 274  GLY C 275 -1  O  GLY C 275   N  PHE C 243           
SHEET    1 AC1 3 ALA C 306  VAL C 307  0                                        
SHEET    2 AC1 3 ALA C 356  PHE C 358 -1  O  ALA C 356   N  VAL C 307           
SHEET    3 AC1 3 LEU C 347  MET C 349 -1  N  THR C 348   O  ALA C 357           
SHEET    1 AC2 2 HIS C 313  GLU C 316  0                                        
SHEET    2 AC2 2 LEU C 321  LYS C 324 -1  O  GLN C 322   N  PHE C 315           
SHEET    1 AC3 2 LEU C 447  ASP C 456  0                                        
SHEET    2 AC3 2 TYR C 464  PRO C 472 -1  O  GLN C 465   N  MET C 455           
SHEET    1 AC4 2 ALA C 479  LEU C 483  0                                        
SHEET    2 AC4 2 ILE d  13  TYR d  17  1  O  ASN d  14   N  PHE C 481           
SHEET    1 AC5 7 VAL d  57  VAL d  59  0                                        
SHEET    2 AC5 7 VAL D 114  HIS D 118 -1  O  VAL D 114   N  VAL d  59           
SHEET    3 AC5 7 LYS d  35  GLY d  40  1  N  THR d  36   O  GLU D 115           
SHEET    4 AC5 7 VAL D 156  ASN D 162  1  O  ILE D 160   N  VAL d  39           
SHEET    5 AC5 7 PHE D 189  SER D 192  1  O  ILE D 190   N  GLY D 161           
SHEET    6 AC5 7 LEU D 236  THR D 239  1  O  THR D 239   N  SER D 191           
SHEET    7 AC5 7 PHE D 344  ILE D 345  1  O  ILE D 345   N  LEU D 238           
SHEET    1 AC6 2 LEU d  73  LYS d  80  0                                        
SHEET    2 AC6 2 GLU d  90  PHE d  97 -1  O  LEU d  91   N  VAL d  79           
SHEET    1 AC7 2 PHE D 243  LEU D 244  0                                        
SHEET    2 AC7 2 TRP D 274  GLY D 275 -1  O  GLY D 275   N  PHE D 243           
SHEET    1 AC8 3 ALA D 306  VAL D 307  0                                        
SHEET    2 AC8 3 ALA D 356  PHE D 358 -1  O  ALA D 356   N  VAL D 307           
SHEET    3 AC8 3 LEU D 347  MET D 349 -1  N  THR D 348   O  ALA D 357           
SHEET    1 AC9 2 HIS D 313  GLU D 316  0                                        
SHEET    2 AC9 2 LEU D 321  LYS D 324 -1  O  GLN D 322   N  PHE D 315           
SHEET    1 AD1 2 LEU D 447  ASP D 456  0                                        
SHEET    2 AD1 2 TYR D 464  PRO D 472 -1  O  GLN D 465   N  MET D 455           
SHEET    1 AD2 2 ALA D 479  LEU D 483  0                                        
SHEET    2 AD2 2 ILE e  13  TYR e  17  1  O  ASN e  14   N  PHE D 481           
SHEET    1 AD3 7 VAL e  57  VAL e  59  0                                        
SHEET    2 AD3 7 VAL E 114  HIS E 118 -1  O  VAL E 114   N  VAL e  59           
SHEET    3 AD3 7 LYS e  35  GLY e  40  1  N  THR e  36   O  GLU E 115           
SHEET    4 AD3 7 VAL E 156  ASN E 162  1  O  ILE E 160   N  VAL e  39           
SHEET    5 AD3 7 PHE E 189  SER E 192  1  O  ILE E 190   N  GLY E 161           
SHEET    6 AD3 7 LEU E 236  THR E 239  1  O  THR E 239   N  SER E 191           
SHEET    7 AD3 7 PHE E 344  ILE E 345  1  O  ILE E 345   N  LEU E 238           
SHEET    1 AD4 2 LEU e  73  LYS e  80  0                                        
SHEET    2 AD4 2 GLU e  90  PHE e  97 -1  O  LEU e  91   N  VAL e  79           
SHEET    1 AD5 2 PHE E 243  LEU E 244  0                                        
SHEET    2 AD5 2 TRP E 274  GLY E 275 -1  O  GLY E 275   N  PHE E 243           
SHEET    1 AD6 3 ALA E 306  VAL E 307  0                                        
SHEET    2 AD6 3 ALA E 356  PHE E 358 -1  O  ALA E 356   N  VAL E 307           
SHEET    3 AD6 3 LEU E 347  MET E 349 -1  N  THR E 348   O  ALA E 357           
SHEET    1 AD7 2 HIS E 313  GLU E 316  0                                        
SHEET    2 AD7 2 LEU E 321  LYS E 324 -1  O  GLN E 322   N  PHE E 315           
SHEET    1 AD8 2 LEU E 447  ASP E 456  0                                        
SHEET    2 AD8 2 TYR E 464  PRO E 472 -1  O  GLN E 465   N  MET E 455           
SHEET    1 AD9 2 ALA E 479  LEU E 483  0                                        
SHEET    2 AD9 2 ILE f  13  TYR f  17  1  O  ASN f  14   N  PHE E 481           
SHEET    1 AE1 7 VAL f  57  VAL f  59  0                                        
SHEET    2 AE1 7 VAL F 114  HIS F 118 -1  O  VAL F 114   N  VAL f  59           
SHEET    3 AE1 7 LYS f  35  GLY f  40  1  N  THR f  36   O  GLU F 115           
SHEET    4 AE1 7 VAL F 156  ASN F 162  1  O  ILE F 160   N  VAL f  39           
SHEET    5 AE1 7 PHE F 189  SER F 192  1  O  ILE F 190   N  GLY F 161           
SHEET    6 AE1 7 LEU F 236  THR F 239  1  O  THR F 239   N  SER F 191           
SHEET    7 AE1 7 PHE F 344  ILE F 345  1  O  ILE F 345   N  LEU F 238           
SHEET    1 AE2 2 LEU f  73  LYS f  80  0                                        
SHEET    2 AE2 2 GLU f  90  PHE f  97 -1  O  LEU f  91   N  VAL f  79           
SHEET    1 AE3 2 PHE F 243  LEU F 244  0                                        
SHEET    2 AE3 2 TRP F 274  GLY F 275 -1  O  GLY F 275   N  PHE F 243           
SHEET    1 AE4 3 ALA F 306  VAL F 307  0                                        
SHEET    2 AE4 3 ALA F 356  PHE F 358 -1  O  ALA F 356   N  VAL F 307           
SHEET    3 AE4 3 LEU F 347  MET F 349 -1  N  THR F 348   O  ALA F 357           
SHEET    1 AE5 2 HIS F 313  GLU F 316  0                                        
SHEET    2 AE5 2 LEU F 321  LYS F 324 -1  O  GLN F 322   N  PHE F 315           
SHEET    1 AE6 2 LEU F 447  ASP F 456  0                                        
SHEET    2 AE6 2 TYR F 464  PRO F 472 -1  O  GLN F 465   N  MET F 455           
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                         
MODEL        1                                                                  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system