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Database: PDB
Entry: 5N8N
LinkDB: 5N8N
Original site: 5N8N 
HEADER    STRUCTURAL PROTEIN                      23-FEB-17   5N8N              
TITLE     CONTRACTED SHEATH OF A PSEUDOMONAS AERUGINOSA TYPE SIX SECRETION      
TITLE    2 SYSTEM CONSISTING OF TSSB1 AND TSSC1                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TYPE VI SECRETION PROTEIN, FAMILY;                         
COMPND   3 CHAIN: A, C, E, G, I, K, M, O, Q, S, U, W, Y, a, c;                  
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: EVPB FAMILY TYPE VI SECRETION PROTEIN;                     
COMPND   7 CHAIN: B, D, F, H, J, L, N, P, R, T, V, X, Z, b, d;                  
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 287;                                                 
SOURCE   4 GENE: AO964_32215, PAERUG_E15_LONDON_28_01_14_04448,                 
SOURCE   5 PAERUG_P32_LONDON_17_VIM_2_10_11_02574, PAMH19_0082;                 
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE  10 ORGANISM_TAXID: 287;                                                 
SOURCE  11 GENE: U769_00445;                                                    
SOURCE  12 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  13 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    TYPE SIX SECRETION SYSTEM, STRUCTURAL PROTEIN                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    O.SALIH,S.HE,L.STACH,J.T.MACDONALD,S.PLANAMENTE,E.MANOLI,S.SCHERES,   
AUTHOR   2 A.FILLOUX,P.S.FREEMONT                                               
REVDAT   3   14-FEB-18 5N8N    1       JRNL                                     
REVDAT   2   17-JAN-18 5N8N    1       JRNL                                     
REVDAT   1   10-JAN-18 5N8N    0                                                
JRNL        AUTH   O.SALIH,S.HE,S.PLANAMENTE,L.STACH,J.T.MACDONALD,E.MANOLI,    
JRNL        AUTH 2 S.H.W.SCHERES,A.FILLOUX,P.S.FREEMONT                         
JRNL        TITL   ATOMIC STRUCTURE OF TYPE VI CONTRACTILE SHEATH FROM          
JRNL        TITL 2 PSEUDOMONAS AERUGINOSA.                                      
JRNL        REF    STRUCTURE                     V.  26   329 2018              
JRNL        REFN                   ISSN 1878-4186                               
JRNL        PMID   29307484                                                     
JRNL        DOI    10.1016/J.STR.2017.12.005                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.28 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          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.280                          
REMARK   3   NUMBER OF PARTICLES               : 71264                          
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 5N8N COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-FEB-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200003689.                                   
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                 : CONTRACTED SHEATH OF A            
REMARK 245  PSEUDOMONAS AERUGINOSA T6SS CONSISTING OF TSSB1 AND TSSC1; AO964_   
REMARK 245  32215, PAERUG_E15_LONDON_28_01_14_04448, PAERUG_P32_LONDON_17_      
REMARK 245  VIM_2_10_11_02574, PAMH19_0082; U769_00445                          
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 1.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 9.00                              
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                     : FEI FALCON II (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: 30-MERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: 30-MERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 201830 ANGSTROM**2                        
REMARK 350 SURFACE AREA OF THE COMPLEX: 378640 ANGSTROM**2                      
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1170.0 KCAL/MOL                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R, S,            
REMARK 350                    AND CHAINS: T, U, V, W, X, Y, Z, a, b, c,         
REMARK 350                    AND CHAINS: d                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   OG1  THR V   441     NZ   LYS V   445              1.75            
REMARK 500   OG1  THR B   441     NZ   LYS B   445              1.76            
REMARK 500   OG1  THR d   441     NZ   LYS d   445              1.76            
REMARK 500   OG1  THR F   441     NZ   LYS F   445              1.76            
REMARK 500   OG1  THR b   441     NZ   LYS b   445              1.76            
REMARK 500   OG1  THR R   441     NZ   LYS R   445              1.76            
REMARK 500   OG1  THR X   441     NZ   LYS X   445              1.76            
REMARK 500   OG1  THR D   441     NZ   LYS D   445              1.76            
REMARK 500   OG1  THR N   441     NZ   LYS N   445              1.76            
REMARK 500   OG1  THR Z   441     NZ   LYS Z   445              1.76            
REMARK 500   OG1  THR L   441     NZ   LYS L   445              1.76            
REMARK 500   OG1  THR P   441     NZ   LYS P   445              1.76            
REMARK 500   OG1  THR T   441     NZ   LYS T   445              1.76            
REMARK 500   OG1  THR J   441     NZ   LYS J   445              1.76            
REMARK 500   OG1  THR H   441     NZ   LYS H   445              1.76            
REMARK 500   NH1  ARG Y    18     OE2  GLU b   342              1.94            
REMARK 500   NH1  ARG a    18     OE2  GLU d   342              1.94            
REMARK 500   NH1  ARG W    18     OE2  GLU Z   342              1.95            
REMARK 500   NH1  ARG S    18     OE2  GLU V   342              1.95            
REMARK 500   NH1  ARG C    18     OE2  GLU F   342              1.95            
REMARK 500   NH1  ARG Q    18     OE2  GLU T   342              1.96            
REMARK 500   NH1  ARG U    18     OE2  GLU X   342              1.96            
REMARK 500   NH1  ARG O    18     OE2  GLU R   342              1.96            
REMARK 500   NH1  ARG I    18     OE2  GLU L   342              1.97            
REMARK 500   NH1  ARG M    18     OE2  GLU P   342              1.97            
REMARK 500   NH2  ARG D   340     OD2  ASP P   139              1.97            
REMARK 500   NH2  ARG N   340     OD2  ASP Z   139              1.97            
REMARK 500   NH2  ARG H   340     OD2  ASP T   139              1.97            
REMARK 500   NH2  ARG B   340     OD2  ASP N   139              1.97            
REMARK 500   NH2  ARG J   340     OD2  ASP V   139              1.97            
REMARK 500   NH1  ARG K    18     OE2  GLU N   342              1.97            
REMARK 500   NH1  ARG G    18     OE2  GLU J   342              1.98            
REMARK 500   NH1  ARG A    18     OE2  GLU D   342              1.98            
REMARK 500   NH2  ARG R   340     OD2  ASP d   139              1.98            
REMARK 500   NH1  ARG E    18     OE2  GLU H   342              1.98            
REMARK 500   NH2  ARG L   340     OD2  ASP X   139              1.98            
REMARK 500   NH2  ARG F   340     OD2  ASP R   139              1.99            
REMARK 500   NH2  ARG P   340     OD2  ASP b   139              1.99            
REMARK 500   OD2  ASP I    66     NZ   LYS X   218              2.01            
REMARK 500   OD2  ASP M    66     NZ   LYS b   218              2.02            
REMARK 500   OD2  ASP O    66     NZ   LYS d   218              2.02            
REMARK 500   OD2  ASP G    66     NZ   LYS V   218              2.02            
REMARK 500   OD2  ASP C    66     NZ   LYS R   218              2.02            
REMARK 500   OD2  ASP K    66     NZ   LYS Z   218              2.02            
REMARK 500   OD2  ASP E    66     NZ   LYS T   218              2.02            
REMARK 500   OD2  ASP A    66     NZ   LYS P   218              2.04            
REMARK 500   NZ   LYS D   123     OD1  ASP D   175              2.04            
REMARK 500   NZ   LYS V   123     OD1  ASP V   175              2.04            
REMARK 500   NZ   LYS J   123     OD1  ASP J   175              2.04            
REMARK 500   NZ   LYS d   123     OD1  ASP d   175              2.04            
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      76 CLOSE CONTACTS                                
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
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,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
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   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A  22   CD    GLU A  22   OE1     0.071                       
REMARK 500    GLU A  26   CD    GLU A  26   OE1     0.071                       
REMARK 500    GLU B 150   CD    GLU B 150   OE1     0.067                       
REMARK 500    GLU B 150   CD    GLU B 150   OE2     0.066                       
REMARK 500    TYR B 168   CE1   TYR B 168   CZ     -0.079                       
REMARK 500    GLU C  22   CD    GLU C  22   OE1     0.072                       
REMARK 500    GLU C  26   CD    GLU C  26   OE1     0.072                       
REMARK 500    GLU D  42   CD    GLU D  42   OE1     0.073                       
REMARK 500    GLU D 150   CD    GLU D 150   OE1     0.067                       
REMARK 500    GLU D 150   CD    GLU D 150   OE2     0.066                       
REMARK 500    TYR D 168   CE1   TYR D 168   CZ     -0.078                       
REMARK 500    GLU E  22   CD    GLU E  22   OE1     0.071                       
REMARK 500    GLU E  26   CD    GLU E  26   OE1     0.071                       
REMARK 500    GLU F  42   CD    GLU F  42   OE1     0.073                       
REMARK 500    GLU F 150   CD    GLU F 150   OE1     0.067                       
REMARK 500    GLU F 150   CD    GLU F 150   OE2     0.067                       
REMARK 500    TYR F 168   CE1   TYR F 168   CZ     -0.078                       
REMARK 500    GLU G  22   CD    GLU G  22   OE1     0.072                       
REMARK 500    GLU G  26   CD    GLU G  26   OE1     0.072                       
REMARK 500    GLU H  42   CD    GLU H  42   OE1     0.072                       
REMARK 500    GLU H 150   CD    GLU H 150   OE1     0.067                       
REMARK 500    GLU H 150   CD    GLU H 150   OE2     0.066                       
REMARK 500    TYR H 168   CE1   TYR H 168   CZ     -0.079                       
REMARK 500    GLU I  22   CD    GLU I  22   OE1     0.072                       
REMARK 500    GLU I  26   CD    GLU I  26   OE1     0.072                       
REMARK 500    GLU J  42   CD    GLU J  42   OE1     0.073                       
REMARK 500    GLU J 150   CD    GLU J 150   OE1     0.067                       
REMARK 500    GLU J 150   CD    GLU J 150   OE2     0.067                       
REMARK 500    TYR J 168   CE1   TYR J 168   CZ     -0.079                       
REMARK 500    GLU K  22   CD    GLU K  22   OE1     0.072                       
REMARK 500    GLU K  26   CD    GLU K  26   OE1     0.072                       
REMARK 500    GLU L  42   CD    GLU L  42   OE1     0.073                       
REMARK 500    GLU L 150   CD    GLU L 150   OE1     0.067                       
REMARK 500    GLU L 150   CD    GLU L 150   OE2     0.066                       
REMARK 500    GLU M  22   CD    GLU M  22   OE1     0.072                       
REMARK 500    GLU M  26   CD    GLU M  26   OE1     0.072                       
REMARK 500    GLU N  42   CD    GLU N  42   OE1     0.072                       
REMARK 500    GLU N 150   CD    GLU N 150   OE1     0.067                       
REMARK 500    GLU N 150   CD    GLU N 150   OE2     0.066                       
REMARK 500    GLU O  22   CD    GLU O  22   OE1     0.072                       
REMARK 500    GLU O  26   CD    GLU O  26   OE1     0.072                       
REMARK 500    GLU P 150   CD    GLU P 150   OE1     0.067                       
REMARK 500    GLU P 150   CD    GLU P 150   OE2     0.066                       
REMARK 500    TYR P 168   CE1   TYR P 168   CZ     -0.078                       
REMARK 500    GLU Q  22   CD    GLU Q  22   OE1     0.071                       
REMARK 500    GLU Q  26   CD    GLU Q  26   OE1     0.072                       
REMARK 500    GLU R  42   CD    GLU R  42   OE1     0.072                       
REMARK 500    GLU R 150   CD    GLU R 150   OE1     0.067                       
REMARK 500    GLU R 150   CD    GLU R 150   OE2     0.066                       
REMARK 500    TYR R 168   CE1   TYR R 168   CZ     -0.078                       
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      82 BOND DEVIATIONS.                              
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG A  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU B 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG B 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    PRO B 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU B 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG C  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG C  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU D 109   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    GLU D 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG D 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO D 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU D 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG E  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG E  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLU F 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG F 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO F 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU F 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG G  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG G  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU H 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.1 DEGREES          
REMARK 500    ARG H 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO H 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU H 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG I  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG I  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLU J 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG J 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO J 437   C   -  N   -  CD  ANGL. DEV. = -16.3 DEGREES          
REMARK 500    LEU J 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG K  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG K  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU L 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG L 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.2 DEGREES          
REMARK 500    PRO L 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU L 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG M  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -5.9 DEGREES          
REMARK 500    ARG M  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.6 DEGREES          
REMARK 500    GLU N 109   OE1 -  CD  -  OE2 ANGL. DEV. =  -7.2 DEGREES          
REMARK 500    GLU N 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG N 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    PRO N 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU N 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500    ARG O  13   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG O  18   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    GLU P 150   OE1 -  CD  -  OE2 ANGL. DEV. =   8.0 DEGREES          
REMARK 500    ARG P 390   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.3 DEGREES          
REMARK 500    PRO P 437   C   -  N   -  CD  ANGL. DEV. = -16.2 DEGREES          
REMARK 500    LEU P 486   CB  -  CG  -  CD2 ANGL. DEV. = -11.3 DEGREES          
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      94 ANGLE DEVIATIONS.                             
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    THR A   5       78.23     44.27                                   
REMARK 500    ALA A  30     -129.19     53.44                                   
REMARK 500    GLN A  35     -112.88     67.17                                   
REMARK 500    LEU A  36       77.03     63.34                                   
REMARK 500    GLN A  54     -123.59     63.63                                   
REMARK 500    ALA A  58      -15.54     74.49                                   
REMARK 500    LYS A  61     -163.91     63.23                                   
REMARK 500    THR A  90       59.23   -142.69                                   
REMARK 500    GLU A  92     -121.50     70.64                                   
REMARK 500    THR B  56      -66.17   -138.51                                   
REMARK 500    SER B  60      -15.04     67.36                                   
REMARK 500    ASN B  61     -136.35     46.99                                   
REMARK 500    ALA B  63      -74.82   -123.32                                   
REMARK 500    ASP B 111     -154.31   -150.23                                   
REMARK 500    GLU B 151      -66.84   -130.58                                   
REMARK 500    TYR B 160       -3.68     77.42                                   
REMARK 500    MET B 204      -66.75   -131.91                                   
REMARK 500    SER B 206      -60.25   -130.30                                   
REMARK 500    TRP B 207       -0.42     78.50                                   
REMARK 500    GLU B 268     -109.35     59.10                                   
REMARK 500    ALA B 272     -140.82     55.82                                   
REMARK 500    ASP B 273      -18.54     72.65                                   
REMARK 500    SER B 274      -12.54     62.85                                   
REMARK 500    ASP B 324     -121.38     59.68                                   
REMARK 500    VAL B 327       71.49     58.11                                   
REMARK 500    GLU B 442      -68.16   -129.41                                   
REMARK 500    ASN B 463      131.69   -176.58                                   
REMARK 500    THR C   5       78.24     44.24                                   
REMARK 500    ALA C  30     -129.26     53.44                                   
REMARK 500    GLN C  35     -112.89     67.05                                   
REMARK 500    LEU C  36       77.01     63.38                                   
REMARK 500    GLN C  54     -123.61     63.69                                   
REMARK 500    ALA C  58      -15.69     74.57                                   
REMARK 500    LYS C  61     -163.93     63.17                                   
REMARK 500    THR C  90       59.26   -142.73                                   
REMARK 500    GLU C  92     -121.56     70.73                                   
REMARK 500    THR D  56      -66.09   -138.53                                   
REMARK 500    SER D  60      -15.13     67.42                                   
REMARK 500    ASN D  61     -136.34     46.95                                   
REMARK 500    ALA D  63      -74.77   -123.29                                   
REMARK 500    ASP D 111     -154.29   -150.21                                   
REMARK 500    GLU D 151      -66.85   -130.57                                   
REMARK 500    TYR D 160       -3.63     77.42                                   
REMARK 500    MET D 204      -66.79   -131.86                                   
REMARK 500    SER D 206      -60.22   -130.35                                   
REMARK 500    TRP D 207       -0.43     78.51                                   
REMARK 500    GLU D 268     -109.39     59.09                                   
REMARK 500    ALA D 272     -140.87     55.85                                   
REMARK 500    ASP D 273      -18.52     72.66                                   
REMARK 500    SER D 274      -12.55     62.82                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS     405 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-3600   RELATED DB: EMDB                              
REMARK 900 CONTRACTED SHEATH OF A PSEUDOMONAS AERUGINOSA TYPE SIX SECRETION     
REMARK 900 SYSTEM CONSISTING OF TSSB1 AND TSSC1                                 
DBREF1 5N8N A    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N A     A0A072ZG09                          4         135             
DBREF1 5N8N B   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N B     A0A0E1AL03                         38         498             
DBREF1 5N8N C    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N C     A0A072ZG09                          4         135             
DBREF1 5N8N D   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N D     A0A0E1AL03                         38         498             
DBREF1 5N8N E    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N E     A0A072ZG09                          4         135             
DBREF1 5N8N F   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N F     A0A0E1AL03                         38         498             
DBREF1 5N8N G    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N G     A0A072ZG09                          4         135             
DBREF1 5N8N H   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N H     A0A0E1AL03                         38         498             
DBREF1 5N8N I    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N I     A0A072ZG09                          4         135             
DBREF1 5N8N J   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N J     A0A0E1AL03                         38         498             
DBREF1 5N8N K    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N K     A0A072ZG09                          4         135             
DBREF1 5N8N L   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N L     A0A0E1AL03                         38         498             
DBREF1 5N8N M    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N M     A0A072ZG09                          4         135             
DBREF1 5N8N N   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N N     A0A0E1AL03                         38         498             
DBREF1 5N8N O    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N O     A0A072ZG09                          4         135             
DBREF1 5N8N P   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N P     A0A0E1AL03                         38         498             
DBREF1 5N8N Q    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N Q     A0A072ZG09                          4         135             
DBREF1 5N8N R   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N R     A0A0E1AL03                         38         498             
DBREF1 5N8N S    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N S     A0A072ZG09                          4         135             
DBREF1 5N8N T   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N T     A0A0E1AL03                         38         498             
DBREF1 5N8N U    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N U     A0A072ZG09                          4         135             
DBREF1 5N8N V   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N V     A0A0E1AL03                         38         498             
DBREF1 5N8N W    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N W     A0A072ZG09                          4         135             
DBREF1 5N8N X   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N X     A0A0E1AL03                         38         498             
DBREF1 5N8N Y    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N Y     A0A072ZG09                          4         135             
DBREF1 5N8N Z   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N Z     A0A0E1AL03                         38         498             
DBREF1 5N8N a    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N a     A0A072ZG09                          4         135             
DBREF1 5N8N b   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N b     A0A0E1AL03                         38         498             
DBREF1 5N8N c    4   135  UNP                  A0A072ZG09_PSEAI                 
DBREF2 5N8N c     A0A072ZG09                          4         135             
DBREF1 5N8N d   38   498  UNP                  A0A0E1AL03_PSEAI                 
DBREF2 5N8N d     A0A0E1AL03                         38         498             
SEQRES   1 A  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 A  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 A  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 A  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 A  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 A  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 A  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 A  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 A  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 A  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 A  132  THR TYR                                                      
SEQRES   1 B  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 B  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 B  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 B  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 B  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 B  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 B  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 B  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 B  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 B  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 B  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 B  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 B  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 B  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 B  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 B  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 B  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 B  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 B  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 B  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 B  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 B  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 B  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 B  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 B  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 B  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 B  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 B  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 B  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 B  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 B  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 B  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 B  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 B  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 B  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 B  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 C  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 C  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 C  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 C  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 C  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 C  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 C  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 C  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 C  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 C  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 C  132  THR TYR                                                      
SEQRES   1 D  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 D  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 D  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 D  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 D  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 D  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 D  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 D  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 D  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 D  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 D  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 D  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 D  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 D  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 D  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 D  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 D  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 D  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 D  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 D  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 D  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 D  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 D  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 D  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 D  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 D  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 D  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 D  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 D  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 D  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 D  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 D  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 D  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 D  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 D  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 D  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 E  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 E  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 E  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 E  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 E  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 E  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 E  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 E  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 E  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 E  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 E  132  THR TYR                                                      
SEQRES   1 F  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 F  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 F  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 F  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 F  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 F  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 F  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 F  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 F  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 F  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 F  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 F  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 F  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 F  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 F  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 F  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 F  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 F  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 F  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 F  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 F  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 F  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 F  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 F  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 F  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 F  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 F  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 F  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 F  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 F  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 F  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 F  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 F  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 F  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 F  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 F  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 G  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 G  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 G  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 G  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 G  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 G  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 G  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 G  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 G  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 G  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 G  132  THR TYR                                                      
SEQRES   1 H  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 H  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 H  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 H  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 H  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 H  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 H  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 H  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 H  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 H  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 H  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 H  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 H  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 H  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 H  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 H  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 H  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 H  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 H  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 H  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 H  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 H  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 H  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 H  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 H  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 H  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 H  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 H  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 H  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 H  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 H  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 H  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 H  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 H  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 H  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 H  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 I  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 I  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 I  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 I  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 I  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 I  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 I  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 I  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 I  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 I  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 I  132  THR TYR                                                      
SEQRES   1 J  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 J  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 J  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 J  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 J  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 J  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 J  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 J  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 J  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 J  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 J  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 J  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 J  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 J  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 J  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 J  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 J  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 J  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 J  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 J  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 J  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 J  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 J  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 J  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 J  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 J  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 J  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 J  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 J  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 J  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 J  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 J  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 J  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 J  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 J  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 J  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 K  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 K  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 K  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 K  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 K  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 K  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 K  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 K  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 K  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 K  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 K  132  THR TYR                                                      
SEQRES   1 L  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 L  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 L  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 L  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 L  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 L  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 L  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 L  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 L  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 L  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 L  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 L  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 L  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 L  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 L  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 L  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 L  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 L  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 L  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 L  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 L  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 L  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 L  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 L  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 L  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 L  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 L  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 L  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 L  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 L  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 L  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 L  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 L  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 L  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 L  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 L  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 M  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 M  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 M  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 M  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 M  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 M  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 M  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 M  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 M  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 M  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 M  132  THR TYR                                                      
SEQRES   1 N  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 N  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 N  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 N  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 N  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 N  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 N  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 N  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 N  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 N  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 N  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 N  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 N  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 N  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 N  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 N  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 N  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 N  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 N  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 N  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 N  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 N  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 N  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 N  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 N  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 N  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 N  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 N  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 N  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 N  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 N  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 N  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 N  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 N  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 N  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 N  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 O  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 O  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 O  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 O  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 O  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 O  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 O  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 O  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 O  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 O  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 O  132  THR TYR                                                      
SEQRES   1 P  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 P  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 P  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 P  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 P  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 P  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 P  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 P  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 P  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 P  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 P  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 P  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 P  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 P  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 P  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 P  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 P  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 P  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 P  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 P  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 P  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 P  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 P  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 P  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 P  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 P  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 P  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 P  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 P  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 P  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 P  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 P  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 P  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 P  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 P  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 P  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 Q  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 Q  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 Q  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 Q  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 Q  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 Q  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 Q  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 Q  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 Q  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 Q  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 Q  132  THR TYR                                                      
SEQRES   1 R  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 R  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 R  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 R  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 R  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 R  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 R  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 R  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 R  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 R  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 R  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 R  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 R  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 R  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 R  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 R  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 R  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 R  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 R  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 R  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 R  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 R  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 R  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 R  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 R  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 R  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 R  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 R  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 R  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 R  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 R  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 R  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 R  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 R  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 R  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 R  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 S  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 S  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 S  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 S  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 S  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 S  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 S  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 S  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 S  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 S  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 S  132  THR TYR                                                      
SEQRES   1 T  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 T  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 T  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 T  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 T  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 T  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 T  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 T  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 T  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 T  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 T  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 T  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 T  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 T  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 T  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 T  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 T  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 T  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 T  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 T  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 T  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 T  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 T  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 T  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 T  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 T  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 T  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 T  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 T  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 T  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 T  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 T  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 T  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 T  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 T  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 T  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 U  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 U  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 U  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 U  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 U  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 U  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 U  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 U  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 U  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 U  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 U  132  THR TYR                                                      
SEQRES   1 V  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 V  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 V  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 V  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 V  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 V  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 V  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 V  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 V  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 V  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 V  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 V  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 V  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 V  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 V  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 V  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 V  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 V  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 V  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 V  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 V  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 V  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 V  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 V  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 V  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 V  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 V  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 V  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 V  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 V  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 V  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 V  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 V  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 V  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 V  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 V  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 W  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 W  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 W  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 W  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 W  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 W  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 W  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 W  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 W  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 W  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 W  132  THR TYR                                                      
SEQRES   1 X  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 X  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 X  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 X  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 X  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 X  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 X  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 X  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 X  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 X  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 X  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 X  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 X  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 X  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 X  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 X  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 X  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 X  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 X  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 X  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 X  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 X  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 X  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 X  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 X  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 X  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 X  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 X  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 X  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 X  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 X  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 X  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 X  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 X  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 X  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 X  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 Y  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 Y  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 Y  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 Y  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 Y  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 Y  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 Y  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 Y  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 Y  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 Y  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 Y  132  THR TYR                                                      
SEQRES   1 Z  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 Z  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 Z  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 Z  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 Z  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 Z  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 Z  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 Z  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 Z  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 Z  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 Z  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 Z  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 Z  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 Z  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 Z  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 Z  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 Z  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 Z  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 Z  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 Z  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 Z  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 Z  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 Z  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 Z  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 Z  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 Z  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 Z  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 Z  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 Z  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 Z  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 Z  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 Z  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 Z  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 Z  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 Z  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 Z  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 a  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 a  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 a  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 a  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 a  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 a  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 a  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 a  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 a  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 a  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 a  132  THR TYR                                                      
SEQRES   1 b  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 b  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 b  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 b  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 b  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 b  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 b  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 b  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 b  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 b  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 b  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 b  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 b  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 b  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 b  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 b  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 b  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 b  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 b  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 b  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 b  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 b  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 b  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 b  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 b  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 b  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 b  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 b  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 b  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 b  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 b  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 b  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 b  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 b  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 b  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 b  461  PRO SER ALA LYS GLU ALA                                      
SEQRES   1 c  132  THR THR SER SER GLN LYS PHE ILE ALA ARG ASN ARG ALA          
SEQRES   2 c  132  PRO ARG VAL GLN ILE GLU TYR ASP VAL GLU LEU TYR GLY          
SEQRES   3 c  132  ALA GLU LYS LYS VAL GLN LEU PRO PHE VAL MET GLY VAL          
SEQRES   4 c  132  MET ALA ASP LEU ALA GLY LYS PRO ALA GLU PRO GLN ALA          
SEQRES   5 c  132  ALA VAL ALA ASP ARG LYS PHE LEU GLU ILE ASP VAL ASP          
SEQRES   6 c  132  ASN PHE ASP ALA ARG LEU LYS ALA MET LYS PRO ARG VAL          
SEQRES   7 c  132  ALA PHE ASN VAL PRO ASN VAL LEU THR GLY GLU GLY ASN          
SEQRES   8 c  132  LEU SER LEU ASP ILE THR PHE GLU SER MET ASP ASP PHE          
SEQRES   9 c  132  SER PRO ALA ALA VAL ALA ARG LYS VAL ASP SER LEU ASN          
SEQRES  10 c  132  LYS LEU LEU GLU ALA ARG THR GLN LEU ALA ASN LEU LEU          
SEQRES  11 c  132  THR TYR                                                      
SEQRES   1 d  461  ARG GLU ALA VAL GLU THR ALA VAL ARG THR LEU ALA GLU          
SEQRES   2 d  461  HIS ALA LEU GLU GLN THR SER LEU ILE SER ASN ASP ALA          
SEQRES   3 d  461  ILE LYS SER ILE GLU SER ILE ILE ALA ALA LEU ASP ALA          
SEQRES   4 d  461  LYS LEU THR ALA GLN VAL ASN LEU ILE MET HIS HIS ALA          
SEQRES   5 d  461  ASP PHE GLN GLN LEU GLU SER ALA TRP ARG GLY LEU HIS          
SEQRES   6 d  461  TYR LEU VAL ASN ASN THR GLU THR ASP GLU GLN LEU LYS          
SEQRES   7 d  461  ILE ARG VAL LEU ASN ILE SER LYS PRO GLU LEU HIS LYS          
SEQRES   8 d  461  THR LEU LYS LYS PHE LYS GLY THR THR TRP ASP GLN SER          
SEQRES   9 d  461  PRO ILE PHE LYS LYS LEU TYR GLU GLU GLU TYR GLY GLN          
SEQRES  10 d  461  PHE GLY GLY GLU PRO TYR GLY CYS LEU VAL GLY ASP TYR          
SEQRES  11 d  461  TYR PHE ASP GLN SER PRO PRO ASP VAL GLU LEU LEU GLY          
SEQRES  12 d  461  GLU MET ALA LYS ILE SER ALA ALA MET HIS ALA PRO PHE          
SEQRES  13 d  461  ILE SER ALA ALA SER PRO THR VAL MET GLY MET GLY SER          
SEQRES  14 d  461  TRP GLN GLU LEU SER ASN PRO ARG ASP LEU THR LYS ILE          
SEQRES  15 d  461  PHE THR THR PRO GLU TYR ALA GLY TRP ARG SER LEU ARG          
SEQRES  16 d  461  GLU SER GLU ASP SER ARG TYR ILE GLY LEU THR MET PRO          
SEQRES  17 d  461  ARG PHE LEU ALA ARG LEU PRO TYR GLY ALA LYS THR ASP          
SEQRES  18 d  461  PRO VAL GLU GLU PHE ALA PHE GLU GLU GLU THR ASP GLY          
SEQRES  19 d  461  ALA ASP SER SER LYS TYR ALA TRP ALA ASN SER ALA TYR          
SEQRES  20 d  461  ALA MET ALA VAL ASN ILE ASN ARG SER PHE LYS LEU TYR          
SEQRES  21 d  461  GLY TRP CYS SER ARG ILE ARG GLY VAL GLU SER GLY GLY          
SEQRES  22 d  461  GLU VAL GLN GLY LEU PRO ALA HIS THR PHE PRO THR ASP          
SEQRES  23 d  461  ASP GLY GLY VAL ASP MET LYS CYS PRO THR GLU ILE ALA          
SEQRES  24 d  461  ILE SER ASP ARG ARG GLU ALA GLU LEU ALA LYS ASN GLY          
SEQRES  25 d  461  PHE MET PRO LEU LEU HIS LYS LYS ASN THR ASP PHE ALA          
SEQRES  26 d  461  ALA PHE ILE GLY ALA GLN SER LEU GLN LYS PRO ALA GLU          
SEQRES  27 d  461  TYR ASP ASP PRO ASP ALA THR ALA ASN ALA ASN LEU ALA          
SEQRES  28 d  461  ALA ARG LEU PRO TYR LEU PHE ALA THR CYS ARG PHE ALA          
SEQRES  29 d  461  HIS TYR LEU LYS CYS ILE VAL ARG ASP LYS ILE GLY SER          
SEQRES  30 d  461  PHE LYS GLU LYS ASP GLU MET GLN ARG TRP LEU GLN ASP          
SEQRES  31 d  461  TRP ILE LEU ASN TYR VAL ASP GLY ASP PRO ALA HIS SER          
SEQRES  32 d  461  THR GLU THR THR LYS ALA GLN HIS PRO LEU ALA ALA ALA          
SEQRES  33 d  461  GLU VAL VAL VAL GLU GLU VAL GLU GLY ASN PRO GLY TYR          
SEQRES  34 d  461  TYR ASN SER LYS PHE PHE LEU ARG PRO HIS TYR GLN LEU          
SEQRES  35 d  461  GLU GLY LEU THR VAL SER LEU ARG LEU VAL SER LYS LEU          
SEQRES  36 d  461  PRO SER ALA LYS GLU ALA                                      
HELIX    1 AA1 SER A    6  ARG A   15  1                                  10    
HELIX    2 AA2 ASN A   69  LYS A   78  1                                  10    
HELIX    3 AA3 SER A  103  PHE A  107  5                                   5    
HELIX    4 AA4 SER A  108  VAL A  116  1                                   9    
HELIX    5 AA5 VAL A  116  THR A  134  1                                  19    
HELIX    6 AA6 GLU B   39  GLN B   55  1                                  17    
HELIX    7 AA7 LYS B   65  GLU B   68  5                                   4    
HELIX    8 AA8 SER B   69  HIS B   87  1                                  19    
HELIX    9 AA9 HIS B   88  ASN B  107  1                                  20    
HELIX   10 AB1 SER B  122  PHE B  133  1                                  12    
HELIX   11 AB2 LYS B  134  GLN B  140  5                                   7    
HELIX   12 AB3 SER B  141  GLU B  149  1                                   9    
HELIX   13 AB4 SER B  172  MET B  189  1                                  18    
HELIX   14 AB5 LYS B  218  GLU B  224  5                                   7    
HELIX   15 AB6 TYR B  225  GLU B  233  1                                   9    
HELIX   16 AB7 ASP B  236  ARG B  238  5                                   3    
HELIX   17 AB8 SER B  282  GLY B  298  1                                  17    
HELIX   18 AB9 SER B  338  ASN B  348  1                                  11    
HELIX   19 AC1 ASP B  378  ALA B  388  1                                  11    
HELIX   20 AC2 ARG B  390  ILE B  412  1                                  23    
HELIX   21 AC3 GLU B  417  LEU B  430  1                                  14    
HELIX   22 AC4 THR B  443  HIS B  448  1                                   6    
HELIX   23 AC5 SER C    6  ARG C   15  1                                  10    
HELIX   24 AC6 ASN C   69  LYS C   78  1                                  10    
HELIX   25 AC7 SER C  103  PHE C  107  5                                   5    
HELIX   26 AC8 SER C  108  VAL C  116  1                                   9    
HELIX   27 AC9 VAL C  116  THR C  134  1                                  19    
HELIX   28 AD1 GLU D   39  GLN D   55  1                                  17    
HELIX   29 AD2 LYS D   65  GLU D   68  5                                   4    
HELIX   30 AD3 SER D   69  HIS D   87  1                                  19    
HELIX   31 AD4 HIS D   88  ASN D  107  1                                  20    
HELIX   32 AD5 SER D  122  PHE D  133  1                                  12    
HELIX   33 AD6 LYS D  134  GLN D  140  5                                   7    
HELIX   34 AD7 SER D  141  GLU D  149  1                                   9    
HELIX   35 AD8 SER D  172  MET D  189  1                                  18    
HELIX   36 AD9 LYS D  218  GLU D  224  5                                   7    
HELIX   37 AE1 TYR D  225  GLU D  233  1                                   9    
HELIX   38 AE2 ASP D  236  ARG D  238  5                                   3    
HELIX   39 AE3 SER D  282  GLY D  298  1                                  17    
HELIX   40 AE4 SER D  338  ASN D  348  1                                  11    
HELIX   41 AE5 ASP D  378  ALA D  388  1                                  11    
HELIX   42 AE6 ARG D  390  ILE D  412  1                                  23    
HELIX   43 AE7 GLU D  417  LEU D  430  1                                  14    
HELIX   44 AE8 THR D  443  HIS D  448  1                                   6    
HELIX   45 AE9 SER E    6  ARG E   15  1                                  10    
HELIX   46 AF1 ASN E   69  LYS E   78  1                                  10    
HELIX   47 AF2 SER E  103  PHE E  107  5                                   5    
HELIX   48 AF3 SER E  108  VAL E  116  1                                   9    
HELIX   49 AF4 VAL E  116  THR E  134  1                                  19    
HELIX   50 AF5 GLU F   39  GLN F   55  1                                  17    
HELIX   51 AF6 LYS F   65  GLU F   68  5                                   4    
HELIX   52 AF7 SER F   69  HIS F   87  1                                  19    
HELIX   53 AF8 HIS F   88  ASN F  107  1                                  20    
HELIX   54 AF9 SER F  122  PHE F  133  1                                  12    
HELIX   55 AG1 LYS F  134  GLN F  140  5                                   7    
HELIX   56 AG2 SER F  141  GLU F  149  1                                   9    
HELIX   57 AG3 SER F  172  MET F  189  1                                  18    
HELIX   58 AG4 LYS F  218  GLU F  224  5                                   7    
HELIX   59 AG5 TYR F  225  GLU F  233  1                                   9    
HELIX   60 AG6 ASP F  236  ARG F  238  5                                   3    
HELIX   61 AG7 SER F  282  GLY F  298  1                                  17    
HELIX   62 AG8 SER F  338  ASN F  348  1                                  11    
HELIX   63 AG9 ASP F  378  ALA F  388  1                                  11    
HELIX   64 AH1 ARG F  390  ILE F  412  1                                  23    
HELIX   65 AH2 GLU F  417  LEU F  430  1                                  14    
HELIX   66 AH3 THR F  443  HIS F  448  1                                   6    
HELIX   67 AH4 SER G    6  ARG G   15  1                                  10    
HELIX   68 AH5 ASN G   69  LYS G   78  1                                  10    
HELIX   69 AH6 SER G  103  PHE G  107  5                                   5    
HELIX   70 AH7 SER G  108  VAL G  116  1                                   9    
HELIX   71 AH8 VAL G  116  THR G  134  1                                  19    
HELIX   72 AH9 GLU H   39  GLN H   55  1                                  17    
HELIX   73 AI1 LYS H   65  GLU H   68  5                                   4    
HELIX   74 AI2 SER H   69  HIS H   87  1                                  19    
HELIX   75 AI3 HIS H   88  ASN H  107  1                                  20    
HELIX   76 AI4 SER H  122  PHE H  133  1                                  12    
HELIX   77 AI5 LYS H  134  GLN H  140  5                                   7    
HELIX   78 AI6 SER H  141  GLU H  149  1                                   9    
HELIX   79 AI7 SER H  172  MET H  189  1                                  18    
HELIX   80 AI8 LYS H  218  GLU H  224  5                                   7    
HELIX   81 AI9 TYR H  225  GLU H  233  1                                   9    
HELIX   82 AJ1 ASP H  236  ARG H  238  5                                   3    
HELIX   83 AJ2 SER H  282  GLY H  298  1                                  17    
HELIX   84 AJ3 SER H  338  ASN H  348  1                                  11    
HELIX   85 AJ4 ASP H  378  ALA H  388  1                                  11    
HELIX   86 AJ5 ARG H  390  ILE H  412  1                                  23    
HELIX   87 AJ6 GLU H  417  LEU H  430  1                                  14    
HELIX   88 AJ7 THR H  443  HIS H  448  1                                   6    
HELIX   89 AJ8 SER I    6  ARG I   15  1                                  10    
HELIX   90 AJ9 ASN I   69  LYS I   78  1                                  10    
HELIX   91 AK1 SER I  103  PHE I  107  5                                   5    
HELIX   92 AK2 SER I  108  VAL I  116  1                                   9    
HELIX   93 AK3 VAL I  116  THR I  134  1                                  19    
HELIX   94 AK4 GLU J   39  GLN J   55  1                                  17    
HELIX   95 AK5 LYS J   65  GLU J   68  5                                   4    
HELIX   96 AK6 SER J   69  HIS J   87  1                                  19    
HELIX   97 AK7 HIS J   88  ASN J  107  1                                  20    
HELIX   98 AK8 SER J  122  PHE J  133  1                                  12    
HELIX   99 AK9 LYS J  134  GLN J  140  5                                   7    
HELIX  100 AL1 SER J  141  GLU J  149  1                                   9    
HELIX  101 AL2 SER J  172  MET J  189  1                                  18    
HELIX  102 AL3 LYS J  218  GLU J  224  5                                   7    
HELIX  103 AL4 TYR J  225  GLU J  233  1                                   9    
HELIX  104 AL5 ASP J  236  ARG J  238  5                                   3    
HELIX  105 AL6 SER J  282  GLY J  298  1                                  17    
HELIX  106 AL7 SER J  338  ASN J  348  1                                  11    
HELIX  107 AL8 ASP J  378  ALA J  388  1                                  11    
HELIX  108 AL9 ARG J  390  ILE J  412  1                                  23    
HELIX  109 AM1 GLU J  417  LEU J  430  1                                  14    
HELIX  110 AM2 THR J  443  HIS J  448  1                                   6    
HELIX  111 AM3 SER K    6  ARG K   15  1                                  10    
HELIX  112 AM4 ASN K   69  LYS K   78  1                                  10    
HELIX  113 AM5 SER K  103  PHE K  107  5                                   5    
HELIX  114 AM6 SER K  108  VAL K  116  1                                   9    
HELIX  115 AM7 VAL K  116  THR K  134  1                                  19    
HELIX  116 AM8 GLU L   39  GLN L   55  1                                  17    
HELIX  117 AM9 LYS L   65  GLU L   68  5                                   4    
HELIX  118 AN1 SER L   69  HIS L   87  1                                  19    
HELIX  119 AN2 HIS L   88  ASN L  107  1                                  20    
HELIX  120 AN3 SER L  122  PHE L  133  1                                  12    
HELIX  121 AN4 LYS L  134  GLN L  140  5                                   7    
HELIX  122 AN5 SER L  141  GLU L  149  1                                   9    
HELIX  123 AN6 SER L  172  MET L  189  1                                  18    
HELIX  124 AN7 LYS L  218  GLU L  224  5                                   7    
HELIX  125 AN8 TYR L  225  GLU L  233  1                                   9    
HELIX  126 AN9 ASP L  236  ARG L  238  5                                   3    
HELIX  127 AO1 SER L  282  GLY L  298  1                                  17    
HELIX  128 AO2 SER L  338  ASN L  348  1                                  11    
HELIX  129 AO3 ASP L  378  ALA L  388  1                                  11    
HELIX  130 AO4 ARG L  390  ILE L  412  1                                  23    
HELIX  131 AO5 GLU L  417  LEU L  430  1                                  14    
HELIX  132 AO6 THR L  443  HIS L  448  1                                   6    
HELIX  133 AO7 SER M    6  ARG M   15  1                                  10    
HELIX  134 AO8 ASN M   69  LYS M   78  1                                  10    
HELIX  135 AO9 SER M  103  PHE M  107  5                                   5    
HELIX  136 AP1 SER M  108  VAL M  116  1                                   9    
HELIX  137 AP2 VAL M  116  THR M  134  1                                  19    
HELIX  138 AP3 GLU N   39  GLN N   55  1                                  17    
HELIX  139 AP4 LYS N   65  GLU N   68  5                                   4    
HELIX  140 AP5 SER N   69  HIS N   87  1                                  19    
HELIX  141 AP6 HIS N   88  ASN N  107  1                                  20    
HELIX  142 AP7 SER N  122  PHE N  133  1                                  12    
HELIX  143 AP8 LYS N  134  GLN N  140  5                                   7    
HELIX  144 AP9 SER N  141  GLU N  149  1                                   9    
HELIX  145 AQ1 SER N  172  MET N  189  1                                  18    
HELIX  146 AQ2 LYS N  218  GLU N  224  5                                   7    
HELIX  147 AQ3 TYR N  225  GLU N  233  1                                   9    
HELIX  148 AQ4 ASP N  236  ARG N  238  5                                   3    
HELIX  149 AQ5 SER N  282  GLY N  298  1                                  17    
HELIX  150 AQ6 SER N  338  ASN N  348  1                                  11    
HELIX  151 AQ7 ASP N  378  ALA N  388  1                                  11    
HELIX  152 AQ8 ARG N  390  ILE N  412  1                                  23    
HELIX  153 AQ9 GLU N  417  LEU N  430  1                                  14    
HELIX  154 AR1 THR N  443  HIS N  448  1                                   6    
HELIX  155 AR2 SER O    6  ARG O   15  1                                  10    
HELIX  156 AR3 ASN O   69  LYS O   78  1                                  10    
HELIX  157 AR4 SER O  103  PHE O  107  5                                   5    
HELIX  158 AR5 SER O  108  VAL O  116  1                                   9    
HELIX  159 AR6 VAL O  116  THR O  134  1                                  19    
HELIX  160 AR7 GLU P   39  GLN P   55  1                                  17    
HELIX  161 AR8 LYS P   65  GLU P   68  5                                   4    
HELIX  162 AR9 SER P   69  HIS P   87  1                                  19    
HELIX  163 AS1 HIS P   88  ASN P  107  1                                  20    
HELIX  164 AS2 SER P  122  PHE P  133  1                                  12    
HELIX  165 AS3 LYS P  134  GLN P  140  5                                   7    
HELIX  166 AS4 SER P  141  GLU P  149  1                                   9    
HELIX  167 AS5 SER P  172  MET P  189  1                                  18    
HELIX  168 AS6 LYS P  218  GLU P  224  5                                   7    
HELIX  169 AS7 TYR P  225  GLU P  233  1                                   9    
HELIX  170 AS8 ASP P  236  ARG P  238  5                                   3    
HELIX  171 AS9 SER P  282  GLY P  298  1                                  17    
HELIX  172 AT1 SER P  338  ASN P  348  1                                  11    
HELIX  173 AT2 ASP P  378  ALA P  388  1                                  11    
HELIX  174 AT3 ARG P  390  ILE P  412  1                                  23    
HELIX  175 AT4 GLU P  417  LEU P  430  1                                  14    
HELIX  176 AT5 THR P  443  HIS P  448  1                                   6    
HELIX  177 AT6 SER Q    6  ARG Q   15  1                                  10    
HELIX  178 AT7 ASN Q   69  LYS Q   78  1                                  10    
HELIX  179 AT8 SER Q  103  PHE Q  107  5                                   5    
HELIX  180 AT9 SER Q  108  VAL Q  116  1                                   9    
HELIX  181 AU1 VAL Q  116  THR Q  134  1                                  19    
HELIX  182 AU2 GLU R   39  GLN R   55  1                                  17    
HELIX  183 AU3 LYS R   65  GLU R   68  5                                   4    
HELIX  184 AU4 SER R   69  HIS R   87  1                                  19    
HELIX  185 AU5 HIS R   88  ASN R  107  1                                  20    
HELIX  186 AU6 SER R  122  PHE R  133  1                                  12    
HELIX  187 AU7 LYS R  134  GLN R  140  5                                   7    
HELIX  188 AU8 SER R  141  GLU R  149  1                                   9    
HELIX  189 AU9 SER R  172  MET R  189  1                                  18    
HELIX  190 AV1 LYS R  218  GLU R  224  5                                   7    
HELIX  191 AV2 TYR R  225  GLU R  233  1                                   9    
HELIX  192 AV3 ASP R  236  ARG R  238  5                                   3    
HELIX  193 AV4 SER R  282  GLY R  298  1                                  17    
HELIX  194 AV5 SER R  338  ASN R  348  1                                  11    
HELIX  195 AV6 ASP R  378  ALA R  388  1                                  11    
HELIX  196 AV7 ARG R  390  ILE R  412  1                                  23    
HELIX  197 AV8 GLU R  417  LEU R  430  1                                  14    
HELIX  198 AV9 THR R  443  HIS R  448  1                                   6    
HELIX  199 AW1 SER S    6  ARG S   15  1                                  10    
HELIX  200 AW2 ASN S   69  LYS S   78  1                                  10    
HELIX  201 AW3 SER S  103  PHE S  107  5                                   5    
HELIX  202 AW4 SER S  108  VAL S  116  1                                   9    
HELIX  203 AW5 VAL S  116  THR S  134  1                                  19    
HELIX  204 AW6 GLU T   39  GLN T   55  1                                  17    
HELIX  205 AW7 LYS T   65  GLU T   68  5                                   4    
HELIX  206 AW8 SER T   69  HIS T   87  1                                  19    
HELIX  207 AW9 HIS T   88  ASN T  107  1                                  20    
HELIX  208 AX1 SER T  122  PHE T  133  1                                  12    
HELIX  209 AX2 LYS T  134  GLN T  140  5                                   7    
HELIX  210 AX3 SER T  141  GLU T  149  1                                   9    
HELIX  211 AX4 SER T  172  MET T  189  1                                  18    
HELIX  212 AX5 LYS T  218  GLU T  224  5                                   7    
HELIX  213 AX6 TYR T  225  GLU T  233  1                                   9    
HELIX  214 AX7 ASP T  236  ARG T  238  5                                   3    
HELIX  215 AX8 SER T  282  GLY T  298  1                                  17    
HELIX  216 AX9 SER T  338  ASN T  348  1                                  11    
HELIX  217 AY1 ASP T  378  ALA T  388  1                                  11    
HELIX  218 AY2 ARG T  390  ILE T  412  1                                  23    
HELIX  219 AY3 GLU T  417  LEU T  430  1                                  14    
HELIX  220 AY4 THR T  443  HIS T  448  1                                   6    
HELIX  221 AY5 SER U    6  ARG U   15  1                                  10    
HELIX  222 AY6 ASN U   69  LYS U   78  1                                  10    
HELIX  223 AY7 SER U  103  PHE U  107  5                                   5    
HELIX  224 AY8 SER U  108  VAL U  116  1                                   9    
HELIX  225 AY9 VAL U  116  THR U  134  1                                  19    
HELIX  226 AZ1 GLU V   39  GLN V   55  1                                  17    
HELIX  227 AZ2 LYS V   65  GLU V   68  5                                   4    
HELIX  228 AZ3 SER V   69  HIS V   87  1                                  19    
HELIX  229 AZ4 HIS V   88  ASN V  107  1                                  20    
HELIX  230 AZ5 SER V  122  PHE V  133  1                                  12    
HELIX  231 AZ6 LYS V  134  GLN V  140  5                                   7    
HELIX  232 AZ7 SER V  141  GLU V  149  1                                   9    
HELIX  233 AZ8 SER V  172  MET V  189  1                                  18    
HELIX  234 AZ9 LYS V  218  GLU V  224  5                                   7    
HELIX  235 BA1 TYR V  225  GLU V  233  1                                   9    
HELIX  236 BA2 ASP V  236  ARG V  238  5                                   3    
HELIX  237 BA3 SER V  282  GLY V  298  1                                  17    
HELIX  238 BA4 SER V  338  ASN V  348  1                                  11    
HELIX  239 BA5 ASP V  378  ALA V  388  1                                  11    
HELIX  240 BA6 ARG V  390  ILE V  412  1                                  23    
HELIX  241 BA7 GLU V  417  LEU V  430  1                                  14    
HELIX  242 BA8 THR V  443  HIS V  448  1                                   6    
HELIX  243 BA9 SER W    6  ARG W   15  1                                  10    
HELIX  244 BB1 ASN W   69  LYS W   78  1                                  10    
HELIX  245 BB2 SER W  103  PHE W  107  5                                   5    
HELIX  246 BB3 SER W  108  VAL W  116  1                                   9    
HELIX  247 BB4 VAL W  116  THR W  134  1                                  19    
HELIX  248 BB5 GLU X   39  GLN X   55  1                                  17    
HELIX  249 BB6 LYS X   65  GLU X   68  5                                   4    
HELIX  250 BB7 SER X   69  HIS X   87  1                                  19    
HELIX  251 BB8 HIS X   88  ASN X  107  1                                  20    
HELIX  252 BB9 SER X  122  PHE X  133  1                                  12    
HELIX  253 BC1 LYS X  134  GLN X  140  5                                   7    
HELIX  254 BC2 SER X  141  GLU X  149  1                                   9    
HELIX  255 BC3 SER X  172  MET X  189  1                                  18    
HELIX  256 BC4 LYS X  218  GLU X  224  5                                   7    
HELIX  257 BC5 TYR X  225  GLU X  233  1                                   9    
HELIX  258 BC6 ASP X  236  ARG X  238  5                                   3    
HELIX  259 BC7 SER X  282  GLY X  298  1                                  17    
HELIX  260 BC8 SER X  338  ASN X  348  1                                  11    
HELIX  261 BC9 ASP X  378  ALA X  388  1                                  11    
HELIX  262 BD1 ARG X  390  ILE X  412  1                                  23    
HELIX  263 BD2 GLU X  417  LEU X  430  1                                  14    
HELIX  264 BD3 THR X  443  HIS X  448  1                                   6    
HELIX  265 BD4 SER Y    6  ARG Y   15  1                                  10    
HELIX  266 BD5 ASN Y   69  LYS Y   78  1                                  10    
HELIX  267 BD6 SER Y  103  PHE Y  107  5                                   5    
HELIX  268 BD7 SER Y  108  VAL Y  116  1                                   9    
HELIX  269 BD8 VAL Y  116  THR Y  134  1                                  19    
HELIX  270 BD9 GLU Z   39  GLN Z   55  1                                  17    
HELIX  271 BE1 LYS Z   65  GLU Z   68  5                                   4    
HELIX  272 BE2 SER Z   69  HIS Z   87  1                                  19    
HELIX  273 BE3 HIS Z   88  ASN Z  107  1                                  20    
HELIX  274 BE4 SER Z  122  PHE Z  133  1                                  12    
HELIX  275 BE5 LYS Z  134  GLN Z  140  5                                   7    
HELIX  276 BE6 SER Z  141  GLU Z  149  1                                   9    
HELIX  277 BE7 SER Z  172  MET Z  189  1                                  18    
HELIX  278 BE8 LYS Z  218  GLU Z  224  5                                   7    
HELIX  279 BE9 TYR Z  225  GLU Z  233  1                                   9    
HELIX  280 BF1 ASP Z  236  ARG Z  238  5                                   3    
HELIX  281 BF2 SER Z  282  GLY Z  298  1                                  17    
HELIX  282 BF3 SER Z  338  ASN Z  348  1                                  11    
HELIX  283 BF4 ASP Z  378  ALA Z  388  1                                  11    
HELIX  284 BF5 ARG Z  390  ILE Z  412  1                                  23    
HELIX  285 BF6 GLU Z  417  LEU Z  430  1                                  14    
HELIX  286 BF7 THR Z  443  HIS Z  448  1                                   6    
HELIX  287 BF8 SER a    6  ARG a   15  1                                  10    
HELIX  288 BF9 ASN a   69  LYS a   78  1                                  10    
HELIX  289 BG1 SER a  103  PHE a  107  5                                   5    
HELIX  290 BG2 SER a  108  VAL a  116  1                                   9    
HELIX  291 BG3 VAL a  116  THR a  134  1                                  19    
HELIX  292 BG4 GLU b   39  GLN b   55  1                                  17    
HELIX  293 BG5 LYS b   65  GLU b   68  5                                   4    
HELIX  294 BG6 SER b   69  HIS b   87  1                                  19    
HELIX  295 BG7 HIS b   88  ASN b  107  1                                  20    
HELIX  296 BG8 SER b  122  PHE b  133  1                                  12    
HELIX  297 BG9 LYS b  134  GLN b  140  5                                   7    
HELIX  298 BH1 SER b  141  GLU b  149  1                                   9    
HELIX  299 BH2 SER b  172  MET b  189  1                                  18    
HELIX  300 BH3 LYS b  218  GLU b  224  5                                   7    
HELIX  301 BH4 TYR b  225  GLU b  233  1                                   9    
HELIX  302 BH5 ASP b  236  ARG b  238  5                                   3    
HELIX  303 BH6 SER b  282  GLY b  298  1                                  17    
HELIX  304 BH7 SER b  338  ASN b  348  1                                  11    
HELIX  305 BH8 ASP b  378  ALA b  388  1                                  11    
HELIX  306 BH9 ARG b  390  ILE b  412  1                                  23    
HELIX  307 BI1 GLU b  417  LEU b  430  1                                  14    
HELIX  308 BI2 THR b  443  HIS b  448  1                                   6    
HELIX  309 BI3 SER c    6  ARG c   15  1                                  10    
HELIX  310 BI4 ASN c   69  LYS c   78  1                                  10    
HELIX  311 BI5 SER c  103  PHE c  107  5                                   5    
HELIX  312 BI6 SER c  108  VAL c  116  1                                   9    
HELIX  313 BI7 VAL c  116  THR c  134  1                                  19    
HELIX  314 BI8 GLU d   39  GLN d   55  1                                  17    
HELIX  315 BI9 LYS d   65  GLU d   68  5                                   4    
HELIX  316 BJ1 SER d   69  HIS d   87  1                                  19    
HELIX  317 BJ2 HIS d   88  ASN d  107  1                                  20    
HELIX  318 BJ3 SER d  122  PHE d  133  1                                  12    
HELIX  319 BJ4 LYS d  134  GLN d  140  5                                   7    
HELIX  320 BJ5 SER d  141  GLU d  149  1                                   9    
HELIX  321 BJ6 SER d  172  MET d  189  1                                  18    
HELIX  322 BJ7 LYS d  218  GLU d  224  5                                   7    
HELIX  323 BJ8 TYR d  225  GLU d  233  1                                   9    
HELIX  324 BJ9 ASP d  236  ARG d  238  5                                   3    
HELIX  325 BK1 SER d  282  GLY d  298  1                                  17    
HELIX  326 BK2 SER d  338  ASN d  348  1                                  11    
HELIX  327 BK3 ASP d  378  ALA d  388  1                                  11    
HELIX  328 BK4 ARG d  390  ILE d  412  1                                  23    
HELIX  329 BK5 GLU d  417  LEU d  430  1                                  14    
HELIX  330 BK6 THR d  443  HIS d  448  1                                   6    
SHEET    1 AA1 4 VAL A  19  TYR A  23  0                                        
SHEET    2 AA1 4 GLY D 481  LEU D 488  1  O  VAL D 484   N  GLN A  20           
SHEET    3 AA1 4 TYR P 466  PRO P 475  1  O  PHE P 471   N  ARG D 487           
SHEET    4 AA1 4 LEU P 450  GLU P 459 -1  N  GLU P 458   O  ASN P 468           
SHEET    1 AA2 6 LEU A  63  ILE A  65  0                                        
SHEET    2 AA2 6 LEU B 114  ASN B 120 -1  O  ILE B 116   N  ILE A  65           
SHEET    3 AA2 6 PHE A  38  ALA A  44  1  N  VAL A  42   O  ARG B 117           
SHEET    4 AA2 6 CYS B 162  PHE B 169  1  O  VAL B 164   N  MET A  43           
SHEET    5 AA2 6 PHE B 193  ALA B 197  1  O  ILE B 194   N  GLY B 165           
SHEET    6 AA2 6 ILE B 240  LEU B 242  1  O  GLY B 241   N  PHE B 193           
SHEET    1 AA3 2 ARG A  80  PRO A  86  0                                        
SHEET    2 AA3 2 ASN A  94  THR A 100 -1  O  LEU A  95   N  VAL A  85           
SHEET    1 AA4 3 GLU B 311  VAL B 312  0                                        
SHEET    2 AA4 3 ALA B 362  PHE B 364 -1  O  ALA B 362   N  VAL B 312           
SHEET    3 AA4 3 LEU B 353  HIS B 355 -1  N  LEU B 354   O  ALA B 363           
SHEET    1 AA5 2 HIS B 318  PHE B 320  0                                        
SHEET    2 AA5 2 ASP B 328  LYS B 330 -1  O  LYS B 330   N  HIS B 318           
SHEET    1 AA6 2 LEU B 450  GLU B 459  0                                        
SHEET    2 AA6 2 TYR B 467  PRO B 475 -1  O  ASN B 468   N  GLU B 458           
SHEET    1 AA7 3 GLY B 481  LEU B 488  0                                        
SHEET    2 AA7 3 TYR N 466  PRO N 475  1  O  PHE N 471   N  ARG B 487           
SHEET    3 AA7 3 LEU N 450  GLU N 459 -1  N  GLU N 458   O  ASN N 468           
SHEET    1 AA8 4 VAL C  19  TYR C  23  0                                        
SHEET    2 AA8 4 GLY F 481  LEU F 488  1  O  VAL F 484   N  GLN C  20           
SHEET    3 AA8 4 TYR R 466  PRO R 475  1  O  PHE R 471   N  ARG F 487           
SHEET    4 AA8 4 LEU R 450  GLU R 459 -1  N  GLU R 458   O  ASN R 468           
SHEET    1 AA9 6 LEU C  63  ILE C  65  0                                        
SHEET    2 AA9 6 LEU D 114  ASN D 120 -1  O  ILE D 116   N  ILE C  65           
SHEET    3 AA9 6 PHE C  38  ALA C  44  1  N  VAL C  42   O  ARG D 117           
SHEET    4 AA9 6 CYS D 162  PHE D 169  1  O  VAL D 164   N  MET C  43           
SHEET    5 AA9 6 PHE D 193  ALA D 197  1  O  ILE D 194   N  GLY D 165           
SHEET    6 AA9 6 ILE D 240  LEU D 242  1  O  GLY D 241   N  PHE D 193           
SHEET    1 AB1 2 ARG C  80  PRO C  86  0                                        
SHEET    2 AB1 2 ASN C  94  THR C 100 -1  O  LEU C  95   N  VAL C  85           
SHEET    1 AB2 3 GLU D 311  VAL D 312  0                                        
SHEET    2 AB2 3 ALA D 362  PHE D 364 -1  O  ALA D 362   N  VAL D 312           
SHEET    3 AB2 3 LEU D 353  HIS D 355 -1  N  LEU D 354   O  ALA D 363           
SHEET    1 AB3 2 HIS D 318  PHE D 320  0                                        
SHEET    2 AB3 2 ASP D 328  LYS D 330 -1  O  LYS D 330   N  HIS D 318           
SHEET    1 AB4 2 LEU D 450  GLU D 459  0                                        
SHEET    2 AB4 2 TYR D 467  PRO D 475 -1  O  ASN D 468   N  GLU D 458           
SHEET    1 AB5 4 VAL E  19  TYR E  23  0                                        
SHEET    2 AB5 4 GLY H 481  LEU H 488  1  O  VAL H 484   N  GLN E  20           
SHEET    3 AB5 4 TYR T 466  PRO T 475  1  O  PHE T 471   N  ARG H 487           
SHEET    4 AB5 4 LEU T 450  GLU T 459 -1  N  GLU T 458   O  ASN T 468           
SHEET    1 AB6 6 LEU E  63  ILE E  65  0                                        
SHEET    2 AB6 6 LEU F 114  ASN F 120 -1  O  ILE F 116   N  ILE E  65           
SHEET    3 AB6 6 PHE E  38  ALA E  44  1  N  VAL E  42   O  ARG F 117           
SHEET    4 AB6 6 CYS F 162  PHE F 169  1  O  VAL F 164   N  MET E  43           
SHEET    5 AB6 6 PHE F 193  ALA F 197  1  O  ILE F 194   N  GLY F 165           
SHEET    6 AB6 6 ILE F 240  LEU F 242  1  O  GLY F 241   N  PHE F 193           
SHEET    1 AB7 2 ARG E  80  PRO E  86  0                                        
SHEET    2 AB7 2 ASN E  94  THR E 100 -1  O  LEU E  95   N  VAL E  85           
SHEET    1 AB8 3 GLU F 311  VAL F 312  0                                        
SHEET    2 AB8 3 ALA F 362  PHE F 364 -1  O  ALA F 362   N  VAL F 312           
SHEET    3 AB8 3 LEU F 353  HIS F 355 -1  N  LEU F 354   O  ALA F 363           
SHEET    1 AB9 2 HIS F 318  PHE F 320  0                                        
SHEET    2 AB9 2 ASP F 328  LYS F 330 -1  O  LYS F 330   N  HIS F 318           
SHEET    1 AC1 2 LEU F 450  GLU F 459  0                                        
SHEET    2 AC1 2 TYR F 467  PRO F 475 -1  O  ASN F 468   N  GLU F 458           
SHEET    1 AC2 4 VAL G  19  TYR G  23  0                                        
SHEET    2 AC2 4 GLY J 481  LEU J 488  1  O  VAL J 484   N  GLN G  20           
SHEET    3 AC2 4 TYR V 466  PRO V 475  1  O  PHE V 471   N  ARG J 487           
SHEET    4 AC2 4 LEU V 450  GLU V 459 -1  N  GLU V 458   O  ASN V 468           
SHEET    1 AC3 6 LEU G  63  ILE G  65  0                                        
SHEET    2 AC3 6 LEU H 114  ASN H 120 -1  O  ILE H 116   N  ILE G  65           
SHEET    3 AC3 6 PHE G  38  ALA G  44  1  N  VAL G  42   O  ARG H 117           
SHEET    4 AC3 6 CYS H 162  PHE H 169  1  O  VAL H 164   N  MET G  43           
SHEET    5 AC3 6 PHE H 193  ALA H 197  1  O  ILE H 194   N  GLY H 165           
SHEET    6 AC3 6 ILE H 240  LEU H 242  1  O  GLY H 241   N  PHE H 193           
SHEET    1 AC4 2 ARG G  80  PRO G  86  0                                        
SHEET    2 AC4 2 ASN G  94  THR G 100 -1  O  LEU G  95   N  VAL G  85           
SHEET    1 AC5 3 GLU H 311  VAL H 312  0                                        
SHEET    2 AC5 3 ALA H 362  PHE H 364 -1  O  ALA H 362   N  VAL H 312           
SHEET    3 AC5 3 LEU H 353  HIS H 355 -1  N  LEU H 354   O  ALA H 363           
SHEET    1 AC6 2 HIS H 318  PHE H 320  0                                        
SHEET    2 AC6 2 ASP H 328  LYS H 330 -1  O  LYS H 330   N  HIS H 318           
SHEET    1 AC7 2 LEU H 450  GLU H 459  0                                        
SHEET    2 AC7 2 TYR H 467  PRO H 475 -1  O  ASN H 468   N  GLU H 458           
SHEET    1 AC8 4 VAL I  19  TYR I  23  0                                        
SHEET    2 AC8 4 GLY L 481  LEU L 488  1  O  VAL L 484   N  GLN I  20           
SHEET    3 AC8 4 TYR X 466  PRO X 475  1  O  PHE X 471   N  ARG L 487           
SHEET    4 AC8 4 LEU X 450  GLU X 459 -1  N  GLU X 458   O  ASN X 468           
SHEET    1 AC9 6 LEU I  63  ILE I  65  0                                        
SHEET    2 AC9 6 LEU J 114  ASN J 120 -1  O  ILE J 116   N  ILE I  65           
SHEET    3 AC9 6 PHE I  38  ALA I  44  1  N  VAL I  42   O  ARG J 117           
SHEET    4 AC9 6 CYS J 162  PHE J 169  1  O  VAL J 164   N  MET I  43           
SHEET    5 AC9 6 PHE J 193  ALA J 197  1  O  ILE J 194   N  GLY J 165           
SHEET    6 AC9 6 ILE J 240  LEU J 242  1  O  GLY J 241   N  PHE J 193           
SHEET    1 AD1 2 ARG I  80  PRO I  86  0                                        
SHEET    2 AD1 2 ASN I  94  THR I 100 -1  O  LEU I  95   N  VAL I  85           
SHEET    1 AD2 3 GLU J 311  VAL J 312  0                                        
SHEET    2 AD2 3 ALA J 362  PHE J 364 -1  O  ALA J 362   N  VAL J 312           
SHEET    3 AD2 3 LEU J 353  HIS J 355 -1  N  LEU J 354   O  ALA J 363           
SHEET    1 AD3 2 HIS J 318  PHE J 320  0                                        
SHEET    2 AD3 2 ASP J 328  LYS J 330 -1  O  LYS J 330   N  HIS J 318           
SHEET    1 AD4 2 LEU J 450  GLU J 459  0                                        
SHEET    2 AD4 2 TYR J 467  PRO J 475 -1  O  ASN J 468   N  GLU J 458           
SHEET    1 AD5 4 VAL K  19  TYR K  23  0                                        
SHEET    2 AD5 4 GLY N 481  LEU N 488  1  O  VAL N 484   N  GLN K  20           
SHEET    3 AD5 4 TYR Z 466  PRO Z 475  1  O  PHE Z 471   N  ARG N 487           
SHEET    4 AD5 4 LEU Z 450  GLU Z 459 -1  N  GLU Z 458   O  ASN Z 468           
SHEET    1 AD6 6 LEU K  63  ILE K  65  0                                        
SHEET    2 AD6 6 LEU L 114  ASN L 120 -1  O  ILE L 116   N  ILE K  65           
SHEET    3 AD6 6 PHE K  38  ALA K  44  1  N  VAL K  42   O  ARG L 117           
SHEET    4 AD6 6 CYS L 162  PHE L 169  1  O  VAL L 164   N  MET K  43           
SHEET    5 AD6 6 PHE L 193  ALA L 197  1  O  ILE L 194   N  GLY L 165           
SHEET    6 AD6 6 ILE L 240  LEU L 242  1  O  GLY L 241   N  PHE L 193           
SHEET    1 AD7 2 ARG K  80  PRO K  86  0                                        
SHEET    2 AD7 2 ASN K  94  THR K 100 -1  O  LEU K  95   N  VAL K  85           
SHEET    1 AD8 3 GLU L 311  VAL L 312  0                                        
SHEET    2 AD8 3 ALA L 362  PHE L 364 -1  O  ALA L 362   N  VAL L 312           
SHEET    3 AD8 3 LEU L 353  HIS L 355 -1  N  LEU L 354   O  ALA L 363           
SHEET    1 AD9 2 HIS L 318  PHE L 320  0                                        
SHEET    2 AD9 2 ASP L 328  LYS L 330 -1  O  LYS L 330   N  HIS L 318           
SHEET    1 AE1 2 LEU L 450  GLU L 459  0                                        
SHEET    2 AE1 2 TYR L 467  PRO L 475 -1  O  ASN L 468   N  GLU L 458           
SHEET    1 AE2 4 VAL M  19  TYR M  23  0                                        
SHEET    2 AE2 4 GLY P 481  LEU P 488  1  O  VAL P 484   N  GLN M  20           
SHEET    3 AE2 4 TYR b 466  PRO b 475  1  O  PHE b 471   N  ARG P 487           
SHEET    4 AE2 4 LEU b 450  GLU b 459 -1  N  GLU b 458   O  ASN b 468           
SHEET    1 AE3 6 LEU M  63  ILE M  65  0                                        
SHEET    2 AE3 6 LEU N 114  ASN N 120 -1  O  ILE N 116   N  ILE M  65           
SHEET    3 AE3 6 PHE M  38  ALA M  44  1  N  VAL M  42   O  ARG N 117           
SHEET    4 AE3 6 CYS N 162  PHE N 169  1  O  VAL N 164   N  MET M  43           
SHEET    5 AE3 6 PHE N 193  ALA N 197  1  O  ILE N 194   N  GLY N 165           
SHEET    6 AE3 6 ILE N 240  LEU N 242  1  O  GLY N 241   N  PHE N 193           
SHEET    1 AE4 2 ARG M  80  PRO M  86  0                                        
SHEET    2 AE4 2 ASN M  94  THR M 100 -1  O  LEU M  95   N  VAL M  85           
SHEET    1 AE5 3 GLU N 311  VAL N 312  0                                        
SHEET    2 AE5 3 ALA N 362  PHE N 364 -1  O  ALA N 362   N  VAL N 312           
SHEET    3 AE5 3 LEU N 353  HIS N 355 -1  N  LEU N 354   O  ALA N 363           
SHEET    1 AE6 2 HIS N 318  PHE N 320  0                                        
SHEET    2 AE6 2 ASP N 328  LYS N 330 -1  O  LYS N 330   N  HIS N 318           
SHEET    1 AE7 4 VAL O  19  TYR O  23  0                                        
SHEET    2 AE7 4 GLY R 481  LEU R 488  1  O  VAL R 484   N  GLN O  20           
SHEET    3 AE7 4 TYR d 466  PRO d 475  1  O  PHE d 471   N  ARG R 487           
SHEET    4 AE7 4 LEU d 450  GLU d 459 -1  N  GLU d 458   O  ASN d 468           
SHEET    1 AE8 6 LEU O  63  ILE O  65  0                                        
SHEET    2 AE8 6 LEU P 114  ASN P 120 -1  O  ILE P 116   N  ILE O  65           
SHEET    3 AE8 6 PHE O  38  ALA O  44  1  N  VAL O  42   O  ARG P 117           
SHEET    4 AE8 6 CYS P 162  PHE P 169  1  O  VAL P 164   N  MET O  43           
SHEET    5 AE8 6 PHE P 193  ALA P 197  1  O  ILE P 194   N  GLY P 165           
SHEET    6 AE8 6 ILE P 240  LEU P 242  1  O  GLY P 241   N  PHE P 193           
SHEET    1 AE9 2 ARG O  80  PRO O  86  0                                        
SHEET    2 AE9 2 ASN O  94  THR O 100 -1  O  LEU O  95   N  VAL O  85           
SHEET    1 AF1 3 GLU P 311  VAL P 312  0                                        
SHEET    2 AF1 3 ALA P 362  PHE P 364 -1  O  ALA P 362   N  VAL P 312           
SHEET    3 AF1 3 LEU P 353  HIS P 355 -1  N  LEU P 354   O  ALA P 363           
SHEET    1 AF2 2 HIS P 318  PHE P 320  0                                        
SHEET    2 AF2 2 ASP P 328  LYS P 330 -1  O  LYS P 330   N  HIS P 318           
SHEET    1 AF3 2 VAL Q  19  TYR Q  23  0                                        
SHEET    2 AF3 2 LEU T 482  LEU T 486  1  O  VAL T 484   N  GLN Q  20           
SHEET    1 AF4 6 LEU Q  63  ILE Q  65  0                                        
SHEET    2 AF4 6 LEU R 114  ASN R 120 -1  O  ILE R 116   N  ILE Q  65           
SHEET    3 AF4 6 PHE Q  38  ALA Q  44  1  N  VAL Q  42   O  ARG R 117           
SHEET    4 AF4 6 CYS R 162  PHE R 169  1  O  VAL R 164   N  MET Q  43           
SHEET    5 AF4 6 PHE R 193  ALA R 197  1  O  ILE R 194   N  GLY R 165           
SHEET    6 AF4 6 ILE R 240  LEU R 242  1  O  GLY R 241   N  PHE R 193           
SHEET    1 AF5 2 ARG Q  80  PRO Q  86  0                                        
SHEET    2 AF5 2 ASN Q  94  THR Q 100 -1  O  LEU Q  95   N  VAL Q  85           
SHEET    1 AF6 3 GLU R 311  VAL R 312  0                                        
SHEET    2 AF6 3 ALA R 362  PHE R 364 -1  O  ALA R 362   N  VAL R 312           
SHEET    3 AF6 3 LEU R 353  HIS R 355 -1  N  LEU R 354   O  ALA R 363           
SHEET    1 AF7 2 HIS R 318  PHE R 320  0                                        
SHEET    2 AF7 2 ASP R 328  LYS R 330 -1  O  LYS R 330   N  HIS R 318           
SHEET    1 AF8 2 VAL S  19  TYR S  23  0                                        
SHEET    2 AF8 2 LEU V 482  LEU V 486  1  O  VAL V 484   N  GLN S  20           
SHEET    1 AF9 6 LEU S  63  ILE S  65  0                                        
SHEET    2 AF9 6 LEU T 114  ASN T 120 -1  O  ILE T 116   N  ILE S  65           
SHEET    3 AF9 6 PHE S  38  ALA S  44  1  N  VAL S  42   O  ARG T 117           
SHEET    4 AF9 6 CYS T 162  PHE T 169  1  O  VAL T 164   N  MET S  43           
SHEET    5 AF9 6 PHE T 193  ALA T 197  1  O  ILE T 194   N  GLY T 165           
SHEET    6 AF9 6 ILE T 240  LEU T 242  1  O  GLY T 241   N  PHE T 193           
SHEET    1 AG1 2 ARG S  80  PRO S  86  0                                        
SHEET    2 AG1 2 ASN S  94  THR S 100 -1  O  LEU S  95   N  VAL S  85           
SHEET    1 AG2 3 GLU T 311  VAL T 312  0                                        
SHEET    2 AG2 3 ALA T 362  PHE T 364 -1  O  ALA T 362   N  VAL T 312           
SHEET    3 AG2 3 LEU T 353  HIS T 355 -1  N  LEU T 354   O  ALA T 363           
SHEET    1 AG3 2 HIS T 318  PHE T 320  0                                        
SHEET    2 AG3 2 ASP T 328  LYS T 330 -1  O  LYS T 330   N  HIS T 318           
SHEET    1 AG4 2 VAL U  19  TYR U  23  0                                        
SHEET    2 AG4 2 LEU X 482  LEU X 486  1  O  VAL X 484   N  GLN U  20           
SHEET    1 AG5 6 LEU U  63  ILE U  65  0                                        
SHEET    2 AG5 6 LEU V 114  ASN V 120 -1  O  ILE V 116   N  ILE U  65           
SHEET    3 AG5 6 PHE U  38  ALA U  44  1  N  VAL U  42   O  ARG V 117           
SHEET    4 AG5 6 CYS V 162  PHE V 169  1  O  VAL V 164   N  MET U  43           
SHEET    5 AG5 6 PHE V 193  ALA V 197  1  O  ILE V 194   N  GLY V 165           
SHEET    6 AG5 6 ILE V 240  LEU V 242  1  O  GLY V 241   N  PHE V 193           
SHEET    1 AG6 2 ARG U  80  PRO U  86  0                                        
SHEET    2 AG6 2 ASN U  94  THR U 100 -1  O  LEU U  95   N  VAL U  85           
SHEET    1 AG7 3 GLU V 311  VAL V 312  0                                        
SHEET    2 AG7 3 ALA V 362  PHE V 364 -1  O  ALA V 362   N  VAL V 312           
SHEET    3 AG7 3 LEU V 353  HIS V 355 -1  N  LEU V 354   O  ALA V 363           
SHEET    1 AG8 2 HIS V 318  PHE V 320  0                                        
SHEET    2 AG8 2 ASP V 328  LYS V 330 -1  O  LYS V 330   N  HIS V 318           
SHEET    1 AG9 2 VAL W  19  TYR W  23  0                                        
SHEET    2 AG9 2 LEU Z 482  LEU Z 486  1  O  VAL Z 484   N  GLN W  20           
SHEET    1 AH1 6 LEU W  63  ILE W  65  0                                        
SHEET    2 AH1 6 LEU X 114  ASN X 120 -1  O  ILE X 116   N  ILE W  65           
SHEET    3 AH1 6 PHE W  38  ALA W  44  1  N  VAL W  42   O  ARG X 117           
SHEET    4 AH1 6 CYS X 162  PHE X 169  1  O  VAL X 164   N  MET W  43           
SHEET    5 AH1 6 PHE X 193  ALA X 197  1  O  ILE X 194   N  GLY X 165           
SHEET    6 AH1 6 ILE X 240  LEU X 242  1  O  GLY X 241   N  PHE X 193           
SHEET    1 AH2 2 ARG W  80  PRO W  86  0                                        
SHEET    2 AH2 2 ASN W  94  THR W 100 -1  O  LEU W  95   N  VAL W  85           
SHEET    1 AH3 3 GLU X 311  VAL X 312  0                                        
SHEET    2 AH3 3 ALA X 362  PHE X 364 -1  O  ALA X 362   N  VAL X 312           
SHEET    3 AH3 3 LEU X 353  HIS X 355 -1  N  LEU X 354   O  ALA X 363           
SHEET    1 AH4 2 HIS X 318  PHE X 320  0                                        
SHEET    2 AH4 2 ASP X 328  LYS X 330 -1  O  LYS X 330   N  HIS X 318           
SHEET    1 AH5 2 VAL Y  19  TYR Y  23  0                                        
SHEET    2 AH5 2 LEU b 482  LEU b 486  1  O  VAL b 484   N  GLN Y  20           
SHEET    1 AH6 6 LEU Y  63  ILE Y  65  0                                        
SHEET    2 AH6 6 LEU Z 114  ASN Z 120 -1  O  ILE Z 116   N  ILE Y  65           
SHEET    3 AH6 6 PHE Y  38  ALA Y  44  1  N  VAL Y  42   O  ARG Z 117           
SHEET    4 AH6 6 CYS Z 162  PHE Z 169  1  O  VAL Z 164   N  MET Y  43           
SHEET    5 AH6 6 PHE Z 193  ALA Z 197  1  O  ILE Z 194   N  GLY Z 165           
SHEET    6 AH6 6 ILE Z 240  LEU Z 242  1  O  GLY Z 241   N  PHE Z 193           
SHEET    1 AH7 2 ARG Y  80  PRO Y  86  0                                        
SHEET    2 AH7 2 ASN Y  94  THR Y 100 -1  O  LEU Y  95   N  VAL Y  85           
SHEET    1 AH8 3 GLU Z 311  VAL Z 312  0                                        
SHEET    2 AH8 3 ALA Z 362  PHE Z 364 -1  O  ALA Z 362   N  VAL Z 312           
SHEET    3 AH8 3 LEU Z 353  HIS Z 355 -1  N  LEU Z 354   O  ALA Z 363           
SHEET    1 AH9 2 HIS Z 318  PHE Z 320  0                                        
SHEET    2 AH9 2 ASP Z 328  LYS Z 330 -1  O  LYS Z 330   N  HIS Z 318           
SHEET    1 AI1 2 VAL a  19  TYR a  23  0                                        
SHEET    2 AI1 2 LEU d 482  LEU d 486  1  O  VAL d 484   N  GLN a  20           
SHEET    1 AI2 6 LEU a  63  ILE a  65  0                                        
SHEET    2 AI2 6 LEU b 114  ASN b 120 -1  O  ILE b 116   N  ILE a  65           
SHEET    3 AI2 6 PHE a  38  ALA a  44  1  N  VAL a  42   O  ARG b 117           
SHEET    4 AI2 6 CYS b 162  PHE b 169  1  O  VAL b 164   N  MET a  43           
SHEET    5 AI2 6 PHE b 193  ALA b 197  1  O  ILE b 194   N  GLY b 165           
SHEET    6 AI2 6 ILE b 240  LEU b 242  1  O  GLY b 241   N  PHE b 193           
SHEET    1 AI3 2 ARG a  80  PRO a  86  0                                        
SHEET    2 AI3 2 ASN a  94  THR a 100 -1  O  LEU a  95   N  VAL a  85           
SHEET    1 AI4 3 GLU b 311  VAL b 312  0                                        
SHEET    2 AI4 3 ALA b 362  PHE b 364 -1  O  ALA b 362   N  VAL b 312           
SHEET    3 AI4 3 LEU b 353  HIS b 355 -1  N  LEU b 354   O  ALA b 363           
SHEET    1 AI5 2 HIS b 318  PHE b 320  0                                        
SHEET    2 AI5 2 ASP b 328  LYS b 330 -1  O  LYS b 330   N  HIS b 318           
SHEET    1 AI6 6 LEU c  63  ILE c  65  0                                        
SHEET    2 AI6 6 LEU d 114  ASN d 120 -1  O  ILE d 116   N  ILE c  65           
SHEET    3 AI6 6 PHE c  38  ALA c  44  1  N  VAL c  42   O  ARG d 117           
SHEET    4 AI6 6 CYS d 162  PHE d 169  1  O  VAL d 164   N  MET c  43           
SHEET    5 AI6 6 PHE d 193  ALA d 197  1  O  ILE d 194   N  GLY d 165           
SHEET    6 AI6 6 ILE d 240  LEU d 242  1  O  GLY d 241   N  PHE d 193           
SHEET    1 AI7 2 ARG c  80  PRO c  86  0                                        
SHEET    2 AI7 2 ASN c  94  THR c 100 -1  O  LEU c  95   N  VAL c  85           
SHEET    1 AI8 3 GLU d 311  VAL d 312  0                                        
SHEET    2 AI8 3 ALA d 362  PHE d 364 -1  O  ALA d 362   N  VAL d 312           
SHEET    3 AI8 3 LEU d 353  HIS d 355 -1  N  LEU d 354   O  ALA d 363           
SHEET    1 AI9 2 HIS d 318  PHE d 320  0                                        
SHEET    2 AI9 2 ASP d 328  LYS d 330 -1  O  LYS d 330   N  HIS d 318           
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system