HEADER    VIRUS                                   03-MAY-10   3MUW              
TITLE     PSEUDO-ATOMIC STRUCTURE OF THE E2-E1 PROTEIN SHELL IN SINDBIS VIRUS   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: STRUCTURAL POLYPROTEIN;                                    
COMPND   3 CHAIN: A, D, E, F;                                                   
COMPND   4 SYNONYM: P130, CAPSID PROTEIN, COAT PROTEIN, C, P62, E3/E2, E3       
COMPND   5 PROTEIN, SPIKE GLYCOPROTEIN E3, E2 ENVELOPE GLYCOPROTEIN, SPIKE      
COMPND   6 GLYCOPROTEIN E2, 6K PROTEIN, E1 ENVELOPE GLYCOPROTEIN, SPIKE         
COMPND   7 GLYCOPROTEIN E1;                                                     
COMPND   8 EC: 3.4.21.-;                                                        
COMPND   9 MOL_ID: 2;                                                           
COMPND  10 MOLECULE: STRUCTURAL POLYPROTEIN;                                    
COMPND  11 CHAIN: U, X, Y, Z;                                                   
COMPND  12 SYNONYM: P130, CAPSID PROTEIN, COAT PROTEIN, C, P62, E3/E2, E3       
COMPND  13 PROTEIN, SPIKE GLYCOPROTEIN E3, E2 ENVELOPE GLYCOPROTEIN, SPIKE      
COMPND  14 GLYCOPROTEIN E2, 6K PROTEIN, E1 ENVELOPE GLYCOPROTEIN, SPIKE         
COMPND  15 GLYCOPROTEIN E1;                                                     
COMPND  16 EC: 3.4.21.-                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SINDBIS VIRUS;                                  
SOURCE   3 ORGANISM_COMMON: SINV;                                               
SOURCE   4 ORGANISM_TAXID: 11034;                                               
SOURCE   5 STRAIN: TOTO64;                                                      
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: SINDBIS VIRUS;                                  
SOURCE   8 ORGANISM_COMMON: SINV;                                               
SOURCE   9 ORGANISM_TAXID: 11034;                                               
SOURCE  10 STRAIN: TOTO64                                                       
KEYWDS    ICOSAHEDRAL PROTEIN SHELL, ICOSAHEDRAL VIRUS, VIRUS                   
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, U, D, X, E, Y, F, Z                           
AUTHOR    L.LI,J.JOSE,Y.XIANG,R.J.KUHN,M.G.ROSSMANN                             
REVDAT   6   21-FEB-24 3MUW    1       REMARK                                   
REVDAT   5   06-NOV-19 3MUW    1       CRYST1 SCALE                             
REVDAT   4   18-JUL-18 3MUW    1       REMARK                                   
REVDAT   3   04-MAY-11 3MUW    1       REMARK                                   
REVDAT   2   12-JAN-11 3MUW    1       JRNL                                     
REVDAT   1   24-NOV-10 3MUW    0                                                
JRNL        AUTH   L.LI,J.JOSE,Y.XIANG,R.J.KUHN,M.G.ROSSMANN                    
JRNL        TITL   STRUCTURAL CHANGES OF ENVELOPE PROTEINS DURING ALPHAVIRUS    
JRNL        TITL 2 FUSION.                                                      
JRNL        REF    NATURE                        V. 468   705 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   21124457                                                     
JRNL        DOI    10.1038/NATURE09546                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    9.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : EMFIT, PURDUE PROGRAMS                    
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3MUU                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : RIGID BODY FIT                      
REMARK   3   REFINEMENT TARGET            : SUMF                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--RIGID BODY                  
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)  : 9.000                          
REMARK   3   NUMBER OF PARTICLES               : 7085                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 3MUW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-10.                  
REMARK 100 THE DEPOSITION ID IS D_1000059023.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : SINDBIS VIRUS; E2-E1 PROTEIN      
REMARK 245                                    SHELL OF SINDBIS VIRUS            
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 5.00                              
REMARK 245   SAMPLE SUPPORT DETAILS         : THIS GRID PLUS SAMPLE WAS KEPT    
REMARK 245                                    AT 100 K                          
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : TNE BUFFER                        
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 21-JUN-00                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI/PHILIPS CM200T             
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1100.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2580.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : 0.00                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 1800.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 38000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 39220                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 THE ASSEMBLY REPRESENTED IN THIS ENTRY HAS REGULAR                   
REMARK 300 ICOSAHEDRAL POINT SYMMETRY (SCHOENFLIES SYMBOL = I).                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, U, D, X, E, Y, F, Z                
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 350   BIOMT1   2  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2   2  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3   2  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   3 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2   3  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3   3  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   4 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2   4 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3   4  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1   5  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2   5 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   5  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1   6 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2   6  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3   6  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   7  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3   7  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1   8  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2   8  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3   8  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1   9  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2   9  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3   9 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  10 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  10  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  10 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  11 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  11 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  11  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  12 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  12 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  12 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  13  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  13  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  13 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  14  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  14 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  14 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  15  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  15 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  15  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  16  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  16  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  16 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  17  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  17 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  17 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  18 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  18 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  18 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  19 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  19  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  19  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  20 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  20  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  20 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  21 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  21  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  21  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  22 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  22  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  22  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1  23 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  23 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  23  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  24  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  24 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  24  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  25  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  25  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  25  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  26  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  26 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  26  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  27 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  27 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  27  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  28 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  28  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  28  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  29 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  29  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  29 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  30 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  30 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  30 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  31  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  31 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  31  0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  32  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  32 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  32 -0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  33  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  33  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  33 -0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  34  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  34  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  34  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  35  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  35  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  35  0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  36 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  36  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  36 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  37  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  37  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  37 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  38  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2  38  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3  38  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT1  39  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  39 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  39 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  40 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  40 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  40 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  41 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  41 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  41 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  42  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  42 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT3  42 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT1  43  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  43 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  43  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  44  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  44  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT3  44  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  45 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  45 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  45  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  46  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  46  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  46  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  47  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  47 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  47  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  48  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT2  48 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  48  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  49  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT2  49 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT3  49 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  50  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  50  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT3  50 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  51 -0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  51  0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  51  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT1  52  0.000000  0.000000 -1.000000        0.00000            
REMARK 350   BIOMT2  52  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3  52  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT1  53 -0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT2  53  0.500000 -0.809017  0.309017        0.00000            
REMARK 350   BIOMT3  53 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT1  54 -0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  54 -0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  54 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT1  55 -0.809017  0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  55 -0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  55  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  56  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2  56  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT3  56 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT1  57 -0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT2  57  0.309017  0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  57 -0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT1  58 -0.500000  0.809017  0.309017        0.00000            
REMARK 350   BIOMT2  58  0.809017  0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  58  0.309017  0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  59  0.500000  0.809017 -0.309017        0.00000            
REMARK 350   BIOMT2  59  0.809017 -0.309017  0.500000        0.00000            
REMARK 350   BIOMT3  59  0.309017 -0.500000 -0.809017        0.00000            
REMARK 350   BIOMT1  60  0.809017 -0.309017 -0.500000        0.00000            
REMARK 350   BIOMT2  60  0.309017 -0.500000  0.809017        0.00000            
REMARK 350   BIOMT3  60 -0.500000 -0.809017 -0.309017        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     LYS A   381                                                      
REMARK 465     PRO A   382                                                      
REMARK 465     PRO A   383                                                      
REMARK 465     ALA A   384                                                      
REMARK 465     SER U     1                                                      
REMARK 465     VAL U     2                                                      
REMARK 465     ILE U     3                                                      
REMARK 465     ASP U     4                                                      
REMARK 465     ASP U     5                                                      
REMARK 465     ARG U   157                                                      
REMARK 465     LEU U   158                                                      
REMARK 465     LYS U   159                                                      
REMARK 465     GLU U   160                                                      
REMARK 465     THR U   161                                                      
REMARK 465     THR U   162                                                      
REMARK 465     ALA U   163                                                      
REMARK 465     GLY U   164                                                      
REMARK 465     TYR U   165                                                      
REMARK 465     ILE U   166                                                      
REMARK 465     THR U   167                                                      
REMARK 465     MET U   168                                                      
REMARK 465     HIS U   169                                                      
REMARK 465     ARG U   170                                                      
REMARK 465     PRO U   171                                                      
REMARK 465     ARG U   172                                                      
REMARK 465     PRO U   173                                                      
REMARK 465     HIS U   174                                                      
REMARK 465     ALA U   175                                                      
REMARK 465     TYR U   176                                                      
REMARK 465     THR U   177                                                      
REMARK 465     SER U   178                                                      
REMARK 465     TYR U   179                                                      
REMARK 465     LEU U   180                                                      
REMARK 465     GLU U   181                                                      
REMARK 465     GLU U   182                                                      
REMARK 465     SER U   183                                                      
REMARK 465     SER U   184                                                      
REMARK 465     GLY U   185                                                      
REMARK 465     LYS U   186                                                      
REMARK 465     VAL U   187                                                      
REMARK 465     TYR U   188                                                      
REMARK 465     ALA U   189                                                      
REMARK 465     LYS U   190                                                      
REMARK 465     PRO U   191                                                      
REMARK 465     PRO U   192                                                      
REMARK 465     SER U   193                                                      
REMARK 465     GLY U   194                                                      
REMARK 465     LYS U   195                                                      
REMARK 465     ASN U   196                                                      
REMARK 465     ILE U   197                                                      
REMARK 465     THR U   198                                                      
REMARK 465     TYR U   199                                                      
REMARK 465     GLU U   200                                                      
REMARK 465     CYS U   201                                                      
REMARK 465     LYS U   202                                                      
REMARK 465     CYS U   203                                                      
REMARK 465     GLY U   204                                                      
REMARK 465     ASP U   205                                                      
REMARK 465     TYR U   206                                                      
REMARK 465     LYS U   207                                                      
REMARK 465     THR U   208                                                      
REMARK 465     GLY U   209                                                      
REMARK 465     THR U   210                                                      
REMARK 465     VAL U   211                                                      
REMARK 465     SER U   212                                                      
REMARK 465     THR U   213                                                      
REMARK 465     ARG U   214                                                      
REMARK 465     THR U   215                                                      
REMARK 465     GLU U   216                                                      
REMARK 465     ILE U   217                                                      
REMARK 465     THR U   218                                                      
REMARK 465     GLY U   219                                                      
REMARK 465     CYS U   220                                                      
REMARK 465     THR U   221                                                      
REMARK 465     ALA U   222                                                      
REMARK 465     ILE U   223                                                      
REMARK 465     LYS U   224                                                      
REMARK 465     GLN U   225                                                      
REMARK 465     CYS U   226                                                      
REMARK 465     VAL U   227                                                      
REMARK 465     ALA U   228                                                      
REMARK 465     TYR U   229                                                      
REMARK 465     LYS U   230                                                      
REMARK 465     SER U   231                                                      
REMARK 465     ASP U   232                                                      
REMARK 465     GLN U   233                                                      
REMARK 465     THR U   234                                                      
REMARK 465     LYS U   235                                                      
REMARK 465     TRP U   236                                                      
REMARK 465     VAL U   237                                                      
REMARK 465     PHE U   238                                                      
REMARK 465     ASN U   239                                                      
REMARK 465     SER U   240                                                      
REMARK 465     PRO U   241                                                      
REMARK 465     ASP U   242                                                      
REMARK 465     LEU U   243                                                      
REMARK 465     ILE U   244                                                      
REMARK 465     ARG U   245                                                      
REMARK 465     HIS U   246                                                      
REMARK 465     ASP U   247                                                      
REMARK 465     ASP U   248                                                      
REMARK 465     HIS U   249                                                      
REMARK 465     THR U   250                                                      
REMARK 465     ALA U   251                                                      
REMARK 465     GLN U   252                                                      
REMARK 465     GLY U   253                                                      
REMARK 465     LYS U   254                                                      
REMARK 465     GLN U   341                                                      
REMARK 465     GLU U   342                                                      
REMARK 465     SER U   343                                                      
REMARK 465     ALA U   344                                                      
REMARK 465     LYS D   381                                                      
REMARK 465     PRO D   382                                                      
REMARK 465     PRO D   383                                                      
REMARK 465     ALA D   384                                                      
REMARK 465     SER X     1                                                      
REMARK 465     VAL X     2                                                      
REMARK 465     ILE X     3                                                      
REMARK 465     ASP X     4                                                      
REMARK 465     ASP X     5                                                      
REMARK 465     ARG X   157                                                      
REMARK 465     LEU X   158                                                      
REMARK 465     LYS X   159                                                      
REMARK 465     GLU X   160                                                      
REMARK 465     THR X   161                                                      
REMARK 465     THR X   162                                                      
REMARK 465     ALA X   163                                                      
REMARK 465     GLY X   164                                                      
REMARK 465     TYR X   165                                                      
REMARK 465     ILE X   166                                                      
REMARK 465     THR X   167                                                      
REMARK 465     MET X   168                                                      
REMARK 465     HIS X   169                                                      
REMARK 465     ARG X   170                                                      
REMARK 465     PRO X   171                                                      
REMARK 465     ARG X   172                                                      
REMARK 465     PRO X   173                                                      
REMARK 465     HIS X   174                                                      
REMARK 465     ALA X   175                                                      
REMARK 465     TYR X   176                                                      
REMARK 465     THR X   177                                                      
REMARK 465     SER X   178                                                      
REMARK 465     TYR X   179                                                      
REMARK 465     LEU X   180                                                      
REMARK 465     GLU X   181                                                      
REMARK 465     GLU X   182                                                      
REMARK 465     SER X   183                                                      
REMARK 465     SER X   184                                                      
REMARK 465     GLY X   185                                                      
REMARK 465     LYS X   186                                                      
REMARK 465     VAL X   187                                                      
REMARK 465     TYR X   188                                                      
REMARK 465     ALA X   189                                                      
REMARK 465     LYS X   190                                                      
REMARK 465     PRO X   191                                                      
REMARK 465     PRO X   192                                                      
REMARK 465     SER X   193                                                      
REMARK 465     GLY X   194                                                      
REMARK 465     LYS X   195                                                      
REMARK 465     ASN X   196                                                      
REMARK 465     ILE X   197                                                      
REMARK 465     THR X   198                                                      
REMARK 465     TYR X   199                                                      
REMARK 465     GLU X   200                                                      
REMARK 465     CYS X   201                                                      
REMARK 465     LYS X   202                                                      
REMARK 465     CYS X   203                                                      
REMARK 465     GLY X   204                                                      
REMARK 465     ASP X   205                                                      
REMARK 465     TYR X   206                                                      
REMARK 465     LYS X   207                                                      
REMARK 465     THR X   208                                                      
REMARK 465     GLY X   209                                                      
REMARK 465     THR X   210                                                      
REMARK 465     VAL X   211                                                      
REMARK 465     SER X   212                                                      
REMARK 465     THR X   213                                                      
REMARK 465     ARG X   214                                                      
REMARK 465     THR X   215                                                      
REMARK 465     GLU X   216                                                      
REMARK 465     ILE X   217                                                      
REMARK 465     THR X   218                                                      
REMARK 465     GLY X   219                                                      
REMARK 465     CYS X   220                                                      
REMARK 465     THR X   221                                                      
REMARK 465     ALA X   222                                                      
REMARK 465     ILE X   223                                                      
REMARK 465     LYS X   224                                                      
REMARK 465     GLN X   225                                                      
REMARK 465     CYS X   226                                                      
REMARK 465     VAL X   227                                                      
REMARK 465     ALA X   228                                                      
REMARK 465     TYR X   229                                                      
REMARK 465     LYS X   230                                                      
REMARK 465     SER X   231                                                      
REMARK 465     ASP X   232                                                      
REMARK 465     GLN X   233                                                      
REMARK 465     THR X   234                                                      
REMARK 465     LYS X   235                                                      
REMARK 465     TRP X   236                                                      
REMARK 465     VAL X   237                                                      
REMARK 465     PHE X   238                                                      
REMARK 465     ASN X   239                                                      
REMARK 465     SER X   240                                                      
REMARK 465     PRO X   241                                                      
REMARK 465     ASP X   242                                                      
REMARK 465     LEU X   243                                                      
REMARK 465     ILE X   244                                                      
REMARK 465     ARG X   245                                                      
REMARK 465     HIS X   246                                                      
REMARK 465     ASP X   247                                                      
REMARK 465     ASP X   248                                                      
REMARK 465     HIS X   249                                                      
REMARK 465     THR X   250                                                      
REMARK 465     ALA X   251                                                      
REMARK 465     GLN X   252                                                      
REMARK 465     GLY X   253                                                      
REMARK 465     LYS X   254                                                      
REMARK 465     GLN X   341                                                      
REMARK 465     GLU X   342                                                      
REMARK 465     SER X   343                                                      
REMARK 465     ALA X   344                                                      
REMARK 465     LYS E   381                                                      
REMARK 465     PRO E   382                                                      
REMARK 465     PRO E   383                                                      
REMARK 465     ALA E   384                                                      
REMARK 465     SER Y     1                                                      
REMARK 465     VAL Y     2                                                      
REMARK 465     ILE Y     3                                                      
REMARK 465     ASP Y     4                                                      
REMARK 465     ASP Y     5                                                      
REMARK 465     ARG Y   157                                                      
REMARK 465     LEU Y   158                                                      
REMARK 465     LYS Y   159                                                      
REMARK 465     GLU Y   160                                                      
REMARK 465     THR Y   161                                                      
REMARK 465     THR Y   162                                                      
REMARK 465     ALA Y   163                                                      
REMARK 465     GLY Y   164                                                      
REMARK 465     TYR Y   165                                                      
REMARK 465     ILE Y   166                                                      
REMARK 465     THR Y   167                                                      
REMARK 465     MET Y   168                                                      
REMARK 465     HIS Y   169                                                      
REMARK 465     ARG Y   170                                                      
REMARK 465     PRO Y   171                                                      
REMARK 465     ARG Y   172                                                      
REMARK 465     PRO Y   173                                                      
REMARK 465     HIS Y   174                                                      
REMARK 465     ALA Y   175                                                      
REMARK 465     TYR Y   176                                                      
REMARK 465     THR Y   177                                                      
REMARK 465     SER Y   178                                                      
REMARK 465     TYR Y   179                                                      
REMARK 465     LEU Y   180                                                      
REMARK 465     GLU Y   181                                                      
REMARK 465     GLU Y   182                                                      
REMARK 465     SER Y   183                                                      
REMARK 465     SER Y   184                                                      
REMARK 465     GLY Y   185                                                      
REMARK 465     LYS Y   186                                                      
REMARK 465     VAL Y   187                                                      
REMARK 465     TYR Y   188                                                      
REMARK 465     ALA Y   189                                                      
REMARK 465     LYS Y   190                                                      
REMARK 465     PRO Y   191                                                      
REMARK 465     PRO Y   192                                                      
REMARK 465     SER Y   193                                                      
REMARK 465     GLY Y   194                                                      
REMARK 465     LYS Y   195                                                      
REMARK 465     ASN Y   196                                                      
REMARK 465     ILE Y   197                                                      
REMARK 465     THR Y   198                                                      
REMARK 465     TYR Y   199                                                      
REMARK 465     GLU Y   200                                                      
REMARK 465     CYS Y   201                                                      
REMARK 465     LYS Y   202                                                      
REMARK 465     CYS Y   203                                                      
REMARK 465     GLY Y   204                                                      
REMARK 465     ASP Y   205                                                      
REMARK 465     TYR Y   206                                                      
REMARK 465     LYS Y   207                                                      
REMARK 465     THR Y   208                                                      
REMARK 465     GLY Y   209                                                      
REMARK 465     THR Y   210                                                      
REMARK 465     VAL Y   211                                                      
REMARK 465     SER Y   212                                                      
REMARK 465     THR Y   213                                                      
REMARK 465     ARG Y   214                                                      
REMARK 465     THR Y   215                                                      
REMARK 465     GLU Y   216                                                      
REMARK 465     ILE Y   217                                                      
REMARK 465     THR Y   218                                                      
REMARK 465     GLY Y   219                                                      
REMARK 465     CYS Y   220                                                      
REMARK 465     THR Y   221                                                      
REMARK 465     ALA Y   222                                                      
REMARK 465     ILE Y   223                                                      
REMARK 465     LYS Y   224                                                      
REMARK 465     GLN Y   225                                                      
REMARK 465     CYS Y   226                                                      
REMARK 465     VAL Y   227                                                      
REMARK 465     ALA Y   228                                                      
REMARK 465     TYR Y   229                                                      
REMARK 465     LYS Y   230                                                      
REMARK 465     SER Y   231                                                      
REMARK 465     ASP Y   232                                                      
REMARK 465     GLN Y   233                                                      
REMARK 465     THR Y   234                                                      
REMARK 465     LYS Y   235                                                      
REMARK 465     TRP Y   236                                                      
REMARK 465     VAL Y   237                                                      
REMARK 465     PHE Y   238                                                      
REMARK 465     ASN Y   239                                                      
REMARK 465     SER Y   240                                                      
REMARK 465     PRO Y   241                                                      
REMARK 465     ASP Y   242                                                      
REMARK 465     LEU Y   243                                                      
REMARK 465     ILE Y   244                                                      
REMARK 465     ARG Y   245                                                      
REMARK 465     HIS Y   246                                                      
REMARK 465     ASP Y   247                                                      
REMARK 465     ASP Y   248                                                      
REMARK 465     HIS Y   249                                                      
REMARK 465     THR Y   250                                                      
REMARK 465     ALA Y   251                                                      
REMARK 465     GLN Y   252                                                      
REMARK 465     GLY Y   253                                                      
REMARK 465     LYS Y   254                                                      
REMARK 465     GLN Y   341                                                      
REMARK 465     GLU Y   342                                                      
REMARK 465     SER Y   343                                                      
REMARK 465     ALA Y   344                                                      
REMARK 465     LYS F   381                                                      
REMARK 465     PRO F   382                                                      
REMARK 465     PRO F   383                                                      
REMARK 465     ALA F   384                                                      
REMARK 465     SER Z     1                                                      
REMARK 465     VAL Z     2                                                      
REMARK 465     ILE Z     3                                                      
REMARK 465     ASP Z     4                                                      
REMARK 465     ASP Z     5                                                      
REMARK 465     ARG Z   157                                                      
REMARK 465     LEU Z   158                                                      
REMARK 465     LYS Z   159                                                      
REMARK 465     GLU Z   160                                                      
REMARK 465     THR Z   161                                                      
REMARK 465     THR Z   162                                                      
REMARK 465     ALA Z   163                                                      
REMARK 465     GLY Z   164                                                      
REMARK 465     TYR Z   165                                                      
REMARK 465     ILE Z   166                                                      
REMARK 465     THR Z   167                                                      
REMARK 465     MET Z   168                                                      
REMARK 465     HIS Z   169                                                      
REMARK 465     ARG Z   170                                                      
REMARK 465     PRO Z   171                                                      
REMARK 465     ARG Z   172                                                      
REMARK 465     PRO Z   173                                                      
REMARK 465     HIS Z   174                                                      
REMARK 465     ALA Z   175                                                      
REMARK 465     TYR Z   176                                                      
REMARK 465     THR Z   177                                                      
REMARK 465     SER Z   178                                                      
REMARK 465     TYR Z   179                                                      
REMARK 465     LEU Z   180                                                      
REMARK 465     GLU Z   181                                                      
REMARK 465     GLU Z   182                                                      
REMARK 465     SER Z   183                                                      
REMARK 465     SER Z   184                                                      
REMARK 465     GLY Z   185                                                      
REMARK 465     LYS Z   186                                                      
REMARK 465     VAL Z   187                                                      
REMARK 465     TYR Z   188                                                      
REMARK 465     ALA Z   189                                                      
REMARK 465     LYS Z   190                                                      
REMARK 465     PRO Z   191                                                      
REMARK 465     PRO Z   192                                                      
REMARK 465     SER Z   193                                                      
REMARK 465     GLY Z   194                                                      
REMARK 465     LYS Z   195                                                      
REMARK 465     ASN Z   196                                                      
REMARK 465     ILE Z   197                                                      
REMARK 465     THR Z   198                                                      
REMARK 465     TYR Z   199                                                      
REMARK 465     GLU Z   200                                                      
REMARK 465     CYS Z   201                                                      
REMARK 465     LYS Z   202                                                      
REMARK 465     CYS Z   203                                                      
REMARK 465     GLY Z   204                                                      
REMARK 465     ASP Z   205                                                      
REMARK 465     TYR Z   206                                                      
REMARK 465     LYS Z   207                                                      
REMARK 465     THR Z   208                                                      
REMARK 465     GLY Z   209                                                      
REMARK 465     THR Z   210                                                      
REMARK 465     VAL Z   211                                                      
REMARK 465     SER Z   212                                                      
REMARK 465     THR Z   213                                                      
REMARK 465     ARG Z   214                                                      
REMARK 465     THR Z   215                                                      
REMARK 465     GLU Z   216                                                      
REMARK 465     ILE Z   217                                                      
REMARK 465     THR Z   218                                                      
REMARK 465     GLY Z   219                                                      
REMARK 465     CYS Z   220                                                      
REMARK 465     THR Z   221                                                      
REMARK 465     ALA Z   222                                                      
REMARK 465     ILE Z   223                                                      
REMARK 465     LYS Z   224                                                      
REMARK 465     GLN Z   225                                                      
REMARK 465     CYS Z   226                                                      
REMARK 465     VAL Z   227                                                      
REMARK 465     ALA Z   228                                                      
REMARK 465     TYR Z   229                                                      
REMARK 465     LYS Z   230                                                      
REMARK 465     SER Z   231                                                      
REMARK 465     ASP Z   232                                                      
REMARK 465     GLN Z   233                                                      
REMARK 465     THR Z   234                                                      
REMARK 465     LYS Z   235                                                      
REMARK 465     TRP Z   236                                                      
REMARK 465     VAL Z   237                                                      
REMARK 465     PHE Z   238                                                      
REMARK 465     ASN Z   239                                                      
REMARK 465     SER Z   240                                                      
REMARK 465     PRO Z   241                                                      
REMARK 465     ASP Z   242                                                      
REMARK 465     LEU Z   243                                                      
REMARK 465     ILE Z   244                                                      
REMARK 465     ARG Z   245                                                      
REMARK 465     HIS Z   246                                                      
REMARK 465     ASP Z   247                                                      
REMARK 465     ASP Z   248                                                      
REMARK 465     HIS Z   249                                                      
REMARK 465     THR Z   250                                                      
REMARK 465     ALA Z   251                                                      
REMARK 465     GLN Z   252                                                      
REMARK 465     GLY Z   253                                                      
REMARK 465     LYS Z   254                                                      
REMARK 465     GLN Z   341                                                      
REMARK 465     GLU Z   342                                                      
REMARK 465     SER Z   343                                                      
REMARK 465     ALA Z   344                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-1121   RELATED DB: EMDB                              
REMARK 900 CRYO-EM RECONSTRUCTION OF SINDBIS VIRUS AT 9A RESOLUTION             
REMARK 900 RELATED ID: 3MUU   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE E2-E1 PROTEIN FROM SINDBIS VIRUS            
DBREF  3MUW A    1   384  UNP    P03316   POLS_SINDV     807   1190             
DBREF  3MUW U    1   344  UNP    P03316   POLS_SINDV     329    672             
DBREF  3MUW D    1   384  UNP    P03316   POLS_SINDV     807   1190             
DBREF  3MUW X    1   344  UNP    P03316   POLS_SINDV     329    672             
DBREF  3MUW E    1   384  UNP    P03316   POLS_SINDV     807   1190             
DBREF  3MUW Y    1   344  UNP    P03316   POLS_SINDV     329    672             
DBREF  3MUW F    1   384  UNP    P03316   POLS_SINDV     807   1190             
DBREF  3MUW Z    1   344  UNP    P03316   POLS_SINDV     329    672             
SEQRES   1 A  384  TYR GLU HIS ALA THR THR VAL PRO ASN VAL PRO GLN ILE          
SEQRES   2 A  384  PRO TYR LYS ALA LEU VAL GLU ARG ALA GLY TYR ALA PRO          
SEQRES   3 A  384  LEU ASN LEU GLU ILE THR VAL MET SER SER GLU VAL LEU          
SEQRES   4 A  384  PRO SER THR ASN GLN GLU TYR ILE THR CYS LYS PHE THR          
SEQRES   5 A  384  THR VAL VAL PRO SER PRO LYS ILE LYS CYS CYS GLY SER          
SEQRES   6 A  384  LEU GLU CYS GLN PRO ALA ALA HIS ALA ASP TYR THR CYS          
SEQRES   7 A  384  LYS VAL PHE GLY GLY VAL TYR PRO PHE MET TRP GLY GLY          
SEQRES   8 A  384  ALA GLN CYS PHE CYS ASP SER GLU ASN SER GLN MET SER          
SEQRES   9 A  384  GLU ALA TYR VAL GLU LEU SER ALA ASP CYS ALA SER ASP          
SEQRES  10 A  384  HIS ALA GLN ALA ILE LYS VAL HIS THR ALA ALA MET LYS          
SEQRES  11 A  384  VAL GLY LEU ARG ILE VAL TYR GLY ASN THR THR SER PHE          
SEQRES  12 A  384  LEU ASP VAL TYR VAL ASN GLY VAL THR PRO GLY THR SER          
SEQRES  13 A  384  LYS ASP LEU LYS VAL ILE ALA GLY PRO ILE SER ALA SER          
SEQRES  14 A  384  PHE THR PRO PHE ASP HIS LYS VAL VAL ILE HIS ARG GLY          
SEQRES  15 A  384  LEU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY ALA MET          
SEQRES  16 A  384  LYS PRO GLY ALA PHE GLY ASP ILE GLN ALA THR SER LEU          
SEQRES  17 A  384  THR SER LYS ASP LEU ILE ALA SER THR ASP ILE ARG LEU          
SEQRES  18 A  384  LEU LYS PRO SER ALA LYS ASN VAL HIS VAL PRO TYR THR          
SEQRES  19 A  384  GLN ALA SER SER GLY PHE GLU MET TRP LYS ASN ASN SER          
SEQRES  20 A  384  GLY ARG PRO LEU GLN GLU THR ALA PRO PHE GLY CYS LYS          
SEQRES  21 A  384  ILE ALA VAL ASN PRO LEU ARG ALA VAL ASP CYS SER TYR          
SEQRES  22 A  384  GLY ASN ILE PRO ILE SER ILE ASP ILE PRO ASN ALA ALA          
SEQRES  23 A  384  PHE ILE ARG THR SER ASP ALA PRO LEU VAL SER THR VAL          
SEQRES  24 A  384  LYS CYS GLU VAL SER GLU CYS THR TYR SER ALA ASP PHE          
SEQRES  25 A  384  GLY GLY MET ALA THR LEU GLN TYR VAL SER ASP ARG GLU          
SEQRES  26 A  384  GLY GLN CYS PRO VAL HIS SER HIS SER SER THR ALA THR          
SEQRES  27 A  384  LEU GLN GLU SER THR VAL HIS VAL LEU GLU LYS GLY ALA          
SEQRES  28 A  384  VAL THR VAL HIS PHE SER THR ALA SER PRO GLN ALA ASN          
SEQRES  29 A  384  PHE ILE VAL SER LEU CYS GLY LYS LYS THR THR CYS ASN          
SEQRES  30 A  384  ALA GLU CYS LYS PRO PRO ALA                                  
SEQRES   1 U  344  SER VAL ILE ASP ASP PHE THR LEU THR SER PRO TYR LEU          
SEQRES   2 U  344  GLY THR CYS SER TYR CYS HIS HIS THR VAL PRO CYS PHE          
SEQRES   3 U  344  SER PRO VAL LYS ILE GLU GLN VAL TRP ASP GLU ALA ASP          
SEQRES   4 U  344  ASP ASN THR ILE ARG ILE GLN THR SER ALA GLN PHE GLY          
SEQRES   5 U  344  TYR ASP GLN SER GLY ALA ALA SER ALA ASN LYS TYR ARG          
SEQRES   6 U  344  TYR MET SER LEU LYS GLN ASP HIS THR VAL LYS GLU GLY          
SEQRES   7 U  344  THR MET ASP ASP ILE LYS ILE SER THR SER GLY PRO CYS          
SEQRES   8 U  344  ARG ARG LEU SER TYR LYS GLY TYR PHE LEU LEU ALA LYS          
SEQRES   9 U  344  CYS PRO PRO GLY ASP SER VAL THR VAL SER ILE VAL SER          
SEQRES  10 U  344  SER ASN SER ALA THR SER CYS THR LEU ALA ARG LYS ILE          
SEQRES  11 U  344  LYS PRO LYS PHE VAL GLY ARG GLU LYS TYR ASP LEU PRO          
SEQRES  12 U  344  PRO VAL HIS GLY LYS LYS ILE PRO CYS THR VAL TYR ASP          
SEQRES  13 U  344  ARG LEU LYS GLU THR THR ALA GLY TYR ILE THR MET HIS          
SEQRES  14 U  344  ARG PRO ARG PRO HIS ALA TYR THR SER TYR LEU GLU GLU          
SEQRES  15 U  344  SER SER GLY LYS VAL TYR ALA LYS PRO PRO SER GLY LYS          
SEQRES  16 U  344  ASN ILE THR TYR GLU CYS LYS CYS GLY ASP TYR LYS THR          
SEQRES  17 U  344  GLY THR VAL SER THR ARG THR GLU ILE THR GLY CYS THR          
SEQRES  18 U  344  ALA ILE LYS GLN CYS VAL ALA TYR LYS SER ASP GLN THR          
SEQRES  19 U  344  LYS TRP VAL PHE ASN SER PRO ASP LEU ILE ARG HIS ASP          
SEQRES  20 U  344  ASP HIS THR ALA GLN GLY LYS LEU HIS LEU PRO PHE LYS          
SEQRES  21 U  344  LEU ILE PRO SER THR CYS MET VAL PRO VAL ALA HIS ALA          
SEQRES  22 U  344  PRO ASN VAL ILE HIS GLY PHE LYS HIS ILE SER LEU GLN          
SEQRES  23 U  344  LEU ASP THR ASP HIS LEU THR LEU LEU THR THR ARG ARG          
SEQRES  24 U  344  LEU GLY ALA ASN PRO GLU PRO THR THR GLU TRP ILE VAL          
SEQRES  25 U  344  GLY LYS THR VAL ARG ASN PHE THR VAL ASP ARG ASP GLY          
SEQRES  26 U  344  LEU GLU TYR ILE TRP GLY ASN HIS GLU PRO VAL ARG VAL          
SEQRES  27 U  344  TYR ALA GLN GLU SER ALA                                      
SEQRES   1 D  384  TYR GLU HIS ALA THR THR VAL PRO ASN VAL PRO GLN ILE          
SEQRES   2 D  384  PRO TYR LYS ALA LEU VAL GLU ARG ALA GLY TYR ALA PRO          
SEQRES   3 D  384  LEU ASN LEU GLU ILE THR VAL MET SER SER GLU VAL LEU          
SEQRES   4 D  384  PRO SER THR ASN GLN GLU TYR ILE THR CYS LYS PHE THR          
SEQRES   5 D  384  THR VAL VAL PRO SER PRO LYS ILE LYS CYS CYS GLY SER          
SEQRES   6 D  384  LEU GLU CYS GLN PRO ALA ALA HIS ALA ASP TYR THR CYS          
SEQRES   7 D  384  LYS VAL PHE GLY GLY VAL TYR PRO PHE MET TRP GLY GLY          
SEQRES   8 D  384  ALA GLN CYS PHE CYS ASP SER GLU ASN SER GLN MET SER          
SEQRES   9 D  384  GLU ALA TYR VAL GLU LEU SER ALA ASP CYS ALA SER ASP          
SEQRES  10 D  384  HIS ALA GLN ALA ILE LYS VAL HIS THR ALA ALA MET LYS          
SEQRES  11 D  384  VAL GLY LEU ARG ILE VAL TYR GLY ASN THR THR SER PHE          
SEQRES  12 D  384  LEU ASP VAL TYR VAL ASN GLY VAL THR PRO GLY THR SER          
SEQRES  13 D  384  LYS ASP LEU LYS VAL ILE ALA GLY PRO ILE SER ALA SER          
SEQRES  14 D  384  PHE THR PRO PHE ASP HIS LYS VAL VAL ILE HIS ARG GLY          
SEQRES  15 D  384  LEU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY ALA MET          
SEQRES  16 D  384  LYS PRO GLY ALA PHE GLY ASP ILE GLN ALA THR SER LEU          
SEQRES  17 D  384  THR SER LYS ASP LEU ILE ALA SER THR ASP ILE ARG LEU          
SEQRES  18 D  384  LEU LYS PRO SER ALA LYS ASN VAL HIS VAL PRO TYR THR          
SEQRES  19 D  384  GLN ALA SER SER GLY PHE GLU MET TRP LYS ASN ASN SER          
SEQRES  20 D  384  GLY ARG PRO LEU GLN GLU THR ALA PRO PHE GLY CYS LYS          
SEQRES  21 D  384  ILE ALA VAL ASN PRO LEU ARG ALA VAL ASP CYS SER TYR          
SEQRES  22 D  384  GLY ASN ILE PRO ILE SER ILE ASP ILE PRO ASN ALA ALA          
SEQRES  23 D  384  PHE ILE ARG THR SER ASP ALA PRO LEU VAL SER THR VAL          
SEQRES  24 D  384  LYS CYS GLU VAL SER GLU CYS THR TYR SER ALA ASP PHE          
SEQRES  25 D  384  GLY GLY MET ALA THR LEU GLN TYR VAL SER ASP ARG GLU          
SEQRES  26 D  384  GLY GLN CYS PRO VAL HIS SER HIS SER SER THR ALA THR          
SEQRES  27 D  384  LEU GLN GLU SER THR VAL HIS VAL LEU GLU LYS GLY ALA          
SEQRES  28 D  384  VAL THR VAL HIS PHE SER THR ALA SER PRO GLN ALA ASN          
SEQRES  29 D  384  PHE ILE VAL SER LEU CYS GLY LYS LYS THR THR CYS ASN          
SEQRES  30 D  384  ALA GLU CYS LYS PRO PRO ALA                                  
SEQRES   1 X  344  SER VAL ILE ASP ASP PHE THR LEU THR SER PRO TYR LEU          
SEQRES   2 X  344  GLY THR CYS SER TYR CYS HIS HIS THR VAL PRO CYS PHE          
SEQRES   3 X  344  SER PRO VAL LYS ILE GLU GLN VAL TRP ASP GLU ALA ASP          
SEQRES   4 X  344  ASP ASN THR ILE ARG ILE GLN THR SER ALA GLN PHE GLY          
SEQRES   5 X  344  TYR ASP GLN SER GLY ALA ALA SER ALA ASN LYS TYR ARG          
SEQRES   6 X  344  TYR MET SER LEU LYS GLN ASP HIS THR VAL LYS GLU GLY          
SEQRES   7 X  344  THR MET ASP ASP ILE LYS ILE SER THR SER GLY PRO CYS          
SEQRES   8 X  344  ARG ARG LEU SER TYR LYS GLY TYR PHE LEU LEU ALA LYS          
SEQRES   9 X  344  CYS PRO PRO GLY ASP SER VAL THR VAL SER ILE VAL SER          
SEQRES  10 X  344  SER ASN SER ALA THR SER CYS THR LEU ALA ARG LYS ILE          
SEQRES  11 X  344  LYS PRO LYS PHE VAL GLY ARG GLU LYS TYR ASP LEU PRO          
SEQRES  12 X  344  PRO VAL HIS GLY LYS LYS ILE PRO CYS THR VAL TYR ASP          
SEQRES  13 X  344  ARG LEU LYS GLU THR THR ALA GLY TYR ILE THR MET HIS          
SEQRES  14 X  344  ARG PRO ARG PRO HIS ALA TYR THR SER TYR LEU GLU GLU          
SEQRES  15 X  344  SER SER GLY LYS VAL TYR ALA LYS PRO PRO SER GLY LYS          
SEQRES  16 X  344  ASN ILE THR TYR GLU CYS LYS CYS GLY ASP TYR LYS THR          
SEQRES  17 X  344  GLY THR VAL SER THR ARG THR GLU ILE THR GLY CYS THR          
SEQRES  18 X  344  ALA ILE LYS GLN CYS VAL ALA TYR LYS SER ASP GLN THR          
SEQRES  19 X  344  LYS TRP VAL PHE ASN SER PRO ASP LEU ILE ARG HIS ASP          
SEQRES  20 X  344  ASP HIS THR ALA GLN GLY LYS LEU HIS LEU PRO PHE LYS          
SEQRES  21 X  344  LEU ILE PRO SER THR CYS MET VAL PRO VAL ALA HIS ALA          
SEQRES  22 X  344  PRO ASN VAL ILE HIS GLY PHE LYS HIS ILE SER LEU GLN          
SEQRES  23 X  344  LEU ASP THR ASP HIS LEU THR LEU LEU THR THR ARG ARG          
SEQRES  24 X  344  LEU GLY ALA ASN PRO GLU PRO THR THR GLU TRP ILE VAL          
SEQRES  25 X  344  GLY LYS THR VAL ARG ASN PHE THR VAL ASP ARG ASP GLY          
SEQRES  26 X  344  LEU GLU TYR ILE TRP GLY ASN HIS GLU PRO VAL ARG VAL          
SEQRES  27 X  344  TYR ALA GLN GLU SER ALA                                      
SEQRES   1 E  384  TYR GLU HIS ALA THR THR VAL PRO ASN VAL PRO GLN ILE          
SEQRES   2 E  384  PRO TYR LYS ALA LEU VAL GLU ARG ALA GLY TYR ALA PRO          
SEQRES   3 E  384  LEU ASN LEU GLU ILE THR VAL MET SER SER GLU VAL LEU          
SEQRES   4 E  384  PRO SER THR ASN GLN GLU TYR ILE THR CYS LYS PHE THR          
SEQRES   5 E  384  THR VAL VAL PRO SER PRO LYS ILE LYS CYS CYS GLY SER          
SEQRES   6 E  384  LEU GLU CYS GLN PRO ALA ALA HIS ALA ASP TYR THR CYS          
SEQRES   7 E  384  LYS VAL PHE GLY GLY VAL TYR PRO PHE MET TRP GLY GLY          
SEQRES   8 E  384  ALA GLN CYS PHE CYS ASP SER GLU ASN SER GLN MET SER          
SEQRES   9 E  384  GLU ALA TYR VAL GLU LEU SER ALA ASP CYS ALA SER ASP          
SEQRES  10 E  384  HIS ALA GLN ALA ILE LYS VAL HIS THR ALA ALA MET LYS          
SEQRES  11 E  384  VAL GLY LEU ARG ILE VAL TYR GLY ASN THR THR SER PHE          
SEQRES  12 E  384  LEU ASP VAL TYR VAL ASN GLY VAL THR PRO GLY THR SER          
SEQRES  13 E  384  LYS ASP LEU LYS VAL ILE ALA GLY PRO ILE SER ALA SER          
SEQRES  14 E  384  PHE THR PRO PHE ASP HIS LYS VAL VAL ILE HIS ARG GLY          
SEQRES  15 E  384  LEU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY ALA MET          
SEQRES  16 E  384  LYS PRO GLY ALA PHE GLY ASP ILE GLN ALA THR SER LEU          
SEQRES  17 E  384  THR SER LYS ASP LEU ILE ALA SER THR ASP ILE ARG LEU          
SEQRES  18 E  384  LEU LYS PRO SER ALA LYS ASN VAL HIS VAL PRO TYR THR          
SEQRES  19 E  384  GLN ALA SER SER GLY PHE GLU MET TRP LYS ASN ASN SER          
SEQRES  20 E  384  GLY ARG PRO LEU GLN GLU THR ALA PRO PHE GLY CYS LYS          
SEQRES  21 E  384  ILE ALA VAL ASN PRO LEU ARG ALA VAL ASP CYS SER TYR          
SEQRES  22 E  384  GLY ASN ILE PRO ILE SER ILE ASP ILE PRO ASN ALA ALA          
SEQRES  23 E  384  PHE ILE ARG THR SER ASP ALA PRO LEU VAL SER THR VAL          
SEQRES  24 E  384  LYS CYS GLU VAL SER GLU CYS THR TYR SER ALA ASP PHE          
SEQRES  25 E  384  GLY GLY MET ALA THR LEU GLN TYR VAL SER ASP ARG GLU          
SEQRES  26 E  384  GLY GLN CYS PRO VAL HIS SER HIS SER SER THR ALA THR          
SEQRES  27 E  384  LEU GLN GLU SER THR VAL HIS VAL LEU GLU LYS GLY ALA          
SEQRES  28 E  384  VAL THR VAL HIS PHE SER THR ALA SER PRO GLN ALA ASN          
SEQRES  29 E  384  PHE ILE VAL SER LEU CYS GLY LYS LYS THR THR CYS ASN          
SEQRES  30 E  384  ALA GLU CYS LYS PRO PRO ALA                                  
SEQRES   1 Y  344  SER VAL ILE ASP ASP PHE THR LEU THR SER PRO TYR LEU          
SEQRES   2 Y  344  GLY THR CYS SER TYR CYS HIS HIS THR VAL PRO CYS PHE          
SEQRES   3 Y  344  SER PRO VAL LYS ILE GLU GLN VAL TRP ASP GLU ALA ASP          
SEQRES   4 Y  344  ASP ASN THR ILE ARG ILE GLN THR SER ALA GLN PHE GLY          
SEQRES   5 Y  344  TYR ASP GLN SER GLY ALA ALA SER ALA ASN LYS TYR ARG          
SEQRES   6 Y  344  TYR MET SER LEU LYS GLN ASP HIS THR VAL LYS GLU GLY          
SEQRES   7 Y  344  THR MET ASP ASP ILE LYS ILE SER THR SER GLY PRO CYS          
SEQRES   8 Y  344  ARG ARG LEU SER TYR LYS GLY TYR PHE LEU LEU ALA LYS          
SEQRES   9 Y  344  CYS PRO PRO GLY ASP SER VAL THR VAL SER ILE VAL SER          
SEQRES  10 Y  344  SER ASN SER ALA THR SER CYS THR LEU ALA ARG LYS ILE          
SEQRES  11 Y  344  LYS PRO LYS PHE VAL GLY ARG GLU LYS TYR ASP LEU PRO          
SEQRES  12 Y  344  PRO VAL HIS GLY LYS LYS ILE PRO CYS THR VAL TYR ASP          
SEQRES  13 Y  344  ARG LEU LYS GLU THR THR ALA GLY TYR ILE THR MET HIS          
SEQRES  14 Y  344  ARG PRO ARG PRO HIS ALA TYR THR SER TYR LEU GLU GLU          
SEQRES  15 Y  344  SER SER GLY LYS VAL TYR ALA LYS PRO PRO SER GLY LYS          
SEQRES  16 Y  344  ASN ILE THR TYR GLU CYS LYS CYS GLY ASP TYR LYS THR          
SEQRES  17 Y  344  GLY THR VAL SER THR ARG THR GLU ILE THR GLY CYS THR          
SEQRES  18 Y  344  ALA ILE LYS GLN CYS VAL ALA TYR LYS SER ASP GLN THR          
SEQRES  19 Y  344  LYS TRP VAL PHE ASN SER PRO ASP LEU ILE ARG HIS ASP          
SEQRES  20 Y  344  ASP HIS THR ALA GLN GLY LYS LEU HIS LEU PRO PHE LYS          
SEQRES  21 Y  344  LEU ILE PRO SER THR CYS MET VAL PRO VAL ALA HIS ALA          
SEQRES  22 Y  344  PRO ASN VAL ILE HIS GLY PHE LYS HIS ILE SER LEU GLN          
SEQRES  23 Y  344  LEU ASP THR ASP HIS LEU THR LEU LEU THR THR ARG ARG          
SEQRES  24 Y  344  LEU GLY ALA ASN PRO GLU PRO THR THR GLU TRP ILE VAL          
SEQRES  25 Y  344  GLY LYS THR VAL ARG ASN PHE THR VAL ASP ARG ASP GLY          
SEQRES  26 Y  344  LEU GLU TYR ILE TRP GLY ASN HIS GLU PRO VAL ARG VAL          
SEQRES  27 Y  344  TYR ALA GLN GLU SER ALA                                      
SEQRES   1 F  384  TYR GLU HIS ALA THR THR VAL PRO ASN VAL PRO GLN ILE          
SEQRES   2 F  384  PRO TYR LYS ALA LEU VAL GLU ARG ALA GLY TYR ALA PRO          
SEQRES   3 F  384  LEU ASN LEU GLU ILE THR VAL MET SER SER GLU VAL LEU          
SEQRES   4 F  384  PRO SER THR ASN GLN GLU TYR ILE THR CYS LYS PHE THR          
SEQRES   5 F  384  THR VAL VAL PRO SER PRO LYS ILE LYS CYS CYS GLY SER          
SEQRES   6 F  384  LEU GLU CYS GLN PRO ALA ALA HIS ALA ASP TYR THR CYS          
SEQRES   7 F  384  LYS VAL PHE GLY GLY VAL TYR PRO PHE MET TRP GLY GLY          
SEQRES   8 F  384  ALA GLN CYS PHE CYS ASP SER GLU ASN SER GLN MET SER          
SEQRES   9 F  384  GLU ALA TYR VAL GLU LEU SER ALA ASP CYS ALA SER ASP          
SEQRES  10 F  384  HIS ALA GLN ALA ILE LYS VAL HIS THR ALA ALA MET LYS          
SEQRES  11 F  384  VAL GLY LEU ARG ILE VAL TYR GLY ASN THR THR SER PHE          
SEQRES  12 F  384  LEU ASP VAL TYR VAL ASN GLY VAL THR PRO GLY THR SER          
SEQRES  13 F  384  LYS ASP LEU LYS VAL ILE ALA GLY PRO ILE SER ALA SER          
SEQRES  14 F  384  PHE THR PRO PHE ASP HIS LYS VAL VAL ILE HIS ARG GLY          
SEQRES  15 F  384  LEU VAL TYR ASN TYR ASP PHE PRO GLU TYR GLY ALA MET          
SEQRES  16 F  384  LYS PRO GLY ALA PHE GLY ASP ILE GLN ALA THR SER LEU          
SEQRES  17 F  384  THR SER LYS ASP LEU ILE ALA SER THR ASP ILE ARG LEU          
SEQRES  18 F  384  LEU LYS PRO SER ALA LYS ASN VAL HIS VAL PRO TYR THR          
SEQRES  19 F  384  GLN ALA SER SER GLY PHE GLU MET TRP LYS ASN ASN SER          
SEQRES  20 F  384  GLY ARG PRO LEU GLN GLU THR ALA PRO PHE GLY CYS LYS          
SEQRES  21 F  384  ILE ALA VAL ASN PRO LEU ARG ALA VAL ASP CYS SER TYR          
SEQRES  22 F  384  GLY ASN ILE PRO ILE SER ILE ASP ILE PRO ASN ALA ALA          
SEQRES  23 F  384  PHE ILE ARG THR SER ASP ALA PRO LEU VAL SER THR VAL          
SEQRES  24 F  384  LYS CYS GLU VAL SER GLU CYS THR TYR SER ALA ASP PHE          
SEQRES  25 F  384  GLY GLY MET ALA THR LEU GLN TYR VAL SER ASP ARG GLU          
SEQRES  26 F  384  GLY GLN CYS PRO VAL HIS SER HIS SER SER THR ALA THR          
SEQRES  27 F  384  LEU GLN GLU SER THR VAL HIS VAL LEU GLU LYS GLY ALA          
SEQRES  28 F  384  VAL THR VAL HIS PHE SER THR ALA SER PRO GLN ALA ASN          
SEQRES  29 F  384  PHE ILE VAL SER LEU CYS GLY LYS LYS THR THR CYS ASN          
SEQRES  30 F  384  ALA GLU CYS LYS PRO PRO ALA                                  
SEQRES   1 Z  344  SER VAL ILE ASP ASP PHE THR LEU THR SER PRO TYR LEU          
SEQRES   2 Z  344  GLY THR CYS SER TYR CYS HIS HIS THR VAL PRO CYS PHE          
SEQRES   3 Z  344  SER PRO VAL LYS ILE GLU GLN VAL TRP ASP GLU ALA ASP          
SEQRES   4 Z  344  ASP ASN THR ILE ARG ILE GLN THR SER ALA GLN PHE GLY          
SEQRES   5 Z  344  TYR ASP GLN SER GLY ALA ALA SER ALA ASN LYS TYR ARG          
SEQRES   6 Z  344  TYR MET SER LEU LYS GLN ASP HIS THR VAL LYS GLU GLY          
SEQRES   7 Z  344  THR MET ASP ASP ILE LYS ILE SER THR SER GLY PRO CYS          
SEQRES   8 Z  344  ARG ARG LEU SER TYR LYS GLY TYR PHE LEU LEU ALA LYS          
SEQRES   9 Z  344  CYS PRO PRO GLY ASP SER VAL THR VAL SER ILE VAL SER          
SEQRES  10 Z  344  SER ASN SER ALA THR SER CYS THR LEU ALA ARG LYS ILE          
SEQRES  11 Z  344  LYS PRO LYS PHE VAL GLY ARG GLU LYS TYR ASP LEU PRO          
SEQRES  12 Z  344  PRO VAL HIS GLY LYS LYS ILE PRO CYS THR VAL TYR ASP          
SEQRES  13 Z  344  ARG LEU LYS GLU THR THR ALA GLY TYR ILE THR MET HIS          
SEQRES  14 Z  344  ARG PRO ARG PRO HIS ALA TYR THR SER TYR LEU GLU GLU          
SEQRES  15 Z  344  SER SER GLY LYS VAL TYR ALA LYS PRO PRO SER GLY LYS          
SEQRES  16 Z  344  ASN ILE THR TYR GLU CYS LYS CYS GLY ASP TYR LYS THR          
SEQRES  17 Z  344  GLY THR VAL SER THR ARG THR GLU ILE THR GLY CYS THR          
SEQRES  18 Z  344  ALA ILE LYS GLN CYS VAL ALA TYR LYS SER ASP GLN THR          
SEQRES  19 Z  344  LYS TRP VAL PHE ASN SER PRO ASP LEU ILE ARG HIS ASP          
SEQRES  20 Z  344  ASP HIS THR ALA GLN GLY LYS LEU HIS LEU PRO PHE LYS          
SEQRES  21 Z  344  LEU ILE PRO SER THR CYS MET VAL PRO VAL ALA HIS ALA          
SEQRES  22 Z  344  PRO ASN VAL ILE HIS GLY PHE LYS HIS ILE SER LEU GLN          
SEQRES  23 Z  344  LEU ASP THR ASP HIS LEU THR LEU LEU THR THR ARG ARG          
SEQRES  24 Z  344  LEU GLY ALA ASN PRO GLU PRO THR THR GLU TRP ILE VAL          
SEQRES  25 Z  344  GLY LYS THR VAL ARG ASN PHE THR VAL ASP ARG ASP GLY          
SEQRES  26 Z  344  LEU GLU TYR ILE TRP GLY ASN HIS GLU PRO VAL ARG VAL          
SEQRES  27 Z  344  TYR ALA GLN GLU SER ALA                                      
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           1          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  CA  TYR A   1      37.223  40.126 273.379  1.00 62.13           C  
ATOM      2  CA  GLU A   2      37.430  43.366 271.396  1.00 56.69           C  
ATOM      3  CA  HIS A   3      34.127  44.305 269.744  1.00 50.50           C  
ATOM      4  CA  ALA A   4      33.472  47.036 267.186  1.00 68.72           C  
ATOM      5  CA  THR A   5      29.999  48.614 266.925  1.00 63.15           C  
ATOM      6  CA  THR A   6      28.605  52.041 266.053  1.00 48.44           C  
ATOM      7  CA  VAL A   7      26.108  53.526 268.480  1.00 54.62           C  
ATOM      8  CA  PRO A   8      23.862  56.411 267.391  1.00 53.68           C  
ATOM      9  CA  ASN A   9      24.409  59.481 269.562  1.00 42.31           C  
ATOM     10  CA  VAL A  10      21.047  59.950 271.262  1.00 46.04           C  
ATOM     11  CA  PRO A  11      20.588  60.273 275.036  1.00 53.66           C  
ATOM     12  CA  GLN A  12      18.686  57.585 276.996  1.00 65.83           C  
ATOM     13  CA  ILE A  13      18.002  55.325 274.020  1.00 65.34           C  
ATOM     14  CA  PRO A  14      19.578  51.865 274.573  1.00 50.85           C  
ATOM     15  CA  TYR A  15      21.310  50.007 271.752  1.00 54.88           C  
ATOM     16  CA  LYS A  16      20.876  46.235 271.677  1.00 55.86           C  
ATOM     17  CA  ALA A  17      23.508  44.162 269.880  1.00 65.23           C  
ATOM     18  CA  LEU A  18      24.814  40.588 269.840  1.00 65.67           C  
ATOM     19  CA  VAL A  19      28.366  39.493 270.490  1.00 65.12           C  
ATOM     20  CA  GLU A  20      29.137  36.636 268.102  1.00 85.56           C  
ATOM     21  CA  ARG A  21      32.161  34.500 268.978  1.00 89.87           C  
ATOM     22  CA  ALA A  22      33.149  31.101 267.578  1.00 90.42           C  
ATOM     23  CA  GLY A  23      31.986  28.313 269.877  1.00 66.49           C  
ATOM     24  CA  TYR A  24      31.050  30.874 272.517  1.00 52.86           C  
ATOM     25  CA  ALA A  25      27.420  31.713 273.317  1.00 67.09           C  
ATOM     26  CA  PRO A  26      26.015  35.126 272.268  1.00 57.34           C  
ATOM     27  CA  LEU A  27      26.341  37.986 274.740  1.00 30.38           C  
ATOM     28  CA  ASN A  28      23.919  40.387 276.360  1.00 40.84           C  
ATOM     29  CA  LEU A  29      25.022  43.806 275.088  1.00 41.35           C  
ATOM     30  CA  GLU A  30      23.118  47.044 275.639  1.00 28.95           C  
ATOM     31  CA  ILE A  31      24.747  50.483 275.525  1.00 36.24           C  
ATOM     32  CA  THR A  32      22.974  53.609 276.738  1.00 37.13           C  
ATOM     33  CA  VAL A  33      24.556  57.011 276.094  1.00 59.56           C  
ATOM     34  CA  MET A  34      23.250  58.533 279.303  1.00 58.66           C  
ATOM     35  CA  SER A  35      24.754  61.957 278.728  1.00 62.62           C  
ATOM     36  CA  SER A  36      26.738  63.692 276.008  1.00 54.63           C  
ATOM     37  CA  GLU A  37      28.686  66.918 276.539  1.00 53.98           C  
ATOM     38  CA  VAL A  38      30.342  68.970 273.832  1.00 46.04           C  
ATOM     39  CA  LEU A  39      33.097  71.035 275.428  1.00 50.20           C  
ATOM     40  CA  PRO A  40      34.840  73.585 273.222  1.00 54.06           C  
ATOM     41  CA  SER A  41      37.817  75.763 274.169  1.00 53.42           C  
ATOM     42  CA  THR A  42      37.053  79.182 275.576  1.00 67.26           C  
ATOM     43  CA  ASN A  43      39.479  82.089 275.204  1.00 53.31           C  
ATOM     44  CA  GLN A  44      37.701  84.779 277.230  1.00 50.73           C  
ATOM     45  CA  GLU A  45      38.570  88.039 275.491  1.00 39.34           C  
ATOM     46  CA  TYR A  46      37.067  90.886 277.511  1.00 39.11           C  
ATOM     47  CA  ILE A  47      34.377  91.980 279.903  1.00 40.77           C  
ATOM     48  CA  THR A  48      31.956  94.775 279.104  1.00 38.47           C  
ATOM     49  CA  CYS A  49      29.137  96.602 280.815  1.00 43.67           C  
ATOM     50  CA  LYS A  50      27.371  99.882 281.513  1.00 57.83           C  
ATOM     51  CA  PHE A  51      30.159 102.455 281.721  1.00 39.52           C  
ATOM     52  CA  THR A  52      30.039 105.582 283.836  1.00 57.00           C  
ATOM     53  CA  THR A  53      31.441 108.890 282.636  1.00 53.75           C  
ATOM     54  CA  VAL A  54      33.440 110.954 285.082  1.00 56.13           C  
ATOM     55  CA  VAL A  55      33.770 114.679 284.568  1.00 43.47           C  
ATOM     56  CA  PRO A  56      36.366 116.459 286.736  1.00 42.25           C  
ATOM     57  CA  SER A  57      35.844 120.174 287.399  1.00 25.58           C  
ATOM     58  CA  PRO A  58      37.317 122.019 284.411  1.00 26.33           C  
ATOM     59  CA  LYS A  59      40.711 123.607 284.900  1.00 22.95           C  
ATOM     60  CA  ILE A  60      40.506 127.264 283.868  1.00 28.72           C  
ATOM     61  CA  LYS A  61      43.472 129.650 284.150  1.00 45.19           C  
ATOM     62  CA  CYS A  62      42.215 133.495 283.937  1.00 27.70           C  
ATOM     63  CA  CYS A  63      44.533 135.067 281.362  1.00 36.92           C  
ATOM     64  CA  GLY A  64      46.373 131.903 280.351  1.00 45.04           C  
ATOM     65  CA  SER A  65      46.699 129.380 277.533  1.00 63.45           C  
ATOM     66  CA  LEU A  66      45.448 125.908 278.457  1.00 59.22           C  
ATOM     67  CA  GLU A  67      46.614 123.452 275.765  1.00 63.61           C  
ATOM     68  CA  CYS A  68      46.107 119.714 276.259  1.00 58.10           C  
ATOM     69  CA  GLN A  69      48.605 116.985 277.041  1.00 63.47           C  
ATOM     70  CA  PRO A  70      48.379 113.388 275.800  1.00 71.48           C  
ATOM     71  CA  ALA A  71      46.689 112.197 278.998  1.00 70.00           C  
ATOM     72  CA  ALA A  72      45.925 108.536 278.299  1.00 71.07           C  
ATOM     73  CA  HIS A  73      43.654 106.919 280.885  1.00 68.85           C  
ATOM     74  CA  ALA A  74      40.540 105.061 279.737  1.00 56.65           C  
ATOM     75  CA  ASP A  75      38.054 107.007 277.627  1.00 38.37           C  
ATOM     76  CA  TYR A  76      39.821 110.318 278.198  1.00 27.45           C  
ATOM     77  CA  THR A  77      38.918 113.305 276.023  1.00 34.65           C  
ATOM     78  CA  CYS A  78      40.051 116.929 276.376  1.00 35.04           C  
ATOM     79  CA  LYS A  79      39.170 119.982 274.347  1.00 47.93           C  
ATOM     80  CA  VAL A  80      40.658 123.445 274.567  1.00 46.03           C  
ATOM     81  CA  PHE A  81      37.973 126.107 274.480  1.00 36.68           C  
ATOM     82  CA  GLY A  82      39.162 129.669 274.008  1.00 51.84           C  
ATOM     83  CA  GLY A  83      37.624 133.022 274.852  1.00 60.82           C  
ATOM     84  CA  VAL A  84      35.234 131.849 277.538  1.00 45.74           C  
ATOM     85  CA  TYR A  85      34.187 133.838 280.615  1.00 40.35           C  
ATOM     86  CA  PRO A  86      34.806 137.593 280.987  1.00 38.92           C  
ATOM     87  CA  PHE A  87      35.590 139.608 284.130  1.00 35.21           C  
ATOM     88  CA  MET A  88      33.983 139.656 287.567  1.00 52.19           C  
ATOM     89  CA  TRP A  89      31.245 136.992 287.526  1.00 48.20           C  
ATOM     90  CA  GLY A  90      29.681 135.758 284.293  1.00 47.53           C  
ATOM     91  CA  GLY A  91      32.054 132.989 283.812  1.00 30.53           C  
ATOM     92  CA  ALA A  92      34.433 132.794 286.789  1.00 38.23           C  
ATOM     93  CA  GLN A  93      36.401 135.294 288.831  1.00 39.05           C  
ATOM     94  CA  CYS A  94      38.722 136.604 286.118  1.00 25.34           C  
ATOM     95  CA  PHE A  95      39.448 140.059 284.699  1.00 23.23           C  
ATOM     96  CA  CYS A  96      40.076 139.531 280.985  1.00 35.34           C  
ATOM     97  CA  ASP A  97      37.530 138.920 278.218  1.00 45.23           C  
ATOM     98  CA  SER A  98      38.895 137.345 275.035  1.00 69.15           C  
ATOM     99  CA  GLU A  99      42.057 136.001 276.586  1.00 60.77           C  
ATOM    100  CA  ASN A 100      40.389 133.137 278.460  1.00 30.07           C  
ATOM    101  CA  SER A 101      40.567 129.371 278.070  1.00 26.10           C  
ATOM    102  CA  GLN A 102      38.887 126.307 279.548  1.00 22.39           C  
ATOM    103  CA  MET A 103      39.960 122.684 279.214  1.00 26.61           C  
ATOM    104  CA  SER A 104      37.091 120.231 279.167  1.00 43.39           C  
ATOM    105  CA  GLU A 105      38.190 116.710 279.995  1.00 36.51           C  
ATOM    106  CA  ALA A 106      36.199 113.543 280.636  1.00 43.82           C  
ATOM    107  CA  TYR A 107      36.692 109.776 280.680  1.00 38.31           C  
ATOM    108  CA  VAL A 108      34.684 106.606 281.346  1.00 41.61           C  
ATOM    109  CA  GLU A 109      34.822 104.024 284.149  1.00 57.66           C  
ATOM    110  CA  LEU A 110      32.866 100.894 285.026  1.00 50.96           C  
ATOM    111  CA  SER A 111      29.516 101.161 286.741  1.00 59.00           C  
ATOM    112  CA  ALA A 112      29.252 100.872 290.499  1.00 60.56           C  
ATOM    113  CA  ASP A 113      27.489  97.704 289.452  1.00 62.21           C  
ATOM    114  CA  CYS A 114      29.481  96.620 286.362  1.00 41.37           C  
ATOM    115  CA  ALA A 115      30.261  93.488 288.325  1.00 45.71           C  
ATOM    116  CA  SER A 116      26.713  92.389 289.066  1.00 48.28           C  
ATOM    117  CA  ASP A 117      25.612  92.795 285.411  1.00 49.12           C  
ATOM    118  CA  HIS A 118      28.080  92.395 282.559  1.00 33.40           C  
ATOM    119  CA  ALA A 119      28.786  90.187 279.601  1.00 33.03           C  
ATOM    120  CA  GLN A 120      31.738  88.178 278.403  1.00 33.15           C  
ATOM    121  CA  ALA A 121      33.200  88.297 274.921  1.00 35.10           C  
ATOM    122  CA  ILE A 122      34.502  84.822 274.264  1.00 31.25           C  
ATOM    123  CA  LYS A 123      36.276  83.117 271.388  1.00 21.15           C  
ATOM    124  CA  VAL A 124      35.371  79.485 270.801  1.00 36.05           C  
ATOM    125  CA  HIS A 125      37.641  77.001 269.077  1.00 42.32           C  
ATOM    126  CA  THR A 126      37.618  73.286 268.322  1.00 60.84           C  
ATOM    127  CA  ALA A 127      35.968  71.093 270.948  1.00 57.78           C  
ATOM    128  CA  ALA A 128      36.059  67.723 272.610  1.00 58.60           C  
ATOM    129  CA  MET A 129      33.075  65.653 273.739  1.00 52.48           C  
ATOM    130  CA  LYS A 130      32.691  63.350 276.723  1.00 46.62           C  
ATOM    131  CA  VAL A 131      29.951  60.706 276.853  1.00 52.71           C  
ATOM    132  CA  GLY A 132      28.345  59.091 279.895  1.00 64.11           C  
ATOM    133  CA  LEU A 133      28.005  55.528 278.694  1.00 53.53           C  
ATOM    134  CA  ARG A 134      26.285  52.636 280.418  1.00 27.81           C  
ATOM    135  CA  ILE A 135      27.104  49.207 279.052  1.00 38.00           C  
ATOM    136  CA  VAL A 136      25.601  45.954 280.261  1.00 35.48           C  
ATOM    137  CA  TYR A 137      27.080  42.546 279.486  1.00 36.01           C  
ATOM    138  CA  GLY A 138      25.569  39.323 280.777  1.00 36.07           C  
ATOM    139  CA  ASN A 139      24.783  39.496 284.494  1.00 55.54           C  
ATOM    140  CA  THR A 140      26.844  42.663 285.059  1.00 39.52           C  
ATOM    141  CA  THR A 141      26.292  46.324 284.157  1.00 39.61           C  
ATOM    142  CA  SER A 142      29.077  48.896 284.059  1.00 49.12           C  
ATOM    143  CA  PHE A 143      29.561  52.515 283.020  1.00 46.63           C  
ATOM    144  CA  LEU A 144      32.425  54.762 281.982  1.00 61.77           C  
ATOM    145  CA  ASP A 145      32.817  58.358 280.822  1.00 54.32           C  
ATOM    146  CA  VAL A 146      34.745  58.491 277.589  1.00 48.79           C  
ATOM    147  CA  TYR A 147      36.116  61.260 275.383  1.00 45.36           C  
ATOM    148  CA  VAL A 148      35.319  60.846 271.722  1.00 46.58           C  
ATOM    149  CA  ASN A 149      38.547  60.338 269.809  1.00 58.45           C  
ATOM    150  CA  GLY A 150      40.171  57.188 268.486  1.00 63.07           C  
ATOM    151  CA  VAL A 151      42.572  57.371 271.421  1.00 61.04           C  
ATOM    152  CA  THR A 152      41.635  58.002 275.057  1.00 47.97           C  
ATOM    153  CA  PRO A 153      40.211  54.941 276.833  1.00 43.75           C  
ATOM    154  CA  GLY A 154      37.903  55.537 279.794  1.00 63.81           C  
ATOM    155  CA  THR A 155      39.846  53.594 282.413  1.00 67.33           C  
ATOM    156  CA  SER A 156      36.726  51.854 283.719  1.00 69.49           C  
ATOM    157  CA  LYS A 157      38.590  49.544 286.098  1.00 60.07           C  
ATOM    158  CA  ASP A 158      37.692  46.422 284.120  1.00 47.29           C  
ATOM    159  CA  LEU A 159      36.652  47.067 280.532  1.00 46.62           C  
ATOM    160  CA  LYS A 160      38.563  49.166 277.998  1.00 50.89           C  
ATOM    161  CA  VAL A 161      36.144  51.340 276.016  1.00 62.14           C  
ATOM    162  CA  ILE A 162      37.679  53.726 273.491  1.00 53.04           C  
ATOM    163  CA  ALA A 163      35.086  55.798 271.658  1.00 49.97           C  
ATOM    164  CA  GLY A 164      36.159  56.431 268.077  1.00 49.94           C  
ATOM    165  CA  PRO A 165      35.972  59.878 266.455  1.00 61.84           C  
ATOM    166  CA  ILE A 166      32.419  61.162 266.106  1.00 70.44           C  
ATOM    167  CA  SER A 167      30.908  60.798 262.605  1.00 75.77           C  
ATOM    168  CA  ALA A 168      30.249  64.512 261.965  1.00 72.27           C  
ATOM    169  CA  SER A 169      31.997  67.429 263.635  1.00 81.61           C  
ATOM    170  CA  PHE A 170      29.127  69.655 264.712  1.00 59.69           C  
ATOM    171  CA  THR A 171      28.986  72.615 267.084  1.00 57.50           C  
ATOM    172  CA  PRO A 172      26.123  74.863 268.231  1.00 55.63           C  
ATOM    173  CA  PHE A 173      28.590  77.738 268.539  1.00 59.80           C  
ATOM    174  CA  ASP A 174      30.366  80.268 266.317  1.00 53.63           C  
ATOM    175  CA  HIS A 175      34.001  81.309 266.680  1.00 42.40           C  
ATOM    176  CA  LYS A 176      32.739  84.299 268.659  1.00 37.94           C  
ATOM    177  CA  VAL A 177      30.099  84.042 271.384  1.00 37.77           C  
ATOM    178  CA  VAL A 178      28.751  86.323 274.080  1.00 35.00           C  
ATOM    179  CA  ILE A 179      27.741  85.109 277.500  1.00 32.69           C  
ATOM    180  CA  HIS A 180      25.466  87.415 279.426  1.00 30.41           C  
ATOM    181  CA  ARG A 181      23.822  86.046 282.530  1.00 54.46           C  
ATOM    182  CA  GLY A 182      23.442  82.315 282.174  1.00 75.06           C  
ATOM    183  CA  LEU A 183      22.819  82.935 278.564  1.00 46.06           C  
ATOM    184  CA  VAL A 184      24.984  82.586 275.527  1.00 35.56           C  
ATOM    185  CA  TYR A 185      24.454  84.207 272.117  1.00 38.52           C  
ATOM    186  CA  ASN A 186      26.357  83.765 268.877  1.00 47.60           C  
ATOM    187  CA  TYR A 187      27.544  87.373 268.390  1.00 49.77           C  
ATOM    188  CA  ASP A 188      30.507  88.656 266.352  1.00 45.53           C  
ATOM    189  CA  PHE A 189      31.736  91.103 269.011  1.00 44.57           C  
ATOM    190  CA  PRO A 190      34.691  93.217 267.908  1.00 42.84           C  
ATOM    191  CA  GLU A 191      38.299  92.314 268.721  1.00 43.44           C  
ATOM    192  CA  TYR A 192      39.783  93.633 271.920  1.00 43.95           C  
ATOM    193  CA  GLY A 193      40.978  97.071 270.940  1.00 48.34           C  
ATOM    194  CA  ALA A 194      38.963  97.770 267.816  1.00 46.24           C  
ATOM    195  CA  MET A 195      35.810  99.057 269.465  1.00 40.69           C  
ATOM    196  CA  LYS A 196      32.907 100.947 267.945  1.00 48.74           C  
ATOM    197  CA  PRO A 197      30.880 103.149 270.319  1.00 48.07           C  
ATOM    198  CA  GLY A 198      27.220 102.596 271.151  1.00 55.96           C  
ATOM    199  CA  ALA A 199      27.570  99.090 269.698  1.00 57.28           C  
ATOM    200  CA  PHE A 200      28.379  96.004 271.786  1.00 36.67           C  
ATOM    201  CA  GLY A 201      31.822  96.150 273.310  1.00 40.58           C  
ATOM    202  CA  ASP A 202      32.042  99.923 273.344  1.00 50.12           C  
ATOM    203  CA  ILE A 203      34.162  99.592 276.480  1.00 54.67           C  
ATOM    204  CA  GLN A 204      36.462  96.621 277.098  1.00 46.16           C  
ATOM    205  CA  ALA A 205      38.450  95.070 279.932  1.00 46.56           C  
ATOM    206  CA  THR A 206      40.375  91.812 280.327  1.00 50.89           C  
ATOM    207  CA  SER A 207      38.906  90.928 283.723  1.00 68.76           C  
ATOM    208  CA  LEU A 208      36.322  92.394 286.099  1.00 83.59           C  
ATOM    209  CA  THR A 209      39.162  93.739 288.242  1.00 86.02           C  
ATOM    210  CA  SER A 210      39.046  96.734 285.901  1.00 80.94           C  
ATOM    211  CA  LYS A 211      42.338  95.521 284.075  1.00 52.82           C  
ATOM    212  CA  ASP A 212      43.791  98.054 281.424  1.00 68.52           C  
ATOM    213  CA  LEU A 213      40.280  98.897 280.157  1.00 54.19           C  
ATOM    214  CA  ILE A 214      39.967 100.573 276.761  1.00 44.41           C  
ATOM    215  CA  ALA A 215      36.806 102.464 275.818  1.00 46.32           C  
ATOM    216  CA  SER A 216      35.534 104.362 272.768  1.00 49.74           C  
ATOM    217  CA  THR A 217      32.254 106.171 273.524  1.00 61.37           C  
ATOM    218  CA  ASP A 218      32.079 109.121 271.076  1.00 49.46           C  
ATOM    219  CA  ILE A 219      32.251 111.750 273.800  1.00 54.76           C  
ATOM    220  CA  ARG A 220      31.892 115.254 272.456  1.00 41.11           C  
ATOM    221  CA  LEU A 221      32.788 118.375 274.410  1.00 44.58           C  
ATOM    222  CA  LEU A 222      30.808 121.557 273.971  1.00 39.36           C  
ATOM    223  CA  LYS A 223      31.877 125.165 274.379  1.00 36.12           C  
ATOM    224  CA  PRO A 224      30.333 126.140 277.725  1.00 30.25           C  
ATOM    225  CA  SER A 225      28.203 129.289 277.946  1.00 47.08           C  
ATOM    226  CA  ALA A 226      29.113 132.088 280.352  1.00 48.00           C  
ATOM    227  CA  LYS A 227      26.787 132.184 283.339  1.00 53.89           C  
ATOM    228  CA  ASN A 228      28.145 129.166 285.239  1.00 41.29           C  
ATOM    229  CA  VAL A 229      31.149 126.876 285.214  1.00 51.80           C  
ATOM    230  CA  HIS A 230      29.437 123.838 283.767  1.00 45.87           C  
ATOM    231  CA  VAL A 231      31.096 121.413 281.369  1.00 48.04           C  
ATOM    232  CA  PRO A 232      28.771 120.300 278.540  1.00 38.66           C  
ATOM    233  CA  TYR A 233      29.210 117.105 276.555  1.00 40.46           C  
ATOM    234  CA  THR A 234      27.342 114.723 274.300  1.00 43.39           C  
ATOM    235  CA  GLN A 235      28.250 111.077 274.145  1.00 45.43           C  
ATOM    236  CA  ALA A 236      27.160 107.862 272.529  1.00 58.59           C  
ATOM    237  CA  SER A 237      24.701 105.378 273.965  1.00 75.78           C  
ATOM    238  CA  SER A 238      25.684 102.406 276.149  1.00 51.89           C  
ATOM    239  CA  GLY A 239      26.583  99.769 273.563  1.00 33.35           C  
ATOM    240  CA  PHE A 240      25.855  97.283 276.314  1.00 36.14           C  
ATOM    241  CA  GLU A 241      22.353  98.246 277.356  1.00 46.68           C  
ATOM    242  CA  MET A 242      21.900  98.720 273.625  1.00 36.69           C  
ATOM    243  CA  TRP A 243      22.893  95.143 272.943  1.00 22.36           C  
ATOM    244  CA  LYS A 244      20.804  93.934 275.882  1.00 39.86           C  
ATOM    245  CA  ASN A 245      17.562  95.475 274.498  1.00 48.42           C  
ATOM    246  CA  ASN A 246      18.487  93.755 271.281  1.00 39.39           C  
ATOM    247  CA  SER A 247      20.077  90.512 272.382  1.00 52.46           C  
ATOM    248  CA  GLY A 248      18.326  87.710 270.595  1.00 63.25           C  
ATOM    249  CA  ARG A 249      16.736  84.629 271.902  1.00 56.81           C  
ATOM    250  CA  PRO A 250      19.600  82.702 273.645  1.00 28.98           C  
ATOM    251  CA  LEU A 251      21.266  79.696 272.069  1.00 35.08           C  
ATOM    252  CA  GLN A 252      19.773  77.540 274.803  1.00 46.31           C  
ATOM    253  CA  GLU A 253      16.622  78.300 272.811  1.00 42.77           C  
ATOM    254  CA  THR A 254      17.942  78.098 269.253  1.00 41.08           C  
ATOM    255  CA  ALA A 255      20.433  75.219 269.418  1.00 49.61           C  
ATOM    256  CA  PRO A 256      20.374  73.259 266.090  1.00 57.53           C  
ATOM    257  CA  PHE A 257      20.105  69.708 267.526  1.00 36.18           C  
ATOM    258  CA  GLY A 258      18.077  70.015 270.676  1.00 34.26           C  
ATOM    259  CA  CYS A 259      21.242  70.731 272.625  1.00 46.46           C  
ATOM    260  CA  LYS A 260      20.895  72.019 276.174  1.00 59.57           C  
ATOM    261  CA  ILE A 261      23.443  74.865 276.271  1.00 70.57           C  
ATOM    262  CA  ALA A 262      25.248  75.316 279.604  1.00 69.76           C  
ATOM    263  CA  VAL A 263      27.448  77.929 281.295  1.00 63.76           C  
ATOM    264  CA  ASN A 264      30.027  77.697 283.418  1.00 64.50           C  
ATOM    265  CA  PRO A 265      32.020  75.291 281.400  1.00 55.82           C  
ATOM    266  CA  LEU A 266      30.720  76.335 277.968  1.00 55.02           C  
ATOM    267  CA  ARG A 267      28.962  73.144 276.904  1.00 25.00           C  
ATOM    268  CA  ALA A 268      26.267  71.580 274.728  1.00 43.38           C  
ATOM    269  CA  VAL A 269      24.566  69.006 276.975  1.00 65.48           C  
ATOM    270  CA  ASP A 270      22.713  66.079 275.399  1.00 67.82           C  
ATOM    271  CA  CYS A 271      22.806  66.969 271.724  1.00 57.33           C  
ATOM    272  CA  SER A 272      21.663  64.291 269.285  1.00 45.58           C  
ATOM    273  CA  TYR A 273      23.394  63.752 265.955  1.00 52.27           C  
ATOM    274  CA  GLY A 274      25.490  61.165 264.142  1.00 65.34           C  
ATOM    275  CA  ASN A 275      26.767  57.818 265.332  1.00 56.38           C  
ATOM    276  CA  ILE A 276      29.638  57.041 267.700  1.00 53.58           C  
ATOM    277  CA  PRO A 277      32.044  54.271 266.806  1.00 51.01           C  
ATOM    278  CA  ILE A 278      32.747  52.221 269.934  1.00 53.01           C  
ATOM    279  CA  SER A 279      35.332  49.550 270.687  1.00 62.34           C  
ATOM    280  CA  ILE A 280      34.663  47.342 273.703  1.00 41.39           C  
ATOM    281  CA  ASP A 281      36.964  44.900 275.524  1.00 32.93           C  
ATOM    282  CA  ILE A 282      34.849  42.217 277.235  1.00 59.73           C  
ATOM    283  CA  PRO A 283      36.704  40.329 279.986  1.00 56.65           C  
ATOM    284  CA  ASN A 284      36.644  36.617 279.135  1.00 54.03           C  
ATOM    285  CA  ALA A 285      35.762  36.201 282.811  1.00 52.68           C  
ATOM    286  CA  ALA A 286      32.005  36.359 282.236  1.00 61.99           C  
ATOM    287  CA  PHE A 287      30.672  36.041 278.687  1.00 59.53           C  
ATOM    288  CA  ILE A 288      30.089  32.290 278.608  1.00 48.21           C  
ATOM    289  CA  ARG A 289      31.234  29.599 276.173  1.00 36.69           C  
ATOM    290  CA  THR A 290      28.753  27.010 274.866  1.00 56.00           C  
ATOM    291  CA  SER A 291      29.065  24.426 277.640  1.00 36.99           C  
ATOM    292  CA  ASP A 292      25.818  25.437 279.344  1.00 42.03           C  
ATOM    293  CA  ALA A 293      22.543  25.417 277.410  1.00 53.83           C  
ATOM    294  CA  PRO A 294      22.063  21.622 281.962  1.00 45.61           C  
ATOM    295  CA  LEU A 295      21.301  21.130 278.263  1.00 48.81           C  
ATOM    296  CA  VAL A 296      19.108  23.250 275.992  1.00 33.23           C  
ATOM    297  CA  SER A 297      18.023  22.355 272.457  1.00 39.46           C  
ATOM    298  CA  THR A 298      15.502  23.266 269.756  1.00 58.12           C  
ATOM    299  CA  VAL A 299      14.038  26.774 269.649  1.00 69.11           C  
ATOM    300  CA  LYS A 300      11.445  27.874 267.090  1.00 61.37           C  
ATOM    301  CA  CYS A 301       9.623  31.204 266.981  1.00 57.52           C  
ATOM    302  CA  GLU A 302       5.905  31.918 266.543  1.00 55.84           C  
ATOM    303  CA  VAL A 303       4.312  35.380 266.612  1.00 51.26           C  
ATOM    304  CA  SER A 304       0.767  35.603 267.989  1.00 68.32           C  
ATOM    305  CA  GLU A 305      -0.030  39.302 267.552  1.00 63.25           C  
ATOM    306  CA  CYS A 306       1.799  42.433 266.396  1.00 55.15           C  
ATOM    307  CA  THR A 307       1.320  46.172 265.956  1.00 39.21           C  
ATOM    308  CA  TYR A 308       3.525  48.404 263.799  1.00 23.93           C  
ATOM    309  CA  SER A 309       5.453  51.259 265.461  1.00 46.57           C  
ATOM    310  CA  ALA A 310       3.924  50.933 268.935  1.00 52.88           C  
ATOM    311  CA  ASP A 311       5.512  50.870 272.389  1.00 71.33           C  
ATOM    312  CA  PHE A 312       5.286  47.084 272.759  1.00 57.11           C  
ATOM    313  CA  GLY A 313       2.620  45.710 270.437  1.00 59.16           C  
ATOM    314  CA  GLY A 314       4.632  42.627 269.539  1.00 44.87           C  
ATOM    315  CA  MET A 315       3.724  39.219 270.949  1.00 32.22           C  
ATOM    316  CA  ALA A 316       5.729  36.078 270.167  1.00 34.95           C  
ATOM    317  CA  THR A 317       6.070  32.653 271.787  1.00 30.81           C  
ATOM    318  CA  LEU A 318       8.961  30.184 271.782  1.00 32.98           C  
ATOM    319  CA  GLN A 319       8.564  26.401 271.809  1.00 29.19           C  
ATOM    320  CA  TYR A 320      11.560  24.248 272.707  1.00 44.50           C  
ATOM    321  CA  VAL A 321      12.902  21.401 274.841  1.00 42.09           C  
ATOM    322  CA  SER A 322      15.009  21.854 277.981  1.00 31.32           C  
ATOM    323  CA  ASP A 323      16.759  19.314 280.218  1.00 45.81           C  
ATOM    324  CA  ARG A 324      15.916  21.215 283.412  1.00 45.96           C  
ATOM    325  CA  GLU A 325      14.831  24.595 284.762  1.00 38.72           C  
ATOM    326  CA  GLY A 326      16.935  27.750 284.710  1.00 33.90           C  
ATOM    327  CA  GLN A 327      17.071  31.399 283.677  1.00 36.59           C  
ATOM    328  CA  CYS A 328      17.778  32.466 280.089  1.00 27.60           C  
ATOM    329  CA  PRO A 329      18.658  35.942 278.752  1.00 36.10           C  
ATOM    330  CA  VAL A 330      16.546  36.726 275.682  1.00 46.52           C  
ATOM    331  CA  HIS A 331      17.806  39.271 273.150  1.00 54.73           C  
ATOM    332  CA  SER A 332      17.488  40.266 269.484  1.00 42.42           C  
ATOM    333  CA  HIS A 333      20.464  40.144 267.103  1.00 60.44           C  
ATOM    334  CA  SER A 334      18.945  42.652 264.675  1.00 64.48           C  
ATOM    335  CA  SER A 335      17.967  46.285 265.235  1.00 83.47           C  
ATOM    336  CA  THR A 336      14.793  45.758 263.197  1.00 64.98           C  
ATOM    337  CA  ALA A 337      13.221  44.741 266.507  1.00 60.03           C  
ATOM    338  CA  THR A 338      13.862  44.874 270.251  1.00 60.32           C  
ATOM    339  CA  LEU A 339      12.523  42.871 273.197  1.00 37.34           C  
ATOM    340  CA  GLN A 340      10.735  44.351 276.219  1.00 57.74           C  
ATOM    341  CA  GLU A 341      12.416  41.831 278.495  1.00 70.68           C  
ATOM    342  CA  SER A 342      15.969  40.507 278.540  1.00 57.58           C  
ATOM    343  CA  THR A 343      15.556  37.476 280.814  1.00 65.45           C  
ATOM    344  CA  VAL A 344      13.069  34.596 280.967  1.00 79.11           C  
ATOM    345  CA  HIS A 345      12.307  31.758 283.401  1.00 63.08           C  
ATOM    346  CA  VAL A 346      12.742  28.669 281.238  1.00 47.49           C  
ATOM    347  CA  LEU A 347      10.606  25.760 282.414  1.00 42.67           C  
ATOM    348  CA  GLU A 348      10.321  22.183 281.166  1.00 43.78           C  
ATOM    349  CA  LYS A 349       6.983  22.985 279.506  1.00 63.74           C  
ATOM    350  CA  GLY A 350       8.773  24.277 276.421  1.00 26.43           C  
ATOM    351  CA  ALA A 351       6.776  27.482 276.057  1.00 37.80           C  
ATOM    352  CA  VAL A 352       8.060  31.037 276.492  1.00 38.27           C  
ATOM    353  CA  THR A 353       5.947  34.120 275.802  1.00 46.82           C  
ATOM    354  CA  VAL A 354       7.782  37.381 275.048  1.00 53.94           C  
ATOM    355  CA  HIS A 355       6.821  40.957 274.150  1.00 35.18           C  
ATOM    356  CA  PHE A 356       8.675  43.032 271.556  1.00 27.65           C  
ATOM    357  CA  SER A 357       8.565  46.386 269.775  1.00 32.74           C  
ATOM    358  CA  THR A 358       9.122  47.218 266.106  1.00 49.31           C  
ATOM    359  CA  ALA A 359       8.384  49.762 263.378  1.00 56.44           C  
ATOM    360  CA  SER A 360       7.950  47.703 260.213  1.00 48.66           C  
ATOM    361  CA  PRO A 361       5.229  45.789 258.320  1.00 38.43           C  
ATOM    362  CA  GLN A 362       6.953  42.463 257.648  1.00 50.31           C  
ATOM    363  CA  ALA A 363      10.056  42.326 259.837  1.00 56.65           C  
ATOM    364  CA  ASN A 364      12.802  39.699 260.007  1.00 61.99           C  
ATOM    365  CA  PHE A 365      14.756  39.317 263.247  1.00 48.22           C  
ATOM    366  CA  ILE A 366      16.923  36.673 264.927  1.00 43.76           C  
ATOM    367  CA  VAL A 367      15.835  36.157 268.538  1.00 42.04           C  
ATOM    368  CA  SER A 368      18.170  34.332 270.921  1.00 30.31           C  
ATOM    369  CA  LEU A 369      17.498  32.287 274.046  1.00 26.24           C  
ATOM    370  CA  CYS A 370      20.227  31.200 276.455  1.00 31.76           C  
ATOM    371  CA  GLY A 371      22.561  29.863 273.775  1.00 62.78           C  
ATOM    372  CA  LYS A 372      20.162  28.945 270.978  1.00 39.55           C  
ATOM    373  CA  LYS A 373      18.978  31.186 268.138  1.00 45.36           C  
ATOM    374  CA  THR A 374      15.959  31.294 265.819  1.00 50.45           C  
ATOM    375  CA  THR A 375      14.035  33.482 263.383  1.00 49.69           C  
ATOM    376  CA  CYS A 376      10.629  35.139 263.783  1.00 55.38           C  
ATOM    377  CA  ASN A 377       8.040  36.506 261.355  1.00 49.75           C  
ATOM    378  CA  ALA A 378       4.676  38.276 261.176  1.00 57.98           C  
ATOM    379  CA  GLU A 379       2.770  41.148 259.571  1.00 55.87           C  
ATOM    380  CA  CYS A 380       1.989  44.325 261.524  1.00 33.17           C  
TER     381      CYS A 380                                                      
ATOM    382  CA  PHE U   6      36.645 110.448 307.803  1.00 48.68           C  
ATOM    383  CA  THR U   7      36.482 113.379 305.998  1.00 40.03           C  
ATOM    384  CA  LEU U   8      39.012 115.116 303.787  1.00 37.27           C  
ATOM    385  CA  THR U   9      36.469 116.634 301.417  1.00 23.09           C  
ATOM    386  CA  SER U  10      33.295 118.721 301.807  1.00 33.37           C  
ATOM    387  CA  PRO U  11      29.874 119.068 300.057  1.00 26.74           C  
ATOM    388  CA  TYR U  12      29.814 121.146 296.864  1.00 51.28           C  
ATOM    389  CA  LEU U  13      27.204 122.895 294.706  1.00 51.62           C  
ATOM    390  CA  GLY U  14      26.074 121.849 291.246  1.00 50.69           C  
ATOM    391  CA  THR U  15      23.874 123.191 288.488  1.00 53.42           C  
ATOM    392  CA  CYS U  16      20.510 121.411 288.423  1.00 51.92           C  
ATOM    393  CA  SER U  17      17.622 121.436 285.952  1.00 53.47           C  
ATOM    394  CA  TYR U  18      14.661 121.433 288.365  1.00 37.20           C  
ATOM    395  CA  CYS U  19      14.608 122.568 292.005  1.00 36.40           C  
ATOM    396  CA  HIS U  20      11.156 122.648 293.664  1.00 46.73           C  
ATOM    397  CA  HIS U  21      10.476 125.258 291.001  1.00 27.61           C  
ATOM    398  CA  THR U  22      10.728 123.842 287.491  1.00 38.69           C  
ATOM    399  CA  VAL U  23      13.392 126.481 286.753  1.00 43.20           C  
ATOM    400  CA  PRO U  24      16.986 125.122 286.666  1.00 45.27           C  
ATOM    401  CA  CYS U  25      18.958 126.261 289.711  1.00 50.33           C  
ATOM    402  CA  PHE U  26      22.380 126.053 291.322  1.00 47.23           C  
ATOM    403  CA  SER U  27      21.719 124.111 294.489  1.00 36.41           C  
ATOM    404  CA  PRO U  28      23.305 121.445 296.723  1.00 27.87           C  
ATOM    405  CA  VAL U  29      22.135 117.835 296.470  1.00 41.79           C  
ATOM    406  CA  LYS U  30      22.990 118.058 292.766  1.00 37.48           C  
ATOM    407  CA  ILE U  31      22.533 114.652 291.189  1.00 43.47           C  
ATOM    408  CA  GLU U  32      25.397 113.688 288.882  1.00 64.95           C  
ATOM    409  CA  GLN U  33      24.766 109.993 288.215  1.00 47.60           C  
ATOM    410  CA  VAL U  34      22.456 107.145 289.141  1.00 31.64           C  
ATOM    411  CA  TRP U  35      22.729 103.368 288.921  1.00 23.64           C  
ATOM    412  CA  ASP U  36      19.826 101.168 287.924  1.00 46.19           C  
ATOM    413  CA  GLU U  37      21.689  97.939 287.288  1.00 62.53           C  
ATOM    414  CA  ALA U  38      20.714  95.567 290.074  1.00 55.43           C  
ATOM    415  CA  ASP U  39      18.316  92.655 289.633  1.00 56.98           C  
ATOM    416  CA  ASP U  40      16.850  93.808 292.907  1.00 56.27           C  
ATOM    417  CA  ASN U  41      14.617  96.865 292.758  1.00 50.64           C  
ATOM    418  CA  THR U  42      17.308  99.013 294.395  1.00 52.19           C  
ATOM    419  CA  ILE U  43      18.932 102.257 293.270  1.00 41.05           C  
ATOM    420  CA  ARG U  44      22.299 103.935 293.820  1.00 34.76           C  
ATOM    421  CA  ILE U  45      22.297 107.750 293.765  1.00 24.73           C  
ATOM    422  CA  GLN U  46      25.252 110.156 293.609  1.00 23.56           C  
ATOM    423  CA  THR U  47      24.684 113.598 295.152  1.00 29.20           C  
ATOM    424  CA  SER U  48      26.833 116.622 296.002  1.00 37.61           C  
ATOM    425  CA  ALA U  49      25.927 116.794 299.684  1.00 25.46           C  
ATOM    426  CA  GLN U  50      27.821 114.862 302.364  1.00 25.78           C  
ATOM    427  CA  PHE U  51      26.303 112.606 305.010  1.00 25.24           C  
ATOM    428  CA  GLY U  52      27.365 110.714 308.128  1.00 32.12           C  
ATOM    429  CA  TYR U  53      29.132 113.802 309.450  1.00 30.11           C  
ATOM    430  CA  ASP U  54      28.440 117.344 310.647  1.00 31.71           C  
ATOM    431  CA  GLN U  55      29.861 120.621 309.338  1.00 45.83           C  
ATOM    432  CA  SER U  56      33.410 119.292 309.648  1.00 63.93           C  
ATOM    433  CA  GLY U  57      35.278 116.050 310.298  1.00 56.44           C  
ATOM    434  CA  ALA U  58      33.491 112.688 310.369  1.00 43.22           C  
ATOM    435  CA  ALA U  59      30.654 112.517 312.899  1.00 51.36           C  
ATOM    436  CA  SER U  60      28.595 109.367 312.451  1.00 60.67           C  
ATOM    437  CA  ALA U  61      25.052 108.156 313.126  1.00 69.39           C  
ATOM    438  CA  ASN U  62      22.473 110.398 311.454  1.00 34.94           C  
ATOM    439  CA  LYS U  63      23.982 113.711 310.356  1.00 24.67           C  
ATOM    440  CA  TYR U  64      24.702 115.361 307.003  1.00 25.76           C  
ATOM    441  CA  ARG U  65      26.274 118.608 305.820  1.00 24.81           C  
ATOM    442  CA  TYR U  66      26.080 120.741 302.697  1.00 23.27           C  
ATOM    443  CA  MET U  67      26.876 124.157 301.252  1.00 40.41           C  
ATOM    444  CA  SER U  68      24.680 127.187 301.866  1.00 44.09           C  
ATOM    445  CA  LEU U  69      21.872 128.859 299.973  1.00 57.33           C  
ATOM    446  CA  LYS U  70      24.483 131.519 299.251  1.00 51.23           C  
ATOM    447  CA  GLN U  71      28.122 131.105 298.208  1.00100.00           C  
ATOM    448  CA  ASP U  72      29.547 132.009 301.647  1.00100.00           C  
ATOM    449  CA  HIS U  73      31.162 128.578 301.598  1.00 57.00           C  
ATOM    450  CA  THR U  74      29.338 128.243 304.891  1.00 45.59           C  
ATOM    451  CA  VAL U  75      29.094 124.511 305.489  1.00 42.86           C  
ATOM    452  CA  LYS U  76      26.024 124.207 307.716  1.00 41.45           C  
ATOM    453  CA  GLU U  77      24.654 120.878 308.908  1.00 29.67           C  
ATOM    454  CA  GLY U  78      21.366 119.273 309.826  1.00 39.65           C  
ATOM    455  CA  THR U  79      20.052 115.880 310.896  1.00 34.75           C  
ATOM    456  CA  MET U  80      20.048 112.815 308.605  1.00 22.52           C  
ATOM    457  CA  ASP U  81      16.416 112.592 309.506  1.00 48.36           C  
ATOM    458  CA  ASP U  82      14.835 115.205 307.289  1.00 45.46           C  
ATOM    459  CA  ILE U  83      16.412 114.024 304.031  1.00 48.96           C  
ATOM    460  CA  LYS U  84      13.990 112.041 301.898  1.00 53.89           C  
ATOM    461  CA  ILE U  85      14.128 110.554 298.401  1.00 73.55           C  
ATOM    462  CA  SER U  86      11.312 110.360 295.878  1.00 59.40           C  
ATOM    463  CA  THR U  87      10.717 109.513 292.235  1.00 53.12           C  
ATOM    464  CA  SER U  88       6.986 109.386 291.636  1.00 60.04           C  
ATOM    465  CA  GLY U  89       6.031 108.521 295.195  1.00 60.46           C  
ATOM    466  CA  PRO U  90       7.667 107.516 298.467  1.00 67.35           C  
ATOM    467  CA  CYS U  91      11.193 106.148 298.723  1.00 57.19           C  
ATOM    468  CA  ARG U  92      12.935 104.791 301.775  1.00 47.97           C  
ATOM    469  CA  ARG U  93      16.699 105.038 301.904  1.00 35.67           C  
ATOM    470  CA  LEU U  94      18.799 102.234 303.303  1.00 51.83           C  
ATOM    471  CA  SER U  95      22.424 103.284 303.727  1.00 46.61           C  
ATOM    472  CA  TYR U  96      24.375 106.549 303.612  1.00 26.66           C  
ATOM    473  CA  LYS U  97      27.861 106.580 302.126  1.00 40.39           C  
ATOM    474  CA  GLY U  98      29.069 110.165 302.372  1.00 44.20           C  
ATOM    475  CA  TYR U  99      28.220 111.472 298.901  1.00 36.03           C  
ATOM    476  CA  PHE U 100      26.086 108.499 297.903  1.00 25.89           C  
ATOM    477  CA  LEU U 101      22.541 107.314 298.541  1.00 24.74           C  
ATOM    478  CA  LEU U 102      20.818 103.972 298.091  1.00 44.88           C  
ATOM    479  CA  ALA U 103      17.117 103.171 298.317  1.00 30.50           C  
ATOM    480  CA  LYS U 104      14.244 101.267 296.703  1.00 31.35           C  
ATOM    481  CA  CYS U 105      12.497 103.740 294.769  1.00 37.46           C  
ATOM    482  CA  PRO U 106       8.746 102.873 293.275  1.00 61.80           C  
ATOM    483  CA  PRO U 107       7.998 103.522 289.589  1.00 62.01           C  
ATOM    484  CA  GLY U 108      10.520 105.785 287.878  1.00 55.78           C  
ATOM    485  CA  ASP U 109      10.426 108.561 285.292  1.00 51.56           C  
ATOM    486  CA  SER U 110      12.650 110.994 287.183  1.00 44.86           C  
ATOM    487  CA  VAL U 111      14.459 111.213 290.513  1.00 64.32           C  
ATOM    488  CA  THR U 112      14.281 113.891 293.196  1.00 43.00           C  
ATOM    489  CA  VAL U 113      16.447 114.237 296.289  1.00 61.11           C  
ATOM    490  CA  SER U 114      15.750 116.970 298.809  1.00 51.91           C  
ATOM    491  CA  ILE U 115      15.624 118.232 302.388  1.00 52.08           C  
ATOM    492  CA  VAL U 116      12.324 119.288 303.960  1.00 54.18           C  
ATOM    493  CA  SER U 117      13.311 120.817 307.296  1.00 79.09           C  
ATOM    494  CA  SER U 118      10.077 122.694 307.474  1.00 73.56           C  
ATOM    495  CA  ASN U 119       8.453 125.365 305.308  1.00 75.33           C  
ATOM    496  CA  SER U 120      11.637 126.176 303.389  1.00 76.71           C  
ATOM    497  CA  ALA U 121      13.777 123.619 301.555  1.00 65.82           C  
ATOM    498  CA  THR U 122      15.505 122.805 298.264  1.00 63.84           C  
ATOM    499  CA  SER U 123      15.545 119.797 295.929  1.00 56.04           C  
ATOM    500  CA  CYS U 124      17.373 118.738 292.772  1.00 54.17           C  
ATOM    501  CA  THR U 125      15.720 116.256 290.417  1.00 57.52           C  
ATOM    502  CA  LEU U 126      17.173 114.204 287.601  1.00 65.90           C  
ATOM    503  CA  ALA U 127      15.680 113.143 284.328  1.00 66.25           C  
ATOM    504  CA  ARG U 128      16.499 109.429 284.582  1.00 69.23           C  
ATOM    505  CA  LYS U 129      14.157 106.570 283.674  1.00 64.22           C  
ATOM    506  CA  ILE U 130      13.838 103.613 286.050  1.00 76.16           C  
ATOM    507  CA  LYS U 131      12.028 100.390 285.272  1.00 56.76           C  
ATOM    508  CA  PRO U 132      10.099  97.679 287.106  1.00 58.38           C  
ATOM    509  CA  LYS U 133      12.618  94.937 287.811  1.00 57.15           C  
ATOM    510  CA  PHE U 134      11.926  92.808 284.608  1.00 72.22           C  
ATOM    511  CA  VAL U 135      14.136  89.749 284.818  1.00 70.83           C  
ATOM    512  CA  GLY U 136      12.148  86.645 283.955  1.00 63.41           C  
ATOM    513  CA  ARG U 137      10.667  85.846 280.563  1.00 52.26           C  
ATOM    514  CA  GLU U 138       7.420  87.201 281.925  1.00 50.16           C  
ATOM    515  CA  LYS U 139       6.592  90.875 282.079  1.00 44.89           C  
ATOM    516  CA  TYR U 140       5.723  92.116 285.549  1.00 50.46           C  
ATOM    517  CA  ASP U 141       5.617  95.463 287.318  1.00 67.36           C  
ATOM    518  CA  LEU U 142       5.659  94.025 290.805  1.00 61.05           C  
ATOM    519  CA  PRO U 143       7.043  90.776 292.241  1.00 68.17           C  
ATOM    520  CA  PRO U 144       4.106  88.338 292.441  1.00 46.69           C  
ATOM    521  CA  VAL U 145       2.986  87.110 295.861  1.00 76.91           C  
ATOM    522  CA  HIS U 146       3.597  83.619 294.563  1.00 55.19           C  
ATOM    523  CA  GLY U 147       5.790  82.802 291.598  1.00 36.47           C  
ATOM    524  CA  LYS U 148       9.088  81.107 290.942  1.00 48.89           C  
ATOM    525  CA  LYS U 149      12.543  81.778 292.343  1.00 60.98           C  
ATOM    526  CA  ILE U 150      15.091  82.749 289.720  1.00 53.66           C  
ATOM    527  CA  PRO U 151      18.779  83.697 289.733  1.00 60.39           C  
ATOM    528  CA  CYS U 152      19.167  87.468 289.609  1.00 96.94           C  
ATOM    529  CA  THR U 153      21.553  90.086 290.985  1.00 97.21           C  
ATOM    530  CA  VAL U 154      20.551  92.961 293.292  1.00 71.03           C  
ATOM    531  CA  TYR U 155      21.880  95.580 295.740  1.00 67.38           C  
ATOM    532  CA  ASP U 156      22.582  94.708 299.397  1.00 41.07           C  
ATOM    533  CA  LEU U 255      37.935 102.111 296.885  1.00 47.67           C  
ATOM    534  CA  HIS U 256      34.522 100.829 297.942  1.00 41.70           C  
ATOM    535  CA  LEU U 257      31.894 101.571 300.608  1.00 61.67           C  
ATOM    536  CA  PRO U 258      28.609 101.371 298.655  1.00 31.95           C  
ATOM    537  CA  PHE U 259      25.776  98.798 298.700  1.00 56.79           C  
ATOM    538  CA  LYS U 260      27.567  95.931 296.939  1.00 37.88           C  
ATOM    539  CA  LEU U 261      25.940  93.927 294.142  1.00 45.72           C  
ATOM    540  CA  ILE U 262      25.218  90.331 295.139  1.00 53.50           C  
ATOM    541  CA  PRO U 263      23.614  87.547 293.085  1.00 63.65           C  
ATOM    542  CA  SER U 264      20.482  86.072 294.688  1.00 76.04           C  
ATOM    543  CA  THR U 265      16.829  85.247 294.021  1.00 64.94           C  
ATOM    544  CA  CYS U 266      14.074  87.320 292.470  1.00 60.54           C  
ATOM    545  CA  MET U 267      10.515  86.102 292.216  1.00 61.23           C  
ATOM    546  CA  VAL U 268       9.281  86.056 288.641  1.00 55.53           C  
ATOM    547  CA  PRO U 269       4.394  84.036 287.760  1.00 31.63           C  
ATOM    548  CA  VAL U 270       3.530  80.857 285.904  1.00 39.31           C  
ATOM    549  CA  ALA U 271       1.208  80.953 282.911  1.00 50.21           C  
ATOM    550  CA  HIS U 272      -2.146  79.289 282.281  1.00 55.61           C  
ATOM    551  CA  ALA U 273      -1.295  75.909 280.785  1.00 45.91           C  
ATOM    552  CA  PRO U 274      -2.144  75.939 277.065  1.00 31.19           C  
ATOM    553  CA  ASN U 275      -4.962  73.650 276.088  1.00 41.16           C  
ATOM    554  CA  VAL U 276      -3.082  71.500 273.601  1.00 35.51           C  
ATOM    555  CA  ILE U 277      -4.529  69.540 270.734  1.00 51.07           C  
ATOM    556  CA  HIS U 278      -2.551  66.747 269.109  1.00 50.60           C  
ATOM    557  CA  GLY U 279      -3.354  65.851 265.510  1.00 47.94           C  
ATOM    558  CA  PHE U 280      -1.828  64.486 262.322  1.00 46.33           C  
ATOM    559  CA  LYS U 281       1.706  65.855 262.510  1.00 49.28           C  
ATOM    560  CA  HIS U 282       0.008  68.731 264.268  1.00 32.59           C  
ATOM    561  CA  ILE U 283      -0.169  70.707 267.495  1.00 38.19           C  
ATOM    562  CA  SER U 284      -2.620  73.573 267.791  1.00 28.40           C  
ATOM    563  CA  LEU U 285      -1.835  75.477 270.981  1.00 34.42           C  
ATOM    564  CA  GLN U 286      -4.879  77.180 272.481  1.00 38.41           C  
ATOM    565  CA  LEU U 287      -3.463  79.938 274.698  1.00 46.00           C  
ATOM    566  CA  ASP U 288      -5.188  82.382 277.043  1.00 58.43           C  
ATOM    567  CA  THR U 289      -3.010  84.645 279.196  1.00 55.34           C  
ATOM    568  CA  ASP U 290      -3.764  87.697 281.264  1.00 62.05           C  
ATOM    569  CA  HIS U 291      -0.307  89.045 280.466  1.00 42.96           C  
ATOM    570  CA  LEU U 292       2.748  88.765 278.246  1.00 42.07           C  
ATOM    571  CA  THR U 293       4.198  85.288 277.936  1.00 38.65           C  
ATOM    572  CA  LEU U 294       7.054  84.231 275.691  1.00 27.12           C  
ATOM    573  CA  LEU U 295       6.449  81.213 273.500  1.00 24.33           C  
ATOM    574  CA  THR U 296       9.365  79.307 272.072  1.00 33.97           C  
ATOM    575  CA  THR U 297       9.699  76.364 269.754  1.00 32.88           C  
ATOM    576  CA  ARG U 298      12.299  74.336 267.904  1.00 45.69           C  
ATOM    577  CA  ARG U 299      12.335  71.015 266.133  1.00 46.74           C  
ATOM    578  CA  LEU U 300      14.166  68.061 267.591  1.00 53.89           C  
ATOM    579  CA  GLY U 301      15.784  67.074 264.294  1.00 62.80           C  
ATOM    580  CA  ALA U 302      18.237  69.086 262.237  1.00 57.52           C  
ATOM    581  CA  ASN U 303      16.596  72.182 260.842  1.00 50.73           C  
ATOM    582  CA  PRO U 304      14.883  73.246 264.108  1.00 27.75           C  
ATOM    583  CA  GLU U 305      13.565  76.451 262.544  1.00 54.30           C  
ATOM    584  CA  PRO U 306      13.425  77.925 266.062  1.00 45.45           C  
ATOM    585  CA  THR U 307      10.514  80.272 266.738  1.00 52.98           C  
ATOM    586  CA  THR U 308      10.054  82.884 269.434  1.00 64.75           C  
ATOM    587  CA  GLU U 309       7.012  85.118 269.960  1.00 41.03           C  
ATOM    588  CA  TRP U 310       5.408  87.014 272.824  1.00 25.47           C  
ATOM    589  CA  ILE U 311       1.714  86.455 273.157  1.00 41.46           C  
ATOM    590  CA  VAL U 312      -1.165  88.048 275.035  1.00 57.05           C  
ATOM    591  CA  GLY U 313      -4.741  87.182 275.619  1.00 60.79           C  
ATOM    592  CA  LYS U 314      -6.401  84.683 273.355  1.00 61.08           C  
ATOM    593  CA  THR U 315      -5.081  82.967 270.294  1.00 59.70           C  
ATOM    594  CA  VAL U 316      -4.305  79.613 268.791  1.00 45.68           C  
ATOM    595  CA  ARG U 317      -1.014  78.558 267.267  1.00 56.94           C  
ATOM    596  CA  ASN U 318      -0.492  75.317 265.416  1.00 43.97           C  
ATOM    597  CA  PHE U 319       2.965  73.885 264.618  1.00 59.35           C  
ATOM    598  CA  THR U 320       4.322  71.365 262.448  1.00 58.54           C  
ATOM    599  CA  VAL U 321       5.473  67.852 264.095  1.00 53.94           C  
ATOM    600  CA  ASP U 322       8.328  66.988 261.743  1.00 58.74           C  
ATOM    601  CA  ARG U 323       8.207  63.327 262.721  1.00 47.49           C  
ATOM    602  CA  ASP U 324      11.068  64.029 265.122  1.00 46.80           C  
ATOM    603  CA  GLY U 325       8.620  65.944 267.279  1.00 29.95           C  
ATOM    604  CA  LEU U 326       9.454  69.335 268.752  1.00 35.02           C  
ATOM    605  CA  GLU U 327       9.936  71.163 272.012  1.00 35.49           C  
ATOM    606  CA  TYR U 328       7.964  74.164 273.181  1.00 20.57           C  
ATOM    607  CA  ILE U 329       8.668  76.346 276.197  1.00 23.10           C  
ATOM    608  CA  TRP U 330       5.800  78.599 277.137  1.00 26.50           C  
ATOM    609  CA  GLY U 331       6.287  81.490 279.546  1.00 36.48           C  
ATOM    610  CA  ASN U 332       8.817  80.140 282.077  1.00 46.37           C  
ATOM    611  CA  HIS U 333       6.939  76.875 282.167  1.00 41.39           C  
ATOM    612  CA  GLU U 334       8.868  73.907 281.767  1.00 65.16           C  
ATOM    613  CA  PRO U 335       9.785  72.974 278.539  1.00 52.48           C  
ATOM    614  CA  VAL U 336       7.593  70.172 277.192  1.00 53.05           C  
ATOM    615  CA  ARG U 337       8.174  68.480 273.893  1.00 38.22           C  
ATOM    616  CA  VAL U 338       5.690  66.601 271.767  1.00 62.30           C  
ATOM    617  CA  TYR U 339       6.126  63.843 269.203  1.00 45.08           C  
ATOM    618  CA  ALA U 340       3.981  62.061 266.616  1.00 54.91           C  
TER     619      ALA U 340                                                      
ATOM    620  CA  TYR D   1      45.622 111.138 251.897  1.00 65.40           C  
ATOM    621  CA  GLU D   2      44.998 107.390 252.090  1.00 65.20           C  
ATOM    622  CA  HIS D   3      47.624 105.353 250.226  1.00 58.36           C  
ATOM    623  CA  ALA D   4      47.583 101.640 249.424  1.00 67.33           C  
ATOM    624  CA  THR D   5      50.875  99.756 248.941  1.00 75.02           C  
ATOM    625  CA  THR D   6      52.138  96.232 249.602  1.00 61.26           C  
ATOM    626  CA  VAL D   7      55.396  95.926 251.505  1.00 51.99           C  
ATOM    627  CA  PRO D   8      57.351  92.650 251.441  1.00 53.11           C  
ATOM    628  CA  ASN D   9      57.771  91.224 254.938  1.00 52.00           C  
ATOM    629  CA  VAL D  10      61.530  91.305 255.460  1.00 52.59           C  
ATOM    630  CA  PRO D  11      63.235  92.918 258.468  1.00 53.03           C  
ATOM    631  CA  GLN D  12      65.486  95.986 258.007  1.00 61.72           C  
ATOM    632  CA  ILE D  13      64.984  96.292 254.254  1.00 60.57           C  
ATOM    633  CA  PRO D  14      63.443  99.702 253.381  1.00 60.50           C  
ATOM    634  CA  TYR D  15      60.747 100.032 250.728  1.00 63.25           C  
ATOM    635  CA  LYS D  16      60.867 103.145 248.557  1.00 59.92           C  
ATOM    636  CA  ALA D  17      57.650 104.292 246.887  1.00 69.68           C  
ATOM    637  CA  LEU D  18      56.157 107.461 245.400  1.00 71.64           C  
ATOM    638  CA  VAL D  19      52.953 109.144 246.468  1.00 67.97           C  
ATOM    639  CA  GLU D  20      51.236 110.432 243.330  1.00 91.60           C  
ATOM    640  CA  ARG D  21      48.531 113.054 243.865  1.00 86.83           C  
ATOM    641  CA  ALA D  22      46.900 115.336 241.293  1.00 85.57           C  
ATOM    642  CA  GLY D  23      48.561 118.751 241.283  1.00 82.13           C  
ATOM    643  CA  TYR D  24      50.495 117.823 244.413  1.00 54.43           C  
ATOM    644  CA  ALA D  25      54.235 117.095 244.332  1.00 73.18           C  
ATOM    645  CA  PRO D  26      55.449 113.490 244.843  1.00 67.30           C  
ATOM    646  CA  LEU D  27      56.161 112.372 248.398  1.00 34.74           C  
ATOM    647  CA  ASN D  28      59.146 110.881 250.166  1.00 47.33           C  
ATOM    648  CA  LEU D  29      57.925 107.453 251.300  1.00 41.04           C  
ATOM    649  CA  GLU D  30      60.127 104.762 252.825  1.00 30.18           C  
ATOM    650  CA  ILE D  31      58.797 101.975 255.052  1.00 35.37           C  
ATOM    651  CA  THR D  32      61.087  99.736 257.084  1.00 44.36           C  
ATOM    652  CA  VAL D  33      59.623  96.702 258.857  1.00 58.81           C  
ATOM    653  CA  MET D  34      62.022  96.905 261.777  1.00 63.00           C  
ATOM    654  CA  SER D  35      60.657  93.879 263.591  1.00 63.08           C  
ATOM    655  CA  SER D  36      58.010  91.241 262.978  1.00 56.43           C  
ATOM    656  CA  GLU D  37      56.580  89.003 265.705  1.00 56.96           C  
ATOM    657  CA  VAL D  38      54.268  86.063 265.164  1.00 52.81           C  
ATOM    658  CA  LEU D  39      52.351  85.456 268.381  1.00 57.95           C  
ATOM    659  CA  PRO D  40      50.158  82.361 268.525  1.00 47.46           C  
ATOM    660  CA  SER D  41      47.824  81.349 271.359  1.00 55.18           C  
ATOM    661  CA  THR D  42      49.248  79.080 274.018  1.00 76.98           C  
ATOM    662  CA  ASN D  43      47.046  76.706 276.015  1.00 60.41           C  
ATOM    663  CA  GLN D  44      49.579  75.254 278.460  1.00 62.94           C  
ATOM    664  CA  GLU D  45      48.414  71.693 279.067  1.00 33.75           C  
ATOM    665  CA  TYR D  46      50.697  70.138 281.677  1.00 40.23           C  
ATOM    666  CA  ILE D  47      54.097  70.122 283.287  1.00 41.20           C  
ATOM    667  CA  THR D  48      56.306  67.051 283.349  1.00 38.33           C  
ATOM    668  CA  CYS D  49      59.653  66.048 284.763  1.00 49.28           C  
ATOM    669  CA  LYS D  50      61.777  63.413 286.471  1.00 62.69           C  
ATOM    670  CA  PHE D  51      59.403  61.664 288.867  1.00 44.77           C  
ATOM    671  CA  THR D  52      60.436  60.083 292.138  1.00 56.52           C  
ATOM    672  CA  THR D  53      58.951  56.821 293.365  1.00 53.19           C  
ATOM    673  CA  VAL D  54      58.026  56.563 297.014  1.00 54.95           C  
ATOM    674  CA  VAL D  55      57.806  53.174 298.661  1.00 44.92           C  
ATOM    675  CA  PRO D  56      56.206  53.084 302.132  1.00 36.65           C  
ATOM    676  CA  SER D  57      57.177  50.209 304.434  1.00 28.58           C  
ATOM    677  CA  PRO D  58      54.931  47.278 303.505  1.00 29.01           C  
ATOM    678  CA  LYS D  59      52.011  46.581 305.800  1.00 24.18           C  
ATOM    679  CA  ILE D  60      52.118  42.920 306.832  1.00 33.31           C  
ATOM    680  CA  LYS D  61      49.588  41.389 309.246  1.00 45.89           C  
ATOM    681  CA  CYS D  62      50.970  37.866 310.690  1.00 28.99           C  
ATOM    682  CA  CYS D  63      48.046  35.479 310.213  1.00 33.74           C  
ATOM    683  CA  GLY D  64      45.758  37.863 308.342  1.00 46.99           C  
ATOM    684  CA  SER D  65      44.340  38.594 304.896  1.00 58.88           C  
ATOM    685  CA  LEU D  66      45.580  41.870 303.413  1.00 56.77           C  
ATOM    686  CA  GLU D  67      43.419  42.708 300.369  1.00 65.45           C  
ATOM    687  CA  CYS D  68      43.798  46.078 298.643  1.00 60.53           C  
ATOM    688  CA  GLN D  69      41.515  49.092 298.626  1.00 63.56           C  
ATOM    689  CA  PRO D  70      41.064  51.482 295.691  1.00 74.25           C  
ATOM    690  CA  ALA D  71      43.630  53.939 297.060  1.00 70.55           C  
ATOM    691  CA  ALA D  72      43.861  56.598 294.349  1.00 71.46           C  
ATOM    692  CA  HIS D  73      46.742  59.035 294.827  1.00 67.93           C  
ATOM    693  CA  ALA D  74      49.160  59.654 291.958  1.00 62.09           C  
ATOM    694  CA  ASP D  75      50.937  56.623 290.518  1.00 46.01           C  
ATOM    695  CA  TYR D  76      49.696  54.313 293.263  1.00 32.25           C  
ATOM    696  CA  THR D  77      50.034  50.550 292.820  1.00 36.81           C  
ATOM    697  CA  CYS D  78      49.339  47.789 295.355  1.00 39.85           C  
ATOM    698  CA  LYS D  79      49.710  44.047 295.069  1.00 43.91           C  
ATOM    699  CA  VAL D  80      48.625  41.395 297.527  1.00 38.40           C  
ATOM    700  CA  PHE D  81      51.309  38.773 297.999  1.00 39.34           C  
ATOM    701  CA  GLY D  82      50.284  35.645 299.867  1.00 50.09           C  
ATOM    702  CA  GLY D  83      52.246  33.050 301.801  1.00 51.41           C  
ATOM    703  CA  VAL D  84      55.302  35.147 302.552  1.00 41.78           C  
ATOM    704  CA  TYR D  85      57.446  34.917 305.694  1.00 41.74           C  
ATOM    705  CA  PRO D  86      57.250  31.993 308.149  1.00 36.40           C  
ATOM    706  CA  PHE D  87      57.696  31.992 311.938  1.00 36.43           C  
ATOM    707  CA  MET D  88      60.350  33.531 314.171  1.00 52.26           C  
ATOM    708  CA  TRP D  89      62.726  35.448 311.875  1.00 39.16           C  
ATOM    709  CA  GLY D  90      63.040  34.649 308.176  1.00 44.30           C  
ATOM    710  CA  GLY D  91      60.454  37.032 307.100  1.00 37.37           C  
ATOM    711  CA  ALA D  92      59.188  39.010 310.108  1.00 39.39           C  
ATOM    712  CA  GLN D  93      58.189  38.171 313.656  1.00 41.37           C  
ATOM    713  CA  CYS D  94      55.197  35.936 312.933  1.00 34.99           C  
ATOM    714  CA  PHE D  95      54.287  32.357 313.849  1.00 29.59           C  
ATOM    715  CA  CYS D  96      52.428  30.968 310.835  1.00 38.37           C  
ATOM    716  CA  ASP D  97      53.863  29.763 307.519  1.00 44.09           C  
ATOM    717  CA  SER D  98      51.414  29.623 304.611  1.00 67.87           C  
ATOM    718  CA  GLU D  99      48.858  31.936 306.138  1.00 60.61           C  
ATOM    719  CA  ASN D 100      50.848  35.136 305.592  1.00 28.43           C  
ATOM    720  CA  SER D 101      50.287  38.155 303.369  1.00 28.05           C  
ATOM    721  CA  GLN D 102      52.143  41.319 302.401  1.00 32.43           C  
ATOM    722  CA  MET D 103      50.769  44.350 300.582  1.00 31.06           C  
ATOM    723  CA  SER D 104      53.280  46.071 298.350  1.00 53.95           C  
ATOM    724  CA  GLU D 105      52.274  49.617 297.511  1.00 45.07           C  
ATOM    725  CA  ALA D 106      54.138  52.402 295.729  1.00 43.90           C  
ATOM    726  CA  TYR D 107      53.424  55.681 293.949  1.00 43.64           C  
ATOM    727  CA  VAL D 108      55.312  58.479 292.179  1.00 46.17           C  
ATOM    728  CA  GLU D 109      55.930  62.131 293.088  1.00 56.56           C  
ATOM    729  CA  LEU D 110      57.841  65.010 291.523  1.00 47.43           C  
ATOM    730  CA  SER D 111      61.580  65.271 291.955  1.00 59.19           C  
ATOM    731  CA  ALA D 112      63.054  67.419 294.692  1.00 58.11           C  
ATOM    732  CA  ASP D 113      64.144  69.362 291.646  1.00 60.97           C  
ATOM    733  CA  CYS D 114      61.169  68.928 289.268  1.00 48.39           C  
ATOM    734  CA  ALA D 115      60.867  72.690 289.429  1.00 45.85           C  
ATOM    735  CA  SER D 116      64.374  73.586 288.313  1.00 56.19           C  
ATOM    736  CA  ASP D 117      64.227  71.230 285.286  1.00 62.74           C  
ATOM    737  CA  HIS D 118      60.931  70.393 283.605  1.00 47.07           C  
ATOM    738  CA  ALA D 119      59.132  70.830 280.335  1.00 39.79           C  
ATOM    739  CA  GLN D 120      55.816  72.267 279.273  1.00 42.00           C  
ATOM    740  CA  ALA D 121      53.296  70.547 277.046  1.00 40.34           C  
ATOM    741  CA  ILE D 122      51.609  73.314 275.122  1.00 49.59           C  
ATOM    742  CA  LYS D 123      48.867  73.491 272.518  1.00 32.88           C  
ATOM    743  CA  VAL D 124      49.269  76.167 269.866  1.00 53.75           C  
ATOM    744  CA  HIS D 125      46.389  77.657 267.924  1.00 40.67           C  
ATOM    745  CA  THR D 126      45.899  80.421 265.375  1.00 50.39           C  
ATOM    746  CA  ALA D 127      48.168  83.440 265.781  1.00 53.10           C  
ATOM    747  CA  ALA D 128      48.397  87.168 265.360  1.00 69.71           C  
ATOM    748  CA  MET D 129      51.434  89.154 264.222  1.00 50.57           C  
ATOM    749  CA  LYS D 130      52.623  92.601 265.255  1.00 45.03           C  
ATOM    750  CA  VAL D 131      55.059  94.591 263.104  1.00 55.59           C  
ATOM    751  CA  GLY D 132      57.464  97.338 264.155  1.00 56.50           C  
ATOM    752  CA  LEU D 133      57.137  99.706 261.233  1.00 47.35           C  
ATOM    753  CA  ARG D 134      59.123 102.846 260.536  1.00 33.66           C  
ATOM    754  CA  ILE D 135      57.660 105.152 257.922  1.00 39.36           C  
ATOM    755  CA  VAL D 136      59.246 108.359 256.698  1.00 32.36           C  
ATOM    756  CA  TYR D 137      57.359 111.029 254.772  1.00 30.61           C  
ATOM    757  CA  GLY D 138      58.982 114.252 253.626  1.00 37.79           C  
ATOM    758  CA  ASN D 139      60.966 115.926 256.407  1.00 52.81           C  
ATOM    759  CA  THR D 140      59.435 113.770 259.165  1.00 37.55           C  
ATOM    760  CA  THR D 141      59.913 110.132 260.192  1.00 42.14           C  
ATOM    761  CA  SER D 142      57.441 108.225 262.345  1.00 46.12           C  
ATOM    762  CA  PHE D 143      56.895 104.674 263.571  1.00 39.85           C  
ATOM    763  CA  LEU D 144      54.013 102.569 264.835  1.00 54.83           C  
ATOM    764  CA  ASP D 145      53.512  98.965 265.924  1.00 54.40           C  
ATOM    765  CA  VAL D 146      50.637  97.416 264.049  1.00 57.88           C  
ATOM    766  CA  TYR D 147      48.809  94.090 264.189  1.00 43.87           C  
ATOM    767  CA  VAL D 148      48.317  92.464 260.824  1.00 44.63           C  
ATOM    768  CA  ASN D 149      44.610  92.292 260.071  1.00 49.79           C  
ATOM    769  CA  GLY D 150      42.423  94.478 257.892  1.00 55.10           C  
ATOM    770  CA  VAL D 151      41.149  96.116 261.071  1.00 48.91           C  
ATOM    771  CA  THR D 152      43.280  97.340 263.979  1.00 39.79           C  
ATOM    772  CA  PRO D 153      44.994 100.686 263.329  1.00 46.82           C  
ATOM    773  CA  GLY D 154      48.188 101.432 265.250  1.00 71.23           C  
ATOM    774  CA  THR D 155      47.092 104.659 266.921  1.00 66.88           C  
ATOM    775  CA  SER D 156      50.338 106.441 266.053  1.00 68.46           C  
ATOM    776  CA  LYS D 157      49.211 109.847 267.317  1.00 62.15           C  
ATOM    777  CA  ASP D 158      49.182 111.374 263.834  1.00 57.36           C  
ATOM    778  CA  LEU D 159      49.017 108.857 261.004  1.00 49.91           C  
ATOM    779  CA  LYS D 160      46.525 105.996 260.705  1.00 44.89           C  
ATOM    780  CA  VAL D 161      48.297 102.844 259.508  1.00 58.53           C  
ATOM    781  CA  ILE D 162      46.183  99.699 259.247  1.00 53.16           C  
ATOM    782  CA  ALA D 163      48.161  96.690 258.058  1.00 54.06           C  
ATOM    783  CA  GLY D 164      46.009  94.437 255.898  1.00 47.15           C  
ATOM    784  CA  PRO D 165      45.889  90.653 256.360  1.00 56.12           C  
ATOM    785  CA  ILE D 166      49.207  88.964 255.628  1.00 67.80           C  
ATOM    786  CA  SER D 167      49.442  87.292 252.189  1.00 78.43           C  
ATOM    787  CA  ALA D 168      50.111  83.732 253.417  1.00 80.79           C  
ATOM    788  CA  SER D 169      49.224  82.320 256.819  1.00 85.57           C  
ATOM    789  CA  PHE D 170      52.438  80.645 257.925  1.00 58.48           C  
ATOM    790  CA  THR D 171      53.564  79.335 261.304  1.00 57.06           C  
ATOM    791  CA  PRO D 172      56.795  77.678 262.479  1.00 55.97           C  
ATOM    792  CA  PHE D 173      54.777  75.687 265.010  1.00 65.85           C  
ATOM    793  CA  ASP D 174      52.548  72.603 265.141  1.00 59.12           C  
ATOM    794  CA  HIS D 175      49.321  72.335 267.127  1.00 45.00           C  
ATOM    795  CA  LYS D 176      51.374  70.666 269.856  1.00 39.37           C  
ATOM    796  CA  VAL D 177      54.742  71.975 271.038  1.00 45.48           C  
ATOM    797  CA  VAL D 178      57.064  71.266 273.936  1.00 29.99           C  
ATOM    798  CA  ILE D 179      59.063  73.938 275.684  1.00 28.44           C  
ATOM    799  CA  HIS D 180      62.004  72.702 277.691  1.00 31.86           C  
ATOM    800  CA  ARG D 181      64.483  75.268 278.908  1.00 52.07           C  
ATOM    801  CA  GLY D 182      64.461  78.209 276.553  1.00 81.23           C  
ATOM    802  CA  LEU D 183      63.894  75.751 273.825  1.00 56.37           C  
ATOM    803  CA  VAL D 184      60.826  74.740 271.928  1.00 37.79           C  
ATOM    804  CA  TYR D 185      60.309  71.546 269.912  1.00 34.13           C  
ATOM    805  CA  ASN D 186      57.413  70.478 267.722  1.00 49.35           C  
ATOM    806  CA  TYR D 187      56.388  67.304 269.602  1.00 49.47           C  
ATOM    807  CA  ASP D 188      53.015  65.514 269.603  1.00 52.25           C  
ATOM    808  CA  PHE D 189      52.912  64.950 273.376  1.00 50.63           C  
ATOM    809  CA  PRO D 190      49.913  62.936 274.548  1.00 48.15           C  
ATOM    810  CA  GLU D 191      46.725  64.546 275.864  1.00 44.50           C  
ATOM    811  CA  TYR D 192      46.481  65.247 279.556  1.00 37.64           C  
ATOM    812  CA  GLY D 193      45.273  61.965 280.959  1.00 40.04           C  
ATOM    813  CA  ALA D 194      46.183  59.525 278.215  1.00 36.53           C  
ATOM    814  CA  MET D 195      49.786  58.909 279.191  1.00 32.57           C  
ATOM    815  CA  LYS D 196      52.146  56.180 278.056  1.00 47.28           C  
ATOM    816  CA  PRO D 197      54.994  55.292 280.442  1.00 41.59           C  
ATOM    817  CA  GLY D 198      58.675  55.758 279.649  1.00 54.10           C  
ATOM    818  CA  ALA D 199      57.618  58.029 276.776  1.00 60.78           C  
ATOM    819  CA  PHE D 200      57.333  61.820 277.069  1.00 47.89           C  
ATOM    820  CA  GLY D 201      54.609  62.886 279.444  1.00 46.57           C  
ATOM    821  CA  ASP D 202      54.677  59.726 281.515  1.00 45.97           C  
ATOM    822  CA  ILE D 203      53.698  61.871 284.495  1.00 44.98           C  
ATOM    823  CA  GLN D 204      51.532  64.983 284.159  1.00 50.09           C  
ATOM    824  CA  ALA D 205      50.491  67.993 286.220  1.00 57.40           C  
ATOM    825  CA  THR D 206      48.583  71.191 285.439  1.00 57.34           C  
ATOM    826  CA  SER D 207      51.028  73.516 287.195  1.00 80.05           C  
ATOM    827  CA  LEU D 208      54.350  73.189 289.021  1.00 80.82           C  
ATOM    828  CA  THR D 209      52.482  73.484 292.321  1.00 91.70           C  
ATOM    829  CA  SER D 210      52.025  69.722 292.000  1.00 80.13           C  
ATOM    830  CA  LYS D 211      48.237  70.201 290.967  1.00 51.15           C  
ATOM    831  CA  ASP D 212      46.169  66.857 290.657  1.00 54.10           C  
ATOM    832  CA  LEU D 213      49.113  65.075 288.982  1.00 54.70           C  
ATOM    833  CA  ILE D 214      48.399  61.867 287.074  1.00 46.42           C  
ATOM    834  CA  ALA D 215      51.193  59.403 286.314  1.00 41.79           C  
ATOM    835  CA  SER D 216      51.512  56.071 284.491  1.00 46.31           C  
ATOM    836  CA  THR D 217      54.976  54.537 284.994  1.00 59.89           C  
ATOM    837  CA  ASP D 218      54.536  50.751 284.547  1.00 49.55           C  
ATOM    838  CA  ILE D 219      55.461  49.941 288.131  1.00 50.25           C  
ATOM    839  CA  ARG D 220      55.600  46.231 288.788  1.00 39.03           C  
ATOM    840  CA  LEU D 221      55.622  44.692 292.251  1.00 49.79           C  
ATOM    841  CA  LEU D 222      57.563  41.529 292.940  1.00 43.22           C  
ATOM    842  CA  LYS D 223      56.945  38.802 295.490  1.00 43.00           C  
ATOM    843  CA  PRO D 224      59.575  39.513 298.156  1.00 36.02           C  
ATOM    844  CA  SER D 225      61.874  36.702 299.303  1.00 55.24           C  
ATOM    845  CA  ALA D 226      62.011  35.670 302.959  1.00 55.18           C  
ATOM    846  CA  LYS D 227      65.196  36.851 304.633  1.00 46.77           C  
ATOM    847  CA  ASN D 228      64.336  40.552 304.987  1.00 43.08           C  
ATOM    848  CA  VAL D 229      61.341  42.838 304.723  1.00 46.62           C  
ATOM    849  CA  HIS D 230      62.259  44.472 301.445  1.00 38.32           C  
ATOM    850  CA  VAL D 231      59.734  45.493 298.807  1.00 41.76           C  
ATOM    851  CA  PRO D 232      60.906  44.708 295.249  1.00 39.22           C  
ATOM    852  CA  TYR D 233      59.610  46.452 292.147  1.00 42.79           C  
ATOM    853  CA  THR D 234      60.454  47.093 288.524  1.00 39.43           C  
ATOM    854  CA  GLN D 235      59.293  50.218 286.782  1.00 44.96           C  
ATOM    855  CA  ALA D 236      59.558  51.988 283.475  1.00 57.70           C  
ATOM    856  CA  SER D 237      62.172  54.547 282.530  1.00 71.14           C  
ATOM    857  CA  SER D 238      61.763  58.310 283.014  1.00 49.47           C  
ATOM    858  CA  GLY D 239      59.876  59.325 279.875  1.00 38.34           C  
ATOM    859  CA  PHE D 240      61.298  62.766 280.518  1.00 35.21           C  
ATOM    860  CA  GLU D 241      65.006  62.071 280.734  1.00 40.16           C  
ATOM    861  CA  MET D 242      64.229  59.695 277.888  1.00 35.68           C  
ATOM    862  CA  TRP D 243      62.818  62.499 275.792  1.00 26.80           C  
ATOM    863  CA  LYS D 244      65.672  64.792 276.820  1.00 42.92           C  
ATOM    864  CA  ASN D 245      68.372  62.389 275.503  1.00 49.56           C  
ATOM    865  CA  ASN D 246      66.315  62.303 272.352  1.00 43.26           C  
ATOM    866  CA  SER D 247      64.956  65.811 272.031  1.00 52.51           C  
ATOM    867  CA  GLY D 248      65.816  67.065 268.595  1.00 61.80           C  
ATOM    868  CA  ARG D 249      67.529  70.166 267.512  1.00 58.63           C  
ATOM    869  CA  PRO D 250      65.276  73.038 268.791  1.00 29.28           C  
ATOM    870  CA  LEU D 251      62.976  74.976 266.501  1.00 37.49           C  
ATOM    871  CA  GLN D 252      65.135  78.038 267.061  1.00 41.50           C  
ATOM    872  CA  GLU D 253      67.493  75.996 264.882  1.00 49.11           C  
ATOM    873  CA  THR D 254      65.058  74.492 262.382  1.00 53.20           C  
ATOM    874  CA  ALA D 255      62.567  77.316 261.797  1.00 50.00           C  
ATOM    875  CA  PRO D 256      61.382  77.260 258.121  1.00 55.84           C  
ATOM    876  CA  PHE D 257      61.862  80.983 257.313  1.00 42.55           C  
ATOM    877  CA  GLY D 258      64.836  82.104 259.321  1.00 37.76           C  
ATOM    878  CA  CYS D 259      62.554  82.873 262.241  1.00 46.40           C  
ATOM    879  CA  LYS D 260      64.147  83.564 265.612  1.00 59.51           C  
ATOM    880  CA  ILE D 261      61.981  81.498 267.987  1.00 66.86           C  
ATOM    881  CA  ALA D 262      61.419  83.044 271.432  1.00 75.90           C  
ATOM    882  CA  VAL D 263      60.093  81.953 274.835  1.00 74.01           C  
ATOM    883  CA  ASN D 264      58.354  83.547 277.211  1.00 70.73           C  
ATOM    884  CA  PRO D 265      55.641  84.788 274.989  1.00 49.81           C  
ATOM    885  CA  LEU D 266      55.800  81.982 272.409  1.00 39.72           C  
ATOM    886  CA  ARG D 267      56.878  83.937 269.339  1.00 31.50           C  
ATOM    887  CA  ALA D 268      58.583  83.827 265.944  1.00 50.06           C  
ATOM    888  CA  VAL D 269      60.747  86.969 265.834  1.00 65.03           C  
ATOM    889  CA  ASP D 270      61.763  88.425 262.468  1.00 56.54           C  
ATOM    890  CA  CYS D 271      60.520  85.788 260.057  1.00 48.67           C  
ATOM    891  CA  SER D 272      60.600  86.673 256.364  1.00 46.08           C  
ATOM    892  CA  TYR D 273      57.829  85.622 253.998  1.00 58.90           C  
ATOM    893  CA  GLY D 274      55.076  87.133 251.876  1.00 67.74           C  
ATOM    894  CA  ASN D 275      54.034  90.738 251.471  1.00 54.58           C  
ATOM    895  CA  ILE D 276      52.063  92.955 253.849  1.00 53.47           C  
ATOM    896  CA  PRO D 277      49.308  95.131 252.456  1.00 54.09           C  
ATOM    897  CA  ILE D 278      49.539  98.565 254.080  1.00 55.03           C  
ATOM    898  CA  SER D 279      47.169 101.526 254.099  1.00 54.42           C  
ATOM    899  CA  ILE D 280      48.644 104.874 255.116  1.00 43.64           C  
ATOM    900  CA  ASP D 281      46.912 108.157 256.009  1.00 41.25           C  
ATOM    901  CA  ILE D 282      49.280 111.066 255.286  1.00 66.49           C  
ATOM    902  CA  PRO D 283      48.313 114.305 257.063  1.00 57.03           C  
ATOM    903  CA  ASN D 284      47.828 117.012 254.428  1.00 51.68           C  
ATOM    904  CA  ALA D 285      49.847 119.153 256.837  1.00 58.07           C  
ATOM    905  CA  ALA D 286      53.203 118.280 255.273  1.00 70.04           C  
ATOM    906  CA  PHE D 287      53.258 116.566 251.876  1.00 58.92           C  
ATOM    907  CA  ILE D 288      53.518 119.642 249.666  1.00 44.92           C  
ATOM    908  CA  ARG D 289      51.444 120.809 246.696  1.00 36.75           C  
ATOM    909  CA  THR D 290      53.164 122.043 243.520  1.00 73.75           C  
ATOM    910  CA  SER D 291      53.609 125.702 244.460  1.00 99.42           C  
ATOM    911  CA  ASP D 292      57.299 125.337 245.306  1.00 47.39           C  
ATOM    912  CA  ALA D 293      59.738 123.973 242.726  1.00 49.33           C  
ATOM    913  CA  PRO D 294      61.422 129.250 245.320  1.00 50.82           C  
ATOM    914  CA  LEU D 295      61.631 127.950 241.747  1.00 49.93           C  
ATOM    915  CA  VAL D 296      63.354 124.814 240.462  1.00 32.56           C  
ATOM    916  CA  SER D 297      63.925 123.909 236.811  1.00 43.19           C  
ATOM    917  CA  THR D 298      65.961 121.618 234.556  1.00 57.68           C  
ATOM    918  CA  VAL D 299      67.233 118.296 235.898  1.00 55.11           C  
ATOM    919  CA  LYS D 300      69.352 115.892 233.846  1.00 48.51           C  
ATOM    920  CA  CYS D 301      70.986 112.687 235.065  1.00 50.93           C  
ATOM    921  CA  GLU D 302      74.558 111.450 234.575  1.00 53.97           C  
ATOM    922  CA  VAL D 303      75.986 108.233 236.037  1.00 52.17           C  
ATOM    923  CA  SER D 304      79.686 108.263 236.943  1.00 73.98           C  
ATOM    924  CA  GLU D 305      80.241 104.696 238.159  1.00 53.13           C  
ATOM    925  CA  CYS D 306      78.119 101.600 238.785  1.00 47.06           C  
ATOM    926  CA  THR D 307      78.357  98.030 240.054  1.00 35.52           C  
ATOM    927  CA  TYR D 308      75.751  95.326 239.430  1.00 20.80           C  
ATOM    928  CA  SER D 309      73.973  93.745 242.425  1.00 47.67           C  
ATOM    929  CA  ALA D 310      76.029  95.419 245.161  1.00 50.77           C  
ATOM    930  CA  ASP D 311      74.991  97.193 248.360  1.00 58.13           C  
ATOM    931  CA  PHE D 312      75.440 100.695 246.927  1.00 47.22           C  
ATOM    932  CA  GLY D 313      77.779 100.586 243.943  1.00 62.36           C  
ATOM    933  CA  GLY D 314      75.794 103.142 241.972  1.00 47.80           C  
ATOM    934  CA  MET D 315      77.057 106.698 241.550  1.00 33.24           C  
ATOM    935  CA  ALA D 316      75.099 109.357 239.654  1.00 34.35           C  
ATOM    936  CA  THR D 317      75.163 113.159 239.553  1.00 37.21           C  
ATOM    937  CA  LEU D 318      72.419 115.666 238.752  1.00 34.63           C  
ATOM    938  CA  GLN D 319      72.984 118.993 236.998  1.00 34.43           C  
ATOM    939  CA  TYR D 320      70.260 121.633 237.151  1.00 31.26           C  
ATOM    940  CA  VAL D 321      69.388 125.262 237.883  1.00 41.36           C  
ATOM    941  CA  SER D 322      67.768 126.494 241.102  1.00 40.25           C  
ATOM    942  CA  ASP D 323      66.495 129.940 242.113  1.00 42.26           C  
ATOM    943  CA  ARG D 324      67.730 129.587 245.701  1.00 54.74           C  
ATOM    944  CA  GLU D 325      68.857 127.071 248.314  1.00 40.43           C  
ATOM    945  CA  GLY D 326      66.631 124.476 249.956  1.00 24.30           C  
ATOM    946  CA  GLN D 327      66.175 120.789 250.732  1.00 26.82           C  
ATOM    947  CA  CYS D 328      64.881 118.316 248.139  1.00 24.50           C  
ATOM    948  CA  PRO D 329      63.652 114.728 248.654  1.00 35.47           C  
ATOM    949  CA  VAL D 330      65.234 112.429 246.063  1.00 46.71           C  
ATOM    950  CA  HIS D 331      63.489 109.176 245.143  1.00 56.19           C  
ATOM    951  CA  SER D 332      63.199 106.620 242.329  1.00 43.67           C  
ATOM    952  CA  HIS D 333      59.902 105.989 240.520  1.00 61.09           C  
ATOM    953  CA  SER D 334      60.918 102.511 239.352  1.00 64.76           C  
ATOM    954  CA  SER D 335      61.807  99.429 241.396  1.00 81.06           C  
ATOM    955  CA  THR D 336      64.652  98.639 238.991  1.00 65.47           C  
ATOM    956  CA  ALA D 337      66.756 100.850 241.261  1.00 48.33           C  
ATOM    957  CA  THR D 338      66.689 102.475 244.696  1.00 52.12           C  
ATOM    958  CA  LEU D 339      68.551 105.423 246.221  1.00 34.57           C  
ATOM    959  CA  GLN D 340      70.711 105.264 249.356  1.00 45.52           C  
ATOM    960  CA  GLU D 341      69.512 108.702 250.403  1.00 43.96           C  
ATOM    961  CA  SER D 342      66.071 110.286 250.247  1.00 56.46           C  
ATOM    962  CA  THR D 343      66.962 113.948 250.816  1.00 52.56           C  
ATOM    963  CA  VAL D 344      69.569 116.302 249.344  1.00 67.47           C  
ATOM    964  CA  HIS D 345      70.820 119.826 250.102  1.00 65.09           C  
ATOM    965  CA  VAL D 346      70.199 121.650 246.831  1.00 43.30           C  
ATOM    966  CA  LEU D 347      72.617 124.525 246.288  1.00 43.77           C  
ATOM    967  CA  GLU D 348      72.867 127.111 243.518  1.00 50.95           C  
ATOM    968  CA  LYS D 349      75.874 125.292 242.036  1.00 74.77           C  
ATOM    969  CA  GLY D 350      73.577 122.963 240.115  1.00 33.30           C  
ATOM    970  CA  ALA D 351      75.350 119.736 241.031  1.00 61.44           C  
ATOM    971  CA  VAL D 352      73.989 116.915 243.190  1.00 52.64           C  
ATOM    972  CA  THR D 353      75.832 113.638 243.749  1.00 51.02           C  
ATOM    973  CA  VAL D 354      73.760 110.606 244.791  1.00 54.15           C  
ATOM    974  CA  HIS D 355      74.411 106.925 245.525  1.00 38.82           C  
ATOM    975  CA  PHE D 356      72.091 104.126 244.403  1.00 31.94           C  
ATOM    976  CA  SER D 357      71.778 100.340 244.356  1.00 33.76           C  
ATOM    977  CA  THR D 358      70.630  98.023 241.568  1.00 43.86           C  
ATOM    978  CA  ALA D 359      70.828  94.464 240.242  1.00 51.96           C  
ATOM    979  CA  SER D 360      70.866  94.831 236.460  1.00 42.01           C  
ATOM    980  CA  PRO D 361      73.348  95.387 233.600  1.00 35.23           C  
ATOM    981  CA  GLN D 362      71.692  98.228 231.684  1.00 44.95           C  
ATOM    982  CA  ALA D 363      68.970  99.667 233.910  1.00 58.92           C  
ATOM    983  CA  ASN D 364      66.402 102.375 233.175  1.00 56.90           C  
ATOM    984  CA  PHE D 365      64.985 104.377 236.081  1.00 50.25           C  
ATOM    985  CA  ILE D 366      63.221 107.712 236.602  1.00 49.56           C  
ATOM    986  CA  VAL D 367      64.869 109.665 239.423  1.00 50.38           C  
ATOM    987  CA  SER D 368      63.009 112.605 240.958  1.00 30.71           C  
ATOM    988  CA  LEU D 369      64.243 115.743 242.699  1.00 37.17           C  
ATOM    989  CA  CYS D 370      61.965 118.084 244.640  1.00 37.00           C  
ATOM    990  CA  GLY D 371      59.311 118.329 241.936  1.00 57.90           C  
ATOM    991  CA  LYS D 372      61.293 117.631 238.772  1.00 46.36           C  
ATOM    992  CA  LYS D 373      61.928 114.243 237.158  1.00 42.06           C  
ATOM    993  CA  THR D 374      64.549 112.780 234.814  1.00 52.53           C  
ATOM    994  CA  THR D 375      65.979 109.539 233.446  1.00 61.44           C  
ATOM    995  CA  CYS D 376      69.328 107.874 234.163  1.00 55.74           C  
ATOM    996  CA  ASN D 377      71.452 105.292 232.350  1.00 50.02           C  
ATOM    997  CA  ALA D 378      74.667 103.273 232.613  1.00 62.38           C  
ATOM    998  CA  GLU D 379      76.174  99.797 232.294  1.00 52.51           C  
ATOM    999  CA  CYS D 380      77.102  97.763 235.380  1.00 30.01           C  
TER    1000      CYS D 380                                                      
ATOM   1001  CA  PHE X   6      60.340  67.362 315.973  1.00 44.85           C  
ATOM   1002  CA  THR X   7      60.576  63.927 316.129  1.00 35.42           C  
ATOM   1003  CA  LEU X   8      57.939  61.217 316.044  1.00 27.63           C  
ATOM   1004  CA  THR X   9      60.109  58.627 314.320  1.00 24.39           C  
ATOM   1005  CA  SER X  10      63.587  57.166 314.910  1.00 39.55           C  
ATOM   1006  CA  PRO X  11      66.547  55.896 312.786  1.00 30.54           C  
ATOM   1007  CA  TYR X  12      66.239  52.357 311.406  1.00 46.71           C  
ATOM   1008  CA  LEU X  13      68.558  49.702 309.959  1.00 46.51           C  
ATOM   1009  CA  GLY X  14      68.710  48.569 306.348  1.00 48.01           C  
ATOM   1010  CA  THR X  15      70.436  45.897 304.316  1.00 50.38           C  
ATOM   1011  CA  CYS X  16      73.365  47.335 302.358  1.00 46.88           C  
ATOM   1012  CA  SER X  17      75.600  45.909 299.635  1.00 43.49           C  
ATOM   1013  CA  TYR X  18      78.981  47.321 300.719  1.00 46.43           C  
ATOM   1014  CA  CYS X  19      80.020  48.492 304.196  1.00 46.69           C  
ATOM   1015  CA  HIS X  20      83.718  49.405 304.597  1.00 70.05           C  
ATOM   1016  CA  HIS X  21      84.211  45.741 303.758  1.00 48.66           C  
ATOM   1017  CA  THR X  22      82.962  44.874 300.283  1.00 54.00           C  
ATOM   1018  CA  VAL X  23      80.668  42.275 301.893  1.00 40.83           C  
ATOM   1019  CA  PRO X  24      76.972  43.312 302.059  1.00 33.67           C  
ATOM   1020  CA  CYS X  25      75.933  44.124 305.626  1.00 47.11           C  
ATOM   1021  CA  PHE X  26      72.965  45.201 307.718  1.00 51.81           C  
ATOM   1022  CA  SER X  27      73.983  48.618 308.954  1.00 54.24           C  
ATOM   1023  CA  PRO X  28      72.516  52.074 309.673  1.00 40.92           C  
ATOM   1024  CA  VAL X  29      72.995  54.885 307.158  1.00 43.67           C  
ATOM   1025  CA  LYS X  30      71.392  52.562 304.602  1.00 36.21           C  
ATOM   1026  CA  ILE X  31      70.928  54.440 301.352  1.00 47.85           C  
ATOM   1027  CA  GLU X  32      67.507  53.880 299.791  1.00 66.17           C  
ATOM   1028  CA  GLN X  33      67.363  56.519 297.049  1.00 61.19           C  
ATOM   1029  CA  VAL X  34      69.324  59.394 295.570  1.00 46.35           C  
ATOM   1030  CA  TRP X  35      68.396  62.352 293.383  1.00 37.43           C  
ATOM   1031  CA  ASP X  36      70.609  63.593 290.586  1.00 65.74           C  
ATOM   1032  CA  GLU X  37      68.149  65.854 288.812  1.00 70.12           C  
ATOM   1033  CA  ALA X  38      69.316  69.404 289.425  1.00 60.71           C  
ATOM   1034  CA  ASP X  39      71.049  71.545 286.810  1.00 60.49           C  
ATOM   1035  CA  ASP X  40      73.370  72.499 289.621  1.00 47.25           C  
ATOM   1036  CA  ASN X  41      75.982  69.929 290.581  1.00 48.08           C  
ATOM   1037  CA  THR X  42      74.107  69.101 293.795  1.00 46.98           C  
ATOM   1038  CA  ILE X  43      72.826  65.791 295.149  1.00 41.67           C  
ATOM   1039  CA  ARG X  44      69.984  64.715 297.433  1.00 24.99           C  
ATOM   1040  CA  ILE X  45      70.596  61.566 299.499  1.00 33.58           C  
ATOM   1041  CA  GLN X  46      68.113  59.491 301.518  1.00 25.14           C  
ATOM   1042  CA  THR X  47      69.562  57.572 304.479  1.00 32.00           C  
ATOM   1043  CA  SER X  48      68.177  55.576 307.408  1.00 34.61           C  
ATOM   1044  CA  ALA X  49      69.889  57.565 310.152  1.00 28.02           C  
ATOM   1045  CA  GLN X  50      68.344  60.675 311.712  1.00 27.12           C  
ATOM   1046  CA  PHE X  51      70.019  64.054 312.130  1.00 19.77           C  
ATOM   1047  CA  GLY X  52      69.378  67.390 313.829  1.00 26.07           C  
ATOM   1048  CA  TYR X  53      68.475  65.618 317.061  1.00 31.06           C  
ATOM   1049  CA  ASP X  54      69.983  63.418 319.772  1.00 30.39           C  
ATOM   1050  CA  GLN X  55      68.862  59.976 320.943  1.00 43.85           C  
ATOM   1051  CA  SER X  56      65.301  61.218 321.426  1.00 62.70           C  
ATOM   1052  CA  GLY X  57      63.119  64.231 320.658  1.00 52.27           C  
ATOM   1053  CA  ALA X  58      64.304  67.030 318.365  1.00 41.19           C  
ATOM   1054  CA  ALA X  59      67.563  68.646 319.483  1.00 44.84           C  
ATOM   1055  CA  SER X  60      68.930  70.975 316.823  1.00 56.84           C  
ATOM   1056  CA  ALA X  61      72.288  72.376 315.712  1.00 63.73           C  
ATOM   1057  CA  ASN X  62      74.764  69.596 314.928  1.00 35.00           C  
ATOM   1058  CA  LYS X  63      73.612  66.247 316.310  1.00 26.18           C  
ATOM   1059  CA  TYR X  64      72.449  62.961 314.781  1.00 26.06           C  
ATOM   1060  CA  ARG X  65      71.206  59.616 316.077  1.00 19.98           C  
ATOM   1061  CA  TYR X  66      71.051  56.075 314.746  1.00 21.98           C  
ATOM   1062  CA  MET X  67      70.524  52.446 315.717  1.00 40.55           C  
ATOM   1063  CA  SER X  68      73.266  50.337 317.272  1.00 60.14           C  
ATOM   1064  CA  LEU X  69      75.821  47.898 315.936  1.00 75.63           C  
ATOM   1065  CA  LYS X  70      73.585  45.291 317.555  1.00 64.33           C  
ATOM   1066  CA  GLN X  71      69.789  45.005 317.505  1.00 48.27           C  
ATOM   1067  CA  ASP X  72      69.324  46.240 321.101  1.00 49.26           C  
ATOM   1068  CA  HIS X  73      67.201  49.005 319.609  1.00 47.29           C  
ATOM   1069  CA  THR X  74      69.627  51.188 321.514  1.00 36.66           C  
ATOM   1070  CA  VAL X  75      69.385  54.584 319.855  1.00 39.30           C  
ATOM   1071  CA  LYS X  76      72.778  56.135 320.596  1.00 43.72           C  
ATOM   1072  CA  GLU X  77      73.816  59.551 319.318  1.00 27.68           C  
ATOM   1073  CA  GLY X  78      76.918  61.414 318.250  1.00 39.64           C  
ATOM   1074  CA  THR X  79      77.864  64.811 316.855  1.00 38.07           C  
ATOM   1075  CA  MET X  80      76.862  65.995 313.357  1.00 31.08           C  
ATOM   1076  CA  ASP X  81      80.516  66.720 312.946  1.00 50.68           C  
ATOM   1077  CA  ASP X  82      81.974  63.316 312.212  1.00 43.93           C  
ATOM   1078  CA  ILE X  83      79.546  62.394 309.429  1.00 50.20           C  
ATOM   1079  CA  LYS X  84      81.080  62.801 305.990  1.00 50.86           C  
ATOM   1080  CA  ILE X  85      79.932  61.999 302.454  1.00 64.73           C  
ATOM   1081  CA  SER X  86      82.052  60.722 299.589  1.00 60.09           C  
ATOM   1082  CA  THR X  87      81.682  59.317 296.091  1.00 61.74           C  
ATOM   1083  CA  SER X  88      85.116  59.099 294.526  1.00 67.39           C  
ATOM   1084  CA  GLY X  89      86.679  61.864 296.585  1.00 56.57           C  
ATOM   1085  CA  PRO X  90      85.665  64.560 299.053  1.00 69.78           C  
ATOM   1086  CA  CYS X  91      82.107  65.804 299.466  1.00 59.71           C  
ATOM   1087  CA  ARG X  92      80.884  68.660 301.596  1.00 47.46           C  
ATOM   1088  CA  ARG X  93      77.333  68.509 302.866  1.00 36.76           C  
ATOM   1089  CA  LEU X  94      75.166  71.593 302.994  1.00 50.62           C  
ATOM   1090  CA  SER X  95      71.945  70.957 304.903  1.00 48.17           C  
ATOM   1091  CA  TYR X  96      70.577  68.210 307.153  1.00 26.73           C  
ATOM   1092  CA  LYS X  97      66.901  67.305 306.958  1.00 35.86           C  
ATOM   1093  CA  GLY X  98      66.379  64.510 309.465  1.00 36.85           C  
ATOM   1094  CA  TYR X  99      66.642  61.447 307.223  1.00 38.96           C  
ATOM   1095  CA  PHE X 100      67.988  63.315 304.209  1.00 26.42           C  
ATOM   1096  CA  LEU X 101      71.346  64.673 303.083  1.00 28.91           C  
ATOM   1097  CA  LEU X 102      72.357  67.156 300.408  1.00 39.07           C  
ATOM   1098  CA  ALA X 103      75.835  67.965 299.127  1.00 31.54           C  
ATOM   1099  CA  LYS X 104      77.930  68.609 296.015  1.00 39.82           C  
ATOM   1100  CA  CYS X 105      79.587  65.484 295.381  1.00 46.88           C  
ATOM   1101  CA  PRO X 106      82.723  65.355 292.697  1.00 59.67           C  
ATOM   1102  CA  PRO X 107      82.734  62.705 289.951  1.00 62.41           C  
ATOM   1103  CA  GLY X 108      80.300  59.853 290.548  1.00 59.98           C  
ATOM   1104  CA  ASP X 109      80.273  56.096 290.022  1.00 67.81           C  
ATOM   1105  CA  SER X 110      78.949  55.183 293.465  1.00 44.37           C  
ATOM   1106  CA  VAL X 111      77.980  56.912 296.703  1.00 50.49           C  
ATOM   1107  CA  THR X 112      79.182  56.271 300.246  1.00 34.59           C  
ATOM   1108  CA  VAL X 113      77.837  57.757 303.465  1.00 55.08           C  
ATOM   1109  CA  SER X 114      79.510  56.981 306.767  1.00 44.25           C  
ATOM   1110  CA  ILE X 115      80.627  58.013 310.246  1.00 55.00           C  
ATOM   1111  CA  VAL X 116      84.320  58.077 311.161  1.00 59.85           C  
ATOM   1112  CA  SER X 117      84.358  58.745 314.902  1.00 79.65           C  
ATOM   1113  CA  SER X 118      87.813  57.334 315.192  1.00 81.15           C  
ATOM   1114  CA  ASN X 119      89.332  53.913 314.519  1.00 71.79           C  
ATOM   1115  CA  SER X 120      85.980  52.124 314.332  1.00 73.35           C  
ATOM   1116  CA  ALA X 121      83.099  53.143 312.062  1.00 65.24           C  
ATOM   1117  CA  THR X 122      80.578  51.900 309.497  1.00 54.91           C  
ATOM   1118  CA  SER X 123      79.533  53.012 306.008  1.00 45.30           C  
ATOM   1119  CA  CYS X 124      76.906  52.046 303.441  1.00 44.79           C  
ATOM   1120  CA  THR X 125      77.570  52.728 299.762  1.00 46.56           C  
ATOM   1121  CA  LEU X 126      75.216  52.772 296.811  1.00 59.32           C  
ATOM   1122  CA  ALA X 127      75.756  51.762 293.239  1.00 63.95           C  
ATOM   1123  CA  ARG X 128      74.418  54.938 291.610  1.00 53.47           C  
ATOM   1124  CA  LYS X 129      76.003  56.766 288.673  1.00 57.52           C  
ATOM   1125  CA  ILE X 130      76.352  60.553 288.820  1.00 67.38           C  
ATOM   1126  CA  LYS X 131      77.394  62.750 285.929  1.00 51.50           C  
ATOM   1127  CA  PRO X 132      79.211  66.035 285.344  1.00 69.00           C  
ATOM   1128  CA  LYS X 133      76.497  68.666 285.074  1.00 60.65           C  
ATOM   1129  CA  PHE X 134      78.209  69.720 283.053  1.00 81.49           C  
ATOM   1130  CA  VAL X 135      75.689  72.184 281.689  1.00 63.71           C  
ATOM   1131  CA  GLY X 136      77.131  73.997 278.694  1.00 58.36           C  
ATOM   1132  CA  ARG X 137      77.997  72.417 275.366  1.00 48.46           C  
ATOM   1133  CA  GLU X 138      81.550  72.271 276.629  1.00 44.89           C  
ATOM   1134  CA  LYS X 139      82.843  69.570 278.918  1.00 49.45           C  
ATOM   1135  CA  TYR X 140      84.348  70.869 282.140  1.00 51.29           C  
ATOM   1136  CA  ASP X 141      85.123  69.461 285.568  1.00 70.38           C  
ATOM   1137  CA  LEU X 142      85.403  72.813 287.276  1.00 59.48           C  
ATOM   1138  CA  PRO X 143      83.846  76.216 286.553  1.00 64.91           C  
ATOM   1139  CA  PRO X 144      86.455  78.211 284.597  1.00 51.04           C  
ATOM   1140  CA  VAL X 145      87.893  81.363 286.168  1.00 65.00           C  
ATOM   1141  CA  HIS X 146      86.672  83.184 283.095  1.00 63.99           C  
ATOM   1142  CA  GLY X 147      83.992  81.885 280.772  1.00 49.21           C  
ATOM   1143  CA  LYS X 148      80.448  82.747 279.833  1.00 49.84           C  
ATOM   1144  CA  LYS X 149      77.342  83.133 281.964  1.00 53.60           C  
ATOM   1145  CA  ILE X 150      74.584  80.692 281.100  1.00 46.96           C  
ATOM   1146  CA  PRO X 151      71.083  79.969 282.412  1.00 56.33           C  
ATOM   1147  CA  CYS X 152      71.154  77.012 284.787  1.00 62.00           C  
ATOM   1148  CA  THR X 153      69.335  75.899 287.931  1.00 77.88           C  
ATOM   1149  CA  VAL X 154      71.008  75.201 291.294  1.00 81.41           C  
ATOM   1150  CA  TYR X 155      70.380  74.784 295.042  1.00 39.34           C  
ATOM   1151  CA  ASP X 156      70.108  77.812 297.362  1.00 58.79           C  
ATOM   1152  CA  LEU X 255      55.595  70.509 303.096  1.00 56.30           C  
ATOM   1153  CA  HIS X 256      58.939  72.177 302.426  1.00 49.38           C  
ATOM   1154  CA  LEU X 257      61.994  73.341 304.395  1.00 52.77           C  
ATOM   1155  CA  PRO X 258      64.914  72.238 302.181  1.00 36.54           C  
ATOM   1156  CA  PHE X 259      67.381  74.235 300.042  1.00 34.20           C  
ATOM   1157  CA  LYS X 260      65.013  75.279 297.244  1.00 46.94           C  
ATOM   1158  CA  LEU X 261      65.959  75.002 293.568  1.00 38.16           C  
ATOM   1159  CA  ILE X 262      66.363  78.391 291.895  1.00 61.67           C  
ATOM   1160  CA  PRO X 263      67.297  79.190 288.285  1.00 65.30           C  
ATOM   1161  CA  SER X 264      70.418  81.358 287.955  1.00 73.38           C  
ATOM   1162  CA  THR X 265      73.806  81.564 286.237  1.00 62.17           C  
ATOM   1163  CA  CYS X 266      76.546  78.985 285.868  1.00 63.14           C  
ATOM   1164  CA  MET X 267      79.852  79.757 284.228  1.00 65.89           C  
ATOM   1165  CA  VAL X 268      80.544  77.484 281.286  1.00 77.24           C  
ATOM   1166  CA  PRO X 269      83.744  78.462 277.095  1.00 38.73           C  
ATOM   1167  CA  VAL X 270      83.774  80.268 273.773  1.00 43.98           C  
ATOM   1168  CA  ALA X 271      85.285  78.625 270.710  1.00 50.20           C  
ATOM   1169  CA  HIS X 272      88.179  79.656 268.480  1.00 46.73           C  
ATOM   1170  CA  ALA X 273      86.623  81.864 265.817  1.00 47.85           C  
ATOM   1171  CA  PRO X 274      86.530  79.961 262.511  1.00 34.70           C  
ATOM   1172  CA  ASN X 275      88.754  81.376 259.831  1.00 48.44           C  
ATOM   1173  CA  VAL X 276      86.098  82.055 257.219  1.00 49.39           C  
ATOM   1174  CA  ILE X 277      86.573  82.283 253.494  1.00 53.68           C  
ATOM   1175  CA  HIS X 278      83.964  83.951 251.312  1.00 49.31           C  
ATOM   1176  CA  GLY X 279      83.756  82.911 247.668  1.00 34.76           C  
ATOM   1177  CA  PHE X 280      81.354  82.550 244.760  1.00 36.64           C  
ATOM   1178  CA  LYS X 281      78.145  81.561 246.528  1.00 48.02           C  
ATOM   1179  CA  HIS X 282      80.526  79.894 248.936  1.00 31.02           C  
ATOM   1180  CA  ILE X 283      81.705  79.785 252.535  1.00 45.50           C  
ATOM   1181  CA  SER X 284      84.451  77.377 253.521  1.00 27.25           C  
ATOM   1182  CA  LEU X 285      84.687  77.339 257.311  1.00 28.94           C  
ATOM   1183  CA  GLN X 286      88.173  76.522 258.573  1.00 35.55           C  
ATOM   1184  CA  LEU X 287      87.654  75.278 262.138  1.00 39.94           C  
ATOM   1185  CA  ASP X 288      90.159  74.278 264.817  1.00 55.52           C  
ATOM   1186  CA  THR X 289      88.837  73.453 268.291  1.00 57.58           C  
ATOM   1187  CA  ASP X 290      90.403  71.816 271.296  1.00 65.31           C  
ATOM   1188  CA  HIS X 291      87.025  70.351 272.213  1.00 39.06           C  
ATOM   1189  CA  LEU X 292      83.507  69.577 271.047  1.00 34.80           C  
ATOM   1190  CA  THR X 293      81.655  72.478 269.484  1.00 39.68           C  
ATOM   1191  CA  LEU X 294      78.237  72.358 267.866  1.00 23.50           C  
ATOM   1192  CA  LEU X 295      77.952  73.864 264.413  1.00 29.33           C  
ATOM   1193  CA  THR X 296      74.584  74.889 263.077  1.00 26.86           C  
ATOM   1194  CA  THR X 297      73.372  76.295 259.805  1.00 36.31           C  
ATOM   1195  CA  ARG X 298      70.192  77.205 257.974  1.00 48.03           C  
ATOM   1196  CA  ARG X 299      69.360  79.202 254.894  1.00 46.54           C  
ATOM   1197  CA  LEU X 300      67.633  82.542 255.158  1.00 57.00           C  
ATOM   1198  CA  GLY X 301      65.157  81.801 252.368  1.00 65.28           C  
ATOM   1199  CA  ALA X 302      62.507  79.105 252.293  1.00 76.12           C  
ATOM   1200  CA  ASN X 303      64.083  75.680 252.202  1.00 55.20           C  
ATOM   1201  CA  PRO X 304      66.651  76.334 254.977  1.00 33.92           C  
ATOM   1202  CA  GLU X 305      67.886  72.739 254.886  1.00 53.45           C  
ATOM   1203  CA  PRO X 306      69.047  73.211 258.491  1.00 45.03           C  
ATOM   1204  CA  THR X 307      72.272  71.429 259.419  1.00 42.35           C  
ATOM   1205  CA  THR X 308      73.663  70.495 262.809  1.00 47.28           C  
ATOM   1206  CA  GLU X 309      76.966  68.732 263.521  1.00 41.22           C  
ATOM   1207  CA  TRP X 310      79.421  68.470 266.397  1.00 29.61           C  
ATOM   1208  CA  ILE X 311      83.000  69.013 265.415  1.00 43.56           C  
ATOM   1209  CA  VAL X 312      86.407  68.484 266.983  1.00 43.30           C  
ATOM   1210  CA  GLY X 313      89.901  69.422 266.091  1.00 54.79           C  
ATOM   1211  CA  LYS X 314      90.672  70.411 262.547  1.00 57.71           C  
ATOM   1212  CA  THR X 315      88.461  70.411 259.519  1.00 52.69           C  
ATOM   1213  CA  VAL X 316      86.978  72.592 256.844  1.00 40.13           C  
ATOM   1214  CA  ARG X 317      83.318  72.843 255.942  1.00 39.84           C  
ATOM   1215  CA  ASN X 318      82.007  74.745 252.965  1.00 28.27           C  
ATOM   1216  CA  PHE X 319      78.326  75.689 252.528  1.00 53.26           C  
ATOM   1217  CA  THR X 320      76.211  76.830 249.859  1.00 52.79           C  
ATOM   1218  CA  VAL X 321      75.124  80.729 249.825  1.00 51.43           C  
ATOM   1219  CA  ASP X 322      71.702  80.389 248.212  1.00 56.20           C  
ATOM   1220  CA  ARG X 323      71.660  84.045 247.210  1.00 42.64           C  
ATOM   1221  CA  ASP X 324      69.571  84.716 250.313  1.00 49.09           C  
ATOM   1222  CA  GLY X 325      72.668  84.060 252.384  1.00 30.69           C  
ATOM   1223  CA  LEU X 326      72.596  81.879 255.483  1.00 35.62           C  
ATOM   1224  CA  GLU X 327      73.132  81.933 259.213  1.00 31.88           C  
ATOM   1225  CA  TYR X 328      75.646  79.858 261.120  1.00 22.71           C  
ATOM   1226  CA  ILE X 329      75.947  79.489 264.878  1.00 30.52           C  
ATOM   1227  CA  TRP X 330      79.186  77.922 265.991  1.00 32.96           C  
ATOM   1228  CA  GLY X 331      79.624  76.631 269.531  1.00 33.61           C  
ATOM   1229  CA  ASN X 332      77.662  79.136 271.655  1.00 46.39           C  
ATOM   1230  CA  HIS X 333      79.137  81.956 269.638  1.00 49.15           C  
ATOM   1231  CA  GLU X 334      76.858  84.384 268.376  1.00 65.41           C  
ATOM   1232  CA  PRO X 335      75.079  83.611 265.482  1.00 54.22           C  
ATOM   1233  CA  VAL X 336      76.554  85.304 262.412  1.00 61.48           C  
ATOM   1234  CA  ARG X 337      74.999  85.144 259.000  1.00 41.98           C  
ATOM   1235  CA  VAL X 338      76.664  85.641 255.653  1.00 56.41           C  
ATOM   1236  CA  TYR X 339      75.314  86.767 252.294  1.00 33.30           C  
ATOM   1237  CA  ALA X 340      76.549  86.959 248.702  1.00 47.38           C  
TER    1238      ALA X 340                                                      
ATOM   1239  CA  TYR E   1      46.295 -10.034 273.979  1.00 59.84           C  
ATOM   1240  CA  GLU E   2      49.324  -8.675 272.121  1.00 58.20           C  
ATOM   1241  CA  HIS E   3      48.640  -5.336 270.418  1.00 60.80           C  
ATOM   1242  CA  ALA E   4      50.836  -3.467 267.943  1.00 71.53           C  
ATOM   1243  CA  THR E   5      50.571   0.335 267.649  1.00 69.76           C  
ATOM   1244  CA  THR E   6      52.948   3.196 266.864  1.00 52.76           C  
ATOM   1245  CA  VAL E   7      52.947   6.113 269.277  1.00 46.93           C  
ATOM   1246  CA  PRO E   8      54.452   9.461 268.235  1.00 55.20           C  
ATOM   1247  CA  ASN E   9      57.310  10.464 270.529  1.00 44.69           C  
ATOM   1248  CA  VAL E  10      56.038  13.649 272.155  1.00 57.43           C  
ATOM   1249  CA  PRO E  11      55.934  14.229 275.925  1.00 60.30           C  
ATOM   1250  CA  GLN E  12      52.579  14.622 277.735  1.00 68.11           C  
ATOM   1251  CA  ILE E  13      50.403  14.122 274.663  1.00 63.90           C  
ATOM   1252  CA  PRO E  14      48.096  11.084 275.131  1.00 58.50           C  
ATOM   1253  CA  TYR E  15      47.422   8.658 272.291  1.00 63.99           C  
ATOM   1254  CA  LYS E  16      43.909   7.232 272.069  1.00 56.67           C  
ATOM   1255  CA  ALA E  17      43.430   3.917 270.268  1.00 64.25           C  
ATOM   1256  CA  LEU E  18      40.922   1.059 270.133  1.00 64.42           C  
ATOM   1257  CA  VAL E  19      41.631  -2.580 270.835  1.00 62.31           C  
ATOM   1258  CA  GLU E  20      39.600  -4.639 268.367  1.00 87.05           C  
ATOM   1259  CA  ARG E  21      39.134  -8.313 269.245  1.00 85.12           C  
ATOM   1260  CA  ALA E  22      36.689 -10.815 267.749  1.00 94.46           C  
ATOM   1261  CA  GLY E  23      33.584 -11.116 269.914  1.00 85.40           C  
ATOM   1262  CA  TYR E  24      35.266  -9.053 272.618  1.00 53.04           C  
ATOM   1263  CA  ALA E  25      34.229  -5.460 273.353  1.00 65.39           C  
ATOM   1264  CA  PRO E  26      36.597  -2.597 272.392  1.00 54.61           C  
ATOM   1265  CA  LEU E  27      39.152  -1.500 274.974  1.00 32.29           C  
ATOM   1266  CA  ASN E  28      40.026   1.787 276.614  1.00 48.33           C  
ATOM   1267  CA  LEU E  29      43.610   2.448 275.498  1.00 40.39           C  
ATOM   1268  CA  GLU E  30      45.514   5.674 276.115  1.00 38.92           C  
ATOM   1269  CA  ILE E  31      49.315   5.890 276.169  1.00 38.54           C  
ATOM   1270  CA  THR E  32      51.154   8.951 277.446  1.00 41.87           C  
ATOM   1271  CA  VAL E  33      54.923   9.189 276.969  1.00 52.63           C  
ATOM   1272  CA  MET E  34      55.492  11.083 280.195  1.00 58.26           C  
ATOM   1273  CA  SER E  35      59.239  11.400 279.784  1.00 63.87           C  
ATOM   1274  CA  SER E  36      61.830  10.473 277.183  1.00 58.35           C  
ATOM   1275  CA  GLU E  37      65.568  10.313 277.882  1.00 54.98           C  
ATOM   1276  CA  VAL E  38      68.281   9.825 275.296  1.00 44.66           C  
ATOM   1277  CA  LEU E  39      71.338   8.406 277.037  1.00 53.61           C  
ATOM   1278  CA  PRO E  40      74.506   8.085 274.973  1.00 55.68           C  
ATOM   1279  CA  SER E  41      77.799   6.521 276.076  1.00 45.20           C  
ATOM   1280  CA  THR E  42      80.369   8.837 277.585  1.00 62.13           C  
ATOM   1281  CA  ASN E  43      84.096   8.098 277.383  1.00 43.23           C  
ATOM   1282  CA  GLN E  44      85.514  10.959 279.457  1.00 48.53           C  
ATOM   1283  CA  GLU E  45      88.867  11.748 277.861  1.00 30.97           C  
ATOM   1284  CA  TYR E  46      90.555  14.443 279.943  1.00 26.36           C  
ATOM   1285  CA  ILE E  47      90.121  17.342 282.301  1.00 40.69           C  
ATOM   1286  CA  THR E  48      91.451  20.801 281.540  1.00 40.99           C  
ATOM   1287  CA  CYS E  49      91.628  24.160 283.241  1.00 46.46           C  
ATOM   1288  CA  LYS E  50      93.629  27.286 284.011  1.00 60.18           C  
ATOM   1289  CA  PHE E  51      97.210  26.073 284.386  1.00 40.94           C  
ATOM   1290  CA  THR E  52      99.801  27.688 286.610  1.00 57.35           C  
ATOM   1291  CA  THR E  53     103.427  28.036 285.567  1.00 48.09           C  
ATOM   1292  CA  VAL E  54     106.084  27.285 288.138  1.00 55.22           C  
ATOM   1293  CA  VAL E  55     109.531  28.775 287.768  1.00 53.15           C  
ATOM   1294  CA  PRO E  56     112.239  27.361 290.067  1.00 30.06           C  
ATOM   1295  CA  SER E  57     115.217  29.604 290.851  1.00 17.55           C  
ATOM   1296  CA  PRO E  58     117.673  29.177 287.971  1.00 34.88           C  
ATOM   1297  CA  LYS E  59     120.668  26.962 288.607  1.00 23.34           C  
ATOM   1298  CA  ILE E  60     123.823  28.887 287.702  1.00 18.35           C  
ATOM   1299  CA  LYS E  61     127.322  27.428 288.150  1.00 40.36           C  
ATOM   1300  CA  CYS E  62     130.102  30.372 288.043  1.00 31.09           C  
ATOM   1301  CA  CYS E  63     132.703  29.076 285.589  1.00 31.02           C  
ATOM   1302  CA  GLY E  64     130.854  25.939 284.513  1.00 48.44           C  
ATOM   1303  CA  SER E  65     128.922  24.427 281.615  1.00 56.49           C  
ATOM   1304  CA  LEU E  66     125.238  23.869 282.379  1.00 53.42           C  
ATOM   1305  CA  GLU E  67     123.761  21.653 279.631  1.00 66.88           C  
ATOM   1306  CA  CYS E  68     120.218  20.310 279.976  1.00 57.51           C  
ATOM   1307  CA  GLN E  69     118.985  16.814 280.723  1.00 60.97           C  
ATOM   1308  CA  PRO E  70     115.778  15.282 279.348  1.00 73.61           C  
ATOM   1309  CA  ALA E  71     113.783  16.214 282.455  1.00 66.07           C  
ATOM   1310  CA  ALA E  72     110.238  15.127 281.604  1.00 64.94           C  
ATOM   1311  CA  HIS E  73     107.617  16.361 284.069  1.00 57.85           C  
ATOM   1312  CA  ALA E  74     104.550  18.197 282.772  1.00 46.64           C  
ATOM   1313  CA  ASP E  75     105.161  21.300 280.669  1.00 38.38           C  
ATOM   1314  CA  TYR E  76     108.884  21.338 281.405  1.00 27.07           C  
ATOM   1315  CA  THR E  77     111.169  23.549 279.318  1.00 44.54           C  
ATOM   1316  CA  CYS E  78     114.873  24.292 279.833  1.00 42.10           C  
ATOM   1317  CA  LYS E  79     117.221  26.517 277.893  1.00 49.95           C  
ATOM   1318  CA  VAL E  80     120.960  26.870 278.277  1.00 43.83           C  
ATOM   1319  CA  PHE E  81     122.014  30.502 278.216  1.00 46.94           C  
ATOM   1320  CA  GLY E  82     125.727  31.162 277.904  1.00 59.80           C  
ATOM   1321  CA  GLY E  83     127.895  34.123 278.829  1.00 55.51           C  
ATOM   1322  CA  VAL E  84     125.604  35.675 281.406  1.00 47.85           C  
ATOM   1323  CA  TYR E  85     126.711  37.564 284.525  1.00 43.15           C  
ATOM   1324  CA  PRO E  86     130.283  38.821 285.049  1.00 45.60           C  
ATOM   1325  CA  PHE E  87     132.285  39.118 288.282  1.00 41.41           C  
ATOM   1326  CA  MET E  88     131.406  40.570 291.676  1.00 58.58           C  
ATOM   1327  CA  TRP E  89     127.762  41.698 291.465  1.00 46.57           C  
ATOM   1328  CA  GLY E  90     126.075  42.461 288.150  1.00 49.87           C  
ATOM   1329  CA  GLY E  91     124.802  39.050 287.631  1.00 28.65           C  
ATOM   1330  CA  ALA E  92     125.638  36.885 290.661  1.00 38.62           C  
ATOM   1331  CA  GLN E  93     128.680  36.366 292.844  1.00 43.25           C  
ATOM   1332  CA  CYS E  94     131.060  34.941 290.243  1.00 25.78           C  
ATOM   1333  CA  PHE E  95     134.501  35.951 288.969  1.00 23.92           C  
ATOM   1334  CA  CYS E  96     134.504  35.125 285.256  1.00 35.70           C  
ATOM   1335  CA  ASP E  97     132.873  37.050 282.403  1.00 48.00           C  
ATOM   1336  CA  SER E  98     132.287  35.079 279.202  1.00 65.10           C  
ATOM   1337  CA  GLU E  99     132.551  31.668 280.786  1.00 52.78           C  
ATOM   1338  CA  ASN E 100     129.157  31.771 282.511  1.00 29.81           C  
ATOM   1339  CA  SER E 101     125.957  29.809 281.989  1.00 27.25           C  
ATOM   1340  CA  GLN E 102     122.401  29.825 283.309  1.00 23.71           C  
ATOM   1341  CA  MET E 103     119.752  27.146 282.873  1.00 24.53           C  
ATOM   1342  CA  SER E 104     116.229  28.488 282.661  1.00 50.49           C  
ATOM   1343  CA  GLU E 105     113.630  25.842 283.390  1.00 43.05           C  
ATOM   1344  CA  ALA E 106     109.872  26.076 283.863  1.00 46.59           C  
ATOM   1345  CA  TYR E 107     106.803  23.840 283.783  1.00 38.08           C  
ATOM   1346  CA  VAL E 108     103.032  24.088 284.281  1.00 41.06           C  
ATOM   1347  CA  GLU E 109     100.708  22.745 286.991  1.00 47.37           C  
ATOM   1348  CA  LEU E 110      96.989  22.968 287.702  1.00 40.02           C  
ATOM   1349  CA  SER E 111      95.543  26.046 289.337  1.00 64.87           C  
ATOM   1350  CA  ALA E 112      94.997  26.161 293.073  1.00 61.71           C  
ATOM   1351  CA  ASP E 113      91.421  26.186 291.866  1.00 54.05           C  
ATOM   1352  CA  CYS E 114      91.561  23.899 288.792  1.00 41.78           C  
ATOM   1353  CA  ALA E 115      89.101  21.726 290.660  1.00 43.29           C  
ATOM   1354  CA  SER E 116      86.406  24.319 291.267  1.00 50.42           C  
ATOM   1355  CA  ASP E 117      86.399  25.459 287.601  1.00 55.47           C  
ATOM   1356  CA  HIS E 118      87.355  23.083 284.803  1.00 39.13           C  
ATOM   1357  CA  ALA E 119      85.888  21.389 281.787  1.00 38.15           C  
ATOM   1358  CA  GLN E 120      85.592  17.828 280.594  1.00 36.25           C  
ATOM   1359  CA  ALA E 121      86.549  16.583 277.160  1.00 37.77           C  
ATOM   1360  CA  ILE E 122      84.154  13.771 276.411  1.00 38.42           C  
ATOM   1361  CA  LYS E 123      83.635  11.379 273.523  1.00 33.53           C  
ATOM   1362  CA  VAL E 124      80.044  10.431 272.781  1.00 54.37           C  
ATOM   1363  CA  HIS E 125      79.027   7.239 271.029  1.00 38.43           C  
ATOM   1364  CA  THR E 126      75.791   5.475 270.139  1.00 53.06           C  
ATOM   1365  CA  ALA E 127      72.962   5.888 272.640  1.00 58.88           C  
ATOM   1366  CA  ALA E 128      69.975   4.203 274.181  1.00 72.85           C  
ATOM   1367  CA  MET E 129      66.683   5.837 275.154  1.00 45.80           C  
ATOM   1368  CA  LYS E 130      64.347   5.089 278.041  1.00 37.48           C  
ATOM   1369  CA  VAL E 131      60.711   6.228 278.004  1.00 55.55           C  
ATOM   1370  CA  GLY E 132      58.391   6.882 280.941  1.00 58.36           C  
ATOM   1371  CA  LEU E 133      55.157   5.467 279.604  1.00 50.17           C  
ATOM   1372  CA  ARG E 134      51.721   5.601 281.175  1.00 30.80           C  
ATOM   1373  CA  ILE E 135      49.166   3.231 279.709  1.00 34.36           C  
ATOM   1374  CA  VAL E 136      45.541   3.000 280.758  1.00 37.09           C  
ATOM   1375  CA  TYR E 137      43.293   0.064 279.900  1.00 30.97           C  
ATOM   1376  CA  GLY E 138      39.687  -0.146 281.032  1.00 43.20           C  
ATOM   1377  CA  ASN E 139      39.297   0.648 284.732  1.00 55.29           C  
ATOM   1378  CA  THR E 140      43.036   0.359 285.465  1.00 38.28           C  
ATOM   1379  CA  THR E 141      46.023   2.592 284.682  1.00 44.43           C  
ATOM   1380  CA  SER E 142      49.615   1.380 284.751  1.00 48.07           C  
ATOM   1381  CA  PHE E 143      53.067   2.683 283.857  1.00 38.62           C  
ATOM   1382  CA  LEU E 144      56.453   1.238 282.976  1.00 55.18           C  
ATOM   1383  CA  ASP E 145      59.846   2.610 281.959  1.00 58.05           C  
ATOM   1384  CA  VAL E 146      61.028   0.963 278.784  1.00 51.47           C  
ATOM   1385  CA  TYR E 147      64.211   1.073 276.718  1.00 35.26           C  
ATOM   1386  CA  VAL E 148      63.630   1.553 273.024  1.00 39.59           C  
ATOM   1387  CA  ASN E 149      64.814  -1.535 271.180  1.00 55.45           C  
ATOM   1388  CA  GLY E 150      62.887  -4.478 269.787  1.00 70.68           C  
ATOM   1389  CA  VAL E 151      64.065  -6.480 272.789  1.00 66.62           C  
ATOM   1390  CA  THR E 152      64.009  -5.334 276.420  1.00 52.34           C  
ATOM   1391  CA  PRO E 153      60.564  -5.540 278.045  1.00 49.90           C  
ATOM   1392  CA  GLY E 154      59.851  -3.211 280.964  1.00 60.17           C  
ATOM   1393  CA  THR E 155      58.960  -5.833 283.561  1.00 70.17           C  
ATOM   1394  CA  SER E 156      55.883  -3.920 284.720  1.00 68.92           C  
ATOM   1395  CA  LYS E 157      54.643  -6.649 287.062  1.00 65.48           C  
ATOM   1396  CA  ASP E 158      51.563  -7.367 284.949  1.00 45.19           C  
ATOM   1397  CA  LEU E 159      51.790  -6.166 281.362  1.00 43.10           C  
ATOM   1398  CA  LYS E 160      54.659  -6.853 278.956  1.00 40.88           C  
ATOM   1399  CA  VAL E 161      55.497  -3.699 276.992  1.00 54.31           C  
ATOM   1400  CA  ILE E 162      58.436  -3.920 274.596  1.00 49.00           C  
ATOM   1401  CA  ALA E 163      59.094  -0.661 272.771  1.00 50.14           C  
ATOM   1402  CA  GLY E 164      60.322  -1.320 269.244  1.00 46.39           C  
ATOM   1403  CA  PRO E 165      63.327   0.485 267.745  1.00 56.85           C  
ATOM   1404  CA  ILE E 166      62.769   4.218 267.349  1.00 60.56           C  
ATOM   1405  CA  SER E 167      61.883   5.349 263.798  1.00 71.93           C  
ATOM   1406  CA  ALA E 168      64.853   7.704 263.277  1.00 70.48           C  
ATOM   1407  CA  SER E 169      68.174   7.575 265.096  1.00 74.39           C  
ATOM   1408  CA  PHE E 170      68.706  11.168 266.178  1.00 57.14           C  
ATOM   1409  CA  THR E 171      71.128  12.723 268.650  1.00 52.92           C  
ATOM   1410  CA  PRO E 172      71.681  16.320 269.802  1.00 61.54           C  
ATOM   1411  CA  PHE E 173      75.367  15.532 270.279  1.00 55.64           C  
ATOM   1412  CA  ASP E 174      78.535  15.173 268.198  1.00 52.21           C  
ATOM   1413  CA  HIS E 175      81.171  12.484 268.695  1.00 50.89           C  
ATOM   1414  CA  LYS E 176      83.101  15.035 270.746  1.00 42.73           C  
ATOM   1415  CA  VAL E 177      81.492  17.244 273.390  1.00 31.28           C  
ATOM   1416  CA  VAL E 178      82.728  19.536 276.130  1.00 34.93           C  
ATOM   1417  CA  ILE E 179      81.028  19.861 279.476  1.00 33.91           C  
ATOM   1418  CA  HIS E 180      81.876  22.975 281.423  1.00 27.44           C  
ATOM   1419  CA  ARG E 181      79.752  23.780 284.432  1.00 46.70           C  
ATOM   1420  CA  GLY E 182      76.313  22.324 283.930  1.00 72.95           C  
ATOM   1421  CA  LEU E 183      76.720  23.146 280.330  1.00 48.77           C  
ATOM   1422  CA  VAL E 184      77.584  21.061 277.341  1.00 39.53           C  
ATOM   1423  CA  TYR E 185      78.904  22.283 273.979  1.00 42.51           C  
ATOM   1424  CA  ASN E 186      79.571  20.382 270.776  1.00 47.92           C  
ATOM   1425  CA  TYR E 187      83.324  21.066 270.452  1.00 43.83           C  
ATOM   1426  CA  ASP E 188      85.958  19.068 268.541  1.00 43.77           C  
ATOM   1427  CA  PHE E 189      88.574  19.177 271.318  1.00 45.54           C  
ATOM   1428  CA  PRO E 190      91.890  17.589 270.371  1.00 47.08           C  
ATOM   1429  CA  GLU E 191      92.788  13.994 271.246  1.00 40.30           C  
ATOM   1430  CA  TYR E 192      94.513  13.342 274.529  1.00 38.22           C  
ATOM   1431  CA  GLY E 193      98.143  13.935 273.705  1.00 44.92           C  
ATOM   1432  CA  ALA E 194      97.931  16.021 270.558  1.00 51.01           C  
ATOM   1433  CA  MET E 195      97.478  19.414 272.168  1.00 38.52           C  
ATOM   1434  CA  LYS E 196      97.814  22.858 270.641  1.00 44.50           C  
ATOM   1435  CA  PRO E 197      98.670  25.706 273.039  1.00 45.95           C  
ATOM   1436  CA  GLY E 198      96.398  28.659 273.754  1.00 57.78           C  
ATOM   1437  CA  ALA E 199      93.555  26.664 272.184  1.00 61.31           C  
ATOM   1438  CA  PHE E 200      91.142  24.487 274.179  1.00 42.81           C  
ATOM   1439  CA  GLY E 201      92.850  21.545 275.798  1.00 42.28           C  
ATOM   1440  CA  ASP E 202      96.263  23.158 275.975  1.00 49.19           C  
ATOM   1441  CA  ILE E 203      96.847  21.156 279.152  1.00 49.16           C  
ATOM   1442  CA  GLN E 204      95.313  17.718 279.722  1.00 45.23           C  
ATOM   1443  CA  ALA E 205      94.779  15.247 282.549  1.00 56.74           C  
ATOM   1444  CA  THR E 206      92.824  11.999 282.877  1.00 44.40           C  
ATOM   1445  CA  SER E 207      91.195  12.885 286.199  1.00 67.58           C  
ATOM   1446  CA  LEU E 208      91.139  15.869 288.558  1.00 75.96           C  
ATOM   1447  CA  THR E 209      93.582  14.032 290.821  1.00 79.79           C  
ATOM   1448  CA  SER E 210      96.258  15.556 288.588  1.00 79.29           C  
ATOM   1449  CA  LYS E 211      96.850  12.074 286.807  1.00 48.10           C  
ATOM   1450  CA  ASP E 212      99.884  11.996 284.289  1.00 56.53           C  
ATOM   1451  CA  LEU E 213      99.000  15.476 282.962  1.00 58.31           C  
ATOM   1452  CA  ILE E 214     100.472  16.533 279.622  1.00 37.63           C  
ATOM   1453  CA  ALA E 215     100.660  20.208 278.665  1.00 43.12           C  
ATOM   1454  CA  SER E 216     101.852  22.216 275.652  1.00 47.27           C  
ATOM   1455  CA  THR E 217     101.836  25.966 276.386  1.00 61.26           C  
ATOM   1456  CA  ASP E 218     104.449  27.519 274.044  1.00 46.35           C  
ATOM   1457  CA  ILE E 219     106.715  28.642 276.865  1.00 45.58           C  
ATOM   1458  CA  ARG E 220     109.676  30.630 275.640  1.00 35.47           C  
ATOM   1459  CA  LEU E 221     112.755  31.349 277.729  1.00 38.12           C  
ATOM   1460  CA  LEU E 222     114.618  34.609 277.352  1.00 49.10           C  
ATOM   1461  CA  LYS E 223     118.275  35.401 277.920  1.00 49.17           C  
ATOM   1462  CA  PRO E 224     118.243  37.243 281.257  1.00 41.47           C  
ATOM   1463  CA  SER E 225     119.976  40.622 281.536  1.00 49.08           C  
ATOM   1464  CA  ALA E 226     122.760  41.179 284.065  1.00 44.07           C  
ATOM   1465  CA  LYS E 227     121.599  43.284 286.991  1.00 47.82           C  
ATOM   1466  CA  ASN E 228     119.516  40.657 288.815  1.00 39.65           C  
ATOM   1467  CA  VAL E 229     118.947  36.923 288.787  1.00 50.54           C  
ATOM   1468  CA  HIS E 230     115.527  36.962 287.186  1.00 44.06           C  
ATOM   1469  CA  VAL E 231     114.301  34.331 284.746  1.00 39.87           C  
ATOM   1470  CA  PRO E 232     112.338  35.822 281.819  1.00 38.62           C  
ATOM   1471  CA  TYR E 233     109.835  33.894 279.731  1.00 42.02           C  
ATOM   1472  CA  THR E 234     106.953  34.379 277.342  1.00 50.36           C  
ATOM   1473  CA  GLN E 235     104.196  31.835 277.079  1.00 40.59           C  
ATOM   1474  CA  ALA E 236     100.927  31.242 275.320  1.00 55.40           C  
ATOM   1475  CA  SER E 237      97.508  32.219 276.600  1.00 76.96           C  
ATOM   1476  CA  SER E 238      95.274  29.944 278.699  1.00 53.09           C  
ATOM   1477  CA  GLY E 239      93.506  27.878 276.044  1.00 35.33           C  
ATOM   1478  CA  PHE E 240      90.856  27.342 278.683  1.00 26.52           C  
ATOM   1479  CA  GLU E 241      89.979  30.883 279.666  1.00 39.31           C  
ATOM   1480  CA  MET E 242      90.344  31.486 275.944  1.00 38.35           C  
ATOM   1481  CA  TRP E 243      87.712  28.898 275.159  1.00 23.70           C  
ATOM   1482  CA  LYS E 244      85.521  30.168 277.996  1.00 37.78           C  
ATOM   1483  CA  ASN E 245      85.384  33.744 276.585  1.00 47.62           C  
ATOM   1484  CA  ASN E 246      84.461  32.089 273.332  1.00 44.21           C  
ATOM   1485  CA  SER E 247      82.329  29.147 274.357  1.00 50.65           C  
ATOM   1486  CA  GLY E 248      79.112  29.331 272.424  1.00 63.64           C  
ATOM   1487  CA  ARG E 249      75.591  29.259 273.576  1.00 52.55           C  
ATOM   1488  CA  PRO E 250      75.195  25.832 275.323  1.00 23.82           C  
ATOM   1489  CA  LEU E 251      73.425  22.921 273.683  1.00 38.22           C  
ATOM   1490  CA  GLN E 252      70.698  23.213 276.297  1.00 39.54           C  
ATOM   1491  CA  GLU E 253      69.946  26.333 274.251  1.00 48.26           C  
ATOM   1492  CA  THR E 254      70.558  25.056 270.724  1.00 40.59           C  
ATOM   1493  CA  ALA E 255      69.217  21.491 270.851  1.00 43.24           C  
ATOM   1494  CA  PRO E 256      67.619  20.584 267.453  1.00 48.50           C  
ATOM   1495  CA  PHE E 257      64.312  19.128 268.752  1.00 47.66           C  
ATOM   1496  CA  GLY E 258      63.471  21.074 271.856  1.00 47.10           C  
ATOM   1497  CA  CYS E 259      65.525  18.651 273.913  1.00 40.22           C  
ATOM   1498  CA  LYS E 260      66.332  19.592 277.496  1.00 45.74           C  
ATOM   1499  CA  ILE E 261      70.042  18.719 277.764  1.00 64.85           C  
ATOM   1500  CA  ALA E 262      71.153  17.370 281.157  1.00 67.38           C  
ATOM   1501  CA  VAL E 263      74.422  16.701 282.999  1.00 63.12           C  
ATOM   1502  CA  ASN E 264      75.358  14.339 285.179  1.00 65.03           C  
ATOM   1503  CA  PRO E 265      74.290  11.424 283.129  1.00 44.75           C  
ATOM   1504  CA  LEU E 266      74.737  13.046 279.704  1.00 46.78           C  
ATOM   1505  CA  ARG E 267      71.144  13.055 278.479  1.00 32.01           C  
ATOM   1506  CA  ALA E 268      68.580  14.658 276.177  1.00 47.05           C  
ATOM   1507  CA  VAL E 269      65.409  14.932 278.284  1.00 53.07           C  
ATOM   1508  CA  ASP E 270      62.026  15.147 276.555  1.00 51.22           C  
ATOM   1509  CA  CYS E 271      63.015  15.470 272.918  1.00 46.61           C  
ATOM   1510  CA  SER E 272      60.228  15.176 270.354  1.00 44.79           C  
ATOM   1511  CA  TYR E 273      60.731  13.379 267.054  1.00 53.45           C  
ATOM   1512  CA  GLY E 274      59.545  10.290 265.204  1.00 69.16           C  
ATOM   1513  CA  ASN E 275      57.168   7.572 266.305  1.00 56.76           C  
ATOM   1514  CA  ILE E 276      57.754   4.694 268.718  1.00 52.84           C  
ATOM   1515  CA  PRO E 277      56.516   1.250 267.788  1.00 45.72           C  
ATOM   1516  CA  ILE E 278      54.915  -0.331 270.857  1.00 50.76           C  
ATOM   1517  CA  SER E 279      53.776  -3.876 271.581  1.00 55.24           C  
ATOM   1518  CA  ILE E 280      51.385  -4.328 274.496  1.00 52.87           C  
ATOM   1519  CA  ASP E 281      50.262  -7.507 276.288  1.00 35.84           C  
ATOM   1520  CA  ILE E 282      46.822  -6.926 277.843  1.00 57.95           C  
ATOM   1521  CA  PRO E 283      45.931  -9.444 280.573  1.00 54.94           C  
ATOM   1522  CA  ASN E 284      42.684 -11.173 279.586  1.00 58.81           C  
ATOM   1523  CA  ALA E 285      41.733 -10.577 283.220  1.00 61.56           C  
ATOM   1524  CA  ALA E 286      40.100  -7.207 282.553  1.00 62.07           C  
ATOM   1525  CA  PHE E 287      39.342  -6.211 278.960  1.00 48.61           C  
ATOM   1526  CA  ILE E 288      35.777  -7.495 278.731  1.00 37.47           C  
ATOM   1527  CA  ARG E 289      34.074  -9.804 276.231  1.00 35.80           C  
ATOM   1528  CA  THR E 290      30.674  -8.874 274.765  1.00 64.21           C  
ATOM   1529  CA  SER E 291      28.433 -10.370 277.451  1.00 52.20           C  
ATOM   1530  CA  ASP E 292      27.691  -7.025 279.104  1.00 44.40           C  
ATOM   1531  CA  ALA E 293      26.193  -4.172 277.084  1.00 44.48           C  
ATOM   1532  CA  PRO E 294      22.430  -5.112 281.619  1.00 69.51           C  
ATOM   1533  CA  LEU E 295      21.389  -4.407 278.025  1.00 40.28           C  
ATOM   1534  CA  VAL E 296      22.333  -1.457 275.819  1.00 37.44           C  
ATOM   1535  CA  SER E 297      20.812  -0.616 272.435  1.00 50.57           C  
ATOM   1536  CA  THR E 298      20.483   2.197 269.894  1.00 55.32           C  
ATOM   1537  CA  VAL E 299      23.158   4.892 269.706  1.00 58.26           C  
ATOM   1538  CA  LYS E 300      22.987   7.836 267.301  1.00 57.25           C  
ATOM   1539  CA  CYS E 301      25.363  10.796 267.151  1.00 54.41           C  
ATOM   1540  CA  GLU E 302      24.583  14.521 266.966  1.00 53.00           C  
ATOM   1541  CA  VAL E 303      27.182  17.310 266.967  1.00 47.92           C  
ATOM   1542  CA  SER E 304      26.162  20.595 268.604  1.00 69.49           C  
ATOM   1543  CA  GLU E 305      29.238  22.766 268.025  1.00 59.21           C  
ATOM   1544  CA  CYS E 306      32.723  22.333 266.558  1.00 56.70           C  
ATOM   1545  CA  THR E 307      35.957  24.225 265.950  1.00 38.87           C  
ATOM   1546  CA  TYR E 308      38.672  23.154 263.506  1.00 29.84           C  
ATOM   1547  CA  SER E 309      42.168  22.379 264.851  1.00 53.31           C  
ATOM   1548  CA  ALA E 310      41.573  23.488 268.447  1.00 51.21           C  
ATOM   1549  CA  ASP E 311      42.393  21.821 271.765  1.00 62.72           C  
ATOM   1550  CA  PHE E 312      38.845  20.565 272.362  1.00 47.56           C  
ATOM   1551  CA  GLY E 313      36.383  22.619 270.335  1.00 59.32           C  
ATOM   1552  CA  GLY E 314      34.225  19.632 269.454  1.00 49.18           C  
ATOM   1553  CA  MET E 315      30.854  19.096 271.117  1.00 36.11           C  
ATOM   1554  CA  ALA E 316      28.648  16.086 270.357  1.00 39.91           C  
ATOM   1555  CA  THR E 317      25.749  14.381 272.132  1.00 38.71           C  
ATOM   1556  CA  LEU E 318      24.560  10.771 272.038  1.00 36.09           C  
ATOM   1557  CA  GLN E 319      20.924   9.691 272.305  1.00 42.02           C  
ATOM   1558  CA  TYR E 320      20.141   6.058 273.085  1.00 35.31           C  
ATOM   1559  CA  VAL E 321      18.194   3.623 275.262  1.00 32.97           C  
ATOM   1560  CA  SER E 322      19.661   1.691 278.197  1.00 26.99           C  
ATOM   1561  CA  ASP E 323      18.159  -1.009 280.427  1.00 51.65           C  
ATOM   1562  CA  ARG E 324      19.854   0.331 283.567  1.00 42.75           C  
ATOM   1563  CA  GLU E 325      22.672   2.553 284.809  1.00 34.11           C  
ATOM   1564  CA  GLY E 326      26.372   1.820 284.417  1.00 33.02           C  
ATOM   1565  CA  GLN E 327      29.707   3.140 283.176  1.00 33.27           C  
ATOM   1566  CA  CYS E 328      30.667   3.078 279.490  1.00 21.26           C  
ATOM   1567  CA  PRO E 329      34.097   3.663 277.897  1.00 33.49           C  
ATOM   1568  CA  VAL E 330      33.774   6.069 274.964  1.00 49.32           C  
ATOM   1569  CA  HIS E 331      36.393   6.008 272.204  1.00 47.59           C  
ATOM   1570  CA  SER E 332      36.892   6.870 268.524  1.00 39.62           C  
ATOM   1571  CA  HIS E 333      37.710   4.199 265.928  1.00 59.04           C  
ATOM   1572  CA  SER E 334      39.255   6.683 263.491  1.00 65.31           C  
ATOM   1573  CA  SER E 335      42.282   8.944 263.923  1.00 76.11           C  
ATOM   1574  CA  THR E 336      40.434  11.776 262.172  1.00 68.09           C  
ATOM   1575  CA  ALA E 337      39.170  12.668 265.647  1.00 59.82           C  
ATOM   1576  CA  THR E 338      39.838  11.936 269.316  1.00 66.20           C  
ATOM   1577  CA  LEU E 339      37.724  12.255 272.464  1.00 45.88           C  
ATOM   1578  CA  GLN E 340      38.660  14.315 275.530  1.00 48.98           C  
ATOM   1579  CA  GLU E 341      37.154  11.686 277.803  1.00 61.97           C  
ATOM   1580  CA  SER E 342      37.277   7.899 277.644  1.00 64.75           C  
ATOM   1581  CA  THR E 343      34.510   7.006 280.108  1.00 63.14           C  
ATOM   1582  CA  VAL E 344      30.926   8.193 280.615  1.00 75.51           C  
ATOM   1583  CA  HIS E 345      28.218   7.687 283.254  1.00 71.19           C  
ATOM   1584  CA  VAL E 346      25.356   6.218 281.238  1.00 59.83           C  
ATOM   1585  CA  LEU E 347      21.963   7.017 282.737  1.00 62.49           C  
ATOM   1586  CA  GLU E 348      18.454   5.979 281.715  1.00 55.09           C  
ATOM   1587  CA  LYS E 349      17.800   9.451 280.280  1.00 73.63           C  
ATOM   1588  CA  GLY E 350      19.417   8.450 276.997  1.00 41.85           C  
ATOM   1589  CA  ALA E 351      21.591  11.536 276.614  1.00 58.60           C  
ATOM   1590  CA  VAL E 352      25.390  11.685 276.749  1.00 49.58           C  
ATOM   1591  CA  THR E 353      27.381  14.848 276.057  1.00 52.10           C  
ATOM   1592  CA  VAL E 354      31.021  14.439 274.982  1.00 53.36           C  
ATOM   1593  CA  HIS E 355      33.885  16.738 273.965  1.00 31.52           C  
ATOM   1594  CA  PHE E 356      36.288  15.951 271.123  1.00 29.66           C  
ATOM   1595  CA  SER E 357      39.196  17.426 269.173  1.00 39.26           C  
ATOM   1596  CA  THR E 358      39.877  17.417 265.431  1.00 48.46           C  
ATOM   1597  CA  ALA E 359      41.725  19.209 262.632  1.00 56.51           C  
ATOM   1598  CA  SER E 360      39.404  18.986 259.630  1.00 51.26           C  
ATOM   1599  CA  PRO E 361      36.458  20.864 258.065  1.00 41.92           C  
ATOM   1600  CA  GLN E 362      33.986  18.037 257.445  1.00 55.29           C  
ATOM   1601  CA  ALA E 363      35.208  15.009 259.389  1.00 62.00           C  
ATOM   1602  CA  ASN E 364      33.834  11.464 259.489  1.00 63.69           C  
ATOM   1603  CA  PHE E 365      34.481   9.348 262.582  1.00 52.28           C  
ATOM   1604  CA  ILE E 366      32.996   6.253 264.232  1.00 44.42           C  
ATOM   1605  CA  VAL E 367      32.402   6.874 267.940  1.00 46.15           C  
ATOM   1606  CA  SER E 368      31.793   3.900 270.230  1.00 32.95           C  
ATOM   1607  CA  LEU E 369      29.906   3.579 273.506  1.00 34.36           C  
ATOM   1608  CA  CYS E 370      30.128   0.522 275.752  1.00 31.73           C  
ATOM   1609  CA  GLY E 371      29.558  -2.005 272.975  1.00 58.11           C  
ATOM   1610  CA  LYS E 372      27.579   0.002 270.430  1.00 44.50           C  
ATOM   1611  CA  LYS E 373      28.970   2.096 267.571  1.00 42.61           C  
ATOM   1612  CA  THR E 374      27.742   5.043 265.493  1.00 53.37           C  
ATOM   1613  CA  THR E 375      28.837   7.778 263.097  1.00 55.47           C  
ATOM   1614  CA  CYS E 376      29.113  11.532 263.671  1.00 59.64           C  
ATOM   1615  CA  ASN E 377      29.202  14.569 261.381  1.00 53.90           C  
ATOM   1616  CA  ALA E 378      29.550  18.358 261.367  1.00 58.83           C  
ATOM   1617  CA  GLU E 379      31.351  21.296 259.760  1.00 60.10           C  
ATOM   1618  CA  CYS E 380      34.146  23.130 261.589  1.00 40.91           C  
TER    1619      CYS E 380                                                      
ATOM   1620  CA  PHE Y   6     106.538  24.296 310.899  1.00 48.59           C  
ATOM   1621  CA  THR Y   7     109.133  25.796 309.196  1.00 35.90           C  
ATOM   1622  CA  LEU Y   8     111.933  24.355 307.102  1.00 41.42           C  
ATOM   1623  CA  THR Y   9     112.196  27.309 304.735  1.00 17.61           C  
ATOM   1624  CA  SER Y  10     112.558  31.088 305.135  1.00 30.20           C  
ATOM   1625  CA  PRO Y  11     111.354  34.278 303.328  1.00 29.58           C  
ATOM   1626  CA  TYR Y  12     113.298  35.290 300.210  1.00 47.65           C  
ATOM   1627  CA  LEU Y  13     113.726  38.409 298.064  1.00 46.84           C  
ATOM   1628  CA  GLY Y  14     112.419  38.919 294.546  1.00 55.47           C  
ATOM   1629  CA  THR Y  15     112.702  41.487 291.794  1.00 60.22           C  
ATOM   1630  CA  CYS Y  16     109.572  43.643 291.595  1.00 51.04           C  
ATOM   1631  CA  SER Y  17     108.358  46.209 289.069  1.00 59.83           C  
ATOM   1632  CA  TYR Y  18     106.885  48.836 291.418  1.00 53.22           C  
ATOM   1633  CA  CYS Y  19     107.715  49.414 295.095  1.00 52.61           C  
ATOM   1634  CA  HIS Y  20     106.120  52.513 296.684  1.00 61.47           C  
ATOM   1635  CA  HIS Y  21     108.225  54.321 294.102  1.00 34.52           C  
ATOM   1636  CA  THR Y  22     107.233  53.435 290.550  1.00 44.24           C  
ATOM   1637  CA  VAL Y  23     110.833  52.297 289.961  1.00 36.14           C  
ATOM   1638  CA  PRO Y  24     111.298  48.482 289.900  1.00 45.20           C  
ATOM   1639  CA  CYS Y  25     113.094  47.268 293.023  1.00 44.51           C  
ATOM   1640  CA  PHE Y  26     114.429  44.142 294.697  1.00 38.41           C  
ATOM   1641  CA  SER Y  27     112.272  43.833 297.777  1.00 42.17           C  
ATOM   1642  CA  PRO Y  28     110.553  41.196 299.947  1.00 34.33           C  
ATOM   1643  CA  VAL Y  29     106.826  40.558 299.542  1.00 44.36           C  
ATOM   1644  CA  LYS Y  30     107.573  39.899 295.866  1.00 33.55           C  
ATOM   1645  CA  ILE Y  31     104.410  38.722 294.159  1.00 47.77           C  
ATOM   1646  CA  GLU Y  32     104.978  35.733 291.879  1.00 61.42           C  
ATOM   1647  CA  GLN Y  33     101.441  34.578 291.067  1.00 56.54           C  
ATOM   1648  CA  VAL Y  34      97.813  35.308 291.843  1.00 42.51           C  
ATOM   1649  CA  TRP Y  35      94.604  33.314 291.494  1.00 31.48           C  
ATOM   1650  CA  ASP Y  36      91.353  34.865 290.359  1.00 61.26           C  
ATOM   1651  CA  GLU Y  37      89.384  31.716 289.647  1.00 66.24           C  
ATOM   1652  CA  ALA Y  38      86.716  31.486 292.325  1.00 53.23           C  
ATOM   1653  CA  ASP Y  39      83.046  32.260 291.732  1.00 53.97           C  
ATOM   1654  CA  ASP Y  40      83.253  34.099 295.014  1.00 52.40           C  
ATOM   1655  CA  ASN Y  41      84.932  37.494 294.929  1.00 41.37           C  
ATOM   1656  CA  THR Y  42      88.012  36.108 296.697  1.00 45.82           C  
ATOM   1657  CA  ILE Y  43      91.682  36.171 295.722  1.00 40.07           C  
ATOM   1658  CA  ARG Y  44      94.705  33.966 296.400  1.00 26.39           C  
ATOM   1659  CA  ILE Y  45      98.084  35.736 296.482  1.00 26.13           C  
ATOM   1660  CA  GLN Y  46     101.589  34.232 296.473  1.00 21.11           C  
ATOM   1661  CA  THR Y  47     104.310  36.334 298.126  1.00 28.55           C  
ATOM   1662  CA  SER Y  48     107.947  35.832 299.126  1.00 34.63           C  
ATOM   1663  CA  ALA Y  49     107.528  36.721 302.794  1.00 26.90           C  
ATOM   1664  CA  GLN Y  50     106.584  34.153 305.440  1.00 27.81           C  
ATOM   1665  CA  PHE Y  51     103.775  34.455 307.973  1.00 19.53           C  
ATOM   1666  CA  GLY Y  52     102.464  32.642 311.042  1.00 35.49           C  
ATOM   1667  CA  TYR Y  53     105.961  32.510 312.509  1.00 30.13           C  
ATOM   1668  CA  ASP Y  54     108.727  34.767 313.819  1.00 31.27           C  
ATOM   1669  CA  GLN Y  55     112.341  35.024 312.657  1.00 49.50           C  
ATOM   1670  CA  SER Y  56     112.795  31.265 312.992  1.00 59.35           C  
ATOM   1671  CA  GLY Y  57     110.762  28.108 313.565  1.00 48.55           C  
ATOM   1672  CA  ALA Y  58     106.955  28.133 313.478  1.00 42.01           C  
ATOM   1673  CA  ALA Y  59     105.387  30.572 315.941  1.00 45.98           C  
ATOM   1674  CA  SER Y  60     101.662  30.935 315.338  1.00 56.48           C  
ATOM   1675  CA  ALA Y  61      98.922  33.515 315.897  1.00 63.71           C  
ATOM   1676  CA  ASN Y  62      99.781  36.836 314.253  1.00 42.67           C  
ATOM   1677  CA  LYS Y  63     103.459  37.033 313.306  1.00 25.56           C  
ATOM   1678  CA  TYR Y  64     105.391  37.155 310.029  1.00 14.95           C  
ATOM   1679  CA  ARG Y  65     109.043  37.264 308.995  1.00 22.11           C  
ATOM   1680  CA  TYR Y  66     110.969  38.420 305.948  1.00 22.63           C  
ATOM   1681  CA  MET Y  67     114.422  39.295 304.643  1.00 31.66           C  
ATOM   1682  CA  SER Y  68     116.063  42.647 305.319  1.00 43.75           C  
ATOM   1683  CA  LEU Y  69     116.321  45.907 303.429  1.00 59.92           C  
ATOM   1684  CA  LYS Y  70     119.915  44.825 302.857  1.00 47.18           C  
ATOM   1685  CA  GLN Y  71     121.276  41.407 301.875  1.00 49.40           C  
ATOM   1686  CA  ASP Y  72     122.594  40.568 305.372  1.00 48.68           C  
ATOM   1687  CA  HIS Y  73     120.307  37.548 305.234  1.00 57.26           C  
ATOM   1688  CA  THR Y  74     119.030  39.014 308.474  1.00 46.29           C  
ATOM   1689  CA  VAL Y  75     115.589  37.502 308.934  1.00 42.00           C  
ATOM   1690  CA  LYS Y  76     113.806  40.084 311.085  1.00 40.99           C  
ATOM   1691  CA  GLU Y  77     110.176  39.757 312.129  1.00 29.59           C  
ATOM   1692  CA  GLY Y  78     107.193  41.928 312.922  1.00 36.63           C  
ATOM   1693  CA  THR Y  79     103.537  41.521 313.843  1.00 26.99           C  
ATOM   1694  CA  MET Y  80     100.915  40.101 311.444  1.00 26.04           C  
ATOM   1695  CA  ASP Y  81      98.999  43.217 312.261  1.00 45.27           C  
ATOM   1696  CA  ASP Y  82     100.673  45.826 310.107  1.00 43.77           C  
ATOM   1697  CA  ILE Y  83     100.491  43.876 306.842  1.00 53.45           C  
ATOM   1698  CA  LYS Y  84      97.701  45.099 304.590  1.00 52.69           C  
ATOM   1699  CA  ILE Y  85      96.593  44.282 301.046  1.00 66.35           C  
ATOM   1700  CA  SER Y  86      95.220  46.683 298.460  1.00 57.98           C  
ATOM   1701  CA  THR Y  87      94.346  46.812 294.778  1.00 59.36           C  
ATOM   1702  CA  SER Y  88      92.531  50.057 294.098  1.00 63.26           C  
ATOM   1703  CA  GLY Y  89      91.176  50.509 297.604  1.00 53.24           C  
ATOM   1704  CA  PRO Y  90      90.909  48.599 300.871  1.00 61.91           C  
ATOM   1705  CA  CYS Y  91      91.319  44.840 301.150  1.00 59.12           C  
ATOM   1706  CA  ARG Y  92      90.800  42.674 304.187  1.00 55.17           C  
ATOM   1707  CA  ARG Y  93      92.755  39.452 304.401  1.00 36.82           C  
ATOM   1708  CA  LEU Y  94      91.188  36.295 305.742  1.00 47.24           C  
ATOM   1709  CA  SER Y  95      93.778  33.570 306.278  1.00 49.18           C  
ATOM   1710  CA  TYR Y  96      97.577  33.355 306.320  1.00 29.45           C  
ATOM   1711  CA  LYS Y  97      99.281  30.277 304.908  1.00 37.57           C  
ATOM   1712  CA  GLY Y  98     103.003  30.869 305.306  1.00 37.55           C  
ATOM   1713  CA  TYR Y  99     103.910  32.221 301.868  1.00 31.01           C  
ATOM   1714  CA  PHE Y 100     100.331  32.732 300.721  1.00 18.63           C  
ATOM   1715  CA  LEU Y 101      97.615  35.326 301.243  1.00 28.77           C  
ATOM   1716  CA  LEU Y 102      93.876  35.302 300.639  1.00 44.76           C  
ATOM   1717  CA  ALA Y 103      91.443  38.211 300.760  1.00 37.11           C  
ATOM   1718  CA  LYS Y 104      88.494  39.871 299.020  1.00 43.08           C  
ATOM   1719  CA  CYS Y 105      89.954  42.563 297.140  1.00 46.57           C  
ATOM   1720  CA  PRO Y 106      87.511  45.482 295.539  1.00 72.70           C  
ATOM   1721  CA  PRO Y 107      87.891  46.440 291.864  1.00 63.34           C  
ATOM   1722  CA  GLY Y 108      91.133  45.251 290.287  1.00 58.70           C  
ATOM   1723  CA  ASP Y 109      93.654  46.616 287.801  1.00 65.98           C  
ATOM   1724  CA  SER Y 110      96.760  45.776 289.823  1.00 52.31           C  
ATOM   1725  CA  VAL Y 111      97.654  44.280 293.194  1.00 68.63           C  
ATOM   1726  CA  THR Y 112      99.833  45.684 295.968  1.00 49.20           C  
ATOM   1727  CA  VAL Y 113     101.014  43.930 299.115  1.00 65.75           C  
ATOM   1728  CA  SER Y 114     103.008  45.819 301.716  1.00 48.98           C  
ATOM   1729  CA  ILE Y 115     103.919  46.522 305.334  1.00 55.07           C  
ATOM   1730  CA  VAL Y 116     103.262  49.938 306.875  1.00 59.19           C  
ATOM   1731  CA  SER Y 117     104.935  49.778 310.283  1.00 78.58           C  
ATOM   1732  CA  SER Y 118     105.092  53.513 310.461  1.00 76.54           C  
ATOM   1733  CA  ASN Y 119     106.794  56.187 308.360  1.00 80.19           C  
ATOM   1734  CA  SER Y 120     109.066  53.738 306.537  1.00 73.91           C  
ATOM   1735  CA  ALA Y 121     107.868  50.653 304.657  1.00 57.78           C  
ATOM   1736  CA  THR Y 122     108.083  48.740 301.375  1.00 55.18           C  
ATOM   1737  CA  SER Y 123     105.535  47.307 298.935  1.00 49.82           C  
ATOM   1738  CA  CYS Y 124     105.574  45.191 295.781  1.00 48.89           C  
ATOM   1739  CA  THR Y 125     102.708  45.501 293.305  1.00 50.63           C  
ATOM   1740  CA  LEU Y 126     101.680  43.257 290.448  1.00 61.20           C  
ATOM   1741  CA  ALA Y 127     100.184  44.083 287.109  1.00 57.77           C  
ATOM   1742  CA  ARG Y 128      97.264  41.636 287.246  1.00 53.25           C  
ATOM   1743  CA  LYS Y 129      93.685  42.385 286.190  1.00 56.81           C  
ATOM   1744  CA  ILE Y 130      90.823  41.301 288.451  1.00 74.28           C  
ATOM   1745  CA  LYS Y 131      87.162  41.409 287.521  1.00 59.17           C  
ATOM   1746  CA  PRO Y 132      83.794  41.865 289.218  1.00 70.40           C  
ATOM   1747  CA  LYS Y 133      82.502  38.364 289.875  1.00 57.22           C  
ATOM   1748  CA  PHE Y 134      79.981  38.237 287.244  1.00 88.55           C  
ATOM   1749  CA  VAL Y 135      78.560  34.744 286.994  1.00 63.00           C  
ATOM   1750  CA  GLY Y 136      74.982  34.880 285.762  1.00 57.32           C  
ATOM   1751  CA  ARG Y 137      73.874  36.017 282.326  1.00 40.42           C  
ATOM   1752  CA  GLU Y 138      73.150  39.357 283.925  1.00 41.05           C  
ATOM   1753  CA  LYS Y 139      75.786  41.969 284.589  1.00 38.59           C  
ATOM   1754  CA  TYR Y 140      76.011  43.047 288.212  1.00 38.73           C  
ATOM   1755  CA  ASP Y 141      78.587  44.732 290.416  1.00 59.63           C  
ATOM   1756  CA  LEU Y 142      77.040  43.633 293.677  1.00 46.92           C  
ATOM   1757  CA  PRO Y 143      74.894  40.632 294.634  1.00 54.23           C  
ATOM   1758  CA  PRO Y 144      71.263  41.826 294.565  1.00 44.05           C  
ATOM   1759  CA  VAL Y 145      69.283  41.828 297.812  1.00 72.28           C  
ATOM   1760  CA  HIS Y 146      66.805  39.597 296.042  1.00 64.60           C  
ATOM   1761  CA  GLY Y 147      67.586  37.575 292.949  1.00 41.57           C  
ATOM   1762  CA  LYS Y 148      67.979  33.951 292.003  1.00 57.36           C  
ATOM   1763  CA  LYS Y 149      70.232  31.251 293.410  1.00 63.53           C  
ATOM   1764  CA  ILE Y 150      72.673  29.834 290.889  1.00 52.59           C  
ATOM   1765  CA  PRO Y 151      75.426  27.204 290.953  1.00 61.45           C  
ATOM   1766  CA  CYS Y 152      78.817  28.861 291.330  1.00 98.49           C  
ATOM   1767  CA  THR Y 153      82.144  28.089 292.995  1.00 83.07           C  
ATOM   1768  CA  VAL Y 154      83.793  30.238 295.689  1.00 62.93           C  
ATOM   1769  CA  TYR Y 155      86.448  30.265 298.439  1.00 38.79           C  
ATOM   1770  CA  ASP Y 156      85.710  28.890 301.930  1.00 52.61           C  
ATOM   1771  CA  LEU Y 255     100.346  19.981 300.118  1.00 44.87           C  
ATOM   1772  CA  HIS Y 256      97.347  22.108 301.065  1.00 40.38           C  
ATOM   1773  CA  LEU Y 257      96.302  24.486 303.859  1.00 51.76           C  
ATOM   1774  CA  PRO Y 258      94.591  27.338 301.966  1.00 37.90           C  
ATOM   1775  CA  PHE Y 259      90.918  28.386 301.723  1.00 26.71           C  
ATOM   1776  CA  LYS Y 260      89.639  25.524 299.556  1.00 40.47           C  
ATOM   1777  CA  LEU Y 261      87.378  26.102 296.549  1.00 33.40           C  
ATOM   1778  CA  ILE Y 262      83.867  24.742 297.068  1.00 49.25           C  
ATOM   1779  CA  PRO Y 263      80.885  24.826 294.692  1.00 58.39           C  
ATOM   1780  CA  SER Y 264      77.816  26.565 296.146  1.00 70.24           C  
ATOM   1781  CA  THR Y 265      75.253  29.287 295.450  1.00 55.09           C  
ATOM   1782  CA  CYS Y 266      75.694  32.845 294.250  1.00 47.04           C  
ATOM   1783  CA  MET Y 267      72.807  35.245 293.908  1.00 48.82           C  
ATOM   1784  CA  VAL Y 268      72.482  36.584 290.385  1.00 70.10           C  
ATOM   1785  CA  PRO Y 269      69.107  39.240 288.999  1.00 38.84           C  
ATOM   1786  CA  VAL Y 270      65.944  38.574 287.036  1.00 36.83           C  
ATOM   1787  CA  ALA Y 271      65.056  40.721 284.042  1.00 45.96           C  
ATOM   1788  CA  HIS Y 272      62.057  42.945 283.351  1.00 48.40           C  
ATOM   1789  CA  ALA Y 273      59.493  40.658 281.744  1.00 46.10           C  
ATOM   1790  CA  PRO Y 274      59.244  41.477 278.025  1.00 29.17           C  
ATOM   1791  CA  ASN Y 275      55.948  42.943 276.966  1.00 35.60           C  
ATOM   1792  CA  VAL Y 276      54.979  40.319 274.413  1.00 34.98           C  
ATOM   1793  CA  ILE Y 277      52.663  40.745 271.478  1.00 50.91           C  
ATOM   1794  CA  HIS Y 278      51.142  37.728 269.764  1.00 48.79           C  
ATOM   1795  CA  GLY Y 279      50.088  38.079 266.136  1.00 55.15           C  
ATOM   1796  CA  PHE Y 280      49.676  36.141 262.907  1.00 51.99           C  
ATOM   1797  CA  LYS Y 281      52.508  33.627 263.147  1.00 47.99           C  
ATOM   1798  CA  HIS Y 282      54.228  36.432 264.997  1.00 32.69           C  
ATOM   1799  CA  ILE Y 283      55.801  37.453 268.289  1.00 34.71           C  
ATOM   1800  CA  SER Y 284      57.210  40.942 268.675  1.00 31.94           C  
ATOM   1801  CA  LEU Y 285      59.164  41.075 271.930  1.00 35.49           C  
ATOM   1802  CA  GLN Y 286      59.230  44.540 273.480  1.00 33.52           C  
ATOM   1803  CA  LEU Y 287      62.261  44.517 275.791  1.00 48.05           C  
ATOM   1804  CA  ASP Y 288      63.567  47.140 278.214  1.00 56.89           C  
ATOM   1805  CA  THR Y 289      66.509  46.214 280.446  1.00 45.75           C  
ATOM   1806  CA  ASP Y 290      68.809  48.257 282.614  1.00 50.94           C  
ATOM   1807  CA  HIS Y 291      71.618  45.816 281.868  1.00 38.83           C  
ATOM   1808  CA  LEU Y 292      72.841  43.004 279.647  1.00 42.38           C  
ATOM   1809  CA  THR Y 293      70.430  40.125 279.222  1.00 41.73           C  
ATOM   1810  CA  LEU Y 294      70.872  37.134 276.948  1.00 26.35           C  
ATOM   1811  CA  LEU Y 295      67.983  36.316 274.656  1.00 12.51           C  
ATOM   1812  CA  THR Y 296      67.674  32.869 273.171  1.00 30.50           C  
ATOM   1813  CA  THR Y 297      65.286  31.253 270.755  1.00 39.37           C  
ATOM   1814  CA  ARG Y 298      64.738  28.038 268.843  1.00 50.84           C  
ATOM   1815  CA  ARG Y 299      61.860  26.506 266.961  1.00 58.85           C  
ATOM   1816  CA  LEU Y 300      60.035  23.503 268.322  1.00 58.40           C  
ATOM   1817  CA  GLY Y 301      60.002  21.658 264.997  1.00 71.57           C  
ATOM   1818  CA  ALA Y 302      62.979  20.431 263.014  1.00 72.74           C  
ATOM   1819  CA  ASN Y 303      65.016  23.329 261.721  1.00 54.61           C  
ATOM   1820  CA  PRO Y 304      65.073  25.294 265.017  1.00 36.28           C  
ATOM   1821  CA  GLU Y 305      67.361  27.959 263.560  1.00 57.06           C  
ATOM   1822  CA  PRO Y 306      68.497  28.711 267.125  1.00 49.00           C  
ATOM   1823  CA  THR Y 307      69.222  32.365 267.875  1.00 54.45           C  
ATOM   1824  CA  THR Y 308      71.247  33.937 270.655  1.00 57.76           C  
ATOM   1825  CA  GLU Y 309      71.817  37.657 271.250  1.00 43.84           C  
ATOM   1826  CA  TRP Y 310      72.675  39.912 274.174  1.00 31.51           C  
ATOM   1827  CA  ILE Y 311      70.472  42.933 274.481  1.00 42.14           C  
ATOM   1828  CA  VAL Y 312      70.506  46.195 276.406  1.00 50.28           C  
ATOM   1829  CA  GLY Y 313      68.077  48.966 276.953  1.00 51.35           C  
ATOM   1830  CA  LYS Y 314      65.165  49.325 274.604  1.00 56.52           C  
ATOM   1831  CA  THR Y 315      64.342  47.407 271.489  1.00 60.53           C  
ATOM   1832  CA  VAL Y 316      61.768  45.198 269.876  1.00 50.45           C  
ATOM   1833  CA  ARG Y 317      62.390  41.810 268.323  1.00 55.95           C  
ATOM   1834  CA  ASN Y 318      59.809  39.884 266.366  1.00 46.06           C  
ATOM   1835  CA  PHE Y 319      60.150  36.168 265.526  1.00 59.20           C  
ATOM   1836  CA  THR Y 320      58.603  33.835 263.275  1.00 64.26           C  
ATOM   1837  CA  VAL Y 321      55.963  31.177 264.805  1.00 55.26           C  
ATOM   1838  CA  ASP Y 322      56.579  28.277 262.431  1.00 64.39           C  
ATOM   1839  CA  ARG Y 323      53.244  26.690 263.284  1.00 49.45           C  
ATOM   1840  CA  ASP Y 324      55.108  24.437 265.713  1.00 35.88           C  
ATOM   1841  CA  GLY Y 325      55.617  27.462 267.929  1.00 34.21           C  
ATOM   1842  CA  LEU Y 326      58.964  28.258 269.517  1.00 35.85           C  
ATOM   1843  CA  GLU Y 327      60.709  28.624 272.837  1.00 21.03           C  
ATOM   1844  CA  TYR Y 328      62.431  31.737 274.103  1.00 21.01           C  
ATOM   1845  CA  ILE Y 329      64.599  32.073 277.192  1.00 29.27           C  
ATOM   1846  CA  TRP Y 330      65.253  35.641 278.202  1.00 26.28           C  
ATOM   1847  CA  GLY Y 331      67.969  36.503 280.707  1.00 26.31           C  
ATOM   1848  CA  ASN Y 332      67.854  33.600 283.197  1.00 42.73           C  
ATOM   1849  CA  HIS Y 333      64.091  33.769 283.174  1.00 34.15           C  
ATOM   1850  CA  GLU Y 334      62.355  30.698 282.677  1.00 59.58           C  
ATOM   1851  CA  PRO Y 335      62.047  29.500 279.421  1.00 52.11           C  
ATOM   1852  CA  VAL Y 336      58.594  30.178 277.976  1.00 45.16           C  
ATOM   1853  CA  ARG Y 337      57.460  28.931 274.624  1.00 33.25           C  
ATOM   1854  CA  VAL Y 338      54.716  30.304 272.431  1.00 69.49           C  
ATOM   1855  CA  TYR Y 339      52.546  28.686 269.777  1.00 56.87           C  
ATOM   1856  CA  ALA Y 340      50.060  29.809 267.127  1.00 54.56           C  
TER    1857      ALA Y 340                                                      
ATOM   1858  CA  TYR F   1     146.329  45.978 232.908  1.00 59.09           C  
ATOM   1859  CA  GLU F   2     143.222  48.169 232.757  1.00 61.34           C  
ATOM   1860  CA  HIS F   3     139.987  46.155 232.786  1.00 49.75           C  
ATOM   1861  CA  ALA F   4     136.448  47.386 232.163  1.00 67.89           C  
ATOM   1862  CA  THR F   5     133.482  45.528 233.702  1.00 64.72           C  
ATOM   1863  CA  THR F   6     130.043  46.470 235.023  1.00 50.67           C  
ATOM   1864  CA  VAL F   7     129.135  45.182 238.464  1.00 48.66           C  
ATOM   1865  CA  PRO F   8     125.492  45.132 239.590  1.00 47.59           C  
ATOM   1866  CA  ASN F   9     124.979  47.248 242.705  1.00 53.29           C  
ATOM   1867  CA  VAL F  10     123.883  44.708 245.305  1.00 44.50           C  
ATOM   1868  CA  PRO F  11     125.533  44.302 248.721  1.00 51.01           C  
ATOM   1869  CA  GLN F  12     127.392  41.069 249.605  1.00 59.38           C  
ATOM   1870  CA  ILE F  13     126.858  39.368 246.251  1.00 58.79           C  
ATOM   1871  CA  PRO F  14     130.233  38.572 244.597  1.00 52.63           C  
ATOM   1872  CA  TYR F  15     130.771  39.047 240.869  1.00 55.99           C  
ATOM   1873  CA  LYS F  16     132.963  36.483 239.124  1.00 54.42           C  
ATOM   1874  CA  ALA F  17     134.675  37.496 235.884  1.00 69.35           C  
ATOM   1875  CA  LEU F  18     137.654  36.451 233.762  1.00 63.51           C  
ATOM   1876  CA  VAL F  19     140.563  38.635 232.754  1.00 65.10           C  
ATOM   1877  CA  GLU F  20     141.496  37.721 229.184  1.00 79.22           C  
ATOM   1878  CA  ARG F  21     144.936  38.852 228.016  1.00 89.82           C  
ATOM   1879  CA  ALA F  22     146.882  37.735 224.942  1.00 77.35           C  
ATOM   1880  CA  GLY F  23     149.377  35.019 225.846  1.00 57.88           C  
ATOM   1881  CA  TYR F  24     148.692  35.611 229.531  1.00 43.56           C  
ATOM   1882  CA  ALA F  25     146.716  33.128 231.641  1.00 55.33           C  
ATOM   1883  CA  PRO F  26     143.183  34.064 232.812  1.00 52.87           C  
ATOM   1884  CA  LEU F  27     142.862  35.860 236.139  1.00 32.72           C  
ATOM   1885  CA  ASN F  28     140.947  35.219 239.329  1.00 37.51           C  
ATOM   1886  CA  LEU F  29     138.582  38.196 239.596  1.00 41.60           C  
ATOM   1887  CA  GLU F  30     135.794  38.530 242.152  1.00 36.65           C  
ATOM   1888  CA  ILE F  31     134.332  41.873 243.238  1.00 50.74           C  
ATOM   1889  CA  THR F  32     132.054  42.206 246.252  1.00 43.71           C  
ATOM   1890  CA  VAL F  33     130.296  45.521 246.894  1.00 57.72           C  
ATOM   1891  CA  MET F  34     130.412  45.170 250.660  1.00 55.54           C  
ATOM   1892  CA  SER F  35     128.638  48.430 251.393  1.00 65.83           C  
ATOM   1893  CA  SER F  36     127.020  51.214 249.399  1.00 52.67           C  
ATOM   1894  CA  GLU F  37     126.218  54.650 250.826  1.00 52.15           C  
ATOM   1895  CA  VAL F  38     124.232  57.356 249.088  1.00 56.39           C  
ATOM   1896  CA  LEU F  39     125.195  60.695 250.610  1.00 65.53           C  
ATOM   1897  CA  PRO F  40     123.208  63.733 249.502  1.00 49.88           C  
ATOM   1898  CA  SER F  41     123.852  67.359 250.476  1.00 56.71           C  
ATOM   1899  CA  THR F  42     122.011  68.667 253.501  1.00 72.48           C  
ATOM   1900  CA  ASN F  43     121.163  72.355 253.889  1.00 57.15           C  
ATOM   1901  CA  GLN F  44     119.617  72.380 257.369  1.00 62.38           C  
ATOM   1902  CA  GLU F  45     116.975  75.102 257.240  1.00 42.95           C  
ATOM   1903  CA  TYR F  46     115.466  75.442 260.711  1.00 34.26           C  
ATOM   1904  CA  ILE F  47     114.694  73.771 263.993  1.00 42.83           C  
ATOM   1905  CA  THR F  48     111.179  73.508 265.367  1.00 48.45           C  
ATOM   1906  CA  CYS F  49     109.484  72.206 268.471  1.00 49.83           C  
ATOM   1907  CA  LYS F  50     106.823  72.667 271.130  1.00 54.08           C  
ATOM   1908  CA  PHE F  51     106.701  76.416 271.735  1.00 37.59           C  
ATOM   1909  CA  THR F  52     105.778  78.031 275.023  1.00 52.89           C  
ATOM   1910  CA  THR F  53     103.677  81.178 275.211  1.00 53.78           C  
ATOM   1911  CA  VAL F  54     104.725  83.857 277.653  1.00 59.41           C  
ATOM   1912  CA  VAL F  55     102.182  86.343 278.917  1.00 49.18           C  
ATOM   1913  CA  PRO F  56     103.567  89.355 280.822  1.00 34.72           C  
ATOM   1914  CA  SER F  57     101.246  91.077 283.303  1.00 29.65           C  
ATOM   1915  CA  PRO F  58      99.143  93.529 281.287  1.00 28.19           C  
ATOM   1916  CA  LYS F  59     100.131  97.171 281.477  1.00 26.22           C  
ATOM   1917  CA  ILE F  60      97.069  99.218 282.433  1.00 27.23           C  
ATOM   1918  CA  LYS F  61      97.202 102.996 282.959  1.00 47.90           C  
ATOM   1919  CA  CYS F  62      93.930 104.255 284.986  1.00 38.10           C  
ATOM   1920  CA  CYS F  63      92.671 107.204 282.939  1.00 46.02           C  
ATOM   1921  CA  GLY F  64      95.120 106.889 280.055  1.00 56.81           C  
ATOM   1922  CA  SER F  65      95.367 105.838 276.414  1.00 62.70           C  
ATOM   1923  CA  LEU F  66      97.497 102.733 275.877  1.00 58.32           C  
ATOM   1924  CA  GLU F  67      98.204 102.391 272.131  1.00 62.65           C  
ATOM   1925  CA  CYS F  68     100.652  99.756 270.895  1.00 61.06           C  
ATOM   1926  CA  GLN F  69     104.155 100.120 269.516  1.00 59.66           C  
ATOM   1927  CA  PRO F  70     105.693  97.898 266.828  1.00 73.91           C  
ATOM   1928  CA  ALA F  71     107.373  95.642 269.395  1.00 67.46           C  
ATOM   1929  CA  ALA F  72     108.976  92.916 267.280  1.00 70.64           C  
ATOM   1930  CA  HIS F  73     110.294  89.977 269.303  1.00 60.52           C  
ATOM   1931  CA  ALA F  74     109.260  86.443 268.355  1.00 59.38           C  
ATOM   1932  CA  ASP F  75     105.536  85.707 268.252  1.00 42.21           C  
ATOM   1933  CA  TYR F  76     104.607  89.045 269.805  1.00 27.96           C  
ATOM   1934  CA  THR F  77     100.986  90.203 269.694  1.00 36.78           C  
ATOM   1935  CA  CYS F  78      99.406  93.226 271.398  1.00 38.27           C  
ATOM   1936  CA  LYS F  79      95.834  94.432 271.432  1.00 40.28           C  
ATOM   1937  CA  VAL F  80      94.468  97.655 272.846  1.00 38.94           C  
ATOM   1938  CA  PHE F  81      91.298  97.059 274.823  1.00 37.59           C  
ATOM   1939  CA  GLY F  82      89.329 100.141 275.797  1.00 53.06           C  
ATOM   1940  CA  GLY F  83      86.819 100.820 278.547  1.00 51.14           C  
ATOM   1941  CA  VAL F  84      87.842  98.040 280.898  1.00 39.59           C  
ATOM   1942  CA  TYR F  85      87.716  98.181 284.705  1.00 37.32           C  
ATOM   1943  CA  PRO F  86      85.795 100.864 286.635  1.00 42.93           C  
ATOM   1944  CA  PHE F  87      86.633 102.491 289.982  1.00 40.15           C  
ATOM   1945  CA  MET F  88      87.682 101.017 293.316  1.00 51.48           C  
ATOM   1946  CA  TRP F  89      87.982  97.245 292.793  1.00 38.87           C  
ATOM   1947  CA  GLY F  90      86.183  95.451 289.970  1.00 44.19           C  
ATOM   1948  CA  GLY F  91      88.944  95.767 287.561  1.00 32.51           C  
ATOM   1949  CA  ALA F  92      91.954  97.394 289.253  1.00 40.45           C  
ATOM   1950  CA  GLN F  93      92.475 100.328 291.579  1.00 45.13           C  
ATOM   1951  CA  CYS F  94      91.313 103.133 289.290  1.00 31.42           C  
ATOM   1952  CA  PHE F  95      88.647 105.835 289.561  1.00 27.82           C  
ATOM   1953  CA  CYS F  96      87.252 106.255 286.047  1.00 37.83           C  
ATOM   1954  CA  ASP F  97      84.797 104.009 284.192  1.00 53.49           C  
ATOM   1955  CA  SER F  98      84.759 104.375 280.406  1.00 66.48           C  
ATOM   1956  CA  GLU F  99      88.130 106.043 280.138  1.00 52.76           C  
ATOM   1957  CA  ASN F 100      90.177 102.901 280.798  1.00 28.28           C  
ATOM   1958  CA  SER F 101      92.506 100.854 278.619  1.00 28.14           C  
ATOM   1959  CA  GLN F 102      94.456  97.609 278.858  1.00 24.74           C  
ATOM   1960  CA  MET F 103      97.185  96.365 276.536  1.00 23.84           C  
ATOM   1961  CA  SER F 104      97.277  92.612 276.146  1.00 45.14           C  
ATOM   1962  CA  GLU F 105     100.599  91.378 274.828  1.00 46.64           C  
ATOM   1963  CA  ALA F 106     101.991  87.872 274.415  1.00 42.90           C  
ATOM   1964  CA  TYR F 107     104.724  86.053 272.503  1.00 35.99           C  
ATOM   1965  CA  VAL F 108     106.124  82.529 272.113  1.00 45.54           C  
ATOM   1966  CA  GLU F 109     109.435  80.954 273.160  1.00 49.76           C  
ATOM   1967  CA  LEU F 110     110.952  77.484 272.949  1.00 42.63           C  
ATOM   1968  CA  SER F 111     110.003  74.835 275.462  1.00 57.90           C  
ATOM   1969  CA  ALA F 112     112.143  74.226 278.515  1.00 66.57           C  
ATOM   1970  CA  ASP F 113     112.715  71.004 276.635  1.00 66.50           C  
ATOM   1971  CA  CYS F 114     112.733  72.160 272.980  1.00 45.27           C  
ATOM   1972  CA  ALA F 115     116.267  70.830 272.882  1.00 41.18           C  
ATOM   1973  CA  SER F 116     115.563  67.277 273.990  1.00 53.98           C  
ATOM   1974  CA  ASP F 117     112.699  66.847 271.471  1.00 53.22           C  
ATOM   1975  CA  HIS F 118     112.649  68.776 268.204  1.00 38.12           C  
ATOM   1976  CA  ALA F 119     112.809  68.225 264.491  1.00 43.88           C  
ATOM   1977  CA  GLN F 120     114.976  69.497 261.686  1.00 33.30           C  
ATOM   1978  CA  ALA F 121     113.718  70.956 258.435  1.00 31.24           C  
ATOM   1979  CA  ILE F 122     116.290  70.004 255.851  1.00 36.43           C  
ATOM   1980  CA  LYS F 123     116.719  70.605 252.137  1.00 33.17           C  
ATOM   1981  CA  VAL F 124     118.292  67.776 250.170  1.00 48.72           C  
ATOM   1982  CA  HIS F 125     120.124  68.250 246.898  1.00 43.74           C  
ATOM   1983  CA  THR F 126     122.113  66.093 244.497  1.00 49.10           C  
ATOM   1984  CA  ALA F 127     124.150  63.315 246.097  1.00 50.17           C  
ATOM   1985  CA  ALA F 128     127.317  61.307 245.834  1.00 69.44           C  
ATOM   1986  CA  MET F 129     127.753  57.616 246.636  1.00 52.92           C  
ATOM   1987  CA  LYS F 130     130.713  55.773 248.117  1.00 42.27           C  
ATOM   1988  CA  VAL F 131     131.094  51.999 247.744  1.00 54.91           C  
ATOM   1989  CA  GLY F 132     133.008  49.572 249.954  1.00 56.03           C  
ATOM   1990  CA  LEU F 133     134.487  47.276 247.348  1.00 46.46           C  
ATOM   1991  CA  ARG F 134     136.442  44.084 247.886  1.00 33.41           C  
ATOM   1992  CA  ILE F 135     138.340  42.812 244.874  1.00 40.51           C  
ATOM   1993  CA  VAL F 136     140.356  39.614 244.748  1.00 26.61           C  
ATOM   1994  CA  TYR F 137     142.910  38.850 242.048  1.00 39.81           C  
ATOM   1995  CA  GLY F 138     144.947  35.660 242.007  1.00 47.54           C  
ATOM   1996  CA  ASN F 139     146.495  34.904 245.398  1.00 65.37           C  
ATOM   1997  CA  THR F 140     145.809  38.394 246.792  1.00 50.40           C  
ATOM   1998  CA  THR F 141     142.636  40.154 247.957  1.00 35.88           C  
ATOM   1999  CA  SER F 142     142.344  43.919 248.309  1.00 48.01           C  
ATOM   2000  CA  PHE F 143     139.658  46.499 249.043  1.00 45.75           C  
ATOM   2001  CA  LEU F 144     139.096  50.194 248.436  1.00 58.30           C  
ATOM   2002  CA  ASP F 145     136.310  52.694 249.085  1.00 60.35           C  
ATOM   2003  CA  VAL F 146     135.422  54.520 245.914  1.00 53.83           C  
ATOM   2004  CA  TYR F 147     133.098  57.388 245.019  1.00 42.16           C  
ATOM   2005  CA  VAL F 148     130.922  56.722 242.013  1.00 37.22           C  
ATOM   2006  CA  ASN F 149     131.857  59.142 239.256  1.00 54.59           C  
ATOM   2007  CA  GLY F 150     134.014  58.681 236.182  1.00 64.86           C  
ATOM   2008  CA  VAL F 151     136.764  60.549 238.012  1.00 59.57           C  
ATOM   2009  CA  THR F 152     137.890  59.945 241.600  1.00 49.71           C  
ATOM   2010  CA  PRO F 153     140.136  56.890 242.013  1.00 55.05           C  
ATOM   2011  CA  GLY F 154     140.203  55.200 245.419  1.00 65.49           C  
ATOM   2012  CA  THR F 155     143.928  55.468 246.100  1.00 68.87           C  
ATOM   2013  CA  SER F 156     144.177  51.850 247.246  1.00 65.77           C  
ATOM   2014  CA  LYS F 157     147.966  51.852 247.575  1.00 63.02           C  
ATOM   2015  CA  ASP F 158     148.437  49.412 244.697  1.00 51.91           C  
ATOM   2016  CA  LEU F 159     145.486  49.167 242.330  1.00 47.16           C  
ATOM   2017  CA  LYS F 160     143.697  52.095 240.685  1.00 41.48           C  
ATOM   2018  CA  VAL F 161     139.929  51.541 240.780  1.00 56.07           C  
ATOM   2019  CA  ILE F 162     137.764  54.335 239.388  1.00 51.82           C  
ATOM   2020  CA  ALA F 163     134.057  53.570 239.607  1.00 43.54           C  
ATOM   2021  CA  GLY F 164     132.207  55.024 236.633  1.00 45.40           C  
ATOM   2022  CA  PRO F 165     128.964  56.996 236.994  1.00 60.33           C  
ATOM   2023  CA  ILE F 166     126.098  54.906 238.343  1.00 63.43           C  
ATOM   2024  CA  SER F 167     123.610  53.684 235.698  1.00 64.42           C  
ATOM   2025  CA  ALA F 168     120.494  55.372 237.139  1.00 74.80           C  
ATOM   2026  CA  SER F 169     120.423  58.397 239.418  1.00 89.18           C  
ATOM   2027  CA  PHE F 170     118.089  57.326 242.204  1.00 59.35           C  
ATOM   2028  CA  THR F 171     117.406  58.809 245.630  1.00 52.19           C  
ATOM   2029  CA  PRO F 172     115.101  57.753 248.482  1.00 49.11           C  
ATOM   2030  CA  PHE F 173     114.673  61.414 249.406  1.00 52.66           C  
ATOM   2031  CA  ASP F 174     112.706  64.467 248.266  1.00 54.98           C  
ATOM   2032  CA  HIS F 175     114.105  67.990 248.022  1.00 48.86           C  
ATOM   2033  CA  LYS F 176     112.606  68.611 251.459  1.00 40.22           C  
ATOM   2034  CA  VAL F 177     112.924  66.167 254.354  1.00 37.06           C  
ATOM   2035  CA  VAL F 178     112.240  66.258 258.070  1.00 30.86           C  
ATOM   2036  CA  ILE F 179     114.411  64.523 260.615  1.00 30.14           C  
ATOM   2037  CA  HIS F 180     112.804  63.926 263.971  1.00 31.59           C  
ATOM   2038  CA  ARG F 181     114.572  61.609 266.362  1.00 47.50           C  
ATOM   2039  CA  GLY F 182     116.610  59.131 264.386  1.00 68.73           C  
ATOM   2040  CA  LEU F 183     113.877  59.210 261.870  1.00 38.46           C  
ATOM   2041  CA  VAL F 184     113.536  60.934 258.561  1.00 32.23           C  
ATOM   2042  CA  TYR F 185     110.310  61.665 256.664  1.00 38.21           C  
ATOM   2043  CA  ASN F 186     109.780  63.135 253.218  1.00 46.08           C  
ATOM   2044  CA  TYR F 187     107.770  66.242 254.202  1.00 48.45           C  
ATOM   2045  CA  ASP F 188     107.331  69.510 252.277  1.00 48.26           C  
ATOM   2046  CA  PHE F 189     107.849  71.780 255.300  1.00 48.10           C  
ATOM   2047  CA  PRO F 190     107.384  75.473 254.550  1.00 47.84           C  
ATOM   2048  CA  GLU F 191     110.287  77.804 253.754  1.00 47.90           C  
ATOM   2049  CA  TYR F 192     111.971  79.584 256.612  1.00 38.88           C  
ATOM   2050  CA  GLY F 193     109.803  82.628 257.104  1.00 43.97           C  
ATOM   2051  CA  ALA F 194     106.571  81.601 255.428  1.00 50.00           C  
ATOM   2052  CA  MET F 195     105.022  79.715 258.319  1.00 43.48           C  
ATOM   2053  CA  LYS F 196     101.447  78.575 258.799  1.00 42.06           C  
ATOM   2054  CA  PRO F 197     100.285  78.091 262.406  1.00 42.50           C  
ATOM   2055  CA  GLY F 198      99.218  74.764 263.884  1.00 54.93           C  
ATOM   2056  CA  ALA F 199     100.876  73.073 260.896  1.00 56.20           C  
ATOM   2057  CA  PHE F 200     104.466  71.785 260.916  1.00 39.38           C  
ATOM   2058  CA  GLY F 201     106.994  74.557 261.260  1.00 44.59           C  
ATOM   2059  CA  ASP F 202     104.668  76.951 263.033  1.00 43.26           C  
ATOM   2060  CA  ILE F 203     107.721  78.278 264.866  1.00 44.62           C  
ATOM   2061  CA  GLN F 204     111.188  78.349 263.293  1.00 40.48           C  
ATOM   2062  CA  ALA F 205     114.799  78.872 264.327  1.00 48.44           C  
ATOM   2063  CA  THR F 206     118.137  78.485 262.541  1.00 51.36           C  
ATOM   2064  CA  SER F 207     119.841  76.576 265.353  1.00 77.10           C  
ATOM   2065  CA  LEU F 208     118.872  75.210 268.771  1.00 78.21           C  
ATOM   2066  CA  THR F 209     120.653  78.164 270.375  1.00 82.32           C  
ATOM   2067  CA  SER F 210     117.340  79.971 269.903  1.00 78.95           C  
ATOM   2068  CA  LYS F 211     118.816  82.025 266.861  1.00 46.74           C  
ATOM   2069  CA  ASP F 212     116.442  84.845 265.460  1.00 56.08           C  
ATOM   2070  CA  LEU F 213     113.376  82.583 265.824  1.00 57.49           C  
ATOM   2071  CA  ILE F 214     110.235  83.521 263.900  1.00 49.45           C  
ATOM   2072  CA  ALA F 215     106.846  82.139 264.934  1.00 47.23           C  
ATOM   2073  CA  SER F 216     103.258  82.412 263.680  1.00 45.06           C  
ATOM   2074  CA  THR F 217     100.806  80.783 266.117  1.00 55.72           C  
ATOM   2075  CA  ASP F 218      97.433  82.524 265.552  1.00 49.12           C  
ATOM   2076  CA  ILE F 219      97.322  84.044 269.021  1.00 50.51           C  
ATOM   2077  CA  ARG F 220      94.106  85.895 269.690  1.00 42.99           C  
ATOM   2078  CA  LEU F 221      93.621  88.335 272.549  1.00 49.33           C  
ATOM   2079  CA  LEU F 222      90.281  88.634 274.279  1.00 44.95           C  
ATOM   2080  CA  LYS F 223      88.709  91.593 276.040  1.00 45.49           C  
ATOM   2081  CA  PRO F 224      89.135  90.720 279.725  1.00 41.41           C  
ATOM   2082  CA  SER F 225      86.108  90.839 282.032  1.00 60.79           C  
ATOM   2083  CA  ALA F 226      86.090  93.074 285.107  1.00 53.91           C  
ATOM   2084  CA  LYS F 227      86.487  91.074 288.298  1.00 48.52           C  
ATOM   2085  CA  ASN F 228      90.211  90.281 288.035  1.00 43.84           C  
ATOM   2086  CA  VAL F 229      93.239  91.361 286.054  1.00 50.76           C  
ATOM   2087  CA  HIS F 230      93.531  88.280 283.890  1.00 34.13           C  
ATOM   2088  CA  VAL F 231      94.635  88.337 280.263  1.00 41.14           C  
ATOM   2089  CA  PRO F 232      92.588  85.978 278.052  1.00 42.16           C  
ATOM   2090  CA  TYR F 233      93.794  84.574 274.747  1.00 46.70           C  
ATOM   2091  CA  THR F 234      93.128  81.802 272.273  1.00 43.39           C  
ATOM   2092  CA  GLN F 235      95.887  80.400 270.135  1.00 46.68           C  
ATOM   2093  CA  ALA F 236      96.521  77.728 267.568  1.00 52.49           C  
ATOM   2094  CA  SER F 237      97.669  74.198 268.274  1.00 69.56           C  
ATOM   2095  CA  SER F 238     101.326  73.112 268.377  1.00 56.39           C  
ATOM   2096  CA  GLY F 239     102.072  72.443 264.711  1.00 38.74           C  
ATOM   2097  CA  PHE F 240     104.844  70.230 266.010  1.00 27.69           C  
ATOM   2098  CA  GLU F 241     102.989  67.908 268.342  1.00 38.28           C  
ATOM   2099  CA  MET F 242     100.372  68.045 265.606  1.00 41.47           C  
ATOM   2100  CA  TRP F 243     102.836  66.784 263.041  1.00 22.93           C  
ATOM   2101  CA  LYS F 244     104.179  64.211 265.497  1.00 36.05           C  
ATOM   2102  CA  ASN F 245     100.733  62.585 266.021  1.00 41.50           C  
ATOM   2103  CA  ASN F 246     100.544  62.514 262.263  1.00 38.84           C  
ATOM   2104  CA  SER F 247     104.089  61.824 261.164  1.00 54.70           C  
ATOM   2105  CA  GLY F 248     104.018  58.872 258.842  1.00 69.59           C  
ATOM   2106  CA  ARG F 249     105.932  55.699 258.907  1.00 53.63           C  
ATOM   2107  CA  PRO F 250     109.634  56.772 258.605  1.00 29.96           C  
ATOM   2108  CA  LEU F 251     111.577  56.444 255.379  1.00 43.00           C  
ATOM   2109  CA  GLN F 252     113.731  53.808 257.041  1.00 37.90           C  
ATOM   2110  CA  GLU F 253     110.502  51.832 256.658  1.00 47.07           C  
ATOM   2111  CA  THR F 254     109.338  52.992 253.232  1.00 46.09           C  
ATOM   2112  CA  ALA F 255     112.591  53.299 251.273  1.00 56.57           C  
ATOM   2113  CA  PRO F 256     111.989  52.301 247.590  1.00 68.78           C  
ATOM   2114  CA  PHE F 257     114.961  49.910 247.156  1.00 46.48           C  
ATOM   2115  CA  GLY F 258     115.465  48.265 250.499  1.00 36.82           C  
ATOM   2116  CA  CYS F 259     117.715  51.121 251.547  1.00 45.04           C  
ATOM   2117  CA  LYS F 260     118.669  51.385 255.208  1.00 50.71           C  
ATOM   2118  CA  ILE F 261     118.185  55.108 255.921  1.00 61.63           C  
ATOM   2119  CA  ALA F 262     120.675  56.629 258.381  1.00 71.40           C  
ATOM   2120  CA  VAL F 263     121.047  59.838 260.403  1.00 73.18           C  
ATOM   2121  CA  ASN F 264     123.709  61.654 261.311  1.00 62.83           C  
ATOM   2122  CA  PRO F 265     125.185  61.968 257.912  1.00 38.31           C  
ATOM   2123  CA  LEU F 266     121.926  61.741 255.941  1.00 46.03           C  
ATOM   2124  CA  ARG F 267     122.507  58.510 254.034  1.00 27.81           C  
ATOM   2125  CA  ALA F 268     120.925  55.547 252.255  1.00 46.97           C  
ATOM   2126  CA  VAL F 269     122.973  52.527 253.372  1.00 60.85           C  
ATOM   2127  CA  ASP F 270     123.048  49.406 251.196  1.00 61.17           C  
ATOM   2128  CA  CYS F 271     120.474  50.226 248.547  1.00 53.68           C  
ATOM   2129  CA  SER F 272     120.273  47.876 245.570  1.00 41.92           C  
ATOM   2130  CA  TYR F 273     119.668  49.156 242.053  1.00 60.03           C  
ATOM   2131  CA  GLY F 274     121.428  49.435 238.707  1.00 69.60           C  
ATOM   2132  CA  ASN F 275     124.929  48.426 237.722  1.00 46.90           C  
ATOM   2133  CA  ILE F 276     128.234  50.144 238.488  1.00 57.33           C  
ATOM   2134  CA  PRO F 277     130.784  50.510 235.726  1.00 55.53           C  
ATOM   2135  CA  ILE F 278     134.222  49.685 237.135  1.00 54.05           C  
ATOM   2136  CA  SER F 279     137.715  50.155 235.736  1.00 55.14           C  
ATOM   2137  CA  ILE F 280     140.485  48.135 237.371  1.00 33.11           C  
ATOM   2138  CA  ASP F 281     144.276  48.447 237.049  1.00 30.55           C  
ATOM   2139  CA  ILE F 282     145.883  45.060 237.789  1.00 54.87           C  
ATOM   2140  CA  PRO F 283     149.601  45.282 238.632  1.00 56.91           C  
ATOM   2141  CA  ASN F 284     151.515  43.102 236.164  1.00 51.06           C  
ATOM   2142  CA  ALA F 285     153.374  41.925 239.266  1.00 66.97           C  
ATOM   2143  CA  ALA F 286     151.012  39.022 239.946  1.00 74.68           C  
ATOM   2144  CA  PHE F 287     148.559  37.973 237.233  1.00 67.53           C  
ATOM   2145  CA  ILE F 288     150.658  35.301 235.538  1.00 48.40           C  
ATOM   2146  CA  ARG F 289     151.650  34.790 231.899  1.00 31.65           C  
ATOM   2147  CA  THR F 290     151.329  31.346 230.288  1.00 46.69           C  
ATOM   2148  CA  SER F 291     154.716  29.911 231.260  1.00 50.81           C  
ATOM   2149  CA  ASP F 292     153.328  27.784 234.090  1.00 39.96           C  
ATOM   2150  CA  ALA F 293     150.576  25.247 233.418  1.00 57.90           C  
ATOM   2151  CA  PRO F 294     153.512  21.813 234.350  1.00 61.37           C  
ATOM   2152  CA  LEU F 295     151.020  20.077 232.053  1.00 64.99           C  
ATOM   2153  CA  VAL F 296     147.273  19.633 232.524  1.00 42.95           C  
ATOM   2154  CA  SER F 297     144.996  17.437 230.412  1.00 42.22           C  
ATOM   2155  CA  THR F 298     141.557  15.805 230.385  1.00 68.84           C  
ATOM   2156  CA  VAL F 299     138.721  17.356 232.386  1.00 68.79           C  
ATOM   2157  CA  LYS F 300     135.231  15.849 232.566  1.00 48.47           C  
ATOM   2158  CA  CYS F 301     132.346  17.037 234.733  1.00 55.08           C  
ATOM   2159  CA  GLU F 302     130.021  15.027 236.987  1.00 67.95           C  
ATOM   2160  CA  VAL F 303     127.274  16.503 239.179  1.00 51.93           C  
ATOM   2161  CA  SER F 304     126.533  14.687 242.445  1.00 58.42           C  
ATOM   2162  CA  GLU F 305     123.645  16.729 243.858  1.00 58.37           C  
ATOM   2163  CA  CYS F 306     121.753  19.898 242.933  1.00 51.44           C  
ATOM   2164  CA  THR F 307     118.975  22.176 244.159  1.00 45.10           C  
ATOM   2165  CA  TYR F 308     117.125  24.703 241.993  1.00 32.73           C  
ATOM   2166  CA  SER F 309     117.321  28.412 242.903  1.00 62.82           C  
ATOM   2167  CA  ALA F 310     119.178  28.014 246.206  1.00 64.24           C  
ATOM   2168  CA  ASP F 311     122.202  29.830 247.629  1.00 63.65           C  
ATOM   2169  CA  PHE F 312     124.658  27.043 246.780  1.00 46.36           C  
ATOM   2170  CA  GLY F 313     122.803  23.762 246.355  1.00 60.07           C  
ATOM   2171  CA  GLY F 314     124.946  22.633 243.442  1.00 48.33           C  
ATOM   2172  CA  MET F 315     127.572  19.925 243.879  1.00 38.65           C  
ATOM   2173  CA  ALA F 316     129.826  18.778 241.033  1.00 32.76           C  
ATOM   2174  CA  THR F 317     133.139  16.920 240.829  1.00 38.39           C  
ATOM   2175  CA  LEU F 318     135.882  17.021 238.200  1.00 33.58           C  
ATOM   2176  CA  GLN F 319     138.035  14.043 237.216  1.00 25.16           C  
ATOM   2177  CA  TYR F 320     141.232  14.656 235.262  1.00 35.12           C  
ATOM   2178  CA  VAL F 321     144.966  13.988 234.987  1.00 32.30           C  
ATOM   2179  CA  SER F 322     147.689  16.437 236.034  1.00 18.27           C  
ATOM   2180  CA  ASP F 323     151.478  16.280 235.677  1.00 50.83           C  
ATOM   2181  CA  ARG F 324     152.086  17.867 239.088  1.00 24.74           C  
ATOM   2182  CA  GLU F 325     150.461  19.920 241.840  1.00 43.37           C  
ATOM   2183  CA  GLY F 326     149.407  23.551 241.529  1.00 54.02           C  
ATOM   2184  CA  GLN F 327     146.554  26.022 241.921  1.00 39.44           C  
ATOM   2185  CA  CYS F 328     143.817  26.391 239.298  1.00 23.56           C  
ATOM   2186  CA  PRO F 329     141.184  29.149 238.952  1.00 33.98           C  
ATOM   2187  CA  VAL F 330     137.754  27.604 238.367  1.00 47.37           C  
ATOM   2188  CA  HIS F 331     135.057  29.651 236.633  1.00 56.09           C  
ATOM   2189  CA  SER F 332     131.871  29.284 234.571  1.00 38.75           C  
ATOM   2190  CA  HIS F 333     131.637  30.563 230.987  1.00 59.03           C  
ATOM   2191  CA  SER F 334     127.838  30.801 231.053  1.00 73.08           C  
ATOM   2192  CA  SER F 335     125.577  32.915 233.263  1.00 88.35           C  
ATOM   2193  CA  THR F 336     123.177  29.983 233.637  1.00 71.78           C  
ATOM   2194  CA  ALA F 337     125.328  29.020 236.622  1.00 59.39           C  
ATOM   2195  CA  THR F 338     128.017  30.429 238.908  1.00 63.66           C  
ATOM   2196  CA  LEU F 339     130.625  28.819 241.164  1.00 48.34           C  
ATOM   2197  CA  GLN F 340     130.970  29.448 244.907  1.00 49.00           C  
ATOM   2198  CA  GLU F 341     134.744  29.269 244.628  1.00 54.54           C  
ATOM   2199  CA  SER F 342     137.107  30.638 241.997  1.00 73.07           C  
ATOM   2200  CA  THR F 343     140.292  28.729 242.858  1.00 51.47           C  
ATOM   2201  CA  VAL F 344     141.080  25.072 243.571  1.00 58.08           C  
ATOM   2202  CA  HIS F 345     144.105  23.115 244.828  1.00 49.89           C  
ATOM   2203  CA  VAL F 346     144.732  20.653 242.007  1.00 68.77           C  
ATOM   2204  CA  LEU F 347     146.371  17.449 243.212  1.00 63.01           C  
ATOM   2205  CA  GLU F 348     147.596  14.387 241.326  1.00 54.66           C  
ATOM   2206  CA  LYS F 349     144.567  12.396 242.510  1.00 72.07           C  
ATOM   2207  CA  GLY F 350     142.493  13.752 239.638  1.00 39.63           C  
ATOM   2208  CA  ALA F 351     139.439  14.676 241.692  1.00 41.09           C  
ATOM   2209  CA  VAL F 352     138.115  18.177 242.371  1.00 46.73           C  
ATOM   2210  CA  THR F 353     134.868  18.859 244.227  1.00 47.92           C  
ATOM   2211  CA  VAL F 354     133.168  22.223 243.624  1.00 51.99           C  
ATOM   2212  CA  HIS F 355     129.977  23.959 244.775  1.00 29.31           C  
ATOM   2213  CA  PHE F 356     127.781  26.040 242.467  1.00 33.75           C  
ATOM   2214  CA  SER F 357     124.503  27.958 242.389  1.00 30.86           C  
ATOM   2215  CA  THR F 358     121.790  28.042 239.725  1.00 42.24           C  
ATOM   2216  CA  ALA F 359     118.104  28.742 239.102  1.00 62.14           C  
ATOM   2217  CA  SER F 360     117.064  26.217 236.458  1.00 46.85           C  
ATOM   2218  CA  PRO F 361     115.799  22.615 236.193  1.00 37.76           C  
ATOM   2219  CA  GLN F 362     118.118  21.178 233.538  1.00 43.63           C  
ATOM   2220  CA  ALA F 363     120.994  23.623 233.096  1.00 58.87           C  
ATOM   2221  CA  ASN F 364     123.887  23.557 230.628  1.00 56.56           C  
ATOM   2222  CA  PHE F 365     127.120  25.329 231.565  1.00 58.36           C  
ATOM   2223  CA  ILE F 366     130.780  25.235 230.520  1.00 56.82           C  
ATOM   2224  CA  VAL F 367     133.035  25.020 233.579  1.00 52.05           C  
ATOM   2225  CA  SER F 368     136.738  25.796 233.196  1.00 29.99           C  
ATOM   2226  CA  LEU F 369     139.777  24.633 235.148  1.00 37.55           C  
ATOM   2227  CA  CYS F 370     143.217  26.203 234.780  1.00 36.87           C  
ATOM   2228  CA  GLY F 371     143.249  26.115 230.984  1.00 58.62           C  
ATOM   2229  CA  LYS F 372     140.914  23.223 230.207  1.00 53.04           C  
ATOM   2230  CA  LYS F 373     137.147  23.388 229.685  1.00 48.17           C  
ATOM   2231  CA  THR F 374     134.238  20.946 229.975  1.00 65.17           C  
ATOM   2232  CA  THR F 375     130.455  20.687 230.183  1.00 58.52           C  
ATOM   2233  CA  CYS F 376     128.249  19.761 233.146  1.00 50.29           C  
ATOM   2234  CA  ASN F 377     124.686  18.481 233.505  1.00 56.59           C  
ATOM   2235  CA  ALA F 378     122.043  17.525 236.071  1.00 72.53           C  
ATOM   2236  CA  GLU F 379     118.404  17.970 237.081  1.00 54.57           C  
ATOM   2237  CA  CYS F 380     117.434  20.219 240.000  1.00 34.05           C  
TER    2238      CYS F 380                                                      
ATOM   2239  CA  PHE Z   6     119.253  85.379 293.613  1.00 45.45           C  
ATOM   2240  CA  THR Z   7     116.209  86.976 293.863  1.00 41.96           C  
ATOM   2241  CA  LEU Z   8     114.860  90.095 292.203  1.00 41.25           C  
ATOM   2242  CA  THR Z   9     111.247  88.945 292.108  1.00 26.30           C  
ATOM   2243  CA  SER Z  10     108.772  87.543 294.655  1.00 35.89           C  
ATOM   2244  CA  PRO Z  11     105.882  84.987 294.720  1.00 29.25           C  
ATOM   2245  CA  TYR Z  12     102.519  86.209 293.413  1.00 39.00           C  
ATOM   2246  CA  LEU Z  13      98.869  85.131 293.629  1.00 42.63           C  
ATOM   2247  CA  GLY Z  14      96.777  83.688 290.822  1.00 50.22           C  
ATOM   2248  CA  THR Z  15      93.177  82.726 290.215  1.00 53.20           C  
ATOM   2249  CA  CYS Z  16      92.710  78.954 290.407  1.00 52.62           C  
ATOM   2250  CA  SER Z  17      89.797  76.665 289.557  1.00 54.81           C  
ATOM   2251  CA  TYR Z  18      90.010  74.186 292.454  1.00 47.95           C  
ATOM   2252  CA  CYS Z  19      91.628  74.710 295.868  1.00 45.91           C  
ATOM   2253  CA  HIS Z  20      91.082  71.895 298.407  1.00 69.50           C  
ATOM   2254  CA  HIS Z  21      87.449  72.904 298.012  1.00 42.74           C  
ATOM   2255  CA  THR Z  22      86.180  72.378 294.477  1.00 47.11           C  
ATOM   2256  CA  VAL Z  23      85.283  76.091 294.381  1.00 37.88           C  
ATOM   2257  CA  PRO Z  24      87.693  78.250 292.306  1.00 40.46           C  
ATOM   2258  CA  CYS Z  25      89.842  80.445 294.546  1.00 43.44           C  
ATOM   2259  CA  PHE Z  26      92.557  83.086 294.450  1.00 41.48           C  
ATOM   2260  CA  SER Z  27      95.494  81.353 296.066  1.00 48.62           C  
ATOM   2261  CA  PRO Z  28      99.296  81.063 295.780  1.00 40.22           C  
ATOM   2262  CA  VAL Z  29     100.832  78.035 294.067  1.00 49.60           C  
ATOM   2263  CA  LYS Z  30      98.697  78.949 291.049  1.00 42.14           C  
ATOM   2264  CA  ILE Z  31      99.578  76.652 288.176  1.00 50.38           C  
ATOM   2265  CA  GLU Z  32      99.986  78.493 284.875  1.00 65.63           C  
ATOM   2266  CA  GLN Z  33     101.552  75.866 282.606  1.00 65.67           C  
ATOM   2267  CA  VAL Z  34     102.859  72.317 282.609  1.00 49.94           C  
ATOM   2268  CA  TRP Z  35     105.172  70.372 280.316  1.00 33.75           C  
ATOM   2269  CA  ASP Z  36     104.573  66.757 279.406  1.00 61.31           C  
ATOM   2270  CA  GLU Z  37     107.001  66.437 276.523  1.00 71.01           C  
ATOM   2271  CA  ALA Z  38     109.815  64.209 277.730  1.00 59.27           C  
ATOM   2272  CA  ASP Z  39     110.243  60.583 276.683  1.00 61.65           C  
ATOM   2273  CA  ASP Z  40     110.973  59.971 280.328  1.00 54.85           C  
ATOM   2274  CA  ASN Z  41     107.980  59.909 282.649  1.00 51.19           C  
ATOM   2275  CA  THR Z  42     108.927  63.306 284.097  1.00 44.55           C  
ATOM   2276  CA  ILE Z  43     106.936  66.527 284.399  1.00 40.15           C  
ATOM   2277  CA  ARG Z  44     107.778  70.233 284.522  1.00 31.15           C  
ATOM   2278  CA  ILE Z  45     105.389  72.428 286.528  1.00 33.17           C  
ATOM   2279  CA  GLN Z  46     105.141  76.232 286.648  1.00 29.21           C  
ATOM   2280  CA  THR Z  47     103.753  77.711 289.878  1.00 36.41           C  
ATOM   2281  CA  SER Z  48     103.406  81.188 291.386  1.00 36.55           C  
ATOM   2282  CA  ALA Z  49     105.259  80.460 294.619  1.00 27.15           C  
ATOM   2283  CA  GLN Z  50     109.032  80.833 294.958  1.00 31.68           C  
ATOM   2284  CA  PHE Z  51     111.440  78.232 296.313  1.00 18.09           C  
ATOM   2285  CA  GLY Z  52     115.095  77.939 297.306  1.00 34.99           C  
ATOM   2286  CA  TYR Z  53     114.840  81.129 299.346  1.00 36.00           C  
ATOM   2287  CA  ASP Z  54     113.110  82.574 302.409  1.00 27.92           C  
ATOM   2288  CA  GLN Z  55     110.889  85.652 302.660  1.00 38.46           C  
ATOM   2289  CA  SER Z  56     113.516  87.781 300.921  1.00 48.55           C  
ATOM   2290  CA  GLY Z  57     116.782  87.428 299.015  1.00 43.07           C  
ATOM   2291  CA  ALA Z  58     118.093  84.030 297.900  1.00 46.50           C  
ATOM   2292  CA  ALA Z  59     118.542  81.553 300.754  1.00 62.00           C  
ATOM   2293  CA  SER Z  60     119.265  78.068 299.453  1.00 68.94           C  
ATOM   2294  CA  ALA Z  61     118.842  74.458 300.581  1.00 71.71           C  
ATOM   2295  CA  ASN Z  62     115.214  73.680 301.421  1.00 47.92           C  
ATOM   2296  CA  LYS Z  63     113.146  76.846 301.822  1.00 28.17           C  
ATOM   2297  CA  TYR Z  64     110.296  78.462 299.885  1.00 29.00           C  
ATOM   2298  CA  ARG Z  65     108.244  81.644 300.163  1.00 29.06           C  
ATOM   2299  CA  TYR Z  66     104.830  82.786 298.987  1.00 21.64           C  
ATOM   2300  CA  MET Z  67     102.154  85.437 299.431  1.00 30.51           C  
ATOM   2301  CA  SER Z  68      99.683  85.371 302.309  1.00 43.55           C  
ATOM   2302  CA  LEU Z  69      96.161  84.081 302.756  1.00 67.68           C  
ATOM   2303  CA  LYS Z  70      95.238  87.764 302.702  1.00 48.66           C  
ATOM   2304  CA  GLN Z  71      96.471  90.524 300.387  1.00 47.44           C  
ATOM   2305  CA  ASP Z  72      98.771  92.129 302.996  1.00 69.82           C  
ATOM   2306  CA  HIS Z  73     101.588  91.476 300.544  1.00 60.30           C  
ATOM   2307  CA  THR Z  74     103.087  89.715 303.532  1.00 45.18           C  
ATOM   2308  CA  VAL Z  75     105.664  87.354 302.075  1.00 42.97           C  
ATOM   2309  CA  LYS Z  76     105.895  84.618 304.707  1.00 38.55           C  
ATOM   2310  CA  GLU Z  77     108.095  81.553 304.322  1.00 28.82           C  
ATOM   2311  CA  GLY Z  78     108.188  77.920 305.331  1.00 32.17           C  
ATOM   2312  CA  THR Z  79     110.375  74.869 304.797  1.00 29.84           C  
ATOM   2313  CA  MET Z  80     110.791  73.155 301.401  1.00 32.77           C  
ATOM   2314  CA  ASP Z  81     109.864  70.037 303.263  1.00 48.04           C  
ATOM   2315  CA  ASP Z  82     106.108  70.301 303.531  1.00 36.63           C  
ATOM   2316  CA  ILE Z  83     105.455  70.986 299.843  1.00 52.29           C  
ATOM   2317  CA  LYS Z  84     104.210  67.915 298.009  1.00 56.75           C  
ATOM   2318  CA  ILE Z  85     102.941  67.254 294.486  1.00 67.60           C  
ATOM   2319  CA  SER Z  86     100.162  64.899 293.453  1.00 54.33           C  
ATOM   2320  CA  THR Z  87      98.070  64.012 290.423  1.00 52.13           C  
ATOM   2321  CA  SER Z  88      96.073  60.902 291.223  1.00 65.22           C  
ATOM   2322  CA  GLY Z  89      98.465  59.541 293.822  1.00 68.14           C  
ATOM   2323  CA  PRO Z  90     101.931  60.222 295.205  1.00 74.66           C  
ATOM   2324  CA  CYS Z  91     104.538  62.312 293.412  1.00 56.97           C  
ATOM   2325  CA  ARG Z  92     108.127  62.883 294.400  1.00 52.91           C  
ATOM   2326  CA  ARG Z  93     109.763  66.099 293.292  1.00 35.32           C  
ATOM   2327  CA  LEU Z  94     113.344  66.170 292.111  1.00 48.09           C  
ATOM   2328  CA  SER Z  95     114.611  69.728 291.709  1.00 50.84           C  
ATOM   2329  CA  TYR Z  96     113.406  73.204 292.680  1.00 35.17           C  
ATOM   2330  CA  LYS Z  97     114.009  76.107 290.318  1.00 43.66           C  
ATOM   2331  CA  GLY Z  98     112.502  79.151 292.000  1.00 37.03           C  
ATOM   2332  CA  TYR Z  99     109.078  79.290 290.347  1.00 44.71           C  
ATOM   2333  CA  PHE Z 100     109.305  75.859 288.748  1.00 31.29           C  
ATOM   2334  CA  LEU Z 101     108.840  72.264 289.862  1.00 31.02           C  
ATOM   2335  CA  LEU Z 102     109.834  68.943 288.337  1.00 44.86           C  
ATOM   2336  CA  ALA Z 103     108.797  65.450 289.397  1.00 33.40           C  
ATOM   2337  CA  LYS Z 104     107.632  62.044 288.162  1.00 39.87           C  
ATOM   2338  CA  CYS Z 105     104.070  62.085 288.630  1.00 42.89           C  
ATOM   2339  CA  PRO Z 106     101.945  58.554 288.357  1.00 66.61           C  
ATOM   2340  CA  PRO Z 107      98.834  58.403 286.151  1.00 62.43           C  
ATOM   2341  CA  GLY Z 108      97.479  61.807 285.158  1.00 53.14           C  
ATOM   2342  CA  ASP Z 109      94.060  63.388 284.703  1.00 63.24           C  
ATOM   2343  CA  SER Z 110      94.782  66.563 286.663  1.00 48.01           C  
ATOM   2344  CA  VAL Z 111      97.609  68.088 288.686  1.00 60.50           C  
ATOM   2345  CA  THR Z 112      97.600  69.421 292.240  1.00 42.21           C  
ATOM   2346  CA  VAL Z 113     100.359  71.320 294.022  1.00 66.91           C  
ATOM   2347  CA  SER Z 114      99.977  72.262 297.663  1.00 55.18           C  
ATOM   2348  CA  ILE Z 115     101.444  72.802 301.125  1.00 56.79           C  
ATOM   2349  CA  VAL Z 116     100.309  70.675 304.068  1.00 58.70           C  
ATOM   2350  CA  SER Z 117     101.959  72.282 307.090  1.00 81.56           C  
ATOM   2351  CA  SER Z 118      99.449  70.715 309.384  1.00 83.61           C  
ATOM   2352  CA  ASN Z 119      95.672  70.976 309.738  1.00 72.96           C  
ATOM   2353  CA  SER Z 120      95.378  74.090 307.572  1.00 75.47           C  
ATOM   2354  CA  ALA Z 121      96.747  74.412 304.035  1.00 66.65           C  
ATOM   2355  CA  THR Z 122      95.915  75.434 300.465  1.00 58.50           C  
ATOM   2356  CA  SER Z 123      96.286  73.789 297.050  1.00 52.95           C  
ATOM   2357  CA  CYS Z 124      95.736  74.749 293.416  1.00 51.84           C  
ATOM   2358  CA  THR Z 125      95.006  72.024 290.870  1.00 43.96           C  
ATOM   2359  CA  LEU Z 126      95.118  72.097 287.098  1.00 56.49           C  
ATOM   2360  CA  ALA Z 127      92.992  70.343 284.554  1.00 63.98           C  
ATOM   2361  CA  ARG Z 128      95.817  68.870 282.464  1.00 54.52           C  
ATOM   2362  CA  LYS Z 129      95.937  65.330 281.069  1.00 56.37           C  
ATOM   2363  CA  ILE Z 130      99.146  63.313 281.413  1.00 72.01           C  
ATOM   2364  CA  LYS Z 131      99.816  59.997 279.732  1.00 62.58           C  
ATOM   2365  CA  PRO Z 132     101.795  56.817 280.368  1.00 74.13           C  
ATOM   2366  CA  LYS Z 133     105.082  57.282 278.540  1.00 63.48           C  
ATOM   2367  CA  PHE Z 134     105.552  55.572 276.266  1.00 89.32           C  
ATOM   2368  CA  VAL Z 135     108.654  55.465 274.109  1.00 63.85           C  
ATOM   2369  CA  GLY Z 136     109.008  52.052 272.508  1.00 58.91           C  
ATOM   2370  CA  ARG Z 137     106.667  50.572 269.928  1.00 66.37           C  
ATOM   2371  CA  GLU Z 138     105.043  48.741 272.801  1.00 49.27           C  
ATOM   2372  CA  LYS Z 139     102.487  50.298 275.093  1.00 44.79           C  
ATOM   2373  CA  TYR Z 140     103.425  50.177 278.759  1.00 42.98           C  
ATOM   2374  CA  ASP Z 141     102.424  52.025 281.908  1.00 70.57           C  
ATOM   2375  CA  LEU Z 142     105.461  51.005 283.902  1.00 61.00           C  
ATOM   2376  CA  PRO Z 143     109.013  50.062 282.892  1.00 55.59           C  
ATOM   2377  CA  PRO Z 144     109.138  46.243 282.793  1.00 49.65           C  
ATOM   2378  CA  VAL Z 145     111.420  44.430 285.236  1.00 67.49           C  
ATOM   2379  CA  HIS Z 146     113.052  42.871 282.211  1.00 56.58           C  
ATOM   2380  CA  GLY Z 147     112.833  44.274 278.712  1.00 39.02           C  
ATOM   2381  CA  LYS Z 148     115.122  45.902 276.203  1.00 54.34           C  
ATOM   2382  CA  LYS Z 149     117.314  48.979 276.479  1.00 62.12           C  
ATOM   2383  CA  ILE Z 150     116.398  51.729 274.046  1.00 49.65           C  
ATOM   2384  CA  PRO Z 151     117.688  55.231 273.292  1.00 58.79           C  
ATOM   2385  CA  CYS Z 152     115.516  57.828 275.002  1.00 53.89           C  
ATOM   2386  CA  THR Z 153     115.971  61.236 276.620  1.00 50.29           C  
ATOM   2387  CA  VAL Z 154     115.135  62.059 280.255  1.00 70.58           C  
ATOM   2388  CA  TYR Z 155     115.716  64.570 283.078  1.00 36.63           C  
ATOM   2389  CA  ASP Z 156     118.845  64.408 285.273  1.00 62.99           C  
ATOM   2390  CA  LEU Z 255     120.538  81.216 281.886  1.00 64.70           C  
ATOM   2391  CA  HIS Z 256     120.246  77.673 283.220  1.00 54.61           C  
ATOM   2392  CA  LEU Z 257     120.108  75.895 286.592  1.00 77.90           C  
ATOM   2393  CA  PRO Z 258     117.377  73.267 286.067  1.00 31.29           C  
ATOM   2394  CA  PHE Z 259     117.540  69.457 285.741  1.00 22.24           C  
ATOM   2395  CA  LYS Z 260     119.103  69.238 282.273  1.00 44.90           C  
ATOM   2396  CA  LEU Z 261     117.784  66.879 279.592  1.00 35.75           C  
ATOM   2397  CA  ILE Z 262     120.218  64.077 278.773  1.00 62.24           C  
ATOM   2398  CA  PRO Z 263     119.842  61.226 276.269  1.00 66.26           C  
ATOM   2399  CA  SER Z 264     120.144  57.761 277.837  1.00 79.04           C  
ATOM   2400  CA  THR Z 265     118.396  54.395 278.128  1.00 62.44           C  
ATOM   2401  CA  CYS Z 266     114.796  53.543 278.908  1.00 62.29           C  
ATOM   2402  CA  MET Z 267     113.587  49.992 279.290  1.00 56.17           C  
ATOM   2403  CA  VAL Z 268     110.799  49.173 276.870  1.00 76.96           C  
ATOM   2404  CA  PRO Z 269     109.648  44.741 276.774  1.00 36.88           C  
ATOM   2405  CA  VAL Z 270     110.196  42.291 273.945  1.00 43.11           C  
ATOM   2406  CA  ALA Z 271     107.248  40.571 272.299  1.00 49.39           C  
ATOM   2407  CA  HIS Z 272     106.334  36.899 271.995  1.00 58.24           C  
ATOM   2408  CA  ALA Z 273     108.053  35.724 268.823  1.00 46.11           C  
ATOM   2409  CA  PRO Z 274     105.431  35.201 266.100  1.00 27.92           C  
ATOM   2410  CA  ASN Z 275     104.977  31.625 265.035  1.00 46.55           C  
ATOM   2411  CA  VAL Z 276     105.812  32.038 261.364  1.00 43.17           C  
ATOM   2412  CA  ILE Z 277     104.693  29.852 258.514  1.00 51.35           C  
ATOM   2413  CA  HIS Z 278     106.500  29.942 255.186  1.00 45.59           C  
ATOM   2414  CA  GLY Z 279     104.572  28.921 252.081  1.00 37.69           C  
ATOM   2415  CA  PHE Z 280     104.315  29.524 248.348  1.00 35.83           C  
ATOM   2416  CA  LYS Z 281     105.247  33.193 248.092  1.00 46.32           C  
ATOM   2417  CA  HIS Z 282     103.599  33.375 251.484  1.00 32.73           C  
ATOM   2418  CA  ILE Z 283     104.135  34.226 255.135  1.00 51.26           C  
ATOM   2419  CA  SER Z 284     101.270  33.848 257.575  1.00 31.78           C  
ATOM   2420  CA  LEU Z 285     102.295  35.447 260.863  1.00 35.64           C  
ATOM   2421  CA  GLN Z 286     100.605  33.866 263.874  1.00 30.50           C  
ATOM   2422  CA  LEU Z 287     100.809  36.511 266.609  1.00 50.92           C  
ATOM   2423  CA  ASP Z 288      99.774  36.399 270.266  1.00 67.28           C  
ATOM   2424  CA  THR Z 289     100.630  39.388 272.464  1.00 58.10           C  
ATOM   2425  CA  ASP Z 290      99.507  40.432 275.901  1.00 62.68           C  
ATOM   2426  CA  HIS Z 291      99.835  44.066 274.863  1.00 51.39           C  
ATOM   2427  CA  LEU Z 292     100.184  46.501 271.985  1.00 45.52           C  
ATOM   2428  CA  THR Z 293     102.954  45.711 269.537  1.00 40.05           C  
ATOM   2429  CA  LEU Z 294     103.696  47.538 266.309  1.00 32.35           C  
ATOM   2430  CA  LEU Z 295     104.067  45.408 263.211  1.00 25.31           C  
ATOM   2431  CA  THR Z 296     105.870  46.764 260.195  1.00 34.07           C  
ATOM   2432  CA  THR Z 297     106.571  45.450 256.742  1.00 39.32           C  
ATOM   2433  CA  ARG Z 298     108.050  46.495 253.424  1.00 54.98           C  
ATOM   2434  CA  ARG Z 299     109.175  44.698 250.314  1.00 45.46           C  
ATOM   2435  CA  LEU Z 300     112.832  44.445 249.438  1.00 52.55           C  
ATOM   2436  CA  GLY Z 301     112.311  45.343 245.780  1.00 58.81           C  
ATOM   2437  CA  ALA Z 302     110.981  48.590 244.371  1.00 71.90           C  
ATOM   2438  CA  ASN Z 303     107.362  49.078 245.311  1.00 49.11           C  
ATOM   2439  CA  PRO Z 304     107.768  48.147 249.012  1.00 30.35           C  
ATOM   2440  CA  GLU Z 305     104.135  48.968 249.770  1.00 52.86           C  
ATOM   2441  CA  PRO Z 306     105.185  49.549 253.393  1.00 51.24           C  
ATOM   2442  CA  THR Z 307     102.658  48.482 256.022  1.00 56.23           C  
ATOM   2443  CA  THR Z 308     102.331  49.487 259.652  1.00 62.88           C  
ATOM   2444  CA  GLU Z 309      99.724  48.254 262.142  1.00 42.61           C  
ATOM   2445  CA  TRP Z 310      99.409  47.904 265.905  1.00 30.89           C  
ATOM   2446  CA  ILE Z 311      98.183  44.547 267.038  1.00 43.40           C  
ATOM   2447  CA  VAL Z 312      96.867  43.023 270.247  1.00 57.42           C  
ATOM   2448  CA  GLY Z 313      96.044  39.574 271.392  1.00 54.30           C  
ATOM   2449  CA  LYS Z 314      95.526  36.879 268.823  1.00 61.04           C  
ATOM   2450  CA  THR Z 315      95.471  37.106 265.081  1.00 61.96           C  
ATOM   2451  CA  VAL Z 316      97.133  35.884 261.942  1.00 48.91           C  
ATOM   2452  CA  ARG Z 317      98.508  38.039 259.161  1.00 58.32           C  
ATOM   2453  CA  ASN Z 318      99.769  36.689 255.876  1.00 39.78           C  
ATOM   2454  CA  PHE Z 319     101.897  38.733 253.441  1.00 60.31           C  
ATOM   2455  CA  THR Z 320     102.906  38.493 250.001  1.00 62.67           C  
ATOM   2456  CA  VAL Z 321     106.708  37.354 249.207  1.00 57.50           C  
ATOM   2457  CA  ASP Z 322     107.261  39.296 245.990  1.00 60.87           C  
ATOM   2458  CA  ARG Z 323     110.150  37.060 244.976  1.00 51.95           C  
ATOM   2459  CA  ASP Z 324     112.492  39.704 246.380  1.00 53.97           C  
ATOM   2460  CA  GLY Z 325     111.340  38.705 249.841  1.00 33.21           C  
ATOM   2461  CA  LEU Z 326     110.414  41.267 252.476  1.00 31.72           C  
ATOM   2462  CA  GLU Z 327     111.384  42.571 255.877  1.00 33.03           C  
ATOM   2463  CA  TYR Z 328     109.177  42.625 258.940  1.00 19.30           C  
ATOM   2464  CA  ILE Z 329     109.880  44.324 262.252  1.00 30.22           C  
ATOM   2465  CA  TRP Z 330     107.589  43.227 265.033  1.00 37.96           C  
ATOM   2466  CA  GLY Z 331     107.372  45.179 268.278  1.00 41.91           C  
ATOM   2467  CA  ASN Z 332     110.960  46.371 268.858  1.00 52.36           C  
ATOM   2468  CA  HIS Z 333     112.220  42.960 267.871  1.00 52.61           C  
ATOM   2469  CA  GLU Z 334     114.838  42.857 265.459  1.00 64.46           C  
ATOM   2470  CA  PRO Z 335     113.984  43.209 262.100  1.00 49.05           C  
ATOM   2471  CA  VAL Z 336     113.946  39.868 260.284  1.00 52.54           C  
ATOM   2472  CA  ARG Z 337     113.379  39.513 256.592  1.00 33.25           C  
ATOM   2473  CA  VAL Z 338     112.142  36.493 254.702  1.00 58.72           C  
ATOM   2474  CA  TYR Z 339     112.629  35.378 251.111  1.00 41.31           C  
ATOM   2475  CA  ALA Z 340     111.222  32.711 248.793  1.00 49.85           C  
TER    2476      ALA Z 340                                                      
MASTER      729    0    0    0    0    0    0    6 2468    8    0  228          
END                                                                             
