HEADER    HYDROLASE/HYDROLASE                     20-NOV-11   4A8B              
TITLE     SYMMETRIZED CRYO-EM RECONSTRUCTION OF E. COLI DEGQ 12-MER IN COMPLEX  
TITLE    2 WITH LYSOZYMES                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PERIPLASMIC PH-DEPENDENT SERINE ENDOPROTEASE DEGQ;         
COMPND   3 CHAIN: A, B, C, D, E, F, G, H, I, J, K, L;                           
COMPND   4 SYNONYM: PROTEASE DO, DEGQ;                                          
COMPND   5 EC: 3.4.21.107;                                                      
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: LYSOZYME C;                                                
COMPND  10 CHAIN: M, N, O, P, Q, R;                                             
COMPND  11 SYNONYM: 1,4-BETA-N-ACETYLMURAMIDASE C, ALLERGEN GAL D IV, GAL D 4;  
COMPND  12 EC: 3.2.1.17                                                         
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 83333;                                               
SOURCE   4 STRAIN: K-12;                                                        
SOURCE   5 TISSUE: PERIPLASM;                                                   
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR: PET26B;                                    
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE  13 ORGANISM_COMMON: CHICKEN;                                            
SOURCE  14 ORGANISM_TAXID: 9031;                                                
SOURCE  15 TISSUE: EGG WHITE                                                    
KEYWDS    HYDROLASE-HYDROLASE COMPLEX, CHAPERONE                                
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C, D, E, F, G, H, I, J, K, L, M, N, O, P,  
MDLTYP   2Q, R                                                                  
AUTHOR    H.MALET,F.CANELLAS,J.SAWA,J.YAN,K.THALASSINOS,M.EHRMANN,T.CLAUSEN,    
AUTHOR   2 H.R.SAIBIL                                                           
REVDAT   3   23-AUG-17 4A8B    1       REMARK                                   
REVDAT   2   15-FEB-12 4A8B    1       JRNL                                     
REVDAT   1   11-JAN-12 4A8B    0                                                
JRNL        AUTH   H.MALET,F.CANELLAS,J.SAWA,J.YAN,K.THALASSINOS,M.EHRMANN,     
JRNL        AUTH 2 T.CLAUSEN,H.R.SAIBIL                                         
JRNL        TITL   NEWLY FOLDED SUBSTRATES INSIDE THE MOLECULAR CAGE OF THE     
JRNL        TITL 2 HTRA CHAPERONE DEGQ                                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  19   152 2012              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   22245966                                                     
JRNL        DOI    10.1038/NSMB.2210                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.   13.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : FLEX-EM, MODELLER, UCSF CHIMERA,          
REMARK   3                            IMAGIC, SPIDER                            
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 3STJ                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : FLEXIBLE FIT                        
REMARK   3   REFINEMENT TARGET            : CROSS-CORRELATION COEFFICIENT       
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : METHOD--RIGID BODY AND FLEXIBLE FITTING          
REMARK   3  REFINEMENT PROTOCOL--X-RAY                                          
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 2.800                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 13.00                          
REMARK   3   NUMBER OF PARTICLES               : 13432                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: SUBMISSION BASED ON EXPERIMENTAL DATA FROM EMDB EMD   
REMARK   3  -1982(DEPOSITION ID: 10365).                                        
REMARK   4                                                                      
REMARK   4 4A8B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290050379.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : ESCHERICHIA COLI DEGQ 12- MER     
REMARK 245                                    IN COMPLEX WITH LYSOZYME          
REMARK 245                                    SUBSTRATES                        
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.20                              
REMARK 245   SAMPLE SUPPORT DETAILS         : CARBON                            
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -- CRYOGEN-       
REMARK 245                                    ETHANE, INSTRUMENT- MANUAL        
REMARK 245                                    PLUNGER, METHOD- BLOT FOR 2       
REMARK 245                                    SECONDS BEFORE PLUNGING,          
REMARK 245   SAMPLE BUFFER                  : 20 MM HEPES/NAOH, 150 MM NACL     
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 91.00                          
REMARK 245   MICROSCOPE MODEL                  : FEI TECNAI F20                 
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 1000.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : -0.10                          
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)  : 15.00                          
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : 50000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 50000                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
REMARK 245   IMAGING DETAILS                   : LOW DOSE MODE                  
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: OCTADECAMERIC                     
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R                
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 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN B, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN C, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN D, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN E, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN F, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN G, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN H, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN I, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN J, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN K, SER 214 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN L, SER 214 TO ALA                        
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     SER A     1                                                      
REMARK 465     ILE A     2                                                      
REMARK 465     PRO A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 465     GLN A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     ALA A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     GLN A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     SER A    36                                                      
REMARK 465     GLN A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     LYS A    40                                                      
REMARK 465     ILE A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     GLU A    43                                                      
REMARK 465     GLU A    44                                                      
REMARK 465     PHE A    45                                                      
REMARK 465     LYS A    46                                                      
REMARK 465     LYS A    47                                                      
REMARK 465     PHE A    48                                                      
REMARK 465     PHE A    49                                                      
REMARK 465     GLY A    50                                                      
REMARK 465     ASP A    51                                                      
REMARK 465     ASP A    52                                                      
REMARK 465     LEU A    53                                                      
REMARK 465     PRO A    54                                                      
REMARK 465     ASP A    55                                                      
REMARK 465     GLN A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     THR A   330                                                      
REMARK 465     LEU A   331                                                      
REMARK 465     ASP A   332                                                      
REMARK 465     THR A   333                                                      
REMARK 465     SER A   334                                                      
REMARK 465     THR A   335                                                      
REMARK 465     SER A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     SER A   338                                                      
REMARK 465     ALA A   339                                                      
REMARK 465     ARG A   428                                                      
REMARK 465     LEU A   429                                                      
REMARK 465     GLU A   430                                                      
REMARK 465     HIS A   431                                                      
REMARK 465     HIS A   432                                                      
REMARK 465     HIS A   433                                                      
REMARK 465     HIS A   434                                                      
REMARK 465     HIS A   435                                                      
REMARK 465     HIS A   436                                                      
REMARK 465     SER B     1                                                      
REMARK 465     ILE B     2                                                      
REMARK 465     PRO B     3                                                      
REMARK 465     GLY B     4                                                      
REMARK 465     GLN B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     ALA B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     GLN B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     SER B    36                                                      
REMARK 465     GLN B    37                                                      
REMARK 465     GLY B    38                                                      
REMARK 465     GLN B    39                                                      
REMARK 465     LYS B    40                                                      
REMARK 465     ILE B    41                                                      
REMARK 465     PRO B    42                                                      
REMARK 465     GLU B    43                                                      
REMARK 465     GLU B    44                                                      
REMARK 465     PHE B    45                                                      
REMARK 465     LYS B    46                                                      
REMARK 465     LYS B    47                                                      
REMARK 465     PHE B    48                                                      
REMARK 465     PHE B    49                                                      
REMARK 465     GLY B    50                                                      
REMARK 465     ASP B    51                                                      
REMARK 465     ASP B    52                                                      
REMARK 465     LEU B    53                                                      
REMARK 465     PRO B    54                                                      
REMARK 465     ASP B    55                                                      
REMARK 465     GLN B    56                                                      
REMARK 465     PRO B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     THR B   330                                                      
REMARK 465     LEU B   331                                                      
REMARK 465     ASP B   332                                                      
REMARK 465     THR B   333                                                      
REMARK 465     SER B   334                                                      
REMARK 465     THR B   335                                                      
REMARK 465     SER B   336                                                      
REMARK 465     SER B   337                                                      
REMARK 465     SER B   338                                                      
REMARK 465     ALA B   339                                                      
REMARK 465     ARG B   428                                                      
REMARK 465     LEU B   429                                                      
REMARK 465     GLU B   430                                                      
REMARK 465     HIS B   431                                                      
REMARK 465     HIS B   432                                                      
REMARK 465     HIS B   433                                                      
REMARK 465     HIS B   434                                                      
REMARK 465     HIS B   435                                                      
REMARK 465     HIS B   436                                                      
REMARK 465     SER C     1                                                      
REMARK 465     ILE C     2                                                      
REMARK 465     PRO C     3                                                      
REMARK 465     GLY C     4                                                      
REMARK 465     GLN C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     ALA C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     GLN C     9                                                      
REMARK 465     ALA C    10                                                      
REMARK 465     SER C    36                                                      
REMARK 465     GLN C    37                                                      
REMARK 465     GLY C    38                                                      
REMARK 465     GLN C    39                                                      
REMARK 465     LYS C    40                                                      
REMARK 465     ILE C    41                                                      
REMARK 465     PRO C    42                                                      
REMARK 465     GLU C    43                                                      
REMARK 465     GLU C    44                                                      
REMARK 465     PHE C    45                                                      
REMARK 465     LYS C    46                                                      
REMARK 465     LYS C    47                                                      
REMARK 465     PHE C    48                                                      
REMARK 465     PHE C    49                                                      
REMARK 465     GLY C    50                                                      
REMARK 465     ASP C    51                                                      
REMARK 465     ASP C    52                                                      
REMARK 465     LEU C    53                                                      
REMARK 465     PRO C    54                                                      
REMARK 465     ASP C    55                                                      
REMARK 465     GLN C    56                                                      
REMARK 465     PRO C    57                                                      
REMARK 465     ALA C    58                                                      
REMARK 465     THR C   330                                                      
REMARK 465     LEU C   331                                                      
REMARK 465     ASP C   332                                                      
REMARK 465     THR C   333                                                      
REMARK 465     SER C   334                                                      
REMARK 465     THR C   335                                                      
REMARK 465     SER C   336                                                      
REMARK 465     SER C   337                                                      
REMARK 465     SER C   338                                                      
REMARK 465     ALA C   339                                                      
REMARK 465     ARG C   428                                                      
REMARK 465     LEU C   429                                                      
REMARK 465     GLU C   430                                                      
REMARK 465     HIS C   431                                                      
REMARK 465     HIS C   432                                                      
REMARK 465     HIS C   433                                                      
REMARK 465     HIS C   434                                                      
REMARK 465     HIS C   435                                                      
REMARK 465     HIS C   436                                                      
REMARK 465     SER D     1                                                      
REMARK 465     ILE D     2                                                      
REMARK 465     PRO D     3                                                      
REMARK 465     GLY D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     VAL D     6                                                      
REMARK 465     ALA D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     GLN D     9                                                      
REMARK 465     ALA D    10                                                      
REMARK 465     SER D    36                                                      
REMARK 465     GLN D    37                                                      
REMARK 465     GLY D    38                                                      
REMARK 465     GLN D    39                                                      
REMARK 465     LYS D    40                                                      
REMARK 465     ILE D    41                                                      
REMARK 465     PRO D    42                                                      
REMARK 465     GLU D    43                                                      
REMARK 465     GLU D    44                                                      
REMARK 465     PHE D    45                                                      
REMARK 465     LYS D    46                                                      
REMARK 465     LYS D    47                                                      
REMARK 465     PHE D    48                                                      
REMARK 465     PHE D    49                                                      
REMARK 465     GLY D    50                                                      
REMARK 465     ASP D    51                                                      
REMARK 465     ASP D    52                                                      
REMARK 465     LEU D    53                                                      
REMARK 465     PRO D    54                                                      
REMARK 465     ASP D    55                                                      
REMARK 465     GLN D    56                                                      
REMARK 465     PRO D    57                                                      
REMARK 465     ALA D    58                                                      
REMARK 465     THR D   330                                                      
REMARK 465     LEU D   331                                                      
REMARK 465     ASP D   332                                                      
REMARK 465     THR D   333                                                      
REMARK 465     SER D   334                                                      
REMARK 465     THR D   335                                                      
REMARK 465     SER D   336                                                      
REMARK 465     SER D   337                                                      
REMARK 465     SER D   338                                                      
REMARK 465     ALA D   339                                                      
REMARK 465     ARG D   428                                                      
REMARK 465     LEU D   429                                                      
REMARK 465     GLU D   430                                                      
REMARK 465     HIS D   431                                                      
REMARK 465     HIS D   432                                                      
REMARK 465     HIS D   433                                                      
REMARK 465     HIS D   434                                                      
REMARK 465     HIS D   435                                                      
REMARK 465     HIS D   436                                                      
REMARK 465     SER E     1                                                      
REMARK 465     ILE E     2                                                      
REMARK 465     PRO E     3                                                      
REMARK 465     GLY E     4                                                      
REMARK 465     GLN E     5                                                      
REMARK 465     VAL E     6                                                      
REMARK 465     ALA E     7                                                      
REMARK 465     ASP E     8                                                      
REMARK 465     GLN E     9                                                      
REMARK 465     ALA E    10                                                      
REMARK 465     SER E    36                                                      
REMARK 465     GLN E    37                                                      
REMARK 465     GLY E    38                                                      
REMARK 465     GLN E    39                                                      
REMARK 465     LYS E    40                                                      
REMARK 465     ILE E    41                                                      
REMARK 465     PRO E    42                                                      
REMARK 465     GLU E    43                                                      
REMARK 465     GLU E    44                                                      
REMARK 465     PHE E    45                                                      
REMARK 465     LYS E    46                                                      
REMARK 465     LYS E    47                                                      
REMARK 465     PHE E    48                                                      
REMARK 465     PHE E    49                                                      
REMARK 465     GLY E    50                                                      
REMARK 465     ASP E    51                                                      
REMARK 465     ASP E    52                                                      
REMARK 465     LEU E    53                                                      
REMARK 465     PRO E    54                                                      
REMARK 465     ASP E    55                                                      
REMARK 465     GLN E    56                                                      
REMARK 465     PRO E    57                                                      
REMARK 465     ALA E    58                                                      
REMARK 465     THR E   330                                                      
REMARK 465     LEU E   331                                                      
REMARK 465     ASP E   332                                                      
REMARK 465     THR E   333                                                      
REMARK 465     SER E   334                                                      
REMARK 465     THR E   335                                                      
REMARK 465     SER E   336                                                      
REMARK 465     SER E   337                                                      
REMARK 465     SER E   338                                                      
REMARK 465     ALA E   339                                                      
REMARK 465     ARG E   428                                                      
REMARK 465     LEU E   429                                                      
REMARK 465     GLU E   430                                                      
REMARK 465     HIS E   431                                                      
REMARK 465     HIS E   432                                                      
REMARK 465     HIS E   433                                                      
REMARK 465     HIS E   434                                                      
REMARK 465     HIS E   435                                                      
REMARK 465     HIS E   436                                                      
REMARK 465     SER F     1                                                      
REMARK 465     ILE F     2                                                      
REMARK 465     PRO F     3                                                      
REMARK 465     GLY F     4                                                      
REMARK 465     GLN F     5                                                      
REMARK 465     VAL F     6                                                      
REMARK 465     ALA F     7                                                      
REMARK 465     ASP F     8                                                      
REMARK 465     GLN F     9                                                      
REMARK 465     ALA F    10                                                      
REMARK 465     SER F    36                                                      
REMARK 465     GLN F    37                                                      
REMARK 465     GLY F    38                                                      
REMARK 465     GLN F    39                                                      
REMARK 465     LYS F    40                                                      
REMARK 465     ILE F    41                                                      
REMARK 465     PRO F    42                                                      
REMARK 465     GLU F    43                                                      
REMARK 465     GLU F    44                                                      
REMARK 465     PHE F    45                                                      
REMARK 465     LYS F    46                                                      
REMARK 465     LYS F    47                                                      
REMARK 465     PHE F    48                                                      
REMARK 465     PHE F    49                                                      
REMARK 465     GLY F    50                                                      
REMARK 465     ASP F    51                                                      
REMARK 465     ASP F    52                                                      
REMARK 465     LEU F    53                                                      
REMARK 465     PRO F    54                                                      
REMARK 465     ASP F    55                                                      
REMARK 465     GLN F    56                                                      
REMARK 465     PRO F    57                                                      
REMARK 465     ALA F    58                                                      
REMARK 465     THR F   330                                                      
REMARK 465     LEU F   331                                                      
REMARK 465     ASP F   332                                                      
REMARK 465     THR F   333                                                      
REMARK 465     SER F   334                                                      
REMARK 465     THR F   335                                                      
REMARK 465     SER F   336                                                      
REMARK 465     SER F   337                                                      
REMARK 465     SER F   338                                                      
REMARK 465     ALA F   339                                                      
REMARK 465     ARG F   428                                                      
REMARK 465     LEU F   429                                                      
REMARK 465     GLU F   430                                                      
REMARK 465     HIS F   431                                                      
REMARK 465     HIS F   432                                                      
REMARK 465     HIS F   433                                                      
REMARK 465     HIS F   434                                                      
REMARK 465     HIS F   435                                                      
REMARK 465     HIS F   436                                                      
REMARK 465     SER G     1                                                      
REMARK 465     ILE G     2                                                      
REMARK 465     PRO G     3                                                      
REMARK 465     GLY G     4                                                      
REMARK 465     GLN G     5                                                      
REMARK 465     VAL G     6                                                      
REMARK 465     ALA G     7                                                      
REMARK 465     ASP G     8                                                      
REMARK 465     GLN G     9                                                      
REMARK 465     ALA G    10                                                      
REMARK 465     SER G    36                                                      
REMARK 465     GLN G    37                                                      
REMARK 465     GLY G    38                                                      
REMARK 465     GLN G    39                                                      
REMARK 465     LYS G    40                                                      
REMARK 465     ILE G    41                                                      
REMARK 465     PRO G    42                                                      
REMARK 465     GLU G    43                                                      
REMARK 465     GLU G    44                                                      
REMARK 465     PHE G    45                                                      
REMARK 465     LYS G    46                                                      
REMARK 465     LYS G    47                                                      
REMARK 465     PHE G    48                                                      
REMARK 465     PHE G    49                                                      
REMARK 465     GLY G    50                                                      
REMARK 465     ASP G    51                                                      
REMARK 465     ASP G    52                                                      
REMARK 465     LEU G    53                                                      
REMARK 465     PRO G    54                                                      
REMARK 465     ASP G    55                                                      
REMARK 465     GLN G    56                                                      
REMARK 465     PRO G    57                                                      
REMARK 465     ALA G    58                                                      
REMARK 465     THR G   330                                                      
REMARK 465     LEU G   331                                                      
REMARK 465     ASP G   332                                                      
REMARK 465     THR G   333                                                      
REMARK 465     SER G   334                                                      
REMARK 465     THR G   335                                                      
REMARK 465     SER G   336                                                      
REMARK 465     SER G   337                                                      
REMARK 465     SER G   338                                                      
REMARK 465     ALA G   339                                                      
REMARK 465     ALA G   341                                                      
REMARK 465     ARG G   428                                                      
REMARK 465     LEU G   429                                                      
REMARK 465     GLU G   430                                                      
REMARK 465     HIS G   431                                                      
REMARK 465     HIS G   432                                                      
REMARK 465     HIS G   433                                                      
REMARK 465     HIS G   434                                                      
REMARK 465     HIS G   435                                                      
REMARK 465     HIS G   436                                                      
REMARK 465     SER H     1                                                      
REMARK 465     ILE H     2                                                      
REMARK 465     PRO H     3                                                      
REMARK 465     GLY H     4                                                      
REMARK 465     GLN H     5                                                      
REMARK 465     VAL H     6                                                      
REMARK 465     ALA H     7                                                      
REMARK 465     ASP H     8                                                      
REMARK 465     GLN H     9                                                      
REMARK 465     ALA H    10                                                      
REMARK 465     SER H    36                                                      
REMARK 465     GLN H    37                                                      
REMARK 465     GLY H    38                                                      
REMARK 465     GLN H    39                                                      
REMARK 465     LYS H    40                                                      
REMARK 465     ILE H    41                                                      
REMARK 465     PRO H    42                                                      
REMARK 465     GLU H    43                                                      
REMARK 465     GLU H    44                                                      
REMARK 465     PHE H    45                                                      
REMARK 465     LYS H    46                                                      
REMARK 465     LYS H    47                                                      
REMARK 465     PHE H    48                                                      
REMARK 465     PHE H    49                                                      
REMARK 465     GLY H    50                                                      
REMARK 465     ASP H    51                                                      
REMARK 465     ASP H    52                                                      
REMARK 465     LEU H    53                                                      
REMARK 465     PRO H    54                                                      
REMARK 465     ASP H    55                                                      
REMARK 465     GLN H    56                                                      
REMARK 465     PRO H    57                                                      
REMARK 465     ALA H    58                                                      
REMARK 465     THR H   330                                                      
REMARK 465     LEU H   331                                                      
REMARK 465     ASP H   332                                                      
REMARK 465     THR H   333                                                      
REMARK 465     SER H   334                                                      
REMARK 465     THR H   335                                                      
REMARK 465     SER H   336                                                      
REMARK 465     SER H   337                                                      
REMARK 465     SER H   338                                                      
REMARK 465     ALA H   339                                                      
REMARK 465     ARG H   428                                                      
REMARK 465     LEU H   429                                                      
REMARK 465     GLU H   430                                                      
REMARK 465     HIS H   431                                                      
REMARK 465     HIS H   432                                                      
REMARK 465     HIS H   433                                                      
REMARK 465     HIS H   434                                                      
REMARK 465     HIS H   435                                                      
REMARK 465     HIS H   436                                                      
REMARK 465     SER I     1                                                      
REMARK 465     ILE I     2                                                      
REMARK 465     PRO I     3                                                      
REMARK 465     GLY I     4                                                      
REMARK 465     GLN I     5                                                      
REMARK 465     VAL I     6                                                      
REMARK 465     ALA I     7                                                      
REMARK 465     ASP I     8                                                      
REMARK 465     GLN I     9                                                      
REMARK 465     ALA I    10                                                      
REMARK 465     SER I    36                                                      
REMARK 465     GLN I    37                                                      
REMARK 465     GLY I    38                                                      
REMARK 465     GLN I    39                                                      
REMARK 465     LYS I    40                                                      
REMARK 465     ILE I    41                                                      
REMARK 465     PRO I    42                                                      
REMARK 465     GLU I    43                                                      
REMARK 465     GLU I    44                                                      
REMARK 465     PHE I    45                                                      
REMARK 465     LYS I    46                                                      
REMARK 465     LYS I    47                                                      
REMARK 465     PHE I    48                                                      
REMARK 465     PHE I    49                                                      
REMARK 465     GLY I    50                                                      
REMARK 465     ASP I    51                                                      
REMARK 465     ASP I    52                                                      
REMARK 465     LEU I    53                                                      
REMARK 465     PRO I    54                                                      
REMARK 465     ASP I    55                                                      
REMARK 465     GLN I    56                                                      
REMARK 465     PRO I    57                                                      
REMARK 465     ALA I    58                                                      
REMARK 465     THR I   330                                                      
REMARK 465     LEU I   331                                                      
REMARK 465     ASP I   332                                                      
REMARK 465     THR I   333                                                      
REMARK 465     SER I   334                                                      
REMARK 465     THR I   335                                                      
REMARK 465     SER I   336                                                      
REMARK 465     SER I   337                                                      
REMARK 465     SER I   338                                                      
REMARK 465     ALA I   339                                                      
REMARK 465     ARG I   428                                                      
REMARK 465     LEU I   429                                                      
REMARK 465     GLU I   430                                                      
REMARK 465     HIS I   431                                                      
REMARK 465     HIS I   432                                                      
REMARK 465     HIS I   433                                                      
REMARK 465     HIS I   434                                                      
REMARK 465     HIS I   435                                                      
REMARK 465     HIS I   436                                                      
REMARK 465     SER J     1                                                      
REMARK 465     ILE J     2                                                      
REMARK 465     PRO J     3                                                      
REMARK 465     GLY J     4                                                      
REMARK 465     GLN J     5                                                      
REMARK 465     VAL J     6                                                      
REMARK 465     ALA J     7                                                      
REMARK 465     ASP J     8                                                      
REMARK 465     GLN J     9                                                      
REMARK 465     ALA J    10                                                      
REMARK 465     SER J    36                                                      
REMARK 465     GLN J    37                                                      
REMARK 465     GLY J    38                                                      
REMARK 465     GLN J    39                                                      
REMARK 465     LYS J    40                                                      
REMARK 465     ILE J    41                                                      
REMARK 465     PRO J    42                                                      
REMARK 465     GLU J    43                                                      
REMARK 465     GLU J    44                                                      
REMARK 465     PHE J    45                                                      
REMARK 465     LYS J    46                                                      
REMARK 465     LYS J    47                                                      
REMARK 465     PHE J    48                                                      
REMARK 465     PHE J    49                                                      
REMARK 465     GLY J    50                                                      
REMARK 465     ASP J    51                                                      
REMARK 465     ASP J    52                                                      
REMARK 465     LEU J    53                                                      
REMARK 465     PRO J    54                                                      
REMARK 465     ASP J    55                                                      
REMARK 465     GLN J    56                                                      
REMARK 465     PRO J    57                                                      
REMARK 465     ALA J    58                                                      
REMARK 465     THR J   330                                                      
REMARK 465     LEU J   331                                                      
REMARK 465     ASP J   332                                                      
REMARK 465     THR J   333                                                      
REMARK 465     SER J   334                                                      
REMARK 465     THR J   335                                                      
REMARK 465     SER J   336                                                      
REMARK 465     SER J   337                                                      
REMARK 465     SER J   338                                                      
REMARK 465     ALA J   339                                                      
REMARK 465     ARG J   428                                                      
REMARK 465     LEU J   429                                                      
REMARK 465     GLU J   430                                                      
REMARK 465     HIS J   431                                                      
REMARK 465     HIS J   432                                                      
REMARK 465     HIS J   433                                                      
REMARK 465     HIS J   434                                                      
REMARK 465     HIS J   435                                                      
REMARK 465     HIS J   436                                                      
REMARK 465     SER K     1                                                      
REMARK 465     ILE K     2                                                      
REMARK 465     PRO K     3                                                      
REMARK 465     GLY K     4                                                      
REMARK 465     GLN K     5                                                      
REMARK 465     VAL K     6                                                      
REMARK 465     ALA K     7                                                      
REMARK 465     ASP K     8                                                      
REMARK 465     GLN K     9                                                      
REMARK 465     ALA K    10                                                      
REMARK 465     SER K    36                                                      
REMARK 465     GLN K    37                                                      
REMARK 465     GLY K    38                                                      
REMARK 465     GLN K    39                                                      
REMARK 465     LYS K    40                                                      
REMARK 465     ILE K    41                                                      
REMARK 465     PRO K    42                                                      
REMARK 465     GLU K    43                                                      
REMARK 465     GLU K    44                                                      
REMARK 465     PHE K    45                                                      
REMARK 465     LYS K    46                                                      
REMARK 465     LYS K    47                                                      
REMARK 465     PHE K    48                                                      
REMARK 465     PHE K    49                                                      
REMARK 465     GLY K    50                                                      
REMARK 465     ASP K    51                                                      
REMARK 465     ASP K    52                                                      
REMARK 465     LEU K    53                                                      
REMARK 465     PRO K    54                                                      
REMARK 465     ASP K    55                                                      
REMARK 465     GLN K    56                                                      
REMARK 465     PRO K    57                                                      
REMARK 465     ALA K    58                                                      
REMARK 465     THR K   330                                                      
REMARK 465     LEU K   331                                                      
REMARK 465     ASP K   332                                                      
REMARK 465     THR K   333                                                      
REMARK 465     SER K   334                                                      
REMARK 465     THR K   335                                                      
REMARK 465     SER K   336                                                      
REMARK 465     SER K   337                                                      
REMARK 465     SER K   338                                                      
REMARK 465     ALA K   339                                                      
REMARK 465     ARG K   428                                                      
REMARK 465     LEU K   429                                                      
REMARK 465     GLU K   430                                                      
REMARK 465     HIS K   431                                                      
REMARK 465     HIS K   432                                                      
REMARK 465     HIS K   433                                                      
REMARK 465     HIS K   434                                                      
REMARK 465     HIS K   435                                                      
REMARK 465     HIS K   436                                                      
REMARK 465     SER L     1                                                      
REMARK 465     ILE L     2                                                      
REMARK 465     PRO L     3                                                      
REMARK 465     GLY L     4                                                      
REMARK 465     GLN L     5                                                      
REMARK 465     VAL L     6                                                      
REMARK 465     ALA L     7                                                      
REMARK 465     ASP L     8                                                      
REMARK 465     GLN L     9                                                      
REMARK 465     ALA L    10                                                      
REMARK 465     SER L    36                                                      
REMARK 465     GLN L    37                                                      
REMARK 465     GLY L    38                                                      
REMARK 465     GLN L    39                                                      
REMARK 465     LYS L    40                                                      
REMARK 465     ILE L    41                                                      
REMARK 465     PRO L    42                                                      
REMARK 465     GLU L    43                                                      
REMARK 465     GLU L    44                                                      
REMARK 465     PHE L    45                                                      
REMARK 465     LYS L    46                                                      
REMARK 465     LYS L    47                                                      
REMARK 465     PHE L    48                                                      
REMARK 465     PHE L    49                                                      
REMARK 465     GLY L    50                                                      
REMARK 465     ASP L    51                                                      
REMARK 465     ASP L    52                                                      
REMARK 465     LEU L    53                                                      
REMARK 465     PRO L    54                                                      
REMARK 465     ASP L    55                                                      
REMARK 465     GLN L    56                                                      
REMARK 465     PRO L    57                                                      
REMARK 465     ALA L    58                                                      
REMARK 465     THR L   330                                                      
REMARK 465     LEU L   331                                                      
REMARK 465     ASP L   332                                                      
REMARK 465     THR L   333                                                      
REMARK 465     SER L   334                                                      
REMARK 465     THR L   335                                                      
REMARK 465     SER L   336                                                      
REMARK 465     SER L   337                                                      
REMARK 465     SER L   338                                                      
REMARK 465     ALA L   339                                                      
REMARK 465     ARG L   428                                                      
REMARK 465     LEU L   429                                                      
REMARK 465     GLU L   430                                                      
REMARK 465     HIS L   431                                                      
REMARK 465     HIS L   432                                                      
REMARK 465     HIS L   433                                                      
REMARK 465     HIS L   434                                                      
REMARK 465     HIS L   435                                                      
REMARK 465     HIS L   436                                                      
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1KXX   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 2YBI   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (6. 62 MGY)         
REMARK 900 RELATED ID: 1T6V   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE SHARK NEW ANTIGENRECEPTOR    
REMARK 900 (NAR) VARIABLE DOMAIN IN COMPLEX WITH LYSOZYME                       
REMARK 900 RELATED ID: 1VDS   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM OF HEN EGGWHITE         
REMARK 900 LYSOZYME AT 1.6 ANGSTROMS RESOLUTION IN SPACE                        
REMARK 900 RELATED ID: 1KIR   RELATED DB: PDB                                   
REMARK 900 FV MUTANT Y(A 50)S (VL DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3     
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME                                
REMARK 900 RELATED ID: 1YIL   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED WITH CU2- XYLYLBICYCLAM   
REMARK 900 RELATED ID: 1HEO   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL (I55V)                   
REMARK 900 RELATED ID: 1IOR   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
REMARK 900 RELATED ID: 1LJG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 5%      
REMARK 900 GLYCEROL                                                             
REMARK 900 RELATED ID: 1JIS   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN AT PH 4 .6            
REMARK 900 RELATED ID: 2W1M   RELATED DB: PDB                                   
REMARK 900 THE INTERDEPENDENCE OF WAVELENGTH, REDUNDANCY AND DOSE IN SULFUR     
REMARK 900 SAD EXPERIMENTS: 2.070 A WAVELENGTH WITH 2THETA 30 DEGREES DATA      
REMARK 900 RELATED ID: 1UIC   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1YKZ   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 1XGQ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE FOR ANTIBODY HYHEL-63 Y33V MUTANT COMPLEXED WITHHEN EGG    
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 2WAR   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME E35Q CHITOPENTAOSE COMPLEX                    
REMARK 900 RELATED ID: 1DPW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME IN COMPLEX WITH MPD              
REMARK 900 RELATED ID: 8LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME IODINE-INACTIVATED                                          
REMARK 900 RELATED ID: 1LJ3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4 .6            
REMARK 900 RELATED ID: 2LYO   RELATED DB: PDB                                   
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 90% ACETONITRILE-WATER      
REMARK 900 RELATED ID: 1G7H   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE  
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1 .3(VLW92A)                    
REMARK 900 RELATED ID: 1LKS   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME NITRATE                                       
REMARK 900 RELATED ID: 5LYT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (100 KELVIN)                                                
REMARK 900 RELATED ID: 1SFB   RELATED DB: PDB                                   
REMARK 900 BINDING OF PENTA-N-ACETYLCHITOPENTAOSE TO HEW LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 1IR7   RELATED DB: PDB                                   
REMARK 900 IM MUTANT OF LYSOZYME                                                
REMARK 900 RELATED ID: 1XEI   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION   
REMARK 900 RELATED ID: 1HEL   RELATED DB: PDB                                   
REMARK 900 HEN EGG-WHITE LYSOZYME WILD TYPE                                     
REMARK 900 RELATED ID: 1LJF   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 10%     
REMARK 900 SUCROSE                                                              
REMARK 900 RELATED ID: 1F10   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5 AT 88%    
REMARK 900 RELATIVE HUMIDITY                                                    
REMARK 900 RELATED ID: 1LJK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 15%     
REMARK 900 TREHALOSE                                                            
REMARK 900 RELATED ID: 6LYT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (298 KELVIN)                                                
REMARK 900 RELATED ID: 1ZMY   RELATED DB: PDB                                   
REMARK 900 CABBCII-10 VHH FRAMEWORK WITH CDR LOOPS OF CABLYS3 GRAFTEDON IT AND  
REMARK 900 IN COMPLEX WITH HEN EGG WHITE LYSOZYME                               
REMARK 900 RELATED ID: 2XTH   RELATED DB: PDB                                   
REMARK 900 K2PTBR6 BINDING TO LYSOZYME                                          
REMARK 900 RELATED ID: 2D91   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HYPER-VIL-LYSOZYME                                      
REMARK 900 RELATED ID: 1LZE   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y) CO-CRYSTALLIZED   
REMARK 900 WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4. 7)                              
REMARK 900 RELATED ID: 1AKI   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGG- WHITE LYSOZYME    
REMARK 900 AT 1.5 ANGSTROMS RESOLUTION                                          
REMARK 900 RELATED ID: 1YIK   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HEN EGG WHITE LYSOZYME SOAKED WITH CU- CYCLAM           
REMARK 900 RELATED ID: 2D6B   RELATED DB: PDB                                   
REMARK 900 NOVEL BROMATE SPECIES TRAPPED WITHIN A PROTEIN CRYSTAL               
REMARK 900 RELATED ID: 1LPI   RELATED DB: PDB                                   
REMARK 900 HEW LYSOZYME: TRP...NA CATION-PI INTERACTION                         
REMARK 900 RELATED ID: 1NDG   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTIBODY HYHEL- 8COMPLEXED      
REMARK 900 WITH ITS ANTIGEN LYSOZYME                                            
REMARK 900 RELATED ID: 1FLW   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE    
REMARK 900 RELATED ID: 4LYT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (298 KELVIN)                                                
REMARK 900 RELATED ID: 1JIT   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE30%        
REMARK 900 TREHALOSE                                                            
REMARK 900 RELATED ID: 1LZN   RELATED DB: PDB                                   
REMARK 900 NEUTRON STRUCTURE OF HEN EGG-WHITE LYSOZYME                          
REMARK 900 RELATED ID: 1WTN   RELATED DB: PDB                                   
REMARK 900 THE STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC CRYSTAL GROWTHUNDER A     
REMARK 900 HIGH MAGNETIC FIELD                                                  
REMARK 900 RELATED ID: 1JA2   RELATED DB: PDB                                   
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 2FBB   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF HEXAGONAL LYSOZYME                     
REMARK 900 RELATED ID: 2LYM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (1 ATMOSPHERE, 1.4 M NACL)                                  
REMARK 900 RELATED ID: 1LZ9   RELATED DB: PDB                                   
REMARK 900 ANOMALOUS SIGNAL OF SOLVENT BROMINES USED FOR PHASING OF LYSOZYME    
REMARK 900 RELATED ID: 1LSE   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (295 K)                                                     
REMARK 900 RELATED ID: 1LSM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY LEU, SER 91 REPLACED BY THR, 
REMARK 900 AND ASP 101 REPLACED BY SER (I55L ,S91T,D101S)                       
REMARK 900 RELATED ID: 3LYM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (1000 ATMOSPHERES, 1.4 M NACL)                              
REMARK 900 RELATED ID: 7LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME TRICLINIC CRYSTAL FORM                                      
REMARK 900 RELATED ID: 1T3P   RELATED DB: PDB                                   
REMARK 900 HALF-SANDWICH ARENE RUTHENIUM(II)-ENZYME COMPLEX                     
REMARK 900 RELATED ID: 1B0D   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME      
REMARK 900 CRYSTALS                                                             
REMARK 900 RELATED ID: 2BLY   RELATED DB: PDB                                   
REMARK 900 HEWL AFTER A HIGH DOSE X-RAY "BURN"                                  
REMARK 900 RELATED ID: 1HER   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER (T40S)                   
REMARK 900 RELATED ID: 1IOQ   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
REMARK 900 RELATED ID: 1NBY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH HEL MUTANT K96A         
REMARK 900 RELATED ID: 1QIO   RELATED DB: PDB                                   
REMARK 900 SPECIFIC CHEMICAL AND STRUCTURAL DAMAGE CAUSED BY INTENSE            
REMARK 900 SYNCHROTRON RADIATION TO HEN EGG WHITE LYSOZYME                      
REMARK 900 RELATED ID: 1PS5   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF THE MONOCLINIC C2 FORM OF HEN EGG- WHITELYSOZYME AT     
REMARK 900 2.0 ANGSTROMS RESOLUTION                                             
REMARK 900 RELATED ID: 1XGP   RELATED DB: PDB                                   
REMARK 900 STRUCTURE FOR ANTIBODY HYHEL-63 Y33A MUTANT COMPLEXED WITHHEN EGG    
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1GWD   RELATED DB: PDB                                   
REMARK 900 TRI-IODIDE DERIVATIVE OF HEN EGG-WHITE LYSOZYME                      
REMARK 900 RELATED ID: 1V7T   RELATED DB: PDB                                   
REMARK 900 TRICLINIC LYSOZYME WITH LOW SOLVENT CONTENT OBTAINED BYPHASE         
REMARK 900 TRANSITION                                                           
REMARK 900 RELATED ID: 1H6M   RELATED DB: PDB                                   
REMARK 900 COVALENT GLYCOSYL-ENZYME INTERMEDIATE OF HEN EGG WHITE LYSOZYME      
REMARK 900 RELATED ID: 2A7D   RELATED DB: PDB                                   
REMARK 900 ON THE ROUTINE USE OF SOFT X-RAYS IN MACROMOLECULARCRYSTALLOGRAPHY,  
REMARK 900 PART III- THE OPTIMAL DATA COLLECTIONWAVELENGTH                      
REMARK 900 RELATED ID: 1DQJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE ANTI-LYSOZYME ANTIBODY HYHEL- 63 COMPLEXED  
REMARK 900 WITH HEN EGG WHITE LYSOZYME                                          
REMARK 900 RELATED ID: 1Z55   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 2C8P   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (60SEC) AND UV LASER EXCITED FLUORESCENCE                   
REMARK 900 RELATED ID: 1LSB   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (180 K)                                                     
REMARK 900 RELATED ID: 1FLQ   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE    
REMARK 900 RELATED ID: 1JJ1   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 4.6IN         
REMARK 900 PRESENCE OF 5% SORBITOL                                              
REMARK 900 RELATED ID: 2YBL   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (17. 9 MGY)         
REMARK 900 RELATED ID: 1YQV   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE ANTIBODY FAB HYHEL5 COMPLEXWITH         
REMARK 900 LYSOZYME AT 1.7A RESOLUTION                                          
REMARK 900 RELATED ID: 1HSX   RELATED DB: PDB                                   
REMARK 900 LYSOZYME GROWN AT BASIC PH AND ITS LOW HUMIDITY VARIANT              
REMARK 900 RELATED ID: 2CDS   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1UIB   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1HF4   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME      
REMARK 900 CRYSTALS                                                             
REMARK 900 RELATED ID: 1IR9   RELATED DB: PDB                                   
REMARK 900 IM MUTANT OF LYSOZYME                                                
REMARK 900 RELATED ID: 1RJC   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE DOMAIN ANTIBODY CAB-LYS2 IN  
REMARK 900 COMPLEX WITH HEN EGG WHITE LYSOZYME                                  
REMARK 900 RELATED ID: 1LJH   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 5%      
REMARK 900 GLYCEROL                                                             
REMARK 900 RELATED ID: 1IC4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD32A)-HEN LYSOZYMECOMPLEX   
REMARK 900 RELATED ID: 1XEJ   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION   
REMARK 900 RELATED ID: 1JA7   RELATED DB: PDB                                   
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 1MEL   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF A CAMEL SINGLE-DOMAIN VH ANTIBODY FRAGMENT IN   
REMARK 900 COMPLEX WITH LYSOZYME                                                
REMARK 900 RELATED ID: 1RI8   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CAMELID SINGLE DOMAIN ANTIBODY1D2L19 IN     
REMARK 900 COMPLEX WITH HEN EGG WHITE LYSOZYME                                  
REMARK 900 RELATED ID: 1C10   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF XENON (8 BAR)    
REMARK 900 RELATED ID: 1LYO   RELATED DB: PDB                                   
REMARK 900 CROSS-LINKED LYSOZYME CRYSTAL IN NEAT WATER                          
REMARK 900 RELATED ID: 2XJW   RELATED DB: PDB                                   
REMARK 900 LYSOZYME-CO RELEASING MOLECULE ADDUCT                                
REMARK 900 RELATED ID: 1N4F   RELATED DB: PDB                                   
REMARK 900 PARA-ARSANILATE DERIVATIVE OF HEN EGG-WHITE LYSOZYME                 
REMARK 900 RELATED ID: 1G7M   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE  
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1 .3 (VLW92V)                   
REMARK 900 RELATED ID: 2W1Y   RELATED DB: PDB                                   
REMARK 900 THE INTERDEPENDENCE OF WAVELENGTH, REDUNDANCY AND DOSE IN SULFUR     
REMARK 900 SAD EXPERIMENTS: 1.540 A WAVELENGTH 180 IMAGES DATA                  
REMARK 900 RELATED ID: 1SF7   RELATED DB: PDB                                   
REMARK 900 BINDING OF TETRA-N-ACETYLCHITOTETRAOSE TO HEW LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 1LSF   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (95 K)                                                      
REMARK 900 RELATED ID: 1FN5   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE    
REMARK 900 RELATED ID: 2D4J   RELATED DB: PDB                                   
REMARK 900 TRANSFORMED MONOCLINIC CRYSTAL OF HEN EGG-WHITE LYSOZYMEFROM A       
REMARK 900 HEAVY WATER SOLUTION                                                 
REMARK 900 RELATED ID: 1C08   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV-HEN LYSOZYME COMPLEX                
REMARK 900 RELATED ID: 3LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1BVK   RELATED DB: PDB                                   
REMARK 900 HUMANIZED ANTI-LYSOZYME FV COMPLEXED WITH LYSOZYME                   
REMARK 900 RELATED ID: 1UIF   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1VAU   RELATED DB: PDB                                   
REMARK 900 XENON DERIVATIVE OF HEN EGG-WHITE LYSOZYME                           
REMARK 900 RELATED ID: 1LMA   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (88 PERCENT HUMIDITY)                                       
REMARK 900 RELATED ID: 1HC0   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF LYSOZYME WITH PERIODATE                                 
REMARK 900 RELATED ID: 4LZT   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K       
REMARK 900 RELATED ID: 1A2Y   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME, D18A MUTANT, IN COMPLEX WITH MOUSE           
REMARK 900 MONOCLONAL ANTIBODY D1.3                                             
REMARK 900 RELATED ID: 1P2C   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF AN ANTI-LYSOZYME ANTIBODY              
REMARK 900 RELATED ID: 1IC5   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD99A)-HEN LYSOZYMECOMPLEX   
REMARK 900 RELATED ID: 1GXV   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE              
REMARK 900 RELATED ID: 1UA6   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT SFSF COMPLEXED WITHHEN EGG   
REMARK 900 WHITE LYSOZYME COMPLEX                                               
REMARK 900 RELATED ID: 1AT5   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME WITH A SUCCINIMIDE RESIDUE                    
REMARK 900 RELATED ID: 1LJ4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4 .6            
REMARK 900 RELATED ID: 1VFB   RELATED DB: PDB                                   
REMARK 900 FV FRAGMENT OF MOUSE MONOCLONAL ANTIBODY D1.3 COMPLEXED WITH HEN     
REMARK 900 EGG LYSOZYME                                                         
REMARK 900 RELATED ID: 1VAT   RELATED DB: PDB                                   
REMARK 900 IODINE DERIVATIVE OF HEN EGG-WHITE LYSOZYME                          
REMARK 900 RELATED ID: 1JA4   RELATED DB: PDB                                   
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 4LYM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)                     
REMARK 900 RELATED ID: 1FLU   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE    
REMARK 900 RELATED ID: 2HFM   RELATED DB: PDB                                   
REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX ( THEORETICAL       
REMARK 900 MODEL)                                                               
REMARK 900 RELATED ID: 1BWH   RELATED DB: PDB                                   
REMARK 900 THE 1.8 A STRUCTURE OF GROUND CONTROL GROWN TETRAGONAL HEN EGG       
REMARK 900 WHITE LYSOZYME                                                       
REMARK 900 RELATED ID: 1IO5   RELATED DB: PDB                                   
REMARK 900 HYDROGEN AND HYDRATION OF HEN EGG-WHITE LYSOZYME DETERMINEDBY        
REMARK 900 NEUTRON DIFFRACTION                                                  
REMARK 900 RELATED ID: 1LZB   RELATED DB: PDB                                   
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4.7)      
REMARK 900 RELATED ID: 2BPU   RELATED DB: PDB                                   
REMARK 900 THE KEDGE HOLMIUM DERIVATIVE OF HEN EGG-WHITE LYSOZYME AT HIGH       
REMARK 900 RESOLUTION FROM SINGLE WAVELENGTH ANOMALOUS DIFFRACTION              
REMARK 900 RELATED ID: 1LSC   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (250 K)                                                     
REMARK 900 RELATED ID: 1W6Z   RELATED DB: PDB                                   
REMARK 900 HIGH ENERGY TATRAGONAL LYSOZYME X-RAY STRUCTURE                      
REMARK 900 RELATED ID: 2YBN   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (28. 6 MGY)         
REMARK 900 RELATED ID: 3LYO   RELATED DB: PDB                                   
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN 95% ACETONITRILE-WATER      
REMARK 900 RELATED ID: 4LYO   RELATED DB: PDB                                   
REMARK 900 CROSS-LINKED CHICKEN LYSOZYME CRYSTAL IN NEAT ACETONITRILE, THEN     
REMARK 900 BACK-SOAKED IN WATER                                                 
REMARK 900 RELATED ID: 1KIP   RELATED DB: PDB                                   
REMARK 900 FV MUTANT Y(B 32)A (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3     
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME                                
REMARK 900 RELATED ID: 1IC7   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD32A99A)- HENLYSOZYME       
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1LZT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM                                    
REMARK 900 RELATED ID: 2XBR   RELATED DB: PDB                                   
REMARK 900 RAMAN CRYSTALLOGRAPHY OF HEN WHITE EGG LYSOZYME - LOW X-RAY DOSE     
REMARK 900 (0.2 MGY)                                                            
REMARK 900 RELATED ID: 1LYS   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 132L   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1BWJ   RELATED DB: PDB                                   
REMARK 900 THE 1.8 A STRUCTURE OF MICROGRAVITY GROWN TETRAGONAL HEN EGG WHITE   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1E8L   RELATED DB: PDB                                   
REMARK 900 NMR SOLUTION STRUCTURE OF HEN LYSOZYME                               
REMARK 900 RELATED ID: 1SFG   RELATED DB: PDB                                   
REMARK 900 BINDING OF HEXA-N-ACETYLCHITOHEXAOSE: A POWDER DIFFRACTIONSTUDY      
REMARK 900 RELATED ID: 1KXW   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 2C8O   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (1SEC) AND UV LASR EXCITED FLUORESCENCE                     
REMARK 900 RELATED ID: 2X0A   RELATED DB: PDB                                   
REMARK 900 MPD-LYSOZYME STRUCTURE AT 55.5 KEV USING A TRIXXEL CSI-ASI BASED     
REMARK 900 DIGITAL IMAGER AND THE NEW ESRF U22 UNDULATOR SOURCE AT ID15         
REMARK 900 RELATED ID: 1G7L   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE  
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1 .3 (VLW92S)                   
REMARK 900 RELATED ID: 1SF4   RELATED DB: PDB                                   
REMARK 900 BINDING OF N,N'-DIACETYLCHITOBIOSE TO HEW LYSOZYME: APOWDER          
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 1YL1   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 1H87   RELATED DB: PDB                                   
REMARK 900 GADOLINIUM DERIVATIVE OF TETRAGONAL HEN EGG-WHITE LYSOZYME AT 1.7 A  
REMARK 900 RESOLUTION                                                           
REMARK 900 RELATED ID: 3LYT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (100 KELVIN)                                                
REMARK 900 RELATED ID: 1DPX   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME                                  
REMARK 900 RELATED ID: 1IOT   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
REMARK 900 RELATED ID: 1V7S   RELATED DB: PDB                                   
REMARK 900 TRICLINIC HEN LYSOZYME CRYSTALLIZED AT 313K FROM A D2OSOLUTION       
REMARK 900 RELATED ID: 1JA6   RELATED DB: PDB                                   
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 1IR8   RELATED DB: PDB                                   
REMARK 900 IM MUTANT OF LYSOZYME                                                
REMARK 900 RELATED ID: 1UIE   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1LJI   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCE10%        
REMARK 900 SORBITOL                                                             
REMARK 900 RELATED ID: 1BWI   RELATED DB: PDB                                   
REMARK 900 THE 1.8 A STRUCTURE OF MICROBATCH OIL DROP GROWN TETRAGONAL HEN EGG  
REMARK 900 WHITE LYSOZYME                                                       
REMARK 900 RELATED ID: 2IFF   RELATED DB: PDB                                   
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-5) COMPLEXED WITH LYSOZYME MUTANT WITH ARG  
REMARK 900 68 REPLACED BY LYS (R68K)                                            
REMARK 900 RELATED ID: 1JJ0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCEOF 30%     
REMARK 900 SUCROSE                                                              
REMARK 900 RELATED ID: 1RFP   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1JIY   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF TETRAGONAL LYSOZYME GROWN IN PRESENCE20%        
REMARK 900 SORBITOL                                                             
REMARK 900 RELATED ID: 4A9G   RELATED DB: PDB                                   
REMARK 900 SYMMETRIZED CRYO-EM RECONSTRUCTION OF E. COLI DEGQ 24 -MER IN        
REMARK 900 COMPLEX WITH BETA-CASEIN                                             
REMARK 900 RELATED ID: 1IEE   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME AT 0. 94 AFROM        
REMARK 900 CRYSTALS GROWN BY THE COUNTER-DIFFUSION METHOD                       
REMARK 900 RELATED ID: 1XEK   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURES OF LYSOZYME AT VERY LOW LEVELS OF HYDRATION   
REMARK 900 RELATED ID: 1AT6   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME WITH A ISOASPARTATE RESIDUE                   
REMARK 900 RELATED ID: 2YDG   RELATED DB: PDB                                   
REMARK 900 ASCORBATE CO-CRYSTALLIZED HEWL.                                      
REMARK 900 RELATED ID: 1MLC   RELATED DB: PDB                                   
REMARK 900 MONOCLONAL ANTIBODY FAB D44.1 RAISED AGAINST CHICKEN EGG-WHITE       
REMARK 900 LYSOZYME COMPLEXED WITH LYSOZYME                                     
REMARK 900 RELATED ID: 2B5Z   RELATED DB: PDB                                   
REMARK 900 HEN LYSOZYME CHEMICALLY GLYCOSYLATED                                 
REMARK 900 RELATED ID: 193L   RELATED DB: PDB                                   
REMARK 900 THE 1.33 A STRUCTURE OF TETRAGONAL HEN EGG WHITE LYSOZYME            
REMARK 900 RELATED ID: 1LSZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S) COMPLEXED WITH    
REMARK 900 GLCNAC4 (TETRA-N-ACETYL CHITOTETRAOSE)                               
REMARK 900 RELATED ID: 2YBM   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (23. 3 MGY)         
REMARK 900 RELATED ID: 1SQ2   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE ANALYSIS OF THE NURSE SHARK NEW ANTIGENRECEPTOR    
REMARK 900 (NAR) VARIABLE DOMAIN IN COMPLEX WITH LYXOZYME                       
REMARK 900 RELATED ID: 1VDQ   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGGWHITE       
REMARK 900 LYSOZYME AT 1.5 ANGSTROMS RESOLUTION                                 
REMARK 900 RELATED ID: 2YBH   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (2. 31 MGY).        
REMARK 900 RELATED ID: 1LJE   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 10%     
REMARK 900 SUCROSE                                                              
REMARK 900 RELATED ID: 1B2K   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME      
REMARK 900 CRYSTALS                                                             
REMARK 900 RELATED ID: 2YBJ   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (12. 31 MGY).       
REMARK 900 RELATED ID: 9LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (NAM-NAG-NAM SUBSTRATE ONLY)                                
REMARK 900 RELATED ID: 1HEN   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH ILE 55 REPLACED BY VAL AND SER 91 REPLACED BY   
REMARK 900 THR (I55V,S91T)                                                      
REMARK 900 RELATED ID: 1UIA   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1XFP   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE CDR2 GERMLINE REVERSION MUTANT OFCAB-LYS3   
REMARK 900 IN COMPLEX WITH HEN EGG WHITE LYSOZYME                               
REMARK 900 RELATED ID: 1LSD   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (280 K)                                                     
REMARK 900 RELATED ID: 2BLX   RELATED DB: PDB                                   
REMARK 900 HEWL BEFORE A HIGH DOSE X-RAY "BURN"                                 
REMARK 900 RELATED ID: 6LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1NBZ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-63 COMPLEXED WITH HEL MUTANT K96A         
REMARK 900 RELATED ID: 1LSG   RELATED DB: PDB                                   
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME MODIFIED WITH HUMAN FIBRINOGEN GAMMA;  
REMARK 900 CHAIN: NULL; ENGINEERED; THE 14- RESIDUE C-TERMINUS (RESIDUES 398 -  
REMARK 900 411) OF THE HUMAN FIBRINOGEN GAMMA CHAIN FUSED TO THE C-TERMINUS OF  
REMARK 900 CHICKEN EGG WHITE LYSOZYME; MUTATION: N-TERM MET                     
REMARK 900 RELATED ID: 1VED   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE ORTHORHOMBIC FORM OF HEN EGGWHITE       
REMARK 900 LYSOZYME AT 1.9 ANGSTROMS RESOLUTION IN SPACE                        
REMARK 900 RELATED ID: 3HFM   RELATED DB: PDB                                   
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX                    
REMARK 900 RELATED ID: 1LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1UUZ   RELATED DB: PDB                                   
REMARK 900 IVY:A NEW FAMILY OF PROTEIN                                          
REMARK 900 RELATED ID: 2D4I   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT PH4. 5FORM HEAVY   
REMARK 900 WATER SOLUTION                                                       
REMARK 900 RELATED ID: 2XBS   RELATED DB: PDB                                   
REMARK 900 RAMAN CRYSTALLOGRAPHY OF HEN WHITE EGG LYSOZYME - HIGH X-RAY DOSE    
REMARK 900 (16 MGY)                                                             
REMARK 900 RELATED ID: 1FDL   RELATED DB: PDB                                   
REMARK 900 IGG1 FAB FRAGMENT (ANTI-LYSOZYME ANTIBODY D1.3, KAPPA ) - LYSOZYME   
REMARK 900 COMPLEX                                                              
REMARK 900 RELATED ID: 1GXX   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE              
REMARK 900 RELATED ID: 1LZH   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (MONOCLINIC)                                                
REMARK 900 RELATED ID: 1JJ3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4 .6            
REMARK 900 RELATED ID: 1YKY   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 1HEQ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER AND SER 91 REPLACED BY   
REMARK 900 THR (T40S,S91T)                                                      
REMARK 900 RELATED ID: 1KIQ   RELATED DB: PDB                                   
REMARK 900 FV MUTANT Y(B 101)F (VH DOMAIN) OF MOUSE MONOCLONAL ANTIBODY D1.3    
REMARK 900 COMPLEXED WITH HEN EGG WHITE LYSOZYME                                
REMARK 900 RELATED ID: 2LZH   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (ORTHORHOMBIC)                                              
REMARK 900 RELATED ID: 1KXY   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1UIH   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 2W1L   RELATED DB: PDB                                   
REMARK 900 THE INTERDEPENDENCE OF WAVELENGTH, REDUNDANCY AND DOSE IN SULFUR     
REMARK 900 SAD EXPERIMENTS: 0.979 A WAVELENGTH 991 IMAGES DATA                  
REMARK 900 RELATED ID: 1G7J   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE  
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1 .3 (VLW92H)                   
REMARK 900 RELATED ID: 1BHZ   RELATED DB: PDB                                   
REMARK 900 LOW TEMPERATURE MIDDLE RESOLUTION STRUCTURE OF HEN EGG WHITE         
REMARK 900 LYSOZYME FROM MASC DATA                                              
REMARK 900 RELATED ID: 1WTM   RELATED DB: PDB                                   
REMARK 900 X-RAY STRUCTURE OF HEW LYSOZYME ORTHORHOMBIC CRYSTAL FORMEDIN THE    
REMARK 900 EARTH'S MAGNETIC FIELD                                               
REMARK 900 RELATED ID: 1HEP   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH THR 40 REPLACED BY SER, ILE 55 REPLACED BY VAL, 
REMARK 900 AND SER 91 REPLACED BY THR (T40S ,I55V,S91T)                         
REMARK 900 RELATED ID: 1JTT   RELATED DB: PDB                                   
REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY COMPLEXES                  
REMARK 900 RELATED ID: 1LZA   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 3ZVQ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF PROTEOLYZED LYSOZYME                            
REMARK 900 RELATED ID: 1JPO   RELATED DB: PDB                                   
REMARK 900 LOW TEMPERATURE ORTHORHOMBIC LYSOZYME                                
REMARK 900 RELATED ID: 1J1P   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT LS91A COMPLEXEDWITH HEN EGG  
REMARK 900 WHITE LYSOZYME                                                       
REMARK 900 RELATED ID: 1LJJ   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN IN PRESENCEOF 10%     
REMARK 900 TREHALOSE                                                            
REMARK 900 RELATED ID: 1F0W   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF ORTHORHOMBIC LYSOZYME GROWN AT PH 6.5           
REMARK 900 RELATED ID: 2W1X   RELATED DB: PDB                                   
REMARK 900 THE INTERDEPENDENCE OF WAVELENGTH, REDUNDANCY AND DOSE IN SULFUR     
REMARK 900 SAD EXPERIMENTS: 1.284 A WAVELENGTH 360 IMAGES DATA                  
REMARK 900 RELATED ID: 1LZG   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY PHE (W62F) CO-CRYSTALLIZED   
REMARK 900 WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4. 7)                              
REMARK 900 RELATED ID: 1LZC   RELATED DB: PDB                                   
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TETRA-N-ACETYL- CHITOTETRAOSE (PH 4.7) 
REMARK 900 RELATED ID: 1RCM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (PARTIALLY REDUCED, CARBOXYMETHYLATED (6,127-RCM ))         
REMARK 900 RELATED ID: 1UID   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1BGI   RELATED DB: PDB                                   
REMARK 900 ORTHORHOMBIC LYSOZYME CRYSTALLIZED AT HIGH TEMPERATURE ( 310K)       
REMARK 900 RELATED ID: 1LCN   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE COMPLEX               
REMARK 900 RELATED ID: 1LZD   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y)                   
REMARK 900 RELATED ID: 1HEW   RELATED DB: PDB                                   
REMARK 900 LYSOZYME COMPLEXED WITH THE INHIBITOR TRI-N- ACETYLCHITOTRIOSE       
REMARK 900 RELATED ID: 2VB1   RELATED DB: PDB                                   
REMARK 900 HEWL AT 0.65 ANGSTROM RESOLUTION                                     
REMARK 900 RELATED ID: 2AUB   RELATED DB: PDB                                   
REMARK 900 LYSOZYME STRUCTURE DERIVED FROM THIN-FILM-BASED CRYSTALS             
REMARK 900 RELATED ID: 2CGI   RELATED DB: PDB                                   
REMARK 900 SIRAS STRUCTURE OF TETRAGONAL LYSOSYME USING DERIVATIVE DATA         
REMARK 900 COLLECTED AT THE HIGH ENERGY REMOTE HOLMIUM KEDGE                    
REMARK 900 RELATED ID: 1IOS   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
REMARK 900 RELATED ID: 1J1X   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT LS93A COMPLEXEDWITH HEN EGG  
REMARK 900 WHITE LYSOZYME                                                       
REMARK 900 RELATED ID: 1UC0   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF WILD-TYPE HEN-EGG WHITE LYSOZYMESINGLY LABELED  
REMARK 900 WITH 2',3'-EPOXYPROPYL BETA- GLYCOSIDE OF N-ACETYLLACTOSAMINE        
REMARK 900 RELATED ID: 1AZF   RELATED DB: PDB                                   
REMARK 900 CHICKEN EGG WHITE LYSOZYME CRYSTAL GROWN IN BROMIDE SOLUTION         
REMARK 900 RELATED ID: 4LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1GPQ   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF IVY COMPLEXED WITH ITS TARGET, HEWL                     
REMARK 900 RELATED ID: 2A6U   RELATED DB: PDB                                   
REMARK 900 PH EVOLUTION OF TETRAGONAL HEWL AT 4 DEGREES CELCIUS.                
REMARK 900 RELATED ID: 2D4K   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT 313K               
REMARK 900 RELATED ID: 1UIG   RELATED DB: PDB                                   
REMARK 900 ANALYSIS OF THE STABILIZATION OF HEN LYSOZYME WITH THE HELIX DIPOLE  
REMARK 900 AND CHARGED SIDE CHAINS                                              
REMARK 900 RELATED ID: 1BVX   RELATED DB: PDB                                   
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME   
REMARK 900 RELATED ID: 1QTK   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEW LYSOZYME UNDER PRESSURE OF KRYPTON (55 BAR) 
REMARK 900 RELATED ID: 4A7D   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HEWL FLASH-COOLED AT HIGH PRESSURE        
REMARK 900 RELATED ID: 1LKR   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME IODIDE                             
REMARK 900 RELATED ID: 1HSW   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (MUCOPEPTIDE N-ACETYLMURAMYL HYDROLASE)                     
REMARK 900 RELATED ID: 1JTO   RELATED DB: PDB                                   
REMARK 900 DEGENERATE INTERFACES IN ANTIGEN-ANTIBODY COMPLEXES                  
REMARK 900 RELATED ID: 5LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 3LZT   RELATED DB: PDB                                   
REMARK 900 REFINEMENT OF TRICLINIC LYSOZYME AT ATOMIC RESOLUTION                
REMARK 900 RELATED ID: 1NDM   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF FAB FRAGMENT OF ANTIBODY HYHEL- 26COMPLEXED     
REMARK 900 WITH LYSOZYME                                                        
REMARK 900 RELATED ID: 1SF6   RELATED DB: PDB                                   
REMARK 900 BINDING OF N,N',N"-TRIACETYLCHITOTRIOSE TO HEW LYSOZYME: APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
REMARK 900 RELATED ID: 2LYZ   RELATED DB: PDB                                   
REMARK 900 LYSOZYME                                                             
REMARK 900 RELATED ID: 1FLY   RELATED DB: PDB                                   
REMARK 900 HEN EGG WHITE LYSOZYME MUTANT WITH ALANINE SUBSTITUTED FORGLYCINE    
REMARK 900 RELATED ID: 1YL0   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 1J1O   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT LY50F COMPLEXEDWITH HEN EGG  
REMARK 900 WHITE LYSOZYME                                                       
REMARK 900 RELATED ID: 2LZT   RELATED DB: PDB                                   
REMARK 900 LYSOZYME , TRICLINIC CRYSTAL FORM                                    
REMARK 900 RELATED ID: 1LSY   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH ASP 52 REPLACED BY SER (D52S)                   
REMARK 900 RELATED ID: 1UCO   RELATED DB: PDB                                   
REMARK 900 HEN EGG-WHITE LYSOZYME, LOW HUMIDITY FORM                            
REMARK 900 RELATED ID: 5LYM   RELATED DB: PDB                                   
REMARK 900 MOL_ID: 1; MOLECULE: LYSOZYME; CHAIN: A, B; EC: 3.2 .1.17            
REMARK 900 RELATED ID: 1LSA   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (120 K)                                                     
REMARK 900 RELATED ID: 1F3J   RELATED DB: PDB                                   
REMARK 900 HISTOCOMPATIBILITY ANTIGEN I-AG7                                     
REMARK 900 RELATED ID: 1HEM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY THR (S91T)                   
REMARK 900 RELATED ID: 2A7F   RELATED DB: PDB                                   
REMARK 900 ON THE ROUTINE USE OF SOFT X-RAYS IN MACROMOLECULARCRYSTALLOGRAPHY,  
REMARK 900 PART III- THE OPTIMAL DATA COLLECTIONWAVELENGTH                      
REMARK 900 RELATED ID: 194L   RELATED DB: PDB                                   
REMARK 900 THE 1.40 A STRUCTURE OF SPACEHAB-01 HEN EGG WHITE LYSOZYME           
REMARK 900 RELATED ID: 1LZ8   RELATED DB: PDB                                   
REMARK 900 LYSOZYME PHASED ON ANOMALOUS SIGNAL OF SULFURS AND CHLORINES         
REMARK 900 RELATED ID: 1YKX   RELATED DB: PDB                                   
REMARK 900 EFFECT OF ALCOHOLS ON PROTEIN HYDRATION                              
REMARK 900 RELATED ID: 1VDT   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE TETRAGONAL FORM OF HEN EGGWHITE         
REMARK 900 LYSOZYME AT 1.7 ANGSTROMS RESOLUTION UNDER BASICCONDITIONS IN SPACE  
REMARK 900 RELATED ID: 1LSN   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY ALA (S91A)                   
REMARK 900 RELATED ID: 1G7I   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HEN EGG WHITE LYSOZYME (HEL) COMPLEXEDWITH THE  
REMARK 900 MUTANT ANTI-HEL MONOCLONAL ANTIBODY D1 .3 (VLW92F)                   
REMARK 900 RELATED ID: 1VDP   RELATED DB: PDB                                   
REMARK 900 THE CRYSTAL STRUCTURE OF THE MONOCLINIC FORM OF HEN EGGWHITE         
REMARK 900 LYSOZYME AT 1.7 ANGSTROMS RESOLUTION IN SPACE                        
REMARK 900 RELATED ID: EMD-1982   RELATED DB: EMDB                              
REMARK 900 SYMMETRIZED CRYO-EM RECONSTRUCTION OF E. COLI DEGQ 12-MER IN         
REMARK 900 COMPLEX WITH LYSOZYMES                                               
DBREF  4A8B A    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B B    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B C    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B D    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B E    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B F    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B G    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B H    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B I    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B J    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B K    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B L    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8B M    1   129  UNP    P00698   LYSC_CHICK      19    147             
DBREF  4A8B N    1   129  UNP    P00698   LYSC_CHICK      19    147             
DBREF  4A8B O    1   129  UNP    P00698   LYSC_CHICK      19    147             
DBREF  4A8B P    1   129  UNP    P00698   LYSC_CHICK      19    147             
DBREF  4A8B Q    1   129  UNP    P00698   LYSC_CHICK      19    147             
DBREF  4A8B R    1   129  UNP    P00698   LYSC_CHICK      19    147             
SEQADV 4A8B ALA A  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU A  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU A  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS A  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA B  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU B  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU B  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS B  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA C  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU C  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU C  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS C  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA D  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU D  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU D  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS D  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA E  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU E  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU E  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS E  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA F  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU F  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU F  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS F  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA G  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU G  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU G  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS G  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA H  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU H  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU H  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS H  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA I  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU I  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU I  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS I  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA J  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU J  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU J  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS J  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA K  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU K  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU K  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS K  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B ALA L  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8B LEU L  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B GLU L  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8B HIS L  436  UNP  P39099              EXPRESSION TAG                 
SEQRES   1 A  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 A  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 A  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 A  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 A  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 A  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 A  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 A  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 A  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 A  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 A  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 A  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 A  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 A  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 A  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 A  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 A  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 A  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 A  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 A  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 A  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 A  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 A  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 A  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 A  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 A  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 A  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 A  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 A  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 A  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 A  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 A  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 A  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 A  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 B  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 B  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 B  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 B  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 B  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 B  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 B  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 B  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 B  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 B  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 B  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 B  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 B  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 B  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 B  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 B  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 B  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 B  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 B  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 B  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 B  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 B  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 B  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 B  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 B  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 B  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 B  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 B  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 B  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 B  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 B  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 B  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 B  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 C  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 C  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 C  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 C  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 C  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 C  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 C  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 C  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 C  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 C  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 C  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 C  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 C  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 C  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 C  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 C  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 C  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 C  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 C  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 C  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 C  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 C  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 C  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 C  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 C  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 C  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 C  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 C  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 C  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 C  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 C  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 C  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 C  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 C  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 D  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 D  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 D  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 D  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 D  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 D  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 D  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 D  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 D  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 D  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 D  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 D  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 D  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 D  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 D  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 D  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 D  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 D  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 D  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 D  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 D  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 D  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 D  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 D  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 D  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 D  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 D  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 D  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 D  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 D  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 D  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 D  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 D  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 D  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 E  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 E  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 E  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 E  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 E  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 E  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 E  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 E  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 E  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 E  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 E  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 E  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 E  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 E  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 E  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 E  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 E  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 E  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 E  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 E  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 E  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 E  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 E  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 E  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 E  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 E  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 E  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 E  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 E  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 E  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 E  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 E  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 E  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 E  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 F  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 F  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 F  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 F  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 F  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 F  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 F  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 F  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 F  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 F  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 F  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 F  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 F  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 F  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 F  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 F  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 F  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 F  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 F  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 F  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 F  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 F  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 F  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 F  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 F  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 F  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 F  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 F  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 F  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 F  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 F  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 F  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 F  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 F  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 G  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 G  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 G  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 G  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 G  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 G  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 G  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 G  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 G  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 G  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 G  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 G  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 G  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 G  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 G  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 G  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 G  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 G  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 G  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 G  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 G  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 G  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 G  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 G  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 G  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 G  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 G  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 G  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 G  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 G  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 G  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 G  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 G  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 G  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 H  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 H  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 H  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 H  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 H  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 H  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 H  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 H  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 H  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 H  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 H  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 H  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 H  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 H  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 H  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 H  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 H  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 H  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 H  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 H  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 H  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 H  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 H  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 H  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 H  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 H  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 H  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 H  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 H  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 H  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 H  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 H  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 H  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 H  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 I  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 I  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 I  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 I  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 I  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 I  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 I  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 I  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 I  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 I  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 I  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 I  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 I  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 I  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 I  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 I  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 I  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 I  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 I  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 I  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 I  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 I  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 I  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 I  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 I  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 I  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 I  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 I  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 I  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 I  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 I  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 I  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 I  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 I  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 J  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 J  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 J  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 J  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 J  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 J  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 J  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 J  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 J  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 J  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 J  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 J  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 J  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 J  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 J  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 J  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 J  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 J  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 J  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 J  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 J  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 J  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 J  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 J  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 J  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 J  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 J  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 J  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 J  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 J  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 J  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 J  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 J  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 J  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 K  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 K  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 K  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 K  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 K  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 K  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 K  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 K  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 K  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 K  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 K  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 K  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 K  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 K  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 K  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 K  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 K  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 K  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 K  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 K  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 K  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 K  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 K  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 K  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 K  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 K  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 K  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 K  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 K  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 K  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 K  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 K  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 K  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 K  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 L  436  SER ILE PRO GLY GLN VAL ALA ASP GLN ALA PRO LEU PRO          
SEQRES   2 L  436  SER LEU ALA PRO MET LEU GLU LYS VAL LEU PRO ALA VAL          
SEQRES   3 L  436  VAL SER VAL ARG VAL GLU GLY THR ALA SER GLN GLY GLN          
SEQRES   4 L  436  LYS ILE PRO GLU GLU PHE LYS LYS PHE PHE GLY ASP ASP          
SEQRES   5 L  436  LEU PRO ASP GLN PRO ALA GLN PRO PHE GLU GLY LEU GLY          
SEQRES   6 L  436  SER GLY VAL ILE ILE ASN ALA SER LYS GLY TYR VAL LEU          
SEQRES   7 L  436  THR ASN ASN HIS VAL ILE ASN GLN ALA GLN LYS ILE SER          
SEQRES   8 L  436  ILE GLN LEU ASN ASP GLY ARG GLU PHE ASP ALA LYS LEU          
SEQRES   9 L  436  ILE GLY SER ASP ASP GLN SER ASP ILE ALA LEU LEU GLN          
SEQRES  10 L  436  ILE GLN ASN PRO SER LYS LEU THR GLN ILE ALA ILE ALA          
SEQRES  11 L  436  ASP SER ASP LYS LEU ARG VAL GLY ASP PHE ALA VAL ALA          
SEQRES  12 L  436  VAL GLY ASN PRO PHE GLY LEU GLY GLN THR ALA THR SER          
SEQRES  13 L  436  GLY ILE VAL SER ALA LEU GLY ARG SER GLY LEU ASN LEU          
SEQRES  14 L  436  GLU GLY LEU GLU ASN PHE ILE GLN THR ASP ALA SER ILE          
SEQRES  15 L  436  ASN ARG GLY ASN ALA GLY GLY ALA LEU LEU ASN LEU ASN          
SEQRES  16 L  436  GLY GLU LEU ILE GLY ILE ASN THR ALA ILE LEU ALA PRO          
SEQRES  17 L  436  GLY GLY GLY SER VAL GLY ILE GLY PHE ALA ILE PRO SER          
SEQRES  18 L  436  ASN MET ALA ARG THR LEU ALA GLN GLN LEU ILE ASP PHE          
SEQRES  19 L  436  GLY GLU ILE LYS ARG GLY LEU LEU GLY ILE LYS GLY THR          
SEQRES  20 L  436  GLU MET SER ALA ASP ILE ALA LYS ALA PHE ASN LEU ASP          
SEQRES  21 L  436  VAL GLN ARG GLY ALA PHE VAL SER GLU VAL LEU PRO GLY          
SEQRES  22 L  436  SER GLY SER ALA LYS ALA GLY VAL LYS ALA GLY ASP ILE          
SEQRES  23 L  436  ILE THR SER LEU ASN GLY LYS PRO LEU ASN SER PHE ALA          
SEQRES  24 L  436  GLU LEU ARG SER ARG ILE ALA THR THR GLU PRO GLY THR          
SEQRES  25 L  436  LYS VAL LYS LEU GLY LEU LEU ARG ASN GLY LYS PRO LEU          
SEQRES  26 L  436  GLU VAL GLU VAL THR LEU ASP THR SER THR SER SER SER          
SEQRES  27 L  436  ALA SER ALA GLU MET ILE THR PRO ALA LEU GLU GLY ALA          
SEQRES  28 L  436  THR LEU SER ASP GLY GLN LEU LYS ASP GLY GLY LYS GLY          
SEQRES  29 L  436  ILE LYS ILE ASP GLU VAL VAL LYS GLY SER PRO ALA ALA          
SEQRES  30 L  436  GLN ALA GLY LEU GLN LYS ASP ASP VAL ILE ILE GLY VAL          
SEQRES  31 L  436  ASN ARG ASP ARG VAL ASN SER ILE ALA GLU MET ARG LYS          
SEQRES  32 L  436  VAL LEU ALA ALA LYS PRO ALA ILE ILE ALA LEU GLN ILE          
SEQRES  33 L  436  VAL ARG GLY ASN GLU SER ILE TYR LEU LEU MET ARG LEU          
SEQRES  34 L  436  GLU HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 M  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 M  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 M  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 M  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 M  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 M  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 M  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 M  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 M  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 M  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
SEQRES   1 N  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 N  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 N  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 N  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 N  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 N  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 N  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 N  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 N  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 N  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
SEQRES   1 O  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 O  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 O  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 O  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 O  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 O  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 O  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 O  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 O  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 O  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
SEQRES   1 P  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 P  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 P  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 P  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 P  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 P  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 P  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 P  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 P  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 P  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
SEQRES   1 Q  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 Q  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 Q  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 Q  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 Q  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 Q  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 Q  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 Q  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 Q  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 Q  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
SEQRES   1 R  129  LYS VAL PHE GLY ARG CYS GLU LEU ALA ALA ALA MET LYS          
SEQRES   2 R  129  ARG HIS GLY LEU ASP ASN TYR ARG GLY TYR SER LEU GLY          
SEQRES   3 R  129  ASN TRP VAL CYS ALA ALA LYS PHE GLU SER ASN PHE ASN          
SEQRES   4 R  129  THR GLN ALA THR ASN ARG ASN THR ASP GLY SER THR ASP          
SEQRES   5 R  129  TYR GLY ILE LEU GLN ILE ASN SER ARG TRP TRP CYS ASN          
SEQRES   6 R  129  ASP GLY ARG THR PRO GLY SER ARG ASN LEU CYS ASN ILE          
SEQRES   7 R  129  PRO CYS SER ALA LEU LEU SER SER ASP ILE THR ALA SER          
SEQRES   8 R  129  VAL ASN CYS ALA LYS LYS ILE VAL SER ASP GLY ASN GLY          
SEQRES   9 R  129  MET ASN ALA TRP VAL ALA TRP ARG ASN ARG CYS LYS GLY          
SEQRES  10 R  129  THR ASP VAL GLN ALA TRP ILE ARG GLY CYS ARG LEU              
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  PRO A  11     -37.492  48.063  42.486  1.00 79.37           C  
ATOM      2  CA  LEU A  12     -35.240  45.667  44.351  1.00 79.97           C  
ATOM      3  CA  PRO A  13     -36.828  43.295  46.735  1.00151.72           C  
ATOM      4  CA  SER A  14     -33.988  43.195  47.259  1.00120.07           C  
ATOM      5  CA  LEU A  15     -32.912  39.589  46.976  1.00111.61           C  
ATOM      6  CA  ALA A  16     -29.940  40.047  49.290  1.00 40.85           C  
ATOM      7  CA  PRO A  17     -31.854  40.526  52.452  1.00 69.87           C  
ATOM      8  CA  MET A  18     -33.757  37.318  51.931  1.00 34.27           C  
ATOM      9  CA  LEU A  19     -30.585  35.533  50.931  1.00 44.31           C  
ATOM     10  CA  GLU A  20     -28.604  36.580  53.939  1.00 42.27           C  
ATOM     11  CA  LYS A  21     -30.741  34.623  56.311  1.00109.59           C  
ATOM     12  CA  VAL A  22     -31.380  31.610  54.069  1.00108.00           C  
ATOM     13  CA  LEU A  23     -27.979  30.949  52.535  1.00114.05           C  
ATOM     14  CA  PRO A  24     -26.381  29.263  55.487  1.00 67.69           C  
ATOM     15  CA  ALA A  25     -29.030  26.584  55.142  1.00 36.87           C  
ATOM     16  CA  VAL A  26     -27.715  25.430  51.800  1.00113.49           C  
ATOM     17  CA  VAL A  27     -24.560  23.421  51.921  1.00120.58           C  
ATOM     18  CA  SER A  28     -22.053  21.862  49.604  1.00 92.36           C  
ATOM     19  CA  VAL A  29     -21.679  18.125  49.644  1.00 36.53           C  
ATOM     20  CA  ARG A  30     -18.339  16.500  49.025  1.00 76.41           C  
ATOM     21  CA  VAL A  31     -18.005  12.852  48.195  1.00 38.80           C  
ATOM     22  CA  GLU A  32     -15.266  10.346  47.574  1.00 42.74           C  
ATOM     23  CA  GLY A  33     -15.576   6.732  46.650  1.00 24.07           C  
ATOM     24  CA  THR A  34     -14.993   3.897  44.234  1.00107.67           C  
ATOM     25  CA  ALA A  35     -12.627   1.110  41.597  1.00 21.93           C  
ATOM     26  CA  GLN A  59     -10.657   4.153  40.680  1.00175.81           C  
ATOM     27  CA  PRO A  60     -11.111   6.853  43.247  1.00161.79           C  
ATOM     28  CA  PHE A  61     -13.104   9.908  42.331  1.00 56.63           C  
ATOM     29  CA  GLU A  62     -14.219  13.046  44.065  1.00 27.36           C  
ATOM     30  CA  GLY A  63     -17.578  14.570  43.383  1.00 18.01           C  
ATOM     31  CA  LEU A  64     -19.188  17.811  44.370  1.00 43.88           C  
ATOM     32  CA  GLY A  65     -22.839  18.525  44.901  1.00 20.05           C  
ATOM     33  CA  SER A  66     -25.048  20.491  47.206  1.00 39.74           C  
ATOM     34  CA  GLY A  67     -27.661  19.836  49.832  1.00 14.86           C  
ATOM     35  CA  VAL A  68     -30.095  21.625  52.076  1.00 39.91           C  
ATOM     36  CA  ILE A  69     -30.318  21.513  55.833  1.00107.60           C  
ATOM     37  CA  ILE A  70     -33.843  20.448  56.625  1.00174.85           C  
ATOM     38  CA  ASN A  71     -33.377  19.979  60.334  1.00153.85           C  
ATOM     39  CA  ALA A  72     -30.771  22.015  62.165  1.00 39.25           C  
ATOM     40  CA  SER A  73     -30.961  20.131  65.414  1.00 37.36           C  
ATOM     41  CA  LYS A  74     -30.738  16.709  63.853  1.00131.58           C  
ATOM     42  CA  GLY A  75     -28.447  17.846  61.123  1.00 30.68           C  
ATOM     43  CA  TYR A  76     -30.532  16.281  58.392  1.00 96.77           C  
ATOM     44  CA  VAL A  77     -29.511  17.354  54.920  1.00 50.27           C  
ATOM     45  CA  LEU A  78     -31.468  16.593  51.791  1.00 50.36           C  
ATOM     46  CA  THR A  79     -29.597  15.836  48.615  1.00 40.62           C  
ATOM     47  CA  ASN A  80     -29.955  14.006  45.364  1.00 59.92           C  
ATOM     48  CA  ASN A  81     -29.362  10.299  45.455  1.00 38.23           C  
ATOM     49  CA  HIS A  82     -27.086  10.493  42.467  1.00 51.72           C  
ATOM     50  CA  VAL A  83     -24.756  12.822  44.259  1.00 39.64           C  
ATOM     51  CA  ILE A  84     -24.426  10.416  47.191  1.00 72.87           C  
ATOM     52  CA  ASN A  85     -24.780   7.071  45.441  1.00 68.02           C  
ATOM     53  CA  GLN A  86     -21.122   6.245  44.804  1.00 72.23           C  
ATOM     54  CA  ALA A  87     -19.785   7.958  47.925  1.00 67.16           C  
ATOM     55  CA  GLN A  88     -17.753   5.918  50.349  1.00101.60           C  
ATOM     56  CA  LYS A  89     -17.363   8.984  52.515  1.00 33.64           C  
ATOM     57  CA  ILE A  90     -19.325  12.181  52.564  1.00 36.58           C  
ATOM     58  CA  SER A  91     -18.513  15.564  53.977  1.00 27.33           C  
ATOM     59  CA  ILE A  92     -20.580  18.695  54.160  1.00 67.93           C  
ATOM     60  CA  GLN A  93     -19.278  22.207  54.128  1.00104.54           C  
ATOM     61  CA  LEU A  94     -21.091  25.301  55.274  1.00 54.58           C  
ATOM     62  CA  ASN A  95     -20.739  28.632  53.565  1.00 51.96           C  
ATOM     63  CA  ASP A  96     -18.893  29.792  56.649  1.00 46.16           C  
ATOM     64  CA  GLY A  97     -16.187  27.280  55.906  1.00 27.03           C  
ATOM     65  CA  ARG A  98     -16.938  24.852  58.682  1.00146.04           C  
ATOM     66  CA  GLU A  99     -17.000  21.256  57.560  1.00 31.21           C  
ATOM     67  CA  PHE A 100     -18.601  18.145  58.966  1.00 46.57           C  
ATOM     68  CA  ASP A 101     -18.825  14.471  58.158  1.00 35.43           C  
ATOM     69  CA  ALA A 102     -22.126  12.977  57.187  1.00 29.99           C  
ATOM     70  CA  LYS A 103     -23.677   9.558  56.959  1.00 54.43           C  
ATOM     71  CA  LEU A 104     -26.353   8.461  54.558  1.00 48.59           C  
ATOM     72  CA  ILE A 105     -29.550   7.934  56.447  1.00130.91           C  
ATOM     73  CA  GLY A 106     -31.347   6.559  53.423  1.00 35.70           C  
ATOM     74  CA  SER A 107     -32.310   7.369  49.876  1.00 95.40           C  
ATOM     75  CA  ASP A 108     -34.202   6.085  46.911  1.00 79.76           C  
ATOM     76  CA  ASP A 109     -33.357   5.766  43.246  1.00 51.72           C  
ATOM     77  CA  GLN A 110     -36.660   6.347  41.567  1.00 81.50           C  
ATOM     78  CA  SER A 111     -37.343   9.829  42.944  1.00 66.55           C  
ATOM     79  CA  ASP A 112     -33.618  10.472  43.391  1.00 74.81           C  
ATOM     80  CA  ILE A 113     -33.930  11.779  46.930  1.00 59.41           C  
ATOM     81  CA  ALA A 114     -31.440  11.019  49.662  1.00 33.74           C  
ATOM     82  CA  LEU A 115     -31.169  12.090  53.259  1.00109.24           C  
ATOM     83  CA  LEU A 116     -27.890  12.648  55.032  1.00 43.88           C  
ATOM     84  CA  GLN A 117     -27.147  13.302  58.650  1.00 60.36           C  
ATOM     85  CA  ILE A 118     -24.370  15.532  59.870  1.00109.42           C  
ATOM     86  CA  GLN A 119     -22.317  14.216  62.708  1.00121.59           C  
ATOM     87  CA  ASN A 120     -22.081  16.664  65.593  1.00 57.13           C  
ATOM     88  CA  PRO A 121     -24.021  19.262  63.694  1.00104.45           C  
ATOM     89  CA  SER A 122     -23.644  22.283  66.037  1.00194.44           C  
ATOM     90  CA  LYS A 123     -25.084  25.719  65.244  1.00 76.27           C  
ATOM     91  CA  LEU A 124     -26.795  25.019  61.974  1.00 90.29           C  
ATOM     92  CA  THR A 125     -29.491  26.935  60.172  1.00116.93           C  
ATOM     93  CA  GLN A 126     -32.522  25.240  58.698  1.00137.91           C  
ATOM     94  CA  ILE A 127     -34.430  26.145  55.620  1.00102.89           C  
ATOM     95  CA  ALA A 128     -38.197  26.482  55.763  1.00 28.31           C  
ATOM     96  CA  ILE A 129     -40.225  24.403  53.370  1.00 88.64           C  
ATOM     97  CA  ALA A 130     -42.917  25.913  51.187  1.00 34.42           C  
ATOM     98  CA  ASP A 131     -45.889  24.140  49.689  1.00 43.14           C  
ATOM     99  CA  SER A 132     -44.873  23.141  46.191  1.00 80.15           C  
ATOM    100  CA  ASP A 133     -48.469  22.560  45.232  1.00 33.94           C  
ATOM    101  CA  LYS A 134     -49.065  26.286  45.525  1.00100.85           C  
ATOM    102  CA  LEU A 135     -46.482  27.182  42.898  1.00 54.25           C  
ATOM    103  CA  ARG A 136     -47.662  28.601  39.607  1.00122.10           C  
ATOM    104  CA  VAL A 137     -45.729  29.407  36.495  1.00 81.31           C  
ATOM    105  CA  GLY A 138     -44.243  32.857  36.622  1.00 19.28           C  
ATOM    106  CA  ASP A 139     -43.304  32.634  40.266  1.00 24.79           C  
ATOM    107  CA  PHE A 140     -39.802  33.819  41.015  1.00 45.04           C  
ATOM    108  CA  ALA A 141     -37.208  31.300  42.046  1.00 27.67           C  
ATOM    109  CA  VAL A 142     -33.631  31.394  43.214  1.00 31.90           C  
ATOM    110  CA  ALA A 143     -31.286  28.479  42.946  1.00 27.85           C  
ATOM    111  CA  VAL A 144     -28.420  27.949  45.317  1.00 33.21           C  
ATOM    112  CA  GLY A 145     -25.745  25.333  44.992  1.00 21.75           C  
ATOM    113  CA  ASN A 146     -22.152  24.823  43.989  1.00136.30           C  
ATOM    114  CA  PRO A 147     -21.746  25.033  40.298  1.00 76.35           C  
ATOM    115  CA  PHE A 148     -18.406  23.719  39.105  1.00 69.50           C  
ATOM    116  CA  GLY A 149     -17.469  23.539  42.753  1.00 24.18           C  
ATOM    117  CA  LEU A 150     -16.802  27.251  42.768  1.00 86.06           C  
ATOM    118  CA  GLY A 151     -18.564  27.755  46.058  1.00 27.30           C  
ATOM    119  CA  GLN A 152     -22.009  28.789  47.128  1.00 39.75           C  
ATOM    120  CA  THR A 153     -23.617  30.461  44.160  1.00 33.63           C  
ATOM    121  CA  ALA A 154     -27.052  31.927  43.756  1.00 32.50           C  
ATOM    122  CA  THR A 155     -28.893  32.274  40.477  1.00116.75           C  
ATOM    123  CA  SER A 156     -32.259  33.761  39.768  1.00 86.66           C  
ATOM    124  CA  GLY A 157     -35.086  32.862  37.446  1.00 30.47           C  
ATOM    125  CA  ILE A 158     -38.783  32.076  37.295  1.00 61.30           C  
ATOM    126  CA  VAL A 159     -40.748  28.873  37.509  1.00 39.61           C  
ATOM    127  CA  SER A 160     -41.034  27.925  33.874  1.00 95.58           C  
ATOM    128  CA  ALA A 161     -43.256  24.899  34.267  1.00 49.68           C  
ATOM    129  CA  LEU A 162     -44.476  22.368  36.753  1.00115.78           C  
ATOM    130  CA  GLY A 163     -45.628  18.804  36.750  1.00 28.87           C  
ATOM    131  CA  ARG A 164     -43.263  17.867  34.041  1.00 80.64           C  
ATOM    132  CA  SER A 165     -42.210  14.397  33.151  1.00 84.71           C  
ATOM    133  CA  GLY A 166     -41.384  11.949  30.508  1.00 37.14           C  
ATOM    134  CA  LEU A 167     -37.884  13.359  30.684  1.00 49.70           C  
ATOM    135  CA  ASN A 168     -36.896   9.823  31.571  1.00 66.58           C  
ATOM    136  CA  LEU A 169     -34.327  11.269  33.891  1.00 50.91           C  
ATOM    137  CA  GLU A 170     -35.871   9.532  36.876  1.00107.74           C  
ATOM    138  CA  GLY A 171     -38.258   6.677  37.585  1.00 36.80           C  
ATOM    139  CA  LEU A 172     -40.639   9.041  39.257  1.00103.85           C  
ATOM    140  CA  GLU A 173     -40.637  12.504  37.988  1.00 74.09           C  
ATOM    141  CA  ASN A 174     -42.531  15.700  38.566  1.00103.01           C  
ATOM    142  CA  PHE A 175     -39.990  18.292  38.020  1.00 87.03           C  
ATOM    143  CA  ILE A 176     -40.558  21.918  38.512  1.00 76.28           C  
ATOM    144  CA  GLN A 177     -38.827  23.556  35.605  1.00 58.30           C  
ATOM    145  CA  THR A 178     -36.794  26.685  36.151  1.00135.86           C  
ATOM    146  CA  ASP A 179     -34.916  29.208  34.053  1.00 67.33           C  
ATOM    147  CA  ALA A 180     -32.464  29.836  36.875  1.00 45.38           C  
ATOM    148  CA  SER A 181     -28.989  28.874  35.841  1.00 43.36           C  
ATOM    149  CA  ILE A 182     -28.329  25.388  37.045  1.00 98.96           C  
ATOM    150  CA  ASN A 183     -25.084  23.693  36.239  1.00 79.22           C  
ATOM    151  CA  ARG A 184     -23.151  20.655  37.281  1.00147.07           C  
ATOM    152  CA  GLY A 185     -22.650  20.743  41.013  1.00 24.82           C  
ATOM    153  CA  ASN A 186     -26.083  22.246  41.491  1.00 54.73           C  
ATOM    154  CA  ALA A 187     -27.634  18.888  42.221  1.00 98.44           C  
ATOM    155  CA  GLY A 188     -29.033  18.520  45.685  1.00 24.13           C  
ATOM    156  CA  GLY A 189     -29.111  22.286  45.890  1.00 22.89           C  
ATOM    157  CA  ALA A 190     -32.100  24.333  46.797  1.00 47.73           C  
ATOM    158  CA  LEU A 191     -34.608  26.221  44.727  1.00 98.98           C  
ATOM    159  CA  LEU A 192     -36.077  28.971  46.824  1.00109.89           C  
ATOM    160  CA  ASN A 193     -38.985  31.327  46.545  1.00 53.57           C  
ATOM    161  CA  LEU A 194     -38.690  35.005  47.352  1.00 85.57           C  
ATOM    162  CA  ASN A 195     -39.548  34.079  50.907  1.00 54.30           C  
ATOM    163  CA  GLY A 196     -36.421  31.985  50.998  1.00 23.29           C  
ATOM    164  CA  GLU A 197     -38.533  28.905  51.528  1.00 41.43           C  
ATOM    165  CA  LEU A 198     -37.612  25.714  49.726  1.00 61.78           C  
ATOM    166  CA  ILE A 199     -39.678  25.087  46.606  1.00103.77           C  
ATOM    167  CA  GLY A 200     -37.685  22.072  45.459  1.00 27.26           C  
ATOM    168  CA  ILE A 201     -34.306  20.416  45.111  1.00 43.99           C  
ATOM    169  CA  ASN A 202     -32.471  20.941  41.836  1.00 82.84           C  
ATOM    170  CA  THR A 203     -32.107  17.508  40.289  1.00 84.66           C  
ATOM    171  CA  ALA A 204     -31.054  17.942  36.679  1.00 54.03           C  
ATOM    172  CA  ILE A 205     -30.802  20.012  33.531  1.00110.26           C  
ATOM    173  CA  LEU A 206     -31.292  19.524  29.838  1.00 57.92           C  
ATOM    174  CA  ALA A 207     -28.360  20.983  28.014  1.00 40.24           C  
ATOM    175  CA  PRO A 208     -26.801  19.967  24.799  1.00 65.23           C  
ATOM    176  CA  GLY A 209     -23.581  21.724  25.746  1.00 29.98           C  
ATOM    177  CA  GLY A 210     -23.477  20.330  29.218  1.00 23.41           C  
ATOM    178  CA  GLY A 211     -23.886  23.907  30.338  1.00 23.50           C  
ATOM    179  CA  SER A 212     -27.041  25.606  31.521  1.00 55.75           C  
ATOM    180  CA  VAL A 213     -29.461  26.135  28.649  1.00 60.56           C  
ATOM    181  CA  GLY A 214     -31.987  27.708  30.948  1.00 43.83           C  
ATOM    182  CA  ILE A 215     -33.955  24.540  31.343  1.00138.44           C  
ATOM    183  CA  GLY A 216     -33.489  23.060  34.757  1.00 24.92           C  
ATOM    184  CA  PHE A 217     -35.582  20.652  36.742  1.00 52.09           C  
ATOM    185  CA  ALA A 218     -36.114  20.274  40.448  1.00 33.92           C  
ATOM    186  CA  ILE A 219     -38.013  17.876  42.640  1.00 70.35           C  
ATOM    187  CA  PRO A 220     -40.744  19.673  44.389  1.00 85.93           C  
ATOM    188  CA  SER A 221     -40.430  20.559  48.047  1.00 38.66           C  
ATOM    189  CA  ASN A 222     -43.476  18.611  48.919  1.00 67.07           C  
ATOM    190  CA  MET A 223     -41.641  15.940  47.168  1.00 99.53           C  
ATOM    191  CA  ALA A 224     -38.472  16.027  49.156  1.00 50.46           C  
ATOM    192  CA  ARG A 225     -40.208  16.861  52.375  1.00128.58           C  
ATOM    193  CA  THR A 226     -42.349  13.853  52.922  1.00 66.74           C  
ATOM    194  CA  LEU A 227     -39.897  11.540  51.148  1.00115.75           C  
ATOM    195  CA  ALA A 228     -37.256  12.832  53.462  1.00 49.67           C  
ATOM    196  CA  GLN A 229     -39.440  12.467  56.472  1.00 87.50           C  
ATOM    197  CA  GLN A 230     -39.897   8.745  56.445  1.00 89.70           C  
ATOM    198  CA  LEU A 231     -36.248   8.443  55.688  1.00 65.89           C  
ATOM    199  CA  ILE A 232     -35.966   9.644  59.212  1.00188.82           C  
ATOM    200  CA  ASP A 233     -39.397   8.263  60.155  1.00175.73           C  
ATOM    201  CA  PHE A 234     -41.663   6.434  59.524  1.00185.16           C  
ATOM    202  CA  GLY A 235     -39.188   4.687  57.339  1.00 39.92           C  
ATOM    203  CA  GLU A 236     -41.520   1.979  56.280  1.00101.25           C  
ATOM    204  CA  ILE A 237     -39.579  -0.129  53.865  1.00 88.35           C  
ATOM    205  CA  LYS A 238     -42.457   0.021  51.458  1.00203.68           C  
ATOM    206  CA  ARG A 239     -43.086   1.579  49.238  1.00204.23           C  
ATOM    207  CA  GLY A 240     -39.573   2.892  49.678  1.00 46.34           C  
ATOM    208  CA  LEU A 241     -40.140   4.254  46.249  1.00189.25           C  
ATOM    209  CA  LEU A 242     -41.267   1.786  43.677  1.00 91.44           C  
ATOM    210  CA  GLY A 243     -38.016   1.049  41.917  1.00 49.46           C  
ATOM    211  CA  ILE A 244     -39.059   1.505  38.317  1.00 68.83           C  
ATOM    212  CA  LYS A 245     -38.060   3.514  35.305  1.00 96.38           C  
ATOM    213  CA  GLY A 246     -40.492   5.148  32.986  1.00 30.93           C  
ATOM    214  CA  THR A 247     -41.191   8.093  30.801  1.00111.36           C  
ATOM    215  CA  GLU A 248     -43.953   9.933  28.998  1.00 48.89           C  
ATOM    216  CA  MET A 249     -46.363   8.093  26.815  1.00 58.82           C  
ATOM    217  CA  SER A 250     -44.492   6.853  23.805  1.00 41.30           C  
ATOM    218  CA  ALA A 251     -45.574   7.995  20.397  1.00 38.26           C  
ATOM    219  CA  ASP A 252     -45.573   4.503  18.975  1.00 57.17           C  
ATOM    220  CA  ILE A 253     -47.394   2.782  21.790  1.00153.69           C  
ATOM    221  CA  ALA A 254     -49.822   5.556  22.505  1.00 59.82           C  
ATOM    222  CA  LYS A 255     -51.136   6.418  19.147  1.00103.17           C  
ATOM    223  CA  ALA A 256     -51.192   3.030  17.563  1.00 76.43           C  
ATOM    224  CA  PHE A 257     -52.702   0.697  20.096  1.00163.32           C  
ATOM    225  CA  ASN A 258     -54.564   3.410  21.684  1.00243.55           C  
ATOM    226  CA  LEU A 259     -54.219   3.354  25.392  1.00143.69           C  
ATOM    227  CA  ASP A 260     -57.407   3.157  27.310  1.00 62.44           C  
ATOM    228  CA  VAL A 261     -56.094   5.924  29.515  1.00108.54           C  
ATOM    229  CA  GLN A 262     -55.057   8.780  27.310  1.00 65.16           C  
ATOM    230  CA  ARG A 263     -51.746   8.986  28.995  1.00201.03           C  
ATOM    231  CA  GLY A 264     -49.963   7.874  32.056  1.00 26.43           C  
ATOM    232  CA  ALA A 265     -46.614   7.133  33.481  1.00 40.18           C  
ATOM    233  CA  PHE A 266     -45.407   4.357  31.350  1.00133.27           C  
ATOM    234  CA  VAL A 267     -42.854   1.973  32.619  1.00 67.40           C  
ATOM    235  CA  SER A 268     -40.257   0.516  30.313  1.00106.96           C  
ATOM    236  CA  GLU A 269     -38.503  -1.385  33.036  1.00104.58           C  
ATOM    237  CA  VAL A 270     -38.814  -3.641  36.032  1.00101.98           C  
ATOM    238  CA  LEU A 271     -36.241  -3.307  38.768  1.00 48.84           C  
ATOM    239  CA  PRO A 272     -34.940  -6.395  40.391  1.00143.63           C  
ATOM    240  CA  GLY A 273     -35.811  -7.009  44.016  1.00 24.47           C  
ATOM    241  CA  SER A 274     -37.582  -3.773  43.475  1.00 41.80           C  
ATOM    242  CA  GLY A 275     -40.782  -2.635  44.935  1.00 32.91           C  
ATOM    243  CA  SER A 276     -42.375  -2.718  41.583  1.00 46.14           C  
ATOM    244  CA  ALA A 277     -41.030  -6.170  41.047  1.00 51.93           C  
ATOM    245  CA  LYS A 278     -42.641  -7.898  43.972  1.00116.47           C  
ATOM    246  CA  ALA A 279     -45.725  -5.771  43.659  1.00 43.96           C  
ATOM    247  CA  GLY A 280     -45.895  -7.437  40.353  1.00 39.37           C  
ATOM    248  CA  VAL A 281     -45.886  -4.316  38.279  1.00 62.95           C  
ATOM    249  CA  LYS A 282     -43.948  -4.984  35.257  1.00122.23           C  
ATOM    250  CA  ALA A 283     -42.934  -3.361  32.080  1.00 87.60           C  
ATOM    251  CA  GLY A 284     -45.073  -1.969  29.378  1.00 39.63           C  
ATOM    252  CA  ASP A 285     -47.071  -0.776  32.355  1.00 99.91           C  
ATOM    253  CA  ILE A 286     -49.243   2.176  32.178  1.00169.29           C  
ATOM    254  CA  ILE A 287     -49.601   3.770  35.554  1.00 69.39           C  
ATOM    255  CA  THR A 288     -52.947   5.470  35.291  1.00 61.38           C  
ATOM    256  CA  SER A 289     -53.381   6.548  38.824  1.00 52.20           C  
ATOM    257  CA  LEU A 290     -51.899   6.672  42.259  1.00 71.72           C  
ATOM    258  CA  ASN A 291     -54.176   6.349  45.231  1.00178.47           C  
ATOM    259  CA  GLY A 292     -57.882   7.160  45.081  1.00 52.50           C  
ATOM    260  CA  LYS A 293     -57.469  10.409  43.206  1.00 71.53           C  
ATOM    261  CA  PRO A 294     -56.560  10.221  39.594  1.00 59.39           C  
ATOM    262  CA  LEU A 295     -52.962  10.425  38.440  1.00119.44           C  
ATOM    263  CA  ASN A 296     -51.842  12.723  35.684  1.00 63.52           C  
ATOM    264  CA  SER A 297     -48.847  12.288  33.473  1.00 46.98           C  
ATOM    265  CA  PHE A 298     -45.590  10.718  34.446  1.00 73.59           C  
ATOM    266  CA  ALA A 299     -44.917  14.181  35.691  1.00 44.96           C  
ATOM    267  CA  GLU A 300     -47.673  14.188  38.206  1.00 88.02           C  
ATOM    268  CA  LEU A 301     -46.468  10.783  39.216  1.00 76.51           C  
ATOM    269  CA  ARG A 302     -43.302  11.790  40.866  1.00191.59           C  
ATOM    270  CA  SER A 303     -44.926  14.925  42.030  1.00 56.79           C  
ATOM    271  CA  ARG A 304     -47.081  13.036  44.368  1.00159.75           C  
ATOM    272  CA  ILE A 305     -44.726  10.163  45.044  1.00134.66           C  
ATOM    273  CA  ALA A 306     -41.667  12.230  45.316  1.00 66.49           C  
ATOM    274  CA  THR A 307     -43.881  14.174  47.620  1.00 59.68           C  
ATOM    275  CA  THR A 308     -44.959  11.157  49.588  1.00 62.90           C  
ATOM    276  CA  GLU A 309     -43.023   9.338  52.265  1.00 81.62           C  
ATOM    277  CA  PRO A 310     -40.768   6.820  50.768  1.00184.20           C  
ATOM    278  CA  GLY A 311     -42.036   4.743  52.439  1.00124.38           C  
ATOM    279  CA  THR A 312     -45.763   5.024  52.660  1.00 51.62           C  
ATOM    280  CA  LYS A 313     -47.710   2.060  51.484  1.00 83.81           C  
ATOM    281  CA  VAL A 314     -49.709   3.120  48.490  1.00 47.88           C  
ATOM    282  CA  LYS A 315     -51.803   1.500  45.799  1.00 70.50           C  
ATOM    283  CA  LEU A 316     -51.206   2.042  42.134  1.00105.77           C  
ATOM    284  CA  GLY A 317     -53.545   1.821  39.224  1.00 46.61           C  
ATOM    285  CA  LEU A 318     -52.167   0.713  35.958  1.00108.52           C  
ATOM    286  CA  LEU A 319     -53.303  -0.490  32.669  1.00112.45           C  
ATOM    287  CA  ARG A 320     -52.001  -3.675  31.512  1.00199.64           C  
ATOM    288  CA  ASN A 321     -53.475  -5.354  28.432  1.00206.20           C  
ATOM    289  CA  GLY A 322     -56.188  -2.897  28.312  1.00 49.00           C  
ATOM    290  CA  LYS A 323     -57.328  -4.185  31.566  1.00123.08           C  
ATOM    291  CA  PRO A 324     -57.358  -2.841  34.965  1.00158.65           C  
ATOM    292  CA  LEU A 325     -55.817  -3.825  38.280  1.00171.23           C  
ATOM    293  CA  GLU A 326     -55.065  -2.412  41.595  1.00127.64           C  
ATOM    294  CA  VAL A 327     -51.862  -3.391  43.260  1.00119.48           C  
ATOM    295  CA  GLU A 328     -50.239  -2.374  46.502  1.00 47.06           C  
ATOM    296  CA  VAL A 329     -46.744  -1.070  46.164  1.00 58.81           C  
ATOM    297  CA  SER A 340     -23.359 -28.026  47.195  1.00 95.83           C  
ATOM    298  CA  ALA A 341     -19.638 -27.590  46.630  1.00 76.80           C  
ATOM    299  CA  GLU A 342     -20.165 -25.593  43.468  1.00 59.05           C  
ATOM    300  CA  MET A 343     -20.752 -22.201  44.862  1.00 88.70           C  
ATOM    301  CA  ILE A 344     -17.897 -22.281  47.258  1.00 57.17           C  
ATOM    302  CA  THR A 345     -15.647 -23.990  44.805  1.00 67.27           C  
ATOM    303  CA  PRO A 346     -15.784 -23.152  41.167  1.00152.59           C  
ATOM    304  CA  ALA A 347     -17.415 -25.451  38.647  1.00 70.38           C  
ATOM    305  CA  LEU A 348     -16.662 -28.395  40.927  1.00 90.07           C  
ATOM    306  CA  GLU A 349     -19.956 -30.167  41.152  1.00139.12           C  
ATOM    307  CA  GLY A 350     -20.104 -32.404  44.119  1.00 28.51           C  
ATOM    308  CA  ALA A 351     -21.408 -33.028  47.567  1.00 34.70           C  
ATOM    309  CA  THR A 352     -23.426 -30.277  49.091  1.00101.18           C  
ATOM    310  CA  LEU A 353     -21.975 -28.270  51.901  1.00 58.74           C  
ATOM    311  CA  SER A 354     -23.488 -26.835  55.022  1.00 35.65           C  
ATOM    312  CA  ASP A 355     -21.946 -24.439  57.462  1.00 40.71           C  
ATOM    313  CA  GLY A 356     -21.821 -24.763  61.171  1.00 48.32           C  
ATOM    314  CA  GLN A 357     -20.703 -27.877  62.927  1.00166.31           C  
ATOM    315  CA  LEU A 358     -24.346 -28.012  62.835  1.00216.87           C  
ATOM    316  CA  LYS A 359     -24.489 -30.904  65.273  1.00150.56           C  
ATOM    317  CA  ASP A 360     -21.693 -29.617  67.538  1.00 52.42           C  
ATOM    318  CA  GLY A 361     -19.629 -26.463  67.865  1.00 30.46           C  
ATOM    319  CA  GLY A 362     -18.522 -25.405  64.423  1.00 40.73           C  
ATOM    320  CA  LYS A 363     -15.490 -27.469  63.662  1.00125.42           C  
ATOM    321  CA  GLY A 364     -16.061 -26.403  60.099  1.00 27.34           C  
ATOM    322  CA  ILE A 365     -18.208 -26.763  57.020  1.00121.02           C  
ATOM    323  CA  LYS A 366     -19.824 -30.106  56.540  1.00 54.14           C  
ATOM    324  CA  ILE A 367     -20.368 -31.867  53.286  1.00 61.77           C  
ATOM    325  CA  ASP A 368     -23.861 -33.247  53.350  1.00 54.79           C  
ATOM    326  CA  GLU A 369     -23.740 -35.859  50.663  1.00 92.63           C  
ATOM    327  CA  VAL A 370     -21.534 -36.888  47.822  1.00137.03           C  
ATOM    328  CA  VAL A 371     -22.894 -36.862  44.287  1.00187.66           C  
ATOM    329  CA  LYS A 372     -19.937 -39.228  43.615  1.00188.08           C  
ATOM    330  CA  GLY A 373     -20.143 -39.080  39.837  1.00 35.04           C  
ATOM    331  CA  SER A 374     -19.329 -35.382  40.307  1.00 48.83           C  
ATOM    332  CA  PRO A 375     -15.869 -33.998  40.347  1.00 81.58           C  
ATOM    333  CA  ALA A 376     -16.059 -32.934  43.966  1.00 41.26           C  
ATOM    334  CA  ALA A 377     -16.176 -36.661  44.434  1.00 49.69           C  
ATOM    335  CA  GLN A 378     -13.223 -37.337  42.168  1.00 54.24           C  
ATOM    336  CA  ALA A 379     -10.589 -35.569  44.266  1.00 60.97           C  
ATOM    337  CA  GLY A 380     -11.396 -37.229  47.559  1.00 61.29           C  
ATOM    338  CA  LEU A 381     -14.369 -35.476  49.043  1.00 59.19           C  
ATOM    339  CA  GLN A 382     -16.629 -37.984  50.710  1.00 64.30           C  
ATOM    340  CA  LYS A 383     -19.746 -37.320  52.722  1.00119.55           C  
ATOM    341  CA  ASP A 384     -19.690 -36.567  56.437  1.00 77.80           C  
ATOM    342  CA  ASP A 385     -16.332 -34.898  56.198  1.00 49.09           C  
ATOM    343  CA  VAL A 386     -15.921 -31.690  58.074  1.00 58.94           C  
ATOM    344  CA  ILE A 387     -13.546 -29.153  56.735  1.00 57.34           C  
ATOM    345  CA  ILE A 388     -11.777 -27.743  59.745  1.00112.52           C  
ATOM    346  CA  GLY A 389      -9.860 -25.194  57.724  1.00 44.78           C  
ATOM    347  CA  VAL A 390      -8.067 -24.383  54.508  1.00 63.24           C  
ATOM    348  CA  ASN A 391      -4.470 -23.415  53.869  1.00 75.44           C  
ATOM    349  CA  ARG A 392      -3.403 -23.203  57.487  1.00155.86           C  
ATOM    350  CA  ASP A 393      -6.540 -21.214  58.084  1.00 50.67           C  
ATOM    351  CA  ARG A 394      -9.273 -22.441  60.332  1.00102.29           C  
ATOM    352  CA  VAL A 395     -12.670 -22.538  58.729  1.00 43.79           C  
ATOM    353  CA  ASN A 396     -15.453 -22.064  61.225  1.00 43.54           C  
ATOM    354  CA  SER A 397     -18.070 -21.758  58.537  1.00 37.56           C  
ATOM    355  CA  ILE A 398     -18.571 -21.282  54.826  1.00 45.60           C  
ATOM    356  CA  ALA A 399     -17.924 -17.573  54.937  1.00 23.57           C  
ATOM    357  CA  GLU A 400     -14.473 -18.078  56.385  1.00 26.71           C  
ATOM    358  CA  MET A 401     -13.748 -20.813  53.896  1.00 31.93           C  
ATOM    359  CA  ARG A 402     -14.762 -18.413  51.191  1.00136.45           C  
ATOM    360  CA  LYS A 403     -12.206 -16.013  52.553  1.00 68.42           C  
ATOM    361  CA  VAL A 404      -9.294 -18.347  52.021  1.00 31.08           C  
ATOM    362  CA  LEU A 405     -10.630 -18.980  48.559  1.00 60.05           C  
ATOM    363  CA  ALA A 406     -10.768 -15.261  48.031  1.00 36.31           C  
ATOM    364  CA  ALA A 407      -6.989 -15.317  48.119  1.00 35.83           C  
ATOM    365  CA  LYS A 408      -7.290 -17.781  45.272  1.00130.00           C  
ATOM    366  CA  PRO A 409      -4.116 -19.598  46.129  1.00 71.61           C  
ATOM    367  CA  ALA A 410      -3.025 -21.924  43.357  1.00 33.57           C  
ATOM    368  CA  ILE A 411      -2.660 -24.489  46.119  1.00142.82           C  
ATOM    369  CA  ILE A 412      -5.746 -25.121  48.182  1.00 49.00           C  
ATOM    370  CA  ALA A 413      -5.428 -27.520  51.022  1.00 51.08           C  
ATOM    371  CA  LEU A 414      -8.477 -28.724  52.828  1.00113.93           C  
ATOM    372  CA  GLN A 415      -8.142 -30.674  55.954  1.00213.72           C  
ATOM    373  CA  ILE A 416     -11.230 -32.333  57.012  1.00115.95           C  
ATOM    374  CA  VAL A 417     -11.831 -34.708  59.792  1.00 50.59           C  
ATOM    375  CA  ARG A 418     -13.312 -37.988  58.786  1.00107.79           C  
ATOM    376  CA  GLY A 419     -14.346 -40.392  61.452  1.00 21.07           C  
ATOM    377  CA  ASN A 420     -11.967 -39.862  64.266  1.00 50.71           C  
ATOM    378  CA  GLU A 421      -9.107 -39.098  61.951  1.00 51.44           C  
ATOM    379  CA  SER A 422      -7.464 -36.173  60.271  1.00 52.31           C  
ATOM    380  CA  ILE A 423      -7.859 -35.972  56.541  1.00 77.87           C  
ATOM    381  CA  TYR A 424      -6.363 -33.738  53.982  1.00180.93           C  
ATOM    382  CA  LEU A 425      -7.930 -32.812  50.749  1.00102.67           C  
ATOM    383  CA  LEU A 426      -6.809 -30.585  48.038  1.00226.65           C  
ATOM    384  CA  MET A 427      -7.458 -28.824  44.808  1.00 67.41           C  
TER     385      MET A 427                                                      
ATOM    386  CA  PRO B  11     -44.845  46.292  37.380  1.00 76.77           C  
ATOM    387  CA  LEU B  12     -42.138  47.690  35.175  1.00 90.51           C  
ATOM    388  CA  PRO B  13     -39.838  50.268  36.510  1.00154.13           C  
ATOM    389  CA  SER B  14     -39.747  50.534  33.641  1.00123.49           C  
ATOM    390  CA  LEU B  15     -36.163  50.131  32.519  1.00 65.98           C  
ATOM    391  CA  ALA B  16     -36.595  52.266  29.432  1.00 44.65           C  
ATOM    392  CA  PRO B  17     -37.008  55.531  31.189  1.00 67.44           C  
ATOM    393  CA  MET B  18     -33.811  55.003  33.120  1.00 43.72           C  
ATOM    394  CA  LEU B  19     -32.053  53.779  30.023  1.00 53.25           C  
ATOM    395  CA  GLU B  20     -32.981  56.670  27.814  1.00 79.68           C  
ATOM    396  CA  LYS B  21     -31.022  59.125  29.843  1.00126.11           C  
ATOM    397  CA  VAL B  22     -28.098  56.788  30.580  1.00 79.98           C  
ATOM    398  CA  LEU B  23     -27.458  55.040  27.286  1.00116.62           C  
ATOM    399  CA  PRO B  24     -25.727  57.846  25.499  1.00 68.14           C  
ATOM    400  CA  ALA B  25     -23.064  57.625  28.187  1.00 38.49           C  
ATOM    401  CA  VAL B  26     -22.041  54.168  27.075  1.00 96.44           C  
ATOM    402  CA  VAL B  27     -19.959  54.100  23.976  1.00109.32           C  
ATOM    403  CA  SER B  28     -18.466  51.644  21.519  1.00107.80           C  
ATOM    404  CA  VAL B  29     -14.735  51.561  21.187  1.00 38.31           C  
ATOM    405  CA  ARG B  30     -13.128  50.756  17.881  1.00 71.25           C  
ATOM    406  CA  VAL B  31      -9.501  49.817  17.644  1.00 38.62           C  
ATOM    407  CA  GLU B  32      -7.022  49.211  14.883  1.00 42.64           C  
ATOM    408  CA  GLY B  33      -3.400  48.295  15.149  1.00 29.04           C  
ATOM    409  CA  THR B  34      -0.671  45.758  14.749  1.00 68.01           C  
ATOM    410  CA  ALA B  35       2.086  43.007  12.756  1.00 26.05           C  
ATOM    411  CA  GLN B  59      -0.896  42.238  10.606  1.00 79.42           C  
ATOM    412  CA  PRO B  60      -3.652  44.723  10.884  1.00 75.09           C  
ATOM    413  CA  PHE B  61      -6.698  43.842  12.874  1.00 56.53           C  
ATOM    414  CA  GLU B  62      -9.778  45.612  14.050  1.00 26.98           C  
ATOM    415  CA  GLY B  63     -11.273  45.045  17.436  1.00 17.09           C  
ATOM    416  CA  LEU B  64     -14.491  46.175  18.997  1.00 44.12           C  
ATOM    417  CA  GLY B  65     -15.207  46.896  22.616  1.00 21.97           C  
ATOM    418  CA  SER B  66     -17.146  49.348  24.704  1.00 78.25           C  
ATOM    419  CA  GLY B  67     -16.421  52.129  27.126  1.00 17.95           C  
ATOM    420  CA  VAL B  68     -18.193  54.518  29.425  1.00 41.43           C  
ATOM    421  CA  ILE B  69     -17.824  58.205  29.489  1.00136.25           C  
ATOM    422  CA  ILE B  70     -16.858  59.346  32.942  1.00 98.87           C  
ATOM    423  CA  ASN B  71     -16.618  63.038  32.305  1.00 72.34           C  
ATOM    424  CA  ALA B  72     -18.359  64.839  29.539  1.00 59.09           C  
ATOM    425  CA  SER B  73     -16.375  67.959  29.546  1.00 39.76           C  
ATOM    426  CA  LYS B  74     -13.026  66.306  29.428  1.00 89.65           C  
ATOM    427  CA  GLY B  75     -14.266  63.443  27.339  1.00 29.61           C  
ATOM    428  CA  TYR B  76     -12.711  60.763  29.482  1.00 65.23           C  
ATOM    429  CA  VAL B  77     -13.900  57.275  28.728  1.00 45.48           C  
ATOM    430  CA  LEU B  78     -13.123  54.227  30.809  1.00 53.54           C  
ATOM    431  CA  THR B  79     -12.447  50.940  29.118  1.00 40.98           C  
ATOM    432  CA  ASN B  80     -10.662  47.695  29.676  1.00 61.57           C  
ATOM    433  CA  ASN B  81      -6.943  47.650  29.090  1.00 47.69           C  
ATOM    434  CA  HIS B  82      -7.183  44.580  26.937  1.00 51.38           C  
ATOM    435  CA  VAL B  83      -9.507  46.264  24.529  1.00 36.37           C  
ATOM    436  CA  ILE B  84      -7.065  49.157  24.052  1.00 72.85           C  
ATOM    437  CA  ASN B  85      -3.748  47.371  24.491  1.00 68.83           C  
ATOM    438  CA  GLN B  86      -2.949  46.550  20.870  1.00 85.56           C  
ATOM    439  CA  ALA B  87      -4.604  49.647  19.410  1.00 67.79           C  
ATOM    440  CA  GLN B  88      -2.532  51.926  17.236  1.00 60.21           C  
ATOM    441  CA  LYS B  89      -5.540  54.149  16.774  1.00 31.28           C  
ATOM    442  CA  ILE B  90      -8.778  54.280  18.652  1.00 41.04           C  
ATOM    443  CA  SER B  91     -12.145  55.664  17.747  1.00 28.07           C  
ATOM    444  CA  ILE B  92     -15.213  56.198  19.873  1.00 95.32           C  
ATOM    445  CA  GLN B  93     -18.714  55.943  18.526  1.00119.62           C  
ATOM    446  CA  LEU B  94     -21.804  57.276  20.243  1.00 51.81           C  
ATOM    447  CA  ASN B  95     -25.130  55.535  19.976  1.00 47.15           C  
ATOM    448  CA  ASP B  96     -26.307  58.515  17.972  1.00 49.97           C  
ATOM    449  CA  GLY B  97     -23.772  57.652  15.311  1.00 27.94           C  
ATOM    450  CA  ARG B  98     -21.353  60.450  16.032  1.00100.79           C  
ATOM    451  CA  GLU B  99     -17.783  59.272  16.116  1.00 98.65           C  
ATOM    452  CA  PHE B 100     -14.624  60.727  17.576  1.00 47.95           C  
ATOM    453  CA  ASP B 101     -10.923  60.018  17.921  1.00139.76           C  
ATOM    454  CA  ALA B 102      -9.510  59.011  21.220  1.00 39.18           C  
ATOM    455  CA  LYS B 103      -6.081  58.889  22.766  1.00 44.83           C  
ATOM    456  CA  LEU B 104      -4.932  56.613  25.536  1.00 45.34           C  
ATOM    457  CA  ILE B 105      -4.473  58.667  28.639  1.00 81.28           C  
ATOM    458  CA  GLY B 106      -3.122  55.725  30.611  1.00 24.56           C  
ATOM    459  CA  SER B 107      -3.963  52.236  31.743  1.00 94.04           C  
ATOM    460  CA  ASP B 108      -2.724  49.355  33.782  1.00 80.77           C  
ATOM    461  CA  ASP B 109      -2.526  45.652  33.102  1.00128.59           C  
ATOM    462  CA  GLN B 110      -3.030  44.123  36.490  1.00 86.35           C  
ATOM    463  CA  SER B 111      -6.498  45.588  37.140  1.00 64.03           C  
ATOM    464  CA  ASP B 112      -7.186  45.841  33.411  1.00 73.18           C  
ATOM    465  CA  ILE B 113      -8.410  49.443  33.553  1.00 99.84           C  
ATOM    466  CA  ALA B 114      -7.623  51.995  30.881  1.00 31.36           C  
ATOM    467  CA  LEU B 115      -8.614  55.600  30.440  1.00 97.26           C  
ATOM    468  CA  LEU B 116      -9.151  57.234  27.084  1.00 45.74           C  
ATOM    469  CA  GLN B 117      -9.778  60.817  26.140  1.00 43.36           C  
ATOM    470  CA  ILE B 118     -11.957  61.893  23.280  1.00 60.34           C  
ATOM    471  CA  GLN B 119     -10.674  64.612  21.048  1.00113.01           C  
ATOM    472  CA  ASN B 120     -13.111  67.478  20.641  1.00 60.17           C  
ATOM    473  CA  PRO B 121     -15.694  65.756  22.770  1.00109.92           C  
ATOM    474  CA  SER B 122     -18.673  68.111  22.212  1.00199.93           C  
ATOM    475  CA  LYS B 123     -22.102  67.492  23.724  1.00 81.17           C  
ATOM    476  CA  LEU B 124     -21.444  64.315  25.575  1.00 73.33           C  
ATOM    477  CA  THR B 125     -23.463  62.759  28.344  1.00118.17           C  
ATOM    478  CA  GLN B 126     -21.801  61.268  31.368  1.00206.47           C  
ATOM    479  CA  ILE B 127     -22.564  58.394  33.600  1.00104.09           C  
ATOM    480  CA  ALA B 128     -22.896  58.800  37.327  1.00 32.72           C  
ATOM    481  CA  ILE B 129     -20.898  56.425  39.458  1.00 85.60           C  
ATOM    482  CA  ALA B 130     -22.422  54.437  42.290  1.00 33.88           C  
ATOM    483  CA  ASP B 131     -20.723  53.052  45.373  1.00 43.65           C  
ATOM    484  CA  SER B 132     -19.736  49.490  44.555  1.00 35.81           C  
ATOM    485  CA  ASP B 133     -19.159  48.711  48.183  1.00 30.64           C  
ATOM    486  CA  LYS B 134     -22.871  49.200  48.741  1.00122.43           C  
ATOM    487  CA  LEU B 135     -23.829  46.456  46.319  1.00 55.03           C  
ATOM    488  CA  ARG B 136     -25.345  43.287  47.688  1.00107.15           C  
ATOM    489  CA  VAL B 137     -26.217  40.078  45.954  1.00 81.53           C  
ATOM    490  CA  GLY B 138     -29.669  40.241  44.482  1.00 23.11           C  
ATOM    491  CA  ASP B 139     -29.393  43.805  43.316  1.00 29.58           C  
ATOM    492  CA  PHE B 140     -30.560  44.349  39.771  1.00 56.03           C  
ATOM    493  CA  ALA B 141     -28.018  45.163  37.124  1.00 26.58           C  
ATOM    494  CA  VAL B 142     -28.095  46.124  33.484  1.00 30.72           C  
ATOM    495  CA  ALA B 143     -25.189  45.634  31.159  1.00 27.41           C  
ATOM    496  CA  VAL B 144     -24.605  47.799  28.147  1.00 31.72           C  
ATOM    497  CA  GLY B 145     -21.991  47.274  25.498  1.00 21.70           C  
ATOM    498  CA  ASN B 146     -21.526  45.985  21.993  1.00142.46           C  
ATOM    499  CA  PRO B 147     -21.656  42.287  21.871  1.00108.77           C  
ATOM    500  CA  PHE B 148     -20.484  40.876  18.563  1.00 65.38           C  
ATOM    501  CA  GLY B 149     -20.225  44.456  17.415  1.00 22.55           C  
ATOM    502  CA  LEU B 150     -23.937  44.479  16.803  1.00 82.29           C  
ATOM    503  CA  GLY B 151     -24.332  47.921  18.295  1.00 28.79           C  
ATOM    504  CA  GLN B 152     -25.392  49.233  21.653  1.00 42.09           C  
ATOM    505  CA  THR B 153     -27.103  46.391  23.444  1.00 34.08           C  
ATOM    506  CA  ALA B 154     -28.613  46.303  26.884  1.00 30.89           C  
ATOM    507  CA  THR B 155     -29.059  43.167  28.928  1.00117.35           C  
ATOM    508  CA  SER B 156     -30.554  42.679  32.330  1.00 39.23           C  
ATOM    509  CA  GLY B 157     -29.714  40.503  35.297  1.00 22.08           C  
ATOM    510  CA  ILE B 158     -28.899  40.591  38.993  1.00 87.97           C  
ATOM    511  CA  VAL B 159     -25.675  40.782  40.931  1.00 36.66           C  
ATOM    512  CA  SER B 160     -24.794  37.145  41.420  1.00 44.58           C  
ATOM    513  CA  ALA B 161     -21.789  37.601  43.658  1.00 43.17           C  
ATOM    514  CA  LEU B 162     -19.129  40.060  44.663  1.00 72.91           C  
ATOM    515  CA  GLY B 163     -15.548  39.981  45.775  1.00 29.11           C  
ATOM    516  CA  ARG B 164     -14.689  37.142  43.495  1.00160.50           C  
ATOM    517  CA  SER B 165     -11.191  36.228  42.501  1.00152.26           C  
ATOM    518  CA  GLY B 166      -8.847  33.404  41.853  1.00 41.09           C  
ATOM    519  CA  LEU B 167     -10.210  33.397  38.355  1.00 53.91           C  
ATOM    520  CA  ASN B 168      -6.656  34.153  37.304  1.00 62.50           C  
ATOM    521  CA  LEU B 169      -8.095  36.389  34.657  1.00 48.81           C  
ATOM    522  CA  GLU B 170      -6.267  39.413  35.989  1.00100.74           C  
ATOM    523  CA  GLY B 171      -3.433  40.286  38.351  1.00 34.47           C  
ATOM    524  CA  LEU B 172      -5.805  42.086  40.653  1.00124.02           C  
ATOM    525  CA  GLU B 173      -9.269  40.734  40.710  1.00 93.02           C  
ATOM    526  CA  ASN B 174     -12.442  41.572  42.568  1.00102.20           C  
ATOM    527  CA  PHE B 175     -15.071  40.916  40.093  1.00 85.91           C  
ATOM    528  CA  ILE B 176     -18.689  41.619  40.589  1.00 71.46           C  
ATOM    529  CA  GLN B 177     -20.409  38.615  39.127  1.00 54.38           C  
ATOM    530  CA  THR B 178     -23.530  39.119  37.087  1.00110.92           C  
ATOM    531  CA  ASP B 179     -26.139  37.015  35.307  1.00 59.72           C  
ATOM    532  CA  ALA B 180     -26.711  39.699  32.687  1.00 38.59           C  
ATOM    533  CA  SER B 181     -25.760  38.378  29.322  1.00 98.50           C  
ATOM    534  CA  ILE B 182     -22.263  39.441  28.532  1.00106.13           C  
ATOM    535  CA  ASN B 183     -20.515  38.357  25.378  1.00 62.70           C  
ATOM    536  CA  ARG B 184     -17.422  39.342  23.519  1.00 67.20           C  
ATOM    537  CA  GLY B 185     -17.480  43.009  22.659  1.00 24.37           C  
ATOM    538  CA  ASN B 186     -18.981  43.727  26.052  1.00136.97           C  
ATOM    539  CA  ALA B 187     -15.564  44.510  27.469  1.00 49.91           C  
ATOM    540  CA  GLY B 188     -15.177  48.023  28.743  1.00 23.57           C  
ATOM    541  CA  GLY B 189     -18.936  48.294  28.792  1.00 22.49           C  
ATOM    542  CA  ALA B 190     -20.958  49.420  31.734  1.00 42.26           C  
ATOM    543  CA  LEU B 191     -22.885  47.539  34.355  1.00 93.53           C  
ATOM    544  CA  LEU B 192     -25.569  49.786  35.716  1.00 54.55           C  
ATOM    545  CA  ASN B 193     -27.937  49.770  38.627  1.00 58.96           C  
ATOM    546  CA  LEU B 194     -31.602  50.658  38.373  1.00 97.29           C  
ATOM    547  CA  ASN B 195     -30.564  54.241  38.945  1.00 46.86           C  
ATOM    548  CA  GLY B 196     -28.508  54.047  35.817  1.00 25.73           C  
ATOM    549  CA  GLU B 197     -25.416  54.615  37.899  1.00 42.02           C  
ATOM    550  CA  LEU B 198     -22.257  52.709  37.085  1.00 60.80           C  
ATOM    551  CA  ILE B 199     -21.700  49.676  39.298  1.00 79.03           C  
ATOM    552  CA  GLY B 200     -18.721  48.345  37.376  1.00 28.89           C  
ATOM    553  CA  ILE B 201     -17.068  47.762  34.026  1.00 46.93           C  
ATOM    554  CA  ASN B 202     -17.671  44.411  32.359  1.00 80.18           C  
ATOM    555  CA  THR B 203     -14.267  42.764  32.089  1.00173.42           C  
ATOM    556  CA  ALA B 204     -14.792  39.096  31.285  1.00 58.04           C  
ATOM    557  CA  ILE B 205     -16.936  35.976  31.195  1.00111.74           C  
ATOM    558  CA  LEU B 206     -16.607  32.306  31.991  1.00 54.64           C  
ATOM    559  CA  ALA B 207     -18.131  30.307  29.208  1.00 42.44           C  
ATOM    560  CA  PRO B 208     -17.184  26.986  27.849  1.00 67.56           C  
ATOM    561  CA  GLY B 209     -18.971  27.769  24.598  1.00 30.06           C  
ATOM    562  CA  GLY B 210     -17.468  31.184  24.237  1.00 24.63           C  
ATOM    563  CA  GLY B 211     -21.002  32.454  24.575  1.00 25.53           C  
ATOM    564  CA  SER B 212     -22.628  33.866  27.672  1.00103.96           C  
ATOM    565  CA  VAL B 213     -23.275  31.172  30.256  1.00 62.87           C  
ATOM    566  CA  GLY B 214     -24.768  33.710  32.590  1.00 41.91           C  
ATOM    567  CA  ILE B 215     -21.558  34.078  34.512  1.00 55.76           C  
ATOM    568  CA  GLY B 216     -19.975  37.435  33.848  1.00 21.41           C  
ATOM    569  CA  PHE B 217     -17.477  39.481  35.781  1.00 44.00           C  
ATOM    570  CA  ALA B 218     -17.039  43.204  36.089  1.00 32.95           C  
ATOM    571  CA  ILE B 219     -14.576  45.438  37.835  1.00 73.74           C  
ATOM    572  CA  PRO B 220     -16.332  47.395  40.456  1.00 83.31           C  
ATOM    573  CA  SER B 221     -17.131  51.054  39.917  1.00 39.72           C  
ATOM    574  CA  ASN B 222     -15.219  52.000  42.968  1.00 61.07           C  
ATOM    575  CA  MET B 223     -12.564  50.150  41.210  1.00 95.73           C  
ATOM    576  CA  ALA B 224     -12.626  51.972  37.951  1.00 51.38           C  
ATOM    577  CA  ARG B 225     -13.383  55.320  39.450  1.00 90.86           C  
ATOM    578  CA  THR B 226     -10.410  55.916  41.604  1.00 63.32           C  
ATOM    579  CA  LEU B 227      -8.128  53.986  39.241  1.00117.26           C  
ATOM    580  CA  ALA B 228      -9.370  56.182  36.455  1.00 44.69           C  
ATOM    581  CA  GLN B 229      -8.983  59.214  38.616  1.00143.43           C  
ATOM    582  CA  GLN B 230      -5.265  59.236  38.989  1.00 96.71           C  
ATOM    583  CA  LEU B 231      -4.961  58.259  35.382  1.00 53.85           C  
ATOM    584  CA  ILE B 232      -6.054  61.788  34.864  1.00122.72           C  
ATOM    585  CA  ASP B 233      -4.836  62.919  38.317  1.00162.22           C  
ATOM    586  CA  PHE B 234      -2.909  62.431  40.483  1.00176.97           C  
ATOM    587  CA  GLY B 235      -1.205  60.048  38.171  1.00 42.06           C  
ATOM    588  CA  GLU B 236       1.417  59.108  40.651  1.00105.77           C  
ATOM    589  CA  ILE B 237       3.692  56.666  38.937  1.00136.20           C  
ATOM    590  CA  LYS B 238       3.334  54.306  41.823  1.00228.87           C  
ATOM    591  CA  ARG B 239       1.728  52.126  42.506  1.00215.51           C  
ATOM    592  CA  GLY B 240       0.497  52.399  38.957  1.00 47.42           C  
ATOM    593  CA  LEU B 241      -0.910  49.019  39.709  1.00185.03           C  
ATOM    594  CA  LEU B 242       1.524  46.486  40.993  1.00 93.56           C  
ATOM    595  CA  GLY B 243       2.254  44.538  37.849  1.00 52.14           C  
ATOM    596  CA  ILE B 244       1.779  40.984  39.051  1.00 74.77           C  
ATOM    597  CA  LYS B 245      -0.185  37.850  38.291  1.00163.42           C  
ATOM    598  CA  GLY B 246      -1.946  35.822  40.891  1.00 35.99           C  
ATOM    599  CA  THR B 247      -4.863  33.611  41.659  1.00 73.68           C  
ATOM    600  CA  GLU B 248      -6.760  32.064  44.544  1.00 55.51           C  
ATOM    601  CA  MET B 249      -4.978  30.028  47.128  1.00147.61           C  
ATOM    602  CA  SER B 250      -3.728  26.917  45.422  1.00 35.11           C  
ATOM    603  CA  ALA B 251      -4.778  23.539  46.691  1.00 37.66           C  
ATOM    604  CA  ASP B 252      -1.247  22.190  46.746  1.00 54.35           C  
ATOM    605  CA  ILE B 253       0.491  25.051  48.490  1.00 61.19           C  
ATOM    606  CA  ALA B 254      -2.323  25.952  50.824  1.00 58.02           C  
ATOM    607  CA  LYS B 255      -3.199  22.640  52.239  1.00155.09           C  
ATOM    608  CA  ALA B 256       0.194  21.075  52.473  1.00 75.88           C  
ATOM    609  CA  PHE B 257       2.512  23.666  53.905  1.00148.02           C  
ATOM    610  CA  ASN B 258      -0.218  25.368  55.651  1.00247.12           C  
ATOM    611  CA  LEU B 259      -0.126  29.001  54.991  1.00171.63           C  
ATOM    612  CA  ASP B 260       0.054  31.196  58.038  1.00 63.18           C  
ATOM    613  CA  VAL B 261      -2.755  33.322  56.704  1.00110.45           C  
ATOM    614  CA  GLN B 262      -5.680  31.140  55.813  1.00 87.76           C  
ATOM    615  CA  ARG B 263      -5.771  32.499  52.340  1.00171.30           C  
ATOM    616  CA  GLY B 264      -4.677  35.446  50.352  1.00 27.91           C  
ATOM    617  CA  ALA B 265      -3.911  36.662  46.928  1.00 41.63           C  
ATOM    618  CA  PHE B 266      -1.137  34.445  45.874  1.00130.55           C  
ATOM    619  CA  VAL B 267       1.266  35.559  43.266  1.00 67.65           C  
ATOM    620  CA  SER B 268       2.713  33.092  40.826  1.00102.50           C  
ATOM    621  CA  GLU B 269       4.701  35.642  38.925  1.00109.41           C  
ATOM    622  CA  VAL B 270       6.901  38.698  39.052  1.00101.64           C  
ATOM    623  CA  LEU B 271       6.646  41.203  36.258  1.00 56.14           C  
ATOM    624  CA  PRO B 272       9.730  42.766  34.909  1.00145.13           C  
ATOM    625  CA  GLY B 273      10.305  46.438  35.543  1.00 23.52           C  
ATOM    626  CA  SER B 274       7.034  46.074  37.297  1.00 89.32           C  
ATOM    627  CA  GLY B 275       5.937  47.710  40.426  1.00 35.12           C  
ATOM    628  CA  SER B 276       5.998  44.471  42.234  1.00 47.48           C  
ATOM    629  CA  ALA B 277       9.453  43.861  40.933  1.00 51.80           C  
ATOM    630  CA  LYS B 278      11.159  46.891  42.374  1.00117.40           C  
ATOM    631  CA  ALA B 279       9.010  46.766  45.458  1.00 39.39           C  
ATOM    632  CA  GLY B 280      10.667  43.480  45.852  1.00 39.77           C  
ATOM    633  CA  VAL B 281       7.545  41.405  45.929  1.00 67.37           C  
ATOM    634  CA  LYS B 282       8.251  38.261  44.191  1.00137.86           C  
ATOM    635  CA  ALA B 283       6.597  35.036  43.409  1.00 94.83           C  
ATOM    636  CA  GLY B 284       5.223  32.479  45.716  1.00 40.50           C  
ATOM    637  CA  ASP B 285       4.047  35.579  47.504  1.00106.16           C  
ATOM    638  CA  ILE B 286       1.023  35.572  49.496  1.00 95.19           C  
ATOM    639  CA  ILE B 287      -0.548  38.964  49.800  1.00 66.98           C  
ATOM    640  CA  THR B 288      -2.284  38.902  53.146  1.00 56.33           C  
ATOM    641  CA  SER B 289      -3.363  42.476  53.361  1.00104.94           C  
ATOM    642  CA  LEU B 290      -3.441  45.774  51.660  1.00 77.65           C  
ATOM    643  CA  ASN B 291      -3.110  48.857  53.779  1.00186.93           C  
ATOM    644  CA  GLY B 292      -3.916  48.939  57.486  1.00 52.27           C  
ATOM    645  CA  LYS B 293      -7.156  47.041  57.176  1.00 91.91           C  
ATOM    646  CA  PRO B 294      -6.991  43.392  56.487  1.00137.44           C  
ATOM    647  CA  LEU B 295      -7.319  42.021  52.984  1.00102.97           C  
ATOM    648  CA  ASN B 296      -9.410  39.049  52.140  1.00159.97           C  
ATOM    649  CA  SER B 297      -9.119  36.811  49.157  1.00 60.44           C  
ATOM    650  CA  PHE B 298      -7.463  37.655  45.922  1.00 91.71           C  
ATOM    651  CA  ALA B 299     -10.946  38.853  45.172  1.00 48.58           C  
ATOM    652  CA  GLU B 300     -10.906  41.602  47.686  1.00110.47           C  
ATOM    653  CA  LEU B 301      -7.490  42.392  46.400  1.00 71.82           C  
ATOM    654  CA  ARG B 302      -8.519  43.829  43.127  1.00161.03           C  
ATOM    655  CA  SER B 303     -11.607  45.171  44.722  1.00 55.22           C  
ATOM    656  CA  ARG B 304      -9.697  47.591  46.767  1.00252.64           C  
ATOM    657  CA  ILE B 305      -6.816  48.145  44.393  1.00 91.92           C  
ATOM    658  CA  ALA B 306      -8.878  48.241  41.314  1.00 69.62           C  
ATOM    659  CA  THR B 307     -10.791  50.672  43.413  1.00 58.91           C  
ATOM    660  CA  THR B 308      -7.832  52.718  44.370  1.00 74.48           C  
ATOM    661  CA  GLU B 309      -5.911  55.219  42.311  1.00 82.45           C  
ATOM    662  CA  PRO B 310      -3.441  53.557  40.127  1.00270.87           C  
ATOM    663  CA  GLY B 311      -1.308  55.321  41.238  1.00129.18           C  
ATOM    664  CA  THR B 312      -1.618  55.819  44.911  1.00125.95           C  
ATOM    665  CA  LYS B 313       1.283  54.713  46.982  1.00127.28           C  
ATOM    666  CA  VAL B 314       0.141  51.921  49.209  1.00 48.08           C  
ATOM    667  CA  LYS B 315       1.740  49.300  51.381  1.00 59.36           C  
ATOM    668  CA  LEU B 316       1.159  45.615  50.989  1.00105.76           C  
ATOM    669  CA  GLY B 317       1.377  42.843  53.489  1.00 51.11           C  
ATOM    670  CA  LEU B 318       2.475  39.479  52.321  1.00182.74           C  
ATOM    671  CA  LEU B 319       3.654  36.304  53.749  1.00114.86           C  
ATOM    672  CA  ARG B 320       6.803  35.006  52.542  1.00232.26           C  
ATOM    673  CA  ASN B 321       8.546  32.082  54.187  1.00205.64           C  
ATOM    674  CA  GLY B 322       6.056  32.155  56.873  1.00 48.39           C  
ATOM    675  CA  LYS B 323       7.304  35.508  57.775  1.00123.27           C  
ATOM    676  CA  PRO B 324       5.982  38.897  57.550  1.00153.83           C  
ATOM    677  CA  LEU B 325       6.991  42.105  55.785  1.00191.68           C  
ATOM    678  CA  GLU B 326       5.563  45.343  54.847  1.00113.35           C  
ATOM    679  CA  VAL B 327       6.636  46.932  51.623  1.00 54.46           C  
ATOM    680  CA  GLU B 328       5.573  49.978  49.707  1.00 82.20           C  
ATOM    681  CA  VAL B 329       4.418  49.093  46.254  1.00 49.98           C  
ATOM    682  CA  SER B 340      31.828  46.748  23.633  1.00 53.29           C  
ATOM    683  CA  ALA B 341      31.343  46.358  19.899  1.00 76.35           C  
ATOM    684  CA  GLU B 342      29.509  43.081  20.302  1.00 57.77           C  
ATOM    685  CA  MET B 343      26.119  44.354  21.218  1.00 58.81           C  
ATOM    686  CA  ILE B 344      26.023  46.844  18.414  1.00 90.63           C  
ATOM    687  CA  THR B 345      27.674  44.502  16.002  1.00 69.49           C  
ATOM    688  CA  PRO B 346      26.940  40.850  16.006  1.00156.17           C  
ATOM    689  CA  ALA B 347      29.428  38.366  17.407  1.00 71.58           C  
ATOM    690  CA  LEU B 348      32.222  40.839  16.646  1.00136.23           C  
ATOM    691  CA  GLU B 349      34.130  40.896  19.879  1.00140.48           C  
ATOM    692  CA  GLY B 350      36.243  43.953  20.141  1.00 28.71           C  
ATOM    693  CA  ALA B 351      36.768  47.379  21.559  1.00 35.63           C  
ATOM    694  CA  THR B 352      34.033  48.696  23.743  1.00101.39           C  
ATOM    695  CA  LEU B 353      31.894  51.522  22.532  1.00 56.25           C  
ATOM    696  CA  SER B 354      30.449  54.572  24.211  1.00 90.92           C  
ATOM    697  CA  ASP B 355      27.908  57.088  22.975  1.00 51.93           C  
ATOM    698  CA  GLY B 356      28.095  60.884  22.964  1.00 65.05           C  
ATOM    699  CA  GLN B 357      31.181  62.557  21.704  1.00217.97           C  
ATOM    700  CA  LEU B 358      32.107  62.125  25.064  1.00320.20           C  
ATOM    701  CA  LYS B 359      32.589  65.567  26.115  1.00207.40           C  
ATOM    702  CA  ASP B 360      31.580  67.571  23.170  1.00136.62           C  
ATOM    703  CA  GLY B 361      28.875  67.565  20.602  1.00 31.41           C  
ATOM    704  CA  GLY B 362      28.290  64.022  19.612  1.00 38.54           C  
ATOM    705  CA  LYS B 363      30.570  63.444  16.693  1.00105.33           C  
ATOM    706  CA  GLY B 364      29.488  59.887  17.062  1.00 31.13           C  
ATOM    707  CA  ILE B 365      30.098  56.711  18.990  1.00 65.96           C  
ATOM    708  CA  LYS B 366      33.449  56.339  20.659  1.00 88.97           C  
ATOM    709  CA  ILE B 367      35.410  53.145  20.801  1.00158.81           C  
ATOM    710  CA  ASP B 368      36.840  53.027  24.277  1.00 59.68           C  
ATOM    711  CA  GLU B 369      39.546  50.448  23.988  1.00 91.53           C  
ATOM    712  CA  VAL B 370      40.685  47.788  21.602  1.00121.49           C  
ATOM    713  CA  VAL B 371      40.764  44.185  22.793  1.00182.26           C  
ATOM    714  CA  LYS B 372      42.979  43.714  19.680  1.00151.08           C  
ATOM    715  CA  GLY B 373      43.073  39.937  19.778  1.00 35.85           C  
ATOM    716  CA  SER B 374      39.331  40.299  19.107  1.00 49.23           C  
ATOM    717  CA  PRO B 375      37.908  40.478  15.665  1.00159.68           C  
ATOM    718  CA  ALA B 376      36.652  44.018  16.080  1.00 45.02           C  
ATOM    719  CA  ALA B 377      40.368  44.615  16.109  1.00 50.60           C  
ATOM    720  CA  GLN B 378      41.014  42.534  13.030  1.00 60.79           C  
ATOM    721  CA  ALA B 379      39.038  44.693  10.601  1.00 66.42           C  
ATOM    722  CA  GLY B 380      40.679  47.981  11.469  1.00 62.50           C  
ATOM    723  CA  LEU B 381      38.969  49.267  14.553  1.00 64.24           C  
ATOM    724  CA  GLN B 382      41.465  50.986  16.795  1.00 68.55           C  
ATOM    725  CA  LYS B 383      40.759  52.759  20.038  1.00138.21           C  
ATOM    726  CA  ASP B 384      39.908  56.455  20.230  1.00 84.49           C  
ATOM    727  CA  ASP B 385      38.176  56.355  16.902  1.00 62.22           C  
ATOM    728  CA  VAL B 386      34.908  58.197  16.616  1.00 56.97           C  
ATOM    729  CA  ILE B 387      32.337  56.742  14.320  1.00 60.07           C  
ATOM    730  CA  ILE B 388      30.753  59.748  12.713  1.00 79.77           C  
ATOM    731  CA  GLY B 389      28.179  57.770  10.813  1.00 55.31           C  
ATOM    732  CA  VAL B 390      27.431  54.607   8.895  1.00 69.76           C  
ATOM    733  CA  ASN B 391      26.411  54.111   5.283  1.00 79.42           C  
ATOM    734  CA  ARG B 392      26.052  57.762   4.381  1.00163.48           C  
ATOM    735  CA  ASP B 393      24.141  58.131   7.603  1.00 52.34           C  
ATOM    736  CA  ARG B 394      25.349  60.282  10.420  1.00113.60           C  
ATOM    737  CA  VAL B 395      25.621  58.506  13.723  1.00 44.58           C  
ATOM    738  CA  ASN B 396      25.061  60.826  16.647  1.00 48.87           C  
ATOM    739  CA  SER B 397      25.036  58.027  19.152  1.00 43.29           C  
ATOM    740  CA  ILE B 398      24.672  54.299  19.587  1.00 41.62           C  
ATOM    741  CA  ALA B 399      20.961  54.310  18.970  1.00 23.70           C  
ATOM    742  CA  GLU B 400      21.324  55.886  15.566  1.00 32.70           C  
ATOM    743  CA  MET B 401      24.137  53.567  14.643  1.00 29.18           C  
ATOM    744  CA  ARG B 402      21.915  50.700  15.594  1.00148.72           C  
ATOM    745  CA  LYS B 403      19.341  52.092  13.227  1.00117.58           C  
ATOM    746  CA  VAL B 404      21.566  51.844  10.186  1.00 30.90           C  
ATOM    747  CA  LEU B 405      22.410  48.345  11.331  1.00 99.21           C  
ATOM    748  CA  ALA B 406      18.712  47.638  11.577  1.00 32.77           C  
ATOM    749  CA  ALA B 407      18.583  48.028   7.823  1.00 39.49           C  
ATOM    750  CA  LYS B 408      21.156  45.280   7.809  1.00138.77           C  
ATOM    751  CA  PRO B 409      22.902  46.315   4.636  1.00161.78           C  
ATOM    752  CA  ALA B 410      25.185  43.670   3.273  1.00 30.07           C  
ATOM    753  CA  ILE B 411      27.744  46.422   3.173  1.00134.81           C  
ATOM    754  CA  ILE B 412      28.341  48.469   6.245  1.00105.08           C  
ATOM    755  CA  ALA B 413      30.642  51.384   5.948  1.00 56.14           C  
ATOM    756  CA  LEU B 414      31.924  53.032   9.072  1.00125.81           C  
ATOM    757  CA  GLN B 415      33.754  56.262   8.838  1.00216.45           C  
ATOM    758  CA  ILE B 416      35.418  57.282  11.907  1.00121.11           C  
ATOM    759  CA  VAL B 417      37.716  60.123  12.558  1.00 47.95           C  
ATOM    760  CA  ARG B 418      41.107  59.142  13.815  1.00161.04           C  
ATOM    761  CA  GLY B 419      43.401  61.865  14.938  1.00 21.04           C  
ATOM    762  CA  ASN B 420      42.861  64.750  12.629  1.00 48.98           C  
ATOM    763  CA  GLU B 421      41.817  62.725   9.644  1.00 93.68           C  
ATOM    764  CA  SER B 422      38.957  60.796   8.191  1.00 49.34           C  
ATOM    765  CA  ILE B 423      38.941  57.045   8.380  1.00107.03           C  
ATOM    766  CA  TYR B 424      36.696  54.488   6.887  1.00173.01           C  
ATOM    767  CA  LEU B 425      35.987  51.161   8.318  1.00 98.66           C  
ATOM    768  CA  LEU B 426      33.822  48.393   7.182  1.00145.65           C  
ATOM    769  CA  MET B 427      32.206  45.074   7.644  1.00 61.05           C  
TER     770      MET B 427                                                      
ATOM    771  CA  PRO C  11     -42.225  41.684  44.565  1.00 73.00           C  
ATOM    772  CA  LEU C  12     -43.861  39.263  42.185  1.00 89.67           C  
ATOM    773  CA  PRO C  13     -46.390  40.581  39.795  1.00153.38           C  
ATOM    774  CA  SER C  14     -46.792  37.741  39.832  1.00122.39           C  
ATOM    775  CA  LEU C  15     -46.445  36.470  36.286  1.00111.77           C  
ATOM    776  CA  ALA C  16     -48.688  33.477  36.903  1.00 40.24           C  
ATOM    777  CA  PRO C  17     -51.893  35.356  37.264  1.00 67.08           C  
ATOM    778  CA  MET C  18     -51.408  37.072  33.943  1.00 34.60           C  
ATOM    779  CA  LEU C  19     -50.317  33.827  32.337  1.00 49.02           C  
ATOM    780  CA  GLU C  20     -53.265  31.865  33.559  1.00 63.01           C  
ATOM    781  CA  LYS C  21     -55.705  33.802  31.459  1.00 53.22           C  
ATOM    782  CA  VAL C  22     -53.474  34.360  28.412  1.00107.00           C  
ATOM    783  CA  LEU C  23     -51.842  30.980  27.905  1.00116.06           C  
ATOM    784  CA  PRO C  24     -54.743  29.203  26.324  1.00 63.37           C  
ATOM    785  CA  ALA C  25     -54.459  31.723  23.512  1.00 36.43           C  
ATOM    786  CA  VAL C  26     -51.095  30.434  22.432  1.00105.26           C  
ATOM    787  CA  VAL C  27     -51.133  27.158  20.602  1.00120.41           C  
ATOM    788  CA  SER C  28     -48.765  24.596  19.206  1.00 46.67           C  
ATOM    789  CA  VAL C  29     -48.798  24.025  15.492  1.00 35.38           C  
ATOM    790  CA  ARG C  30     -48.034  20.637  14.051  1.00 87.19           C  
ATOM    791  CA  VAL C  31     -47.379  20.088  10.412  1.00 46.63           C  
ATOM    792  CA  GLU C  32     -46.540  17.328   8.010  1.00104.32           C  
ATOM    793  CA  GLY C  33     -45.914  17.469   4.329  1.00 31.25           C  
ATOM    794  CA  THR C  34     -43.656  17.059   1.341  1.00112.56           C  
ATOM    795  CA  ALA C  35     -40.906  14.643  -1.365  1.00 21.13           C  
ATOM    796  CA  GLN C  59     -39.922  12.787   1.753  1.00 66.76           C  
ATOM    797  CA  PRO C  60     -42.310  13.271   4.568  1.00 70.33           C  
ATOM    798  CA  PHE C  61     -41.386  15.504   7.434  1.00 54.38           C  
ATOM    799  CA  GLU C  62     -42.991  16.513  10.668  1.00 31.06           C  
ATOM    800  CA  GLY C  63     -42.457  19.935  12.090  1.00 17.45           C  
ATOM    801  CA  LEU C  64     -43.448  21.651  15.279  1.00 39.41           C  
ATOM    802  CA  GLY C  65     -44.077  25.325  15.818  1.00 21.07           C  
ATOM    803  CA  SER C  66     -46.411  27.625  17.674  1.00 78.53           C  
ATOM    804  CA  GLY C  67     -49.133  30.087  16.849  1.00 17.16           C  
ATOM    805  CA  VAL C  68     -51.413  32.588  18.506  1.00 39.04           C  
ATOM    806  CA  ILE C  69     -55.158  32.739  18.336  1.00 52.93           C  
ATOM    807  CA  ILE C  70     -56.075  36.170  17.063  1.00175.44           C  
ATOM    808  CA  ASN C  71     -59.802  35.546  16.700  1.00176.12           C  
ATOM    809  CA  ALA C  72     -61.516  33.108  18.957  1.00 43.80           C  
ATOM    810  CA  SER C  73     -64.724  33.178  17.008  1.00 43.74           C  
ATOM    811  CA  LYS C  74     -63.215  32.804  13.589  1.00 92.72           C  
ATOM    812  CA  GLY C  75     -60.459  30.579  14.834  1.00 29.01           C  
ATOM    813  CA  TYR C  76     -57.727  32.557  13.144  1.00 79.26           C  
ATOM    814  CA  VAL C  77     -54.250  31.714  14.308  1.00 49.77           C  
ATOM    815  CA  LEU C  78     -51.166  33.667  13.398  1.00 59.30           C  
ATOM    816  CA  THR C  79     -47.968  31.818  12.757  1.00119.24           C  
ATOM    817  CA  ASN C  80     -44.724  32.131  10.907  1.00 59.96           C  
ATOM    818  CA  ASN C  81     -44.771  31.321   7.235  1.00 49.47           C  
ATOM    819  CA  HIS C  82     -41.760  29.098   7.534  1.00 55.83           C  
ATOM    820  CA  VAL C  83     -43.490  26.901  10.019  1.00 39.82           C  
ATOM    821  CA  ILE C  84     -46.438  26.386   7.656  1.00 81.40           C  
ATOM    822  CA  ASN C  85     -44.783  26.618   4.250  1.00 84.61           C  
ATOM    823  CA  GLN C  86     -44.198  22.938   3.527  1.00144.01           C  
ATOM    824  CA  ALA C  87     -47.244  21.710   5.410  1.00 75.13           C  
ATOM    825  CA  GLN C  88     -49.592  19.424   3.548  1.00143.19           C  
ATOM    826  CA  LYS C  89     -51.679  19.118   6.669  1.00 29.87           C  
ATOM    827  CA  ILE C  90     -51.769  21.318   9.700  1.00 38.89           C  
ATOM    828  CA  SER C  91     -53.034  20.620  13.178  1.00 86.01           C  
ATOM    829  CA  ILE C  92     -53.404  22.924  16.120  1.00 93.13           C  
ATOM    830  CA  GLN C  93     -53.114  21.763  19.686  1.00125.69           C  
ATOM    831  CA  LEU C  94     -54.430  23.676  22.657  1.00 47.73           C  
ATOM    832  CA  ASN C  95     -52.730  23.656  26.021  1.00 34.91           C  
ATOM    833  CA  ASP C  96     -55.734  21.754  27.293  1.00 47.53           C  
ATOM    834  CA  GLY C  97     -54.895  18.934  24.935  1.00 25.44           C  
ATOM    835  CA  ARG C  98     -57.704  19.498  22.486  1.00 90.31           C  
ATOM    836  CA  GLU C  99     -56.599  19.333  18.886  1.00 38.29           C  
ATOM    837  CA  PHE C 100     -58.070  20.750  15.725  1.00 44.23           C  
ATOM    838  CA  ASP C 101     -57.323  20.816  12.033  1.00 36.70           C  
ATOM    839  CA  ALA C 102     -56.384  24.043  10.370  1.00 30.40           C  
ATOM    840  CA  LYS C 103     -56.274  25.412   6.864  1.00 56.46           C  
ATOM    841  CA  LEU C 104     -53.907  28.023   5.570  1.00 46.08           C  
ATOM    842  CA  ILE C 105     -55.805  31.202   4.938  1.00132.61           C  
ATOM    843  CA  GLY C 106     -52.832  32.954   3.443  1.00 24.46           C  
ATOM    844  CA  SER C 107     -49.277  33.917   4.151  1.00 48.56           C  
ATOM    845  CA  ASP C 108     -46.339  35.782   2.792  1.00 83.46           C  
ATOM    846  CA  ASP C 109     -42.672  34.934   2.614  1.00128.15           C  
ATOM    847  CA  GLN C 110     -40.999  38.276   2.878  1.00 82.46           C  
ATOM    848  CA  SER C 111     -42.404  39.238   6.291  1.00 62.51           C  
ATOM    849  CA  ASP C 112     -42.797  35.567   7.188  1.00 74.86           C  
ATOM    850  CA  ILE C 113     -46.340  35.910   8.483  1.00 66.06           C  
ATOM    851  CA  ALA C 114     -49.029  33.331   7.885  1.00 34.92           C  
ATOM    852  CA  LEU C 115     -52.658  33.099   8.880  1.00107.69           C  
ATOM    853  CA  LEU C 116     -54.350  29.826   9.701  1.00 48.92           C  
ATOM    854  CA  GLN C 117     -57.958  29.035  10.400  1.00 43.98           C  
ATOM    855  CA  ILE C 118     -59.071  26.336  12.755  1.00 61.11           C  
ATOM    856  CA  GLN C 119     -61.918  24.199  11.599  1.00122.08           C  
ATOM    857  CA  ASN C 120     -64.828  24.182  14.017  1.00 68.12           C  
ATOM    858  CA  PRO C 121     -62.904  26.171  16.539  1.00104.95           C  
ATOM    859  CA  SER C 122     -65.214  25.845  19.588  1.00247.04           C  
ATOM    860  CA  LYS C 123     -64.478  27.522  22.910  1.00 80.05           C  
ATOM    861  CA  LEU C 124     -61.248  29.247  22.107  1.00 87.66           C  
ATOM    862  CA  THR C 125     -59.483  32.039  23.883  1.00 97.50           C  
ATOM    863  CA  GLN C 126     -58.145  35.031  22.022  1.00107.43           C  
ATOM    864  CA  ILE C 127     -55.098  37.099  22.769  1.00104.16           C  
ATOM    865  CA  ALA C 128     -55.299  40.877  22.810  1.00 30.43           C  
ATOM    866  CA  ILE C 129     -52.869  42.791  20.664  1.00 94.79           C  
ATOM    867  CA  ALA C 130     -50.814  45.661  21.993  1.00 36.19           C  
ATOM    868  CA  ASP C 131     -49.359  48.565  20.058  1.00 39.98           C  
ATOM    869  CA  SER C 132     -45.846  47.579  19.036  1.00 39.88           C  
ATOM    870  CA  ASP C 133     -44.909  51.141  18.311  1.00 39.19           C  
ATOM    871  CA  LYS C 134     -45.366  51.901  21.996  1.00 97.89           C  
ATOM    872  CA  LEU C 135     -42.685  49.439  23.034  1.00 57.30           C  
ATOM    873  CA  ARG C 136     -39.470  50.787  24.437  1.00 92.75           C  
ATOM    874  CA  VAL C 137     -36.325  48.989  25.392  1.00 81.66           C  
ATOM    875  CA  GLY C 138     -36.466  47.707  28.917  1.00 22.98           C  
ATOM    876  CA  ASP C 139     -40.070  46.660  28.749  1.00 27.07           C  
ATOM    877  CA  PHE C 140     -40.683  43.207  30.122  1.00 47.45           C  
ATOM    878  CA  ALA C 141     -41.622  40.451  27.749  1.00 28.97           C  
ATOM    879  CA  VAL C 142     -42.699  36.860  28.056  1.00 32.98           C  
ATOM    880  CA  ALA C 143     -42.329  34.373  25.276  1.00 31.07           C  
ATOM    881  CA  VAL C 144     -44.618  31.430  24.912  1.00106.81           C  
ATOM    882  CA  GLY C 145     -44.257  28.618  22.435  1.00 24.69           C  
ATOM    883  CA  ASN C 146     -43.087  25.071  22.231  1.00 66.08           C  
ATOM    884  CA  PRO C 147     -39.400  24.775  22.226  1.00101.65           C  
ATOM    885  CA  PHE C 148     -38.076  21.372  21.267  1.00 64.00           C  
ATOM    886  CA  GLY C 149     -41.711  20.374  21.087  1.00 23.88           C  
ATOM    887  CA  LEU C 150     -41.734  19.978  24.840  1.00 85.42           C  
ATOM    888  CA  GLY C 151     -45.109  21.593  25.203  1.00 27.94           C  
ATOM    889  CA  GLN C 152     -46.296  25.039  26.091  1.00 50.39           C  
ATOM    890  CA  THR C 153     -43.352  26.811  27.664  1.00 37.76           C  
ATOM    891  CA  ALA C 154     -43.065  30.326  28.953  1.00 32.57           C  
ATOM    892  CA  THR C 155     -39.845  32.240  29.224  1.00107.07           C  
ATOM    893  CA  SER C 156     -39.209  35.717  30.525  1.00 33.37           C  
ATOM    894  CA  GLY C 157     -36.984  38.565  29.458  1.00 25.12           C  
ATOM    895  CA  ILE C 158     -36.937  42.208  28.441  1.00 60.87           C  
ATOM    896  CA  VAL C 159     -37.195  43.975  25.124  1.00 41.95           C  
ATOM    897  CA  SER C 160     -33.571  44.306  24.174  1.00 87.92           C  
ATOM    898  CA  ALA C 161     -34.000  46.361  21.027  1.00 40.90           C  
ATOM    899  CA  LEU C 162     -36.443  47.348  18.331  1.00 91.30           C  
ATOM    900  CA  GLY C 163     -36.374  48.208  14.676  1.00 32.26           C  
ATOM    901  CA  ARG C 164     -33.598  45.861  13.925  1.00 69.58           C  
ATOM    902  CA  SER C 165     -32.672  44.553  10.541  1.00 85.35           C  
ATOM    903  CA  GLY C 166     -30.011  43.579   8.167  1.00 35.98           C  
ATOM    904  CA  LEU C 167     -30.153  40.188   9.820  1.00 50.58           C  
ATOM    905  CA  ASN C 168     -30.985  38.893   6.365  1.00 65.35           C  
ATOM    906  CA  LEU C 169     -33.292  36.432   7.997  1.00 54.14           C  
ATOM    907  CA  GLU C 170     -36.298  37.769   6.138  1.00111.54           C  
ATOM    908  CA  GLY C 171     -37.050  39.934   3.135  1.00 38.52           C  
ATOM    909  CA  LEU C 172     -38.736  42.502   5.289  1.00120.54           C  
ATOM    910  CA  GLU C 173     -37.467  42.752   8.753  1.00 74.37           C  
ATOM    911  CA  ASN C 174     -38.103  44.876  11.799  1.00103.77           C  
ATOM    912  CA  PHE C 175     -37.519  42.555  14.581  1.00 86.02           C  
ATOM    913  CA  ILE C 176     -38.158  43.276  18.173  1.00 73.89           C  
ATOM    914  CA  GLN C 177     -35.170  41.833  19.952  1.00 58.07           C  
ATOM    915  CA  THR C 178     -35.701  39.939  23.179  1.00136.90           C  
ATOM    916  CA  ASP C 179     -33.553  38.295  25.825  1.00 74.34           C  
ATOM    917  CA  ALA C 180     -36.314  35.803  26.584  1.00 46.42           C  
ATOM    918  CA  SER C 181     -35.178  32.302  25.848  1.00 46.87           C  
ATOM    919  CA  ILE C 182     -36.278  31.403  22.383  1.00 65.13           C  
ATOM    920  CA  ASN C 183     -35.373  28.107  20.832  1.00 51.74           C  
ATOM    921  CA  ARG C 184     -36.435  26.038  17.897  1.00 98.24           C  
ATOM    922  CA  GLY C 185     -40.141  25.376  18.032  1.00 25.69           C  
ATOM    923  CA  ASN C 186     -40.754  28.855  19.376  1.00139.87           C  
ATOM    924  CA  ALA C 187     -41.511  30.125  15.891  1.00 50.02           C  
ATOM    925  CA  GLY C 188     -44.989  31.485  15.464  1.00 23.23           C  
ATOM    926  CA  GLY C 189     -45.198  31.763  19.214  1.00 25.03           C  
ATOM    927  CA  ALA C 190     -46.187  34.841  21.085  1.00 48.53           C  
ATOM    928  CA  LEU C 191     -44.209  37.492  22.835  1.00 86.61           C  
ATOM    929  CA  LEU C 192     -46.347  39.083  25.460  1.00 56.30           C  
ATOM    930  CA  ASN C 193     -46.169  42.106  27.680  1.00 53.91           C  
ATOM    931  CA  LEU C 194     -47.007  42.054  31.369  1.00 95.07           C  
ATOM    932  CA  ASN C 195     -50.587  42.689  30.371  1.00 47.56           C  
ATOM    933  CA  GLY C 196     -50.535  39.470  28.448  1.00 26.72           C  
ATOM    934  CA  GLU C 197     -51.058  41.429  25.257  1.00 41.49           C  
ATOM    935  CA  LEU C 198     -49.236  40.366  22.114  1.00 70.17           C  
ATOM    936  CA  ILE C 199     -46.223  42.525  21.327  1.00160.16           C  
ATOM    937  CA  GLY C 200     -44.952  40.328  18.511  1.00 32.35           C  
ATOM    938  CA  ILE C 201     -44.536  36.868  17.037  1.00 45.46           C  
ATOM    939  CA  ASN C 202     -41.229  35.136  17.689  1.00 84.71           C  
ATOM    940  CA  THR C 203     -39.651  34.589  14.299  1.00 85.32           C  
ATOM    941  CA  ALA C 204     -36.017  33.650  14.825  1.00 55.42           C  
ATOM    942  CA  ILE C 205     -32.866  33.625  16.911  1.00 96.25           C  
ATOM    943  CA  LEU C 206     -29.190  34.277  16.405  1.00 57.63           C  
ATOM    944  CA  ALA C 207     -27.237  31.532  18.032  1.00 41.35           C  
ATOM    945  CA  PRO C 208     -23.971  30.057  17.093  1.00 67.85           C  
ATOM    946  CA  GLY C 209     -24.808  26.909  19.033  1.00 30.40           C  
ATOM    947  CA  GLY C 210     -28.273  26.577  17.638  1.00 25.39           C  
ATOM    948  CA  GLY C 211     -29.438  27.149  21.177  1.00 26.41           C  
ATOM    949  CA  SER C 212     -30.729  30.353  22.694  1.00 57.31           C  
ATOM    950  CA  VAL C 213     -27.931  32.878  23.163  1.00137.47           C  
ATOM    951  CA  GLY C 214     -30.370  35.374  24.542  1.00 38.79           C  
ATOM    952  CA  ILE C 215     -30.721  37.117  21.226  1.00104.19           C  
ATOM    953  CA  GLY C 216     -34.163  36.492  19.797  1.00 22.19           C  
ATOM    954  CA  PHE C 217     -36.203  38.351  17.241  1.00 46.72           C  
ATOM    955  CA  ALA C 218     -39.916  38.754  16.791  1.00 37.44           C  
ATOM    956  CA  ILE C 219     -42.118  40.461  14.274  1.00 71.79           C  
ATOM    957  CA  PRO C 220     -43.939  43.252  15.894  1.00 86.91           C  
ATOM    958  CA  SER C 221     -47.600  42.870  16.760  1.00 44.73           C  
ATOM    959  CA  ASN C 222     -48.466  45.835  14.681  1.00 64.56           C  
ATOM    960  CA  MET C 223     -46.696  43.861  12.124  1.00104.60           C  
ATOM    961  CA  ALA C 224     -48.646  40.690  12.410  1.00 50.41           C  
ATOM    962  CA  ARG C 225     -51.913  42.383  13.104  1.00 85.22           C  
ATOM    963  CA  THR C 226     -52.467  44.382  10.005  1.00 69.62           C  
ATOM    964  CA  LEU C 227     -50.662  41.818   7.866  1.00 95.55           C  
ATOM    965  CA  ALA C 228     -52.937  39.186   9.288  1.00 52.58           C  
ATOM    966  CA  GLN C 229     -55.892  41.421   8.763  1.00166.00           C  
ATOM    967  CA  GLN C 230     -55.888  41.531   5.039  1.00105.37           C  
ATOM    968  CA  LEU C 231     -55.168  37.861   4.953  1.00138.63           C  
ATOM    969  CA  ILE C 232     -58.679  37.615   6.184  1.00 88.96           C  
ATOM    970  CA  ASP C 233     -59.624  41.018   4.683  1.00166.81           C  
ATOM    971  CA  PHE C 234     -59.042  43.077   2.634  1.00215.91           C  
ATOM    972  CA  GLY C 235     -56.824  40.525   1.059  1.00 41.30           C  
ATOM    973  CA  GLU C 236     -55.780  42.752  -1.746  1.00 86.94           C  
ATOM    974  CA  ILE C 237     -53.432  40.705  -3.835  1.00 88.88           C  
ATOM    975  CA  LYS C 238     -50.972  43.541  -3.805  1.00203.83           C  
ATOM    976  CA  ARG C 239     -48.732  44.235  -2.299  1.00217.72           C  
ATOM    977  CA  GLY C 240     -49.174  40.834  -0.760  1.00 49.25           C  
ATOM    978  CA  LEU C 241     -45.743  41.523   0.553  1.00184.00           C  
ATOM    979  CA  LEU C 242     -43.182  42.429  -2.014  1.00 91.11           C  
ATOM    980  CA  GLY C 243     -41.403  39.131  -2.455  1.00 51.72           C  
ATOM    981  CA  ILE C 244     -37.799  40.211  -2.069  1.00 68.13           C  
ATOM    982  CA  LYS C 245     -34.669  39.438  -0.097  1.00168.58           C  
ATOM    983  CA  GLY C 246     -32.527  42.080   1.460  1.00 38.97           C  
ATOM    984  CA  THR C 247     -30.261  43.004   4.290  1.00 75.43           C  
ATOM    985  CA  GLU C 248     -28.564  45.970   5.912  1.00100.47           C  
ATOM    986  CA  MET C 249     -26.372  48.260   3.914  1.00 56.82           C  
ATOM    987  CA  SER C 250     -23.369  46.282   2.870  1.00 34.79           C  
ATOM    988  CA  ALA C 251     -19.921  47.452   3.779  1.00 39.22           C  
ATOM    989  CA  ASP C 252     -18.652  47.156   0.250  1.00 97.14           C  
ATOM    990  CA  ILE C 253     -21.494  48.894  -1.510  1.00163.90           C  
ATOM    991  CA  ALA C 254     -22.085  51.566   1.038  1.00 56.22           C  
ATOM    992  CA  LYS C 255     -18.646  52.768   1.739  1.00 74.32           C  
ATOM    993  CA  ALA C 256     -17.203  52.749  -1.686  1.00 74.31           C  
ATOM    994  CA  PHE C 257     -19.656  54.152  -4.122  1.00192.65           C  
ATOM    995  CA  ASN C 258     -21.363  55.945  -1.413  1.00239.83           C  
ATOM    996  CA  LEU C 259     -25.051  55.643  -1.611  1.00135.62           C  
ATOM    997  CA  ASP C 260     -27.046  58.752  -2.074  1.00 67.57           C  
ATOM    998  CA  VAL C 261     -29.214  57.674   0.819  1.00106.67           C  
ATOM    999  CA  GLN C 262     -27.063  57.018   3.830  1.00 87.34           C  
ATOM   1000  CA  ARG C 263     -28.598  53.645   4.241  1.00135.66           C  
ATOM   1001  CA  GLY C 264     -31.661  51.720   3.368  1.00 24.43           C  
ATOM   1002  CA  ALA C 265     -33.052  48.308   2.890  1.00 40.67           C  
ATOM   1003  CA  PHE C 266     -30.893  46.884   0.232  1.00134.32           C  
ATOM   1004  CA  VAL C 267     -32.159  44.125  -1.925  1.00 68.41           C  
ATOM   1005  CA  SER C 268     -29.839  41.411  -3.126  1.00107.04           C  
ATOM   1006  CA  GLU C 269     -32.459  39.484  -4.998  1.00111.08           C  
ATOM   1007  CA  VAL C 270     -35.555  39.525  -7.145  1.00100.87           C  
ATOM   1008  CA  LEU C 271     -38.240  36.919  -6.652  1.00 95.16           C  
ATOM   1009  CA  PRO C 272     -39.915  35.420  -9.605  1.00144.42           C  
ATOM   1010  CA  GLY C 273     -43.563  36.179 -10.236  1.00 24.49           C  
ATOM   1011  CA  SER C 274     -42.985  38.251  -7.188  1.00 44.01           C  
ATOM   1012  CA  GLY C 275     -44.475  41.533  -6.350  1.00 32.67           C  
ATOM   1013  CA  SER C 276     -41.129  43.130  -6.570  1.00 44.19           C  
ATOM   1014  CA  ALA C 277     -40.633  41.466  -9.882  1.00 56.44           C  
ATOM   1015  CA  LYS C 278     -43.535  42.936 -11.753  1.00152.70           C  
ATOM   1016  CA  ALA C 279     -43.236  46.184  -9.885  1.00 43.79           C  
ATOM   1017  CA  GLY C 280     -39.926  46.214 -11.556  1.00 39.53           C  
ATOM   1018  CA  VAL C 281     -37.852  46.480  -8.445  1.00 68.52           C  
ATOM   1019  CA  LYS C 282     -34.810  44.505  -8.957  1.00138.47           C  
ATOM   1020  CA  ALA C 283     -31.640  43.723  -7.206  1.00 96.05           C  
ATOM   1021  CA  GLY C 284     -28.947  46.003  -6.062  1.00 39.73           C  
ATOM   1022  CA  ASP C 285     -31.941  48.068  -5.080  1.00104.21           C  
ATOM   1023  CA  ILE C 286     -31.805  50.360  -2.260  1.00 87.33           C  
ATOM   1024  CA  ILE C 287     -35.182  50.965  -0.734  1.00 66.47           C  
ATOM   1025  CA  THR C 288     -34.928  54.438   0.684  1.00 52.91           C  
ATOM   1026  CA  SER C 289     -38.445  54.900   1.758  1.00 53.09           C  
ATOM   1027  CA  LEU C 290     -41.881  53.441   1.986  1.00 72.84           C  
ATOM   1028  CA  ASN C 291     -44.845  55.681   1.386  1.00176.25           C  
ATOM   1029  CA  GLY C 292     -44.696  59.445   1.916  1.00 52.94           C  
ATOM   1030  CA  LYS C 293     -42.925  59.256   5.248  1.00 74.99           C  
ATOM   1031  CA  PRO C 294     -39.304  58.389   5.129  1.00 64.05           C  
ATOM   1032  CA  LEU C 295     -38.079  54.863   5.662  1.00 97.11           C  
ATOM   1033  CA  ASN C 296     -35.325  53.937   8.016  1.00 80.77           C  
ATOM   1034  CA  SER C 297     -33.073  50.960   7.870  1.00 48.38           C  
ATOM   1035  CA  PHE C 298     -33.989  47.567   6.595  1.00 75.09           C  
ATOM   1036  CA  ALA C 299     -35.254  47.193  10.107  1.00 46.70           C  
ATOM   1037  CA  GLU C 300     -37.836  49.886   9.864  1.00106.48           C  
ATOM   1038  CA  LEU C 301     -38.781  48.391   6.566  1.00 75.21           C  
ATOM   1039  CA  ARG C 302     -40.398  45.299   7.846  1.00195.27           C  
ATOM   1040  CA  SER C 303     -41.605  47.158  10.843  1.00 62.91           C  
ATOM   1041  CA  ARG C 304     -43.942  49.134   8.761  1.00178.56           C  
ATOM   1042  CA  ILE C 305     -44.573  46.589   6.059  1.00125.71           C  
ATOM   1043  CA  ALA C 306     -44.842  43.707   8.388  1.00 67.97           C  
ATOM   1044  CA  THR C 307     -47.187  45.947  10.212  1.00163.74           C  
ATOM   1045  CA  THR C 308     -49.125  46.849   7.111  1.00 69.50           C  
ATOM   1046  CA  GLU C 309     -51.750  44.721   5.439  1.00 94.77           C  
ATOM   1047  CA  PRO C 310     -50.253  42.324   3.071  1.00189.05           C  
ATOM   1048  CA  GLY C 311     -51.942  43.408   0.906  1.00123.36           C  
ATOM   1049  CA  THR C 312     -52.220  47.133   0.938  1.00 46.23           C  
ATOM   1050  CA  LYS C 313     -51.074  48.864  -2.175  1.00 96.21           C  
ATOM   1051  CA  VAL C 314     -48.074  50.948  -1.337  1.00 49.83           C  
ATOM   1052  CA  LYS C 315     -45.402  52.896  -3.157  1.00 74.23           C  
ATOM   1053  CA  LEU C 316     -41.735  52.356  -2.579  1.00109.60           C  
ATOM   1054  CA  GLY C 317     -38.843  54.684  -3.018  1.00 50.51           C  
ATOM   1055  CA  LEU C 318     -35.560  53.230  -4.012  1.00180.60           C  
ATOM   1056  CA  LEU C 319     -32.322  54.373  -5.314  1.00118.67           C  
ATOM   1057  CA  ARG C 320     -31.069  52.766  -8.305  1.00233.86           C  
ATOM   1058  CA  ASN C 321     -28.048  54.049 -10.190  1.00207.92           C  
ATOM   1059  CA  GLY C 322     -27.975  56.972  -7.984  1.00 50.12           C  
ATOM   1060  CA  LYS C 323     -31.238  57.941  -9.380  1.00134.18           C  
ATOM   1061  CA  PRO C 324     -34.655  58.019  -8.062  1.00115.80           C  
ATOM   1062  CA  LEU C 325     -37.979  56.367  -8.871  1.00197.43           C  
ATOM   1063  CA  GLU C 326     -41.286  55.800  -7.370  1.00118.53           C  
ATOM   1064  CA  VAL C 327     -42.938  52.515  -8.044  1.00115.74           C  
ATOM   1065  CA  GLU C 328     -46.143  50.924  -6.852  1.00 49.44           C  
ATOM   1066  CA  VAL C 329     -45.524  47.535  -5.409  1.00 57.51           C  
ATOM   1067  CA  SER C 340     -48.277  25.255 -29.772  1.00109.11           C  
ATOM   1068  CA  ALA C 341     -47.769  21.485 -29.634  1.00 76.99           C  
ATOM   1069  CA  GLU C 342     -44.495  22.105 -27.835  1.00 82.09           C  
ATOM   1070  CA  MET C 343     -45.689  22.509 -24.336  1.00 73.52           C  
ATOM   1071  CA  ILE C 344     -47.955  19.553 -24.393  1.00 54.82           C  
ATOM   1072  CA  THR C 345     -45.469  17.495 -26.279  1.00 67.85           C  
ATOM   1073  CA  PRO C 346     -41.804  17.806 -25.638  1.00153.29           C  
ATOM   1074  CA  ALA C 347     -39.512  19.588 -28.062  1.00 68.92           C  
ATOM   1075  CA  LEU C 348     -41.926  18.771 -30.867  1.00 83.66           C  
ATOM   1076  CA  GLU C 349     -42.464  22.110 -32.469  1.00 75.66           C  
ATOM   1077  CA  GLY C 350     -45.520  22.186 -34.603  1.00 27.93           C  
ATOM   1078  CA  ALA C 351     -49.083  23.260 -34.966  1.00 40.34           C  
ATOM   1079  CA  THR C 352     -50.630  25.102 -32.109  1.00106.53           C  
ATOM   1080  CA  LEU C 353     -53.256  23.478 -30.010  1.00 63.98           C  
ATOM   1081  CA  SER C 354     -56.365  24.794 -28.335  1.00 89.02           C  
ATOM   1082  CA  ASP C 355     -58.533  23.136 -25.757  1.00 42.71           C  
ATOM   1083  CA  GLY C 356     -62.231  22.672 -25.900  1.00 44.91           C  
ATOM   1084  CA  GLN C 357     -64.144  21.457 -28.894  1.00163.23           C  
ATOM   1085  CA  LEU C 358     -64.325  25.098 -28.863  1.00198.79           C  
ATOM   1086  CA  LYS C 359     -67.055  25.163 -31.468  1.00 72.21           C  
ATOM   1087  CA  ASP C 360     -68.977  22.140 -30.164  1.00 45.22           C  
ATOM   1088  CA  GLY C 361     -68.884  20.012 -27.053  1.00 28.91           C  
ATOM   1089  CA  GLY C 362     -65.298  19.143 -26.327  1.00 39.04           C  
ATOM   1090  CA  LYS C 363     -64.421  16.363 -28.697  1.00103.28           C  
ATOM   1091  CA  GLY C 364     -60.897  17.077 -27.694  1.00 28.82           C  
ATOM   1092  CA  ILE C 365     -57.989  19.407 -28.217  1.00 66.64           C  
ATOM   1093  CA  LYS C 366     -57.799  21.170 -31.515  1.00 58.47           C  
ATOM   1094  CA  ILE C 367     -54.707  21.845 -33.536  1.00152.43           C  
ATOM   1095  CA  ASP C 368     -55.041  25.380 -34.785  1.00 56.63           C  
ATOM   1096  CA  GLU C 369     -52.488  25.478 -37.536  1.00 85.36           C  
ATOM   1097  CA  VAL C 370     -49.612  23.460 -38.869  1.00121.94           C  
ATOM   1098  CA  VAL C 371     -46.168  25.048 -38.953  1.00178.26           C  
ATOM   1099  CA  LYS C 372     -45.448  22.053 -41.241  1.00231.97           C  
ATOM   1100  CA  GLY C 373     -41.729  22.590 -41.551  1.00 38.80           C  
ATOM   1101  CA  SER C 374     -41.888  21.691 -37.833  1.00 46.42           C  
ATOM   1102  CA  PRO C 375     -41.651  18.193 -36.563  1.00 68.74           C  
ATOM   1103  CA  ALA C 376     -45.180  18.164 -35.222  1.00 44.51           C  
ATOM   1104  CA  ALA C 377     -45.872  18.310 -38.916  1.00 49.25           C  
ATOM   1105  CA  GLN C 378     -43.506  15.489 -39.786  1.00 52.05           C  
ATOM   1106  CA  ALA C 379     -45.359  12.731 -37.938  1.00 57.82           C  
ATOM   1107  CA  GLY C 380     -48.773  13.368 -39.421  1.00 61.71           C  
ATOM   1108  CA  LEU C 381     -50.270  16.243 -37.498  1.00 66.80           C  
ATOM   1109  CA  GLN C 382     -52.370  18.346 -39.854  1.00138.27           C  
ATOM   1110  CA  LYS C 383     -54.399  21.343 -38.809  1.00139.77           C  
ATOM   1111  CA  ASP C 384     -58.096  21.105 -38.042  1.00149.59           C  
ATOM   1112  CA  ASP C 385     -57.528  17.771 -36.426  1.00 61.57           C  
ATOM   1113  CA  VAL C 386     -59.286  17.124 -33.163  1.00 53.78           C  
ATOM   1114  CA  ILE C 387     -57.561  14.863 -30.740  1.00 62.10           C  
ATOM   1115  CA  ILE C 388     -60.357  12.830 -29.245  1.00 75.12           C  
ATOM   1116  CA  GLY C 389     -58.107  11.010 -26.839  1.00 44.93           C  
ATOM   1117  CA  VAL C 390     -54.765   9.388 -26.266  1.00 63.29           C  
ATOM   1118  CA  ASN C 391     -53.868   5.828 -25.394  1.00 79.12           C  
ATOM   1119  CA  ARG C 392     -57.408   4.534 -25.015  1.00161.40           C  
ATOM   1120  CA  ASP C 393     -58.034   7.607 -22.937  1.00 55.05           C  
ATOM   1121  CA  ARG C 394     -60.533  10.210 -23.940  1.00 36.89           C  
ATOM   1122  CA  VAL C 395     -59.100  13.680 -24.059  1.00 41.85           C  
ATOM   1123  CA  ASN C 396     -61.708  16.303 -23.369  1.00 47.61           C  
ATOM   1124  CA  SER C 397     -59.183  19.074 -23.060  1.00 92.99           C  
ATOM   1125  CA  ILE C 398     -55.479  19.864 -22.862  1.00 96.94           C  
ATOM   1126  CA  ALA C 399     -55.319  19.067 -19.188  1.00 25.64           C  
ATOM   1127  CA  GLU C 400     -56.593  15.559 -19.715  1.00 30.10           C  
ATOM   1128  CA  MET C 401     -54.238  15.020 -22.603  1.00 33.60           C  
ATOM   1129  CA  ARG C 402     -51.448  16.139 -20.356  1.00132.40           C  
ATOM   1130  CA  LYS C 403     -52.496  13.481 -17.902  1.00 72.34           C  
ATOM   1131  CA  VAL C 404     -52.013  10.705 -20.389  1.00102.93           C  
ATOM   1132  CA  LEU C 405     -48.639  12.163 -21.147  1.00 70.48           C  
ATOM   1133  CA  ALA C 406     -47.940  12.302 -17.455  1.00 36.53           C  
ATOM   1134  CA  ALA C 407     -47.828   8.529 -17.588  1.00 34.60           C  
ATOM   1135  CA  LYS C 408     -45.140   9.047 -20.196  1.00130.26           C  
ATOM   1136  CA  PRO C 409     -45.941   5.876 -22.037  1.00 70.47           C  
ATOM   1137  CA  ALA C 410     -43.228   4.983 -24.506  1.00 31.36           C  
ATOM   1138  CA  ILE C 411     -46.087   4.541 -26.939  1.00 81.69           C  
ATOM   1139  CA  ILE C 412     -48.392   7.478 -27.387  1.00 46.43           C  
ATOM   1140  CA  ALA C 413     -51.329   7.026 -29.640  1.00 49.63           C  
ATOM   1141  CA  LEU C 414     -53.381   9.977 -30.678  1.00114.20           C  
ATOM   1142  CA  GLN C 415     -56.601   9.492 -32.448  1.00212.05           C  
ATOM   1143  CA  ILE C 416     -57.908  12.545 -33.974  1.00 92.24           C  
ATOM   1144  CA  VAL C 417     -60.821  13.034 -36.213  1.00 47.91           C  
ATOM   1145  CA  ARG C 418     -60.081  14.620 -39.520  1.00 97.26           C  
ATOM   1146  CA  GLY C 419     -62.982  15.524 -41.701  1.00 20.37           C  
ATOM   1147  CA  ASN C 420     -65.611  12.948 -41.100  1.00 45.65           C  
ATOM   1148  CA  GLU C 421     -63.180  10.154 -40.448  1.00 48.50           C  
ATOM   1149  CA  SER C 422     -61.083   8.675 -37.722  1.00 49.21           C  
ATOM   1150  CA  ILE C 423     -57.376   9.313 -37.729  1.00114.96           C  
ATOM   1151  CA  TYR C 424     -54.664   7.915 -35.616  1.00162.55           C  
ATOM   1152  CA  LEU C 425     -51.501   9.695 -34.846  1.00 94.12           C  
ATOM   1153  CA  LEU C 426     -48.560   8.738 -32.822  1.00147.63           C  
ATOM   1154  CA  MET C 427     -45.245   9.376 -31.238  1.00 61.11           C  
TER    1155      MET C 427                                                      
ATOM   1156  CA  PRO D  11      40.008 -44.639  44.259  1.00 90.25           C  
ATOM   1157  CA  LEU D  12      37.904 -41.898  45.763  1.00 90.30           C  
ATOM   1158  CA  PRO D  13      39.457 -39.523  48.155  1.00153.89           C  
ATOM   1159  CA  SER D  14      36.617 -39.337  48.587  1.00119.81           C  
ATOM   1160  CA  LEU D  15      35.512 -35.730  48.278  1.00155.91           C  
ATOM   1161  CA  ALA D  16      32.556 -36.077  50.567  1.00 45.40           C  
ATOM   1162  CA  PRO D  17      34.506 -36.428  53.719  1.00 72.76           C  
ATOM   1163  CA  MET D  18      36.509 -33.307  53.008  1.00 36.23           C  
ATOM   1164  CA  LEU D  19      33.411 -31.481  51.867  1.00 58.67           C  
ATOM   1165  CA  GLU D  20      31.339 -32.365  54.882  1.00104.89           C  
ATOM   1166  CA  LYS D  21      33.498 -30.309  57.150  1.00130.15           C  
ATOM   1167  CA  VAL D  22      34.180 -27.433  54.751  1.00141.41           C  
ATOM   1168  CA  LEU D  23      30.796 -26.808  53.179  1.00121.51           C  
ATOM   1169  CA  PRO D  24      29.198 -24.970  56.028  1.00 65.24           C  
ATOM   1170  CA  ALA D  25      31.918 -22.371  55.566  1.00 35.47           C  
ATOM   1171  CA  VAL D  26      30.613 -21.422  52.155  1.00 95.68           C  
ATOM   1172  CA  VAL D  27      27.567 -19.253  52.212  1.00100.07           C  
ATOM   1173  CA  SER D  28      24.974 -17.765  49.891  1.00 48.73           C  
ATOM   1174  CA  VAL D  29      24.755 -14.013  49.714  1.00 32.91           C  
ATOM   1175  CA  ARG D  30      21.436 -12.354  49.072  1.00 80.97           C  
ATOM   1176  CA  VAL D  31      21.206  -8.738  48.086  1.00 42.16           C  
ATOM   1177  CA  GLU D  32      18.484  -6.142  47.695  1.00 58.74           C  
ATOM   1178  CA  GLY D  33      18.873  -2.612  46.520  1.00 25.89           C  
ATOM   1179  CA  THR D  34      18.336   0.250  44.141  1.00 98.88           C  
ATOM   1180  CA  ALA D  35      15.915   2.810  41.193  1.00 18.67           C  
ATOM   1181  CA  GLN D  59      13.904  -0.280  40.511  1.00 71.01           C  
ATOM   1182  CA  PRO D  60      14.303  -2.821  43.209  1.00 70.99           C  
ATOM   1183  CA  PHE D  61      16.350  -5.845  42.373  1.00 49.97           C  
ATOM   1184  CA  GLU D  62      17.358  -9.005  44.108  1.00 26.50           C  
ATOM   1185  CA  GLY D  63      20.659 -10.629  43.400  1.00 17.77           C  
ATOM   1186  CA  LEU D  64      22.235 -13.850  44.499  1.00 49.27           C  
ATOM   1187  CA  GLY D  65      25.873 -14.642  44.998  1.00 21.84           C  
ATOM   1188  CA  SER D  66      28.063 -16.573  47.364  1.00 77.08           C  
ATOM   1189  CA  GLY D  67      30.664 -15.841  49.975  1.00 16.63           C  
ATOM   1190  CA  VAL D  68      33.079 -17.595  52.268  1.00 38.03           C  
ATOM   1191  CA  ILE D  69      33.335 -17.282  56.000  1.00 51.54           C  
ATOM   1192  CA  ILE D  70      36.861 -16.199  56.788  1.00114.51           C  
ATOM   1193  CA  ASN D  71      36.489 -15.953  60.510  1.00 60.98           C  
ATOM   1194  CA  ALA D  72      33.741 -17.626  62.425  1.00 33.28           C  
ATOM   1195  CA  SER D  73      34.086 -15.575  65.542  1.00 35.51           C  
ATOM   1196  CA  LYS D  74      33.895 -12.207  63.890  1.00112.29           C  
ATOM   1197  CA  GLY D  75      31.594 -13.430  61.190  1.00 33.95           C  
ATOM   1198  CA  TYR D  76      33.615 -11.987  58.351  1.00 77.62           C  
ATOM   1199  CA  VAL D  77      32.615 -13.236  54.961  1.00122.25           C  
ATOM   1200  CA  LEU D  78      34.542 -12.597  51.776  1.00 58.84           C  
ATOM   1201  CA  THR D  79      32.674 -11.953  48.578  1.00 41.79           C  
ATOM   1202  CA  ASN D  80      33.040 -10.247  45.259  1.00 61.96           C  
ATOM   1203  CA  ASN D  81      32.525  -6.526  45.184  1.00 49.55           C  
ATOM   1204  CA  HIS D  82      30.210  -6.824  42.244  1.00 53.47           C  
ATOM   1205  CA  VAL D  83      27.797  -8.982  44.121  1.00120.47           C  
ATOM   1206  CA  ILE D  84      27.636  -6.476  46.978  1.00 78.24           C  
ATOM   1207  CA  ASN D  85      28.024  -3.177  45.163  1.00118.26           C  
ATOM   1208  CA  GLN D  86      24.389  -2.221  44.584  1.00 67.85           C  
ATOM   1209  CA  ALA D  87      23.076  -3.864  47.740  1.00 68.13           C  
ATOM   1210  CA  GLN D  88      21.122  -1.699  50.122  1.00135.28           C  
ATOM   1211  CA  LYS D  89      20.654  -4.689  52.373  1.00 30.93           C  
ATOM   1212  CA  ILE D  90      22.565  -7.913  52.514  1.00 36.65           C  
ATOM   1213  CA  SER D  91      21.616 -11.257  53.946  1.00 27.52           C  
ATOM   1214  CA  ILE D  92      23.684 -14.368  54.452  1.00 95.79           C  
ATOM   1215  CA  GLN D  93      22.245 -17.852  54.273  1.00172.29           C  
ATOM   1216  CA  LEU D  94      23.969 -20.906  55.671  1.00 48.96           C  
ATOM   1217  CA  ASN D  95      23.623 -24.325  54.125  1.00 31.10           C  
ATOM   1218  CA  ASP D  96      21.729 -25.329  57.232  1.00 49.70           C  
ATOM   1219  CA  GLY D  97      19.079 -22.795  56.369  1.00 27.03           C  
ATOM   1220  CA  ARG D  98      19.888 -20.278  59.044  1.00111.48           C  
ATOM   1221  CA  GLU D  99      19.970 -16.735  57.781  1.00 37.12           C  
ATOM   1222  CA  PHE D 100      21.704 -13.639  59.044  1.00 52.43           C  
ATOM   1223  CA  ASP D 101      21.998  -9.958  58.277  1.00121.77           C  
ATOM   1224  CA  ALA D 102      25.330  -8.636  57.096  1.00 36.32           C  
ATOM   1225  CA  LYS D 103      26.932  -5.260  56.696  1.00 53.99           C  
ATOM   1226  CA  LEU D 104      29.651  -4.259  54.314  1.00 49.57           C  
ATOM   1227  CA  ILE D 105      32.923  -3.799  56.115  1.00125.97           C  
ATOM   1228  CA  GLY D 106      34.702  -2.567  53.041  1.00 24.87           C  
ATOM   1229  CA  SER D 107      35.577  -3.516  49.518  1.00 94.74           C  
ATOM   1230  CA  ASP D 108      37.467  -2.379  46.508  1.00 86.47           C  
ATOM   1231  CA  ASP D 109      36.568  -2.122  42.851  1.00 59.51           C  
ATOM   1232  CA  GLN D 110      39.820  -2.919  41.160  1.00143.27           C  
ATOM   1233  CA  SER D 111      40.463  -6.346  42.642  1.00 70.61           C  
ATOM   1234  CA  ASP D 112      36.741  -6.890  43.124  1.00 73.25           C  
ATOM   1235  CA  ILE D 113      37.073  -8.059  46.713  1.00 64.07           C  
ATOM   1236  CA  ALA D 114      34.614  -7.151  49.427  1.00 32.86           C  
ATOM   1237  CA  LEU D 115      34.383  -8.000  53.096  1.00105.11           C  
ATOM   1238  CA  LEU D 116      31.099  -8.518  54.893  1.00 54.80           C  
ATOM   1239  CA  GLN D 117      30.344  -9.005  58.542  1.00 54.52           C  
ATOM   1240  CA  ILE D 118      27.509 -11.081  59.833  1.00 62.85           C  
ATOM   1241  CA  GLN D 119      25.468  -9.626  62.617  1.00108.10           C  
ATOM   1242  CA  ASN D 120      25.397 -11.913  65.645  1.00 67.60           C  
ATOM   1243  CA  PRO D 121      27.126 -14.686  63.798  1.00110.11           C  
ATOM   1244  CA  SER D 122      26.640 -17.576  66.272  1.00202.07           C  
ATOM   1245  CA  LYS D 123      28.022 -21.061  65.658  1.00 81.18           C  
ATOM   1246  CA  LEU D 124      29.681 -20.550  62.355  1.00 72.90           C  
ATOM   1247  CA  THR D 125      32.351 -22.541  60.607  1.00 96.75           C  
ATOM   1248  CA  GLN D 126      35.396 -20.950  59.048  1.00 46.08           C  
ATOM   1249  CA  ILE D 127      37.362 -22.030  56.042  1.00104.46           C  
ATOM   1250  CA  ALA D 128      41.129 -22.365  56.170  1.00 29.80           C  
ATOM   1251  CA  ILE D 129      43.149 -20.511  53.590  1.00 91.50           C  
ATOM   1252  CA  ALA D 130      45.839 -22.151  51.507  1.00 35.76           C  
ATOM   1253  CA  ASP D 131      48.830 -20.518  49.880  1.00 36.83           C  
ATOM   1254  CA  SER D 132      47.833 -19.586  46.346  1.00 40.37           C  
ATOM   1255  CA  ASP D 133      51.417 -19.144  45.330  1.00 50.03           C  
ATOM   1256  CA  LYS D 134      51.919 -22.846  45.810  1.00132.45           C  
ATOM   1257  CA  LEU D 135      49.301 -23.855  43.275  1.00109.10           C  
ATOM   1258  CA  ARG D 136      50.446 -25.447  40.061  1.00 97.57           C  
ATOM   1259  CA  VAL D 137      48.521 -26.402  36.974  1.00 41.34           C  
ATOM   1260  CA  GLY D 138      46.952 -29.787  37.367  1.00 24.91           C  
ATOM   1261  CA  ASP D 139      46.033 -29.370  40.992  1.00 26.54           C  
ATOM   1262  CA  PHE D 140      42.511 -30.448  41.794  1.00 48.50           C  
ATOM   1263  CA  ALA D 141      39.970 -27.837  42.716  1.00 27.40           C  
ATOM   1264  CA  VAL D 142      36.399 -27.812  43.909  1.00 32.40           C  
ATOM   1265  CA  ALA D 143      34.114 -24.864  43.489  1.00 30.05           C  
ATOM   1266  CA  VAL D 144      31.260 -24.151  45.831  1.00 34.74           C  
ATOM   1267  CA  GLY D 145      28.641 -21.496  45.372  1.00 23.12           C  
ATOM   1268  CA  ASN D 146      25.062 -21.008  44.344  1.00127.10           C  
ATOM   1269  CA  PRO D 147      24.632 -21.298  40.672  1.00152.06           C  
ATOM   1270  CA  PHE D 148      21.284 -20.038  39.463  1.00 77.66           C  
ATOM   1271  CA  GLY D 149      20.409 -19.623  43.103  1.00 25.69           C  
ATOM   1272  CA  LEU D 150      19.725 -23.320  43.276  1.00 53.06           C  
ATOM   1273  CA  GLY D 151      21.435 -23.721  46.620  1.00 30.54           C  
ATOM   1274  CA  GLN D 152      24.898 -24.690  47.612  1.00111.10           C  
ATOM   1275  CA  THR D 153      26.432 -26.629  44.800  1.00 37.64           C  
ATOM   1276  CA  ALA D 154      29.840 -28.175  44.528  1.00 31.58           C  
ATOM   1277  CA  THR D 155      31.622 -28.755  41.279  1.00109.63           C  
ATOM   1278  CA  SER D 156      34.970 -30.337  40.607  1.00 34.08           C  
ATOM   1279  CA  GLY D 157      37.809 -29.614  38.235  1.00 23.10           C  
ATOM   1280  CA  ILE D 158      41.508 -28.874  38.022  1.00108.07           C  
ATOM   1281  CA  VAL D 159      43.530 -25.694  38.028  1.00 44.10           C  
ATOM   1282  CA  SER D 160      43.792 -24.914  34.343  1.00 48.53           C  
ATOM   1283  CA  ALA D 161      46.118 -21.955  34.579  1.00 37.04           C  
ATOM   1284  CA  LEU D 162      47.335 -19.263  36.898  1.00 95.22           C  
ATOM   1285  CA  GLY D 163      48.583 -15.765  36.617  1.00 36.20           C  
ATOM   1286  CA  ARG D 164      46.144 -14.866  33.953  1.00114.57           C  
ATOM   1287  CA  SER D 165      45.113 -11.412  32.943  1.00 87.19           C  
ATOM   1288  CA  GLY D 166      44.293  -9.047  30.223  1.00 37.78           C  
ATOM   1289  CA  LEU D 167      40.765 -10.361  30.479  1.00 56.10           C  
ATOM   1290  CA  ASN D 168      39.849  -6.768  31.292  1.00 70.76           C  
ATOM   1291  CA  LEU D 169      37.300  -8.096  33.688  1.00 51.05           C  
ATOM   1292  CA  GLU D 170      38.881  -6.219  36.569  1.00115.33           C  
ATOM   1293  CA  GLY D 171      41.350  -3.414  37.205  1.00 40.18           C  
ATOM   1294  CA  LEU D 172      43.756  -5.756  38.863  1.00137.72           C  
ATOM   1295  CA  GLU D 173      43.612  -9.262  37.713  1.00 82.91           C  
ATOM   1296  CA  ASN D 174      45.448 -12.445  38.426  1.00140.54           C  
ATOM   1297  CA  PHE D 175      42.945 -15.080  37.961  1.00 93.75           C  
ATOM   1298  CA  ILE D 176      43.346 -18.699  38.779  1.00144.48           C  
ATOM   1299  CA  GLN D 177      41.715 -20.453  35.863  1.00 50.40           C  
ATOM   1300  CA  THR D 178      39.600 -23.503  36.586  1.00137.63           C  
ATOM   1301  CA  ASP D 179      37.682 -26.131  34.647  1.00 68.78           C  
ATOM   1302  CA  ALA D 180      35.233 -26.551  37.515  1.00 45.24           C  
ATOM   1303  CA  SER D 181      31.790 -25.574  36.406  1.00 98.76           C  
ATOM   1304  CA  ILE D 182      31.164 -22.029  37.417  1.00 60.23           C  
ATOM   1305  CA  ASN D 183      27.973 -20.278  36.540  1.00 74.60           C  
ATOM   1306  CA  ARG D 184      26.113 -17.157  37.449  1.00168.39           C  
ATOM   1307  CA  GLY D 185      25.598 -17.038  41.187  1.00 24.27           C  
ATOM   1308  CA  ASN D 186      29.006 -18.581  41.725  1.00 59.56           C  
ATOM   1309  CA  ALA D 187      30.630 -15.234  42.308  1.00104.32           C  
ATOM   1310  CA  GLY D 188      32.040 -14.730  45.753  1.00 24.38           C  
ATOM   1311  CA  GLY D 189      32.041 -18.486  46.118  1.00 24.69           C  
ATOM   1312  CA  ALA D 190      35.003 -20.550  47.108  1.00 47.72           C  
ATOM   1313  CA  LEU D 191      37.463 -22.599  45.148  1.00 78.68           C  
ATOM   1314  CA  LEU D 192      38.919 -25.240  47.359  1.00 55.36           C  
ATOM   1315  CA  ASN D 193      41.755 -27.688  47.193  1.00 73.64           C  
ATOM   1316  CA  LEU D 194      41.489 -31.309  48.216  1.00 99.14           C  
ATOM   1317  CA  ASN D 195      42.253 -30.319  51.754  1.00132.91           C  
ATOM   1318  CA  GLY D 196      39.248 -28.066  51.693  1.00 29.37           C  
ATOM   1319  CA  GLU D 197      41.381 -24.997  52.043  1.00 54.61           C  
ATOM   1320  CA  LEU D 198      40.522 -21.881  50.097  1.00 66.37           C  
ATOM   1321  CA  ILE D 199      42.537 -21.472  46.905  1.00 84.84           C  
ATOM   1322  CA  GLY D 200      40.606 -18.476  45.628  1.00 31.43           C  
ATOM   1323  CA  ILE D 201      37.279 -16.696  45.220  1.00116.66           C  
ATOM   1324  CA  ASN D 202      35.405 -17.400  41.992  1.00 88.63           C  
ATOM   1325  CA  THR D 203      35.089 -14.038  40.275  1.00 88.51           C  
ATOM   1326  CA  ALA D 204      34.014 -14.632  36.689  1.00 53.35           C  
ATOM   1327  CA  ILE D 205      33.677 -16.838  33.643  1.00 62.30           C  
ATOM   1328  CA  LEU D 206      34.269 -16.646  29.931  1.00 59.51           C  
ATOM   1329  CA  ALA D 207      31.354 -18.142  28.154  1.00 64.80           C  
ATOM   1330  CA  PRO D 208      29.726 -17.397  24.943  1.00189.53           C  
ATOM   1331  CA  GLY D 209      26.312 -18.672  25.879  1.00234.34           C  
ATOM   1332  CA  GLY D 210      26.327 -17.358  29.396  1.00 45.84           C  
ATOM   1333  CA  GLY D 211      26.757 -20.880  30.673  1.00 26.60           C  
ATOM   1334  CA  SER D 212      29.880 -22.553  31.955  1.00 62.34           C  
ATOM   1335  CA  VAL D 213      32.274 -23.275  29.105  1.00 68.95           C  
ATOM   1336  CA  GLY D 214      34.764 -24.762  31.489  1.00 37.17           C  
ATOM   1337  CA  ILE D 215      36.769 -21.574  31.634  1.00 91.12           C  
ATOM   1338  CA  GLY D 216      36.365 -19.911  34.997  1.00 21.64           C  
ATOM   1339  CA  PHE D 217      38.498 -17.438  36.870  1.00 47.45           C  
ATOM   1340  CA  ALA D 218      39.036 -16.866  40.551  1.00 38.64           C  
ATOM   1341  CA  ILE D 219      40.974 -14.409  42.635  1.00163.87           C  
ATOM   1342  CA  PRO D 220      43.656 -16.230  44.417  1.00105.77           C  
ATOM   1343  CA  SER D 221      43.355 -16.873  48.127  1.00 44.42           C  
ATOM   1344  CA  ASN D 222      46.492 -15.007  48.845  1.00 67.62           C  
ATOM   1345  CA  MET D 223      44.655 -12.358  47.049  1.00123.55           C  
ATOM   1346  CA  ALA D 224      41.540 -12.322  49.075  1.00 54.59           C  
ATOM   1347  CA  ARG D 225      43.279 -13.055  52.316  1.00 80.20           C  
ATOM   1348  CA  THR D 226      45.526 -10.105  52.704  1.00 67.98           C  
ATOM   1349  CA  LEU D 227      43.099  -7.824  50.872  1.00120.45           C  
ATOM   1350  CA  ALA D 228      40.433  -8.940  53.272  1.00 49.41           C  
ATOM   1351  CA  GLN D 229      42.643  -8.565  56.259  1.00 80.90           C  
ATOM   1352  CA  GLN D 230      43.296  -4.875  55.895  1.00169.83           C  
ATOM   1353  CA  LEU D 231      39.584  -4.452  55.355  1.00128.22           C  
ATOM   1354  CA  ILE D 232      39.273  -5.490  58.915  1.00124.67           C  
ATOM   1355  CA  ASP D 233      42.789  -4.291  59.819  1.00176.43           C  
ATOM   1356  CA  PHE D 234      44.988  -2.459  59.150  1.00188.89           C  
ATOM   1357  CA  GLY D 235      42.595  -0.757  56.854  1.00 40.02           C  
ATOM   1358  CA  GLU D 236      45.041   1.809  55.693  1.00 94.39           C  
ATOM   1359  CA  ILE D 237      43.162   3.979  53.280  1.00 36.19           C  
ATOM   1360  CA  LYS D 238      45.950   3.600  50.813  1.00226.77           C  
ATOM   1361  CA  ARG D 239      46.466   2.009  48.618  1.00210.33           C  
ATOM   1362  CA  GLY D 240      42.936   0.778  49.139  1.00 52.03           C  
ATOM   1363  CA  LEU D 241      43.406  -0.717  45.748  1.00197.20           C  
ATOM   1364  CA  LEU D 242      44.554   1.679  43.110  1.00100.99           C  
ATOM   1365  CA  GLY D 243      41.279   2.385  41.363  1.00 55.30           C  
ATOM   1366  CA  ILE D 244      42.208   1.780  37.747  1.00 79.27           C  
ATOM   1367  CA  LYS D 245      41.160  -0.249  34.729  1.00189.13           C  
ATOM   1368  CA  GLY D 246      43.539  -2.095  32.534  1.00 37.71           C  
ATOM   1369  CA  THR D 247      44.122  -5.111  30.402  1.00110.60           C  
ATOM   1370  CA  GLU D 248      46.829  -7.067  28.651  1.00102.01           C  
ATOM   1371  CA  MET D 249      49.233  -5.373  26.338  1.00 56.07           C  
ATOM   1372  CA  SER D 250      47.272  -4.205  23.361  1.00 32.76           C  
ATOM   1373  CA  ALA D 251      48.220  -5.360  19.919  1.00 31.53           C  
ATOM   1374  CA  ASP D 252      48.209  -1.844  18.535  1.00 53.14           C  
ATOM   1375  CA  ILE D 253      50.265  -0.112  21.176  1.00 55.48           C  
ATOM   1376  CA  ALA D 254      52.623  -2.945  21.931  1.00 53.59           C  
ATOM   1377  CA  LYS D 255      53.660  -3.941  18.502  1.00130.12           C  
ATOM   1378  CA  ALA D 256      53.915  -0.595  16.864  1.00 70.07           C  
ATOM   1379  CA  PHE D 257      55.571   1.750  19.278  1.00134.59           C  
ATOM   1380  CA  ASN D 258      57.301  -1.000  20.952  1.00185.76           C  
ATOM   1381  CA  LEU D 259      57.121  -0.659  24.620  1.00143.62           C  
ATOM   1382  CA  ASP D 260      60.324  -0.541  26.512  1.00 70.88           C  
ATOM   1383  CA  VAL D 261      58.997  -3.220  28.809  1.00106.81           C  
ATOM   1384  CA  GLN D 262      57.999  -6.238  26.805  1.00 65.36           C  
ATOM   1385  CA  ARG D 263      54.626  -6.150  28.408  1.00124.23           C  
ATOM   1386  CA  GLY D 264      52.909  -5.027  31.510  1.00 23.12           C  
ATOM   1387  CA  ALA D 265      49.604  -4.160  32.966  1.00 40.38           C  
ATOM   1388  CA  PHE D 266      48.418  -1.412  30.789  1.00125.12           C  
ATOM   1389  CA  VAL D 267      45.918   1.051  32.020  1.00 70.85           C  
ATOM   1390  CA  SER D 268      43.277   2.453  29.731  1.00 67.67           C  
ATOM   1391  CA  GLU D 269      41.707   4.622  32.332  1.00 91.44           C  
ATOM   1392  CA  VAL D 270      42.016   6.819  35.374  1.00103.04           C  
ATOM   1393  CA  LEU D 271      39.489   6.659  38.179  1.00 71.40           C  
ATOM   1394  CA  PRO D 272      38.309   9.909  39.561  1.00188.59           C  
ATOM   1395  CA  GLY D 273      39.009  10.313  43.287  1.00133.16           C  
ATOM   1396  CA  SER D 274      40.855   7.106  42.842  1.00128.60           C  
ATOM   1397  CA  GLY D 275      44.149   6.141  44.244  1.00 37.27           C  
ATOM   1398  CA  SER D 276      45.729   6.011  40.877  1.00 48.81           C  
ATOM   1399  CA  ALA D 277      44.408   9.461  40.304  1.00 65.43           C  
ATOM   1400  CA  LYS D 278      46.149  11.225  43.131  1.00127.38           C  
ATOM   1401  CA  ALA D 279      49.199   9.056  42.812  1.00 49.51           C  
ATOM   1402  CA  GLY D 280      49.290  10.598  39.443  1.00 42.97           C  
ATOM   1403  CA  VAL D 281      49.109   7.419  37.469  1.00 76.06           C  
ATOM   1404  CA  LYS D 282      47.061   8.032  34.468  1.00153.73           C  
ATOM   1405  CA  ALA D 283      46.063   6.382  31.323  1.00 84.56           C  
ATOM   1406  CA  GLY D 284      48.156   4.894  28.640  1.00 34.59           C  
ATOM   1407  CA  ASP D 285      50.159   3.744  31.619  1.00128.52           C  
ATOM   1408  CA  ILE D 286      52.148   0.700  31.509  1.00 85.11           C  
ATOM   1409  CA  ILE D 287      52.702  -0.793  34.908  1.00 60.02           C  
ATOM   1410  CA  THR D 288      56.011  -2.566  34.644  1.00 53.45           C  
ATOM   1411  CA  SER D 289      56.424  -3.603  38.201  1.00 97.69           C  
ATOM   1412  CA  LEU D 290      55.040  -3.524  41.672  1.00 78.06           C  
ATOM   1413  CA  ASN D 291      57.398  -3.117  44.568  1.00177.70           C  
ATOM   1414  CA  GLY D 292      61.080  -4.028  44.386  1.00 52.61           C  
ATOM   1415  CA  LYS D 293      60.520  -7.312  42.613  1.00 72.23           C  
ATOM   1416  CA  PRO D 294      59.613  -7.220  39.004  1.00 61.26           C  
ATOM   1417  CA  LEU D 295      55.993  -7.460  37.960  1.00132.43           C  
ATOM   1418  CA  ASN D 296      54.751  -9.778  35.263  1.00113.43           C  
ATOM   1419  CA  SER D 297      51.761  -9.389  33.080  1.00 55.00           C  
ATOM   1420  CA  PHE D 298      48.544  -7.736  34.052  1.00 73.63           C  
ATOM   1421  CA  ALA D 299      47.823 -11.140  35.466  1.00 45.91           C  
ATOM   1422  CA  GLU D 300      50.635 -11.052  37.924  1.00122.08           C  
ATOM   1423  CA  LEU D 301      49.493  -7.603  38.801  1.00 79.38           C  
ATOM   1424  CA  ARG D 302      46.333  -8.495  40.537  1.00204.84           C  
ATOM   1425  CA  SER D 303      47.996 -11.567  41.798  1.00 68.13           C  
ATOM   1426  CA  ARG D 304      50.152  -9.630  44.065  1.00211.91           C  
ATOM   1427  CA  ILE D 305      47.838  -6.691  44.623  1.00136.83           C  
ATOM   1428  CA  ALA D 306      44.793  -8.736  45.041  1.00 72.68           C  
ATOM   1429  CA  THR D 307      46.937 -10.655  47.397  1.00166.70           C  
ATOM   1430  CA  THR D 308      48.145  -7.627  49.254  1.00138.79           C  
ATOM   1431  CA  GLU D 309      46.269  -5.659  51.859  1.00 89.96           C  
ATOM   1432  CA  PRO D 310      44.095  -3.137  50.322  1.00232.58           C  
ATOM   1433  CA  GLY D 311      45.396  -1.042  51.932  1.00124.96           C  
ATOM   1434  CA  THR D 312      49.118  -1.455  52.088  1.00 53.15           C  
ATOM   1435  CA  LYS D 313      51.154   1.432  50.855  1.00 98.45           C  
ATOM   1436  CA  VAL D 314      53.052   0.274  47.828  1.00 49.07           C  
ATOM   1437  CA  LYS D 315      55.186   1.702  45.039  1.00124.32           C  
ATOM   1438  CA  LEU D 316      54.442   1.089  41.405  1.00113.12           C  
ATOM   1439  CA  GLY D 317      56.755   1.212  38.449  1.00 56.75           C  
ATOM   1440  CA  LEU D 318      55.337   2.113  35.160  1.00214.73           C  
ATOM   1441  CA  LEU D 319      56.432   3.349  31.874  1.00112.80           C  
ATOM   1442  CA  ARG D 320      55.141   6.446  30.566  1.00251.69           C  
ATOM   1443  CA  ASN D 321      56.568   8.047  27.421  1.00205.67           C  
ATOM   1444  CA  GLY D 322      59.236   5.539  27.315  1.00 49.69           C  
ATOM   1445  CA  LYS D 323      60.457   6.884  30.520  1.00137.84           C  
ATOM   1446  CA  PRO D 324      60.499   5.664  33.971  1.00157.49           C  
ATOM   1447  CA  LEU D 325      58.994   6.749  37.287  1.00204.01           C  
ATOM   1448  CA  GLU D 326      58.309   5.454  40.627  1.00156.63           C  
ATOM   1449  CA  VAL D 327      55.232   6.571  42.468  1.00 52.28           C  
ATOM   1450  CA  GLU D 328      53.590   5.649  45.731  1.00 81.85           C  
ATOM   1451  CA  VAL D 329      50.065   4.506  45.202  1.00 55.37           C  
ATOM   1452  CA  SER D 340      26.344  33.489  46.113  1.00100.41           C  
ATOM   1453  CA  ALA D 341      22.632  32.947  45.620  1.00 79.12           C  
ATOM   1454  CA  GLU D 342      23.191  30.777  42.582  1.00 54.77           C  
ATOM   1455  CA  MET D 343      24.036  27.535  44.237  1.00 63.14           C  
ATOM   1456  CA  ILE D 344      21.083  27.607  46.526  1.00 60.70           C  
ATOM   1457  CA  THR D 345      18.886  29.167  43.912  1.00160.54           C  
ATOM   1458  CA  PRO D 346      19.012  27.964  40.381  1.00159.15           C  
ATOM   1459  CA  ALA D 347      20.600  30.188  37.762  1.00 72.26           C  
ATOM   1460  CA  LEU D 348      19.623  33.270  39.743  1.00 90.73           C  
ATOM   1461  CA  GLU D 349      22.884  35.086  40.028  1.00 76.09           C  
ATOM   1462  CA  GLY D 350      22.963  37.618  42.754  1.00 26.71           C  
ATOM   1463  CA  ALA D 351      24.223  38.463  46.175  1.00 34.60           C  
ATOM   1464  CA  THR D 352      26.313  35.859  47.859  1.00105.11           C  
ATOM   1465  CA  LEU D 353      24.969  34.015  50.831  1.00 59.35           C  
ATOM   1466  CA  SER D 354      26.517  32.871  54.079  1.00 88.45           C  
ATOM   1467  CA  ASP D 355      25.069  30.537  56.634  1.00 45.74           C  
ATOM   1468  CA  GLY D 356      24.866  31.092  60.313  1.00 45.96           C  
ATOM   1469  CA  GLN D 357      23.582  34.253  61.874  1.00161.54           C  
ATOM   1470  CA  LEU D 358      27.214  34.515  61.849  1.00199.80           C  
ATOM   1471  CA  LYS D 359      27.201  37.466  64.217  1.00125.20           C  
ATOM   1472  CA  ASP D 360      24.293  36.322  66.404  1.00 46.99           C  
ATOM   1473  CA  GLY D 361      22.457  33.065  66.887  1.00 30.01           C  
ATOM   1474  CA  GLY D 362      21.467  31.797  63.484  1.00 37.81           C  
ATOM   1475  CA  LYS D 363      18.422  33.759  62.493  1.00129.77           C  
ATOM   1476  CA  GLY D 364      19.079  32.389  59.081  1.00 32.05           C  
ATOM   1477  CA  ILE D 365      21.235  32.706  56.009  1.00121.91           C  
ATOM   1478  CA  LYS D 366      22.807  36.056  55.349  1.00 74.15           C  
ATOM   1479  CA  ILE D 367      23.216  37.615  51.973  1.00 63.36           C  
ATOM   1480  CA  ASP D 368      26.672  39.103  51.900  1.00 54.26           C  
ATOM   1481  CA  GLU D 369      26.487  41.547  49.062  1.00 87.71           C  
ATOM   1482  CA  VAL D 370      24.222  42.347  46.188  1.00121.86           C  
ATOM   1483  CA  VAL D 371      25.595  42.172  42.656  1.00179.39           C  
ATOM   1484  CA  LYS D 372      22.474  44.266  41.831  1.00149.08           C  
ATOM   1485  CA  GLY D 373      22.755  43.996  38.072  1.00 35.86           C  
ATOM   1486  CA  SER D 374      22.082  40.302  38.775  1.00 44.97           C  
ATOM   1487  CA  PRO D 375      18.654  38.834  38.913  1.00 71.30           C  
ATOM   1488  CA  ALA D 376      18.905  37.964  42.575  1.00 42.90           C  
ATOM   1489  CA  ALA D 377      18.873  41.719  42.802  1.00 49.66           C  
ATOM   1490  CA  GLN D 378      15.888  42.179  40.522  1.00 98.48           C  
ATOM   1491  CA  ALA D 379      13.338  40.420  42.736  1.00 59.96           C  
ATOM   1492  CA  GLY D 380      14.080  42.334  45.908  1.00 62.52           C  
ATOM   1493  CA  LEU D 381      17.113  40.785  47.500  1.00 58.38           C  
ATOM   1494  CA  GLN D 382      19.275  43.465  49.033  1.00 71.07           C  
ATOM   1495  CA  LYS D 383      22.414  42.932  51.041  1.00158.80           C  
ATOM   1496  CA  ASP D 384      22.424  42.438  54.798  1.00 82.50           C  
ATOM   1497  CA  ASP D 385      19.088  40.711  54.705  1.00 46.76           C  
ATOM   1498  CA  VAL D 386      18.734  37.609  56.813  1.00 56.10           C  
ATOM   1499  CA  ILE D 387      16.497  34.904  55.540  1.00 58.83           C  
ATOM   1500  CA  ILE D 388      14.750  33.612  58.617  1.00109.51           C  
ATOM   1501  CA  GLY D 389      12.940  30.866  56.765  1.00 46.42           C  
ATOM   1502  CA  VAL D 390      11.183  29.814  53.610  1.00 62.09           C  
ATOM   1503  CA  ASN D 391       7.645  28.661  53.002  1.00 81.90           C  
ATOM   1504  CA  ARG D 392       6.536  28.648  56.616  1.00158.11           C  
ATOM   1505  CA  ASP D 393       9.739  26.816  57.366  1.00 54.27           C  
ATOM   1506  CA  ARG D 394      12.412  28.292  59.532  1.00102.37           C  
ATOM   1507  CA  VAL D 395      15.817  28.389  57.939  1.00 43.98           C  
ATOM   1508  CA  ASN D 396      18.597  28.131  60.472  1.00 42.93           C  
ATOM   1509  CA  SER D 397      21.250  27.796  57.822  1.00 37.86           C  
ATOM   1510  CA  ILE D 398      21.881  27.063  54.173  1.00 37.19           C  
ATOM   1511  CA  ALA D 399      21.261  23.366  54.520  1.00 23.96           C  
ATOM   1512  CA  GLU D 400      17.776  23.853  55.870  1.00 30.45           C  
ATOM   1513  CA  MET D 401      16.997  26.429  53.240  1.00 34.55           C  
ATOM   1514  CA  ARG D 402      18.118  23.935  50.673  1.00 74.17           C  
ATOM   1515  CA  LYS D 403      15.655  21.479  52.111  1.00104.32           C  
ATOM   1516  CA  VAL D 404      12.655  23.684  51.514  1.00 31.01           C  
ATOM   1517  CA  LEU D 405      13.964  24.187  48.021  1.00 62.73           C  
ATOM   1518  CA  ALA D 406      14.240  20.447  47.720  1.00 29.18           C  
ATOM   1519  CA  ALA D 407      10.470  20.379  47.771  1.00 30.02           C  
ATOM   1520  CA  LYS D 408      10.680  22.743  44.824  1.00105.68           C  
ATOM   1521  CA  PRO D 409       7.411  24.417  45.568  1.00 69.56           C  
ATOM   1522  CA  ALA D 410       6.197  26.509  42.659  1.00 31.09           C  
ATOM   1523  CA  ILE D 411       5.779  29.249  45.232  1.00125.58           C  
ATOM   1524  CA  ILE D 412       8.839  30.090  47.252  1.00 48.28           C  
ATOM   1525  CA  ALA D 413       8.438  32.648  49.944  1.00 50.05           C  
ATOM   1526  CA  LEU D 414      11.447  34.049  51.673  1.00112.38           C  
ATOM   1527  CA  GLN D 415      11.020  36.206  54.633  1.00119.60           C  
ATOM   1528  CA  ILE D 416      14.060  37.990  55.662  1.00116.76           C  
ATOM   1529  CA  VAL D 417      14.590  40.577  58.271  1.00 45.13           C  
ATOM   1530  CA  ARG D 418      15.927  43.865  57.085  1.00 84.34           C  
ATOM   1531  CA  GLY D 419      16.902  46.349  59.708  1.00 20.06           C  
ATOM   1532  CA  ASN D 420      14.478  45.931  62.521  1.00 47.36           C  
ATOM   1533  CA  GLU D 421      11.641  44.915  60.274  1.00 48.15           C  
ATOM   1534  CA  SER D 422      10.165  41.877  58.663  1.00 89.84           C  
ATOM   1535  CA  ILE D 423      10.558  41.428  54.972  1.00 77.62           C  
ATOM   1536  CA  TYR D 424       9.156  39.010  52.493  1.00169.80           C  
ATOM   1537  CA  LEU D 425      10.791  37.951  49.349  1.00 99.84           C  
ATOM   1538  CA  LEU D 426       9.774  35.545  46.730  1.00148.29           C  
ATOM   1539  CA  MET D 427      10.432  33.645  43.619  1.00141.85           C  
TER    1540      MET D 427                                                      
ATOM   1541  CA  PRO E  11      47.387 -43.206  39.009  1.00 77.03           C  
ATOM   1542  CA  LEU E  12      44.574 -44.613  36.982  1.00127.29           C  
ATOM   1543  CA  PRO E  13      42.438 -47.106  38.665  1.00321.13           C  
ATOM   1544  CA  SER E  14      42.081 -47.883  35.210  1.00135.55           C  
ATOM   1545  CA  LEU E  15      38.497 -47.176  34.351  1.00119.92           C  
ATOM   1546  CA  ALA E  16      38.787 -49.526  31.406  1.00 48.54           C  
ATOM   1547  CA  PRO E  17      39.192 -52.654  33.397  1.00 69.47           C  
ATOM   1548  CA  MET E  18      36.000 -51.998  35.286  1.00 36.19           C  
ATOM   1549  CA  LEU E  19      34.219 -50.920  32.136  1.00 54.56           C  
ATOM   1550  CA  GLU E  20      35.149 -53.954  30.126  1.00 81.38           C  
ATOM   1551  CA  LYS E  21      33.077 -56.217  32.272  1.00 90.56           C  
ATOM   1552  CA  VAL E  22      30.171 -53.846  32.919  1.00139.38           C  
ATOM   1553  CA  LEU E  23      29.584 -52.285  29.528  1.00123.73           C  
ATOM   1554  CA  PRO E  24      27.768 -55.145  27.913  1.00 67.22           C  
ATOM   1555  CA  ALA E  25      25.127 -54.673  30.587  1.00 37.28           C  
ATOM   1556  CA  VAL E  26      24.199 -51.261  29.280  1.00 98.41           C  
ATOM   1557  CA  VAL E  27      22.108 -51.307  26.187  1.00101.18           C  
ATOM   1558  CA  SER E  28      20.671 -48.929  23.651  1.00 37.17           C  
ATOM   1559  CA  VAL E  29      16.938 -48.820  23.292  1.00 38.18           C  
ATOM   1560  CA  ARG E  30      15.381 -48.074  19.973  1.00118.03           C  
ATOM   1561  CA  VAL E  31      11.772 -47.174  19.619  1.00 42.07           C  
ATOM   1562  CA  GLU E  32       9.338 -46.602  16.814  1.00 68.81           C  
ATOM   1563  CA  GLY E  33       5.798 -45.472  17.070  1.00 31.86           C  
ATOM   1564  CA  THR E  34       3.223 -42.912  16.257  1.00 72.34           C  
ATOM   1565  CA  ALA E  35       0.638 -40.734  13.359  1.00 29.18           C  
ATOM   1566  CA  GLN E  59       3.848 -39.871  11.604  1.00 78.65           C  
ATOM   1567  CA  PRO E  60       6.484 -42.383  12.285  1.00 73.53           C  
ATOM   1568  CA  PHE E  61       9.258 -41.348  14.561  1.00 59.75           C  
ATOM   1569  CA  GLU E  62      12.290 -43.142  15.779  1.00 30.93           C  
ATOM   1570  CA  GLY E  63      13.711 -42.432  19.160  1.00 27.86           C  
ATOM   1571  CA  LEU E  64      16.888 -43.589  20.775  1.00102.14           C  
ATOM   1572  CA  GLY E  65      17.571 -44.076  24.430  1.00 28.95           C  
ATOM   1573  CA  SER E  66      19.448 -46.449  26.653  1.00 81.03           C  
ATOM   1574  CA  GLY E  67      18.645 -49.044  29.241  1.00 17.35           C  
ATOM   1575  CA  VAL E  68      20.351 -51.359  31.664  1.00 34.47           C  
ATOM   1576  CA  ILE E  69      19.982 -55.086  31.922  1.00 47.70           C  
ATOM   1577  CA  ILE E  70      18.932 -55.883  35.453  1.00 88.17           C  
ATOM   1578  CA  ASN E  71      18.344 -59.564  34.999  1.00148.65           C  
ATOM   1579  CA  ALA E  72      20.258 -61.490  32.379  1.00 37.84           C  
ATOM   1580  CA  SER E  73      18.212 -64.633  32.608  1.00 36.33           C  
ATOM   1581  CA  LYS E  74      14.876 -62.888  32.419  1.00132.30           C  
ATOM   1582  CA  GLY E  75      16.135 -60.239  30.092  1.00 29.34           C  
ATOM   1583  CA  TYR E  76      14.704 -57.410  32.141  1.00 83.19           C  
ATOM   1584  CA  VAL E  77      15.963 -54.000  31.143  1.00 42.28           C  
ATOM   1585  CA  LEU E  78      15.319 -50.806  33.052  1.00 48.54           C  
ATOM   1586  CA  THR E  79      14.710 -47.616  31.165  1.00 48.82           C  
ATOM   1587  CA  ASN E  80      13.038 -44.283  31.517  1.00 65.11           C  
ATOM   1588  CA  ASN E  81       9.326 -44.176  30.931  1.00 36.87           C  
ATOM   1589  CA  HIS E  82       9.683 -41.223  28.620  1.00 56.41           C  
ATOM   1590  CA  VAL E  83      11.922 -43.150  26.315  1.00 43.21           C  
ATOM   1591  CA  ILE E  84       9.361 -45.946  26.000  1.00 73.21           C  
ATOM   1592  CA  ASN E  85       6.109 -44.014  26.272  1.00 69.79           C  
ATOM   1593  CA  GLN E  86       5.293 -43.455  22.582  1.00140.81           C  
ATOM   1594  CA  ALA E  87       6.888 -46.666  21.365  1.00 67.23           C  
ATOM   1595  CA  GLN E  88       4.737 -48.989  19.322  1.00 85.58           C  
ATOM   1596  CA  LYS E  89       7.671 -51.337  19.012  1.00 29.70           C  
ATOM   1597  CA  ILE E  90      10.856 -51.508  20.983  1.00 37.61           C  
ATOM   1598  CA  SER E  91      14.196 -52.996  20.107  1.00 28.77           C  
ATOM   1599  CA  ILE E  92      17.260 -53.489  22.244  1.00 95.71           C  
ATOM   1600  CA  GLN E  93      20.759 -53.464  20.853  1.00 49.73           C  
ATOM   1601  CA  LEU E  94      23.797 -54.806  22.619  1.00 49.10           C  
ATOM   1602  CA  ASN E  95      27.196 -53.223  22.302  1.00 36.08           C  
ATOM   1603  CA  ASP E  96      28.215 -56.350  20.435  1.00 51.71           C  
ATOM   1604  CA  GLY E  97      25.716 -55.489  17.749  1.00 27.73           C  
ATOM   1605  CA  ARG E  98      23.173 -58.163  18.483  1.00116.94           C  
ATOM   1606  CA  GLU E  99      19.633 -56.901  18.609  1.00 34.50           C  
ATOM   1607  CA  PHE E 100      16.485 -58.175  20.236  1.00 45.36           C  
ATOM   1608  CA  ASP E 101      12.877 -57.142  20.466  1.00 29.99           C  
ATOM   1609  CA  ALA E 102      11.446 -56.105  23.778  1.00 27.62           C  
ATOM   1610  CA  LYS E 103       8.037 -55.691  25.298  1.00 45.55           C  
ATOM   1611  CA  LEU E 104       7.044 -53.250  27.965  1.00 49.36           C  
ATOM   1612  CA  ILE E 105       6.551 -55.055  31.226  1.00135.27           C  
ATOM   1613  CA  GLY E 106       5.262 -51.989  32.986  1.00 25.38           C  
ATOM   1614  CA  SER E 107       6.235 -48.488  33.915  1.00 97.20           C  
ATOM   1615  CA  ASP E 108       5.076 -45.481  35.780  1.00107.85           C  
ATOM   1616  CA  ASP E 109       4.858 -41.808  34.961  1.00 67.27           C  
ATOM   1617  CA  GLN E 110       5.608 -40.132  38.220  1.00163.77           C  
ATOM   1618  CA  SER E 111       9.042 -41.547  38.910  1.00127.73           C  
ATOM   1619  CA  ASP E 112       9.622 -42.141  35.197  1.00 76.21           C  
ATOM   1620  CA  ILE E 113      10.747 -45.751  35.556  1.00 95.78           C  
ATOM   1621  CA  ALA E 114       9.887 -48.416  33.016  1.00 31.06           C  
ATOM   1622  CA  LEU E 115      10.712 -52.093  32.786  1.00102.67           C  
ATOM   1623  CA  LEU E 116      11.256 -53.887  29.496  1.00102.75           C  
ATOM   1624  CA  GLN E 117      11.731 -57.556  28.812  1.00 49.36           C  
ATOM   1625  CA  ILE E 118      13.858 -58.885  26.007  1.00107.77           C  
ATOM   1626  CA  GLN E 119      12.383 -61.689  24.023  1.00 95.42           C  
ATOM   1627  CA  ASN E 120      14.672 -64.702  23.816  1.00 59.76           C  
ATOM   1628  CA  PRO E 121      17.398 -62.910  25.677  1.00105.33           C  
ATOM   1629  CA  SER E 122      20.320 -65.371  25.263  1.00245.56           C  
ATOM   1630  CA  LYS E 123      23.783 -64.743  26.692  1.00 80.23           C  
ATOM   1631  CA  LEU E 124      23.233 -61.447  28.399  1.00 89.43           C  
ATOM   1632  CA  THR E 125      25.261 -59.687  31.036  1.00 49.24           C  
ATOM   1633  CA  GLN E 126      23.667 -58.155  34.096  1.00147.30           C  
ATOM   1634  CA  ILE E 127      24.637 -55.096  36.028  1.00101.36           C  
ATOM   1635  CA  ALA E 128      25.039 -55.269  39.773  1.00 31.79           C  
ATOM   1636  CA  ILE E 129      23.097 -52.741  41.776  1.00 90.31           C  
ATOM   1637  CA  ALA E 130      24.703 -50.631  44.470  1.00 34.65           C  
ATOM   1638  CA  ASP E 131      23.088 -49.022  47.489  1.00 51.05           C  
ATOM   1639  CA  SER E 132      22.156 -45.502  46.461  1.00 35.52           C  
ATOM   1640  CA  ASP E 133      21.647 -44.459  50.033  1.00 39.65           C  
ATOM   1641  CA  LYS E 134      25.329 -45.053  50.615  1.00171.86           C  
ATOM   1642  CA  LEU E 135      26.365 -42.494  48.016  1.00 59.36           C  
ATOM   1643  CA  ARG E 136      27.853 -39.229  49.153  1.00123.35           C  
ATOM   1644  CA  VAL E 137      28.886 -36.182  47.225  1.00 82.70           C  
ATOM   1645  CA  GLY E 138      32.320 -36.506  45.746  1.00 22.46           C  
ATOM   1646  CA  ASP E 139      31.929 -40.123  44.816  1.00 27.86           C  
ATOM   1647  CA  PHE E 140      33.085 -40.920  41.317  1.00 43.59           C  
ATOM   1648  CA  ALA E 141      30.508 -41.809  38.731  1.00 29.11           C  
ATOM   1649  CA  VAL E 142      30.527 -42.989  35.156  1.00 33.45           C  
ATOM   1650  CA  ALA E 143      27.614 -42.544  32.831  1.00 34.16           C  
ATOM   1651  CA  VAL E 144      26.963 -44.893  29.981  1.00107.85           C  
ATOM   1652  CA  GLY E 145      24.340 -44.469  27.312  1.00 30.29           C  
ATOM   1653  CA  ASN E 146      23.946 -43.415  23.730  1.00141.07           C  
ATOM   1654  CA  PRO E 147      24.187 -39.716  23.337  1.00 90.41           C  
ATOM   1655  CA  PHE E 148      22.952 -38.450  20.011  1.00 73.67           C  
ATOM   1656  CA  GLY E 149      22.605 -42.088  19.075  1.00 30.31           C  
ATOM   1657  CA  LEU E 150      26.310 -42.254  18.461  1.00 90.19           C  
ATOM   1658  CA  GLY E 151      26.627 -45.607  20.139  1.00 42.05           C  
ATOM   1659  CA  GLN E 152      27.631 -46.749  23.567  1.00 53.33           C  
ATOM   1660  CA  THR E 153      29.535 -43.925  25.177  1.00137.80           C  
ATOM   1661  CA  ALA E 154      30.993 -43.559  28.600  1.00 36.89           C  
ATOM   1662  CA  THR E 155      31.517 -40.292  30.406  1.00 37.65           C  
ATOM   1663  CA  SER E 156      33.072 -39.640  33.783  1.00 84.00           C  
ATOM   1664  CA  GLY E 157      32.287 -37.293  36.620  1.00 25.26           C  
ATOM   1665  CA  ILE E 158      31.487 -37.165  40.321  1.00 98.63           C  
ATOM   1666  CA  VAL E 159      28.255 -37.129  42.262  1.00125.13           C  
ATOM   1667  CA  SER E 160      27.526 -33.476  42.535  1.00 94.41           C  
ATOM   1668  CA  ALA E 161      24.519 -33.738  44.800  1.00 51.22           C  
ATOM   1669  CA  LEU E 162      21.831 -36.069  46.001  1.00 75.44           C  
ATOM   1670  CA  GLY E 163      18.281 -35.864  47.163  1.00 30.50           C  
ATOM   1671  CA  ARG E 164      17.448 -33.100  44.818  1.00193.17           C  
ATOM   1672  CA  SER E 165      14.018 -32.064  43.803  1.00 91.02           C  
ATOM   1673  CA  GLY E 166      11.674 -29.314  43.018  1.00 36.46           C  
ATOM   1674  CA  LEU E 167      13.060 -29.520  39.510  1.00 64.07           C  
ATOM   1675  CA  ASN E 168       9.466 -30.391  38.585  1.00137.84           C  
ATOM   1676  CA  LEU E 169      10.822 -32.651  35.932  1.00 47.08           C  
ATOM   1677  CA  GLU E 170       8.957 -35.572  37.447  1.00108.65           C  
ATOM   1678  CA  GLY E 171       6.105 -36.203  39.861  1.00 37.34           C  
ATOM   1679  CA  LEU E 172       8.392 -37.928  42.269  1.00133.35           C  
ATOM   1680  CA  GLU E 173      11.912 -36.806  42.209  1.00 72.59           C  
ATOM   1681  CA  ASN E 174      15.087 -37.538  44.092  1.00103.19           C  
ATOM   1682  CA  PHE E 175      17.697 -37.090  41.550  1.00 84.57           C  
ATOM   1683  CA  ILE E 176      21.299 -37.839  42.040  1.00 72.07           C  
ATOM   1684  CA  GLN E 177      23.069 -34.966  40.377  1.00 50.85           C  
ATOM   1685  CA  THR E 178      26.160 -35.665  38.351  1.00111.91           C  
ATOM   1686  CA  ASP E 179      28.787 -33.715  36.431  1.00 60.62           C  
ATOM   1687  CA  ALA E 180      29.274 -36.574  33.995  1.00 42.97           C  
ATOM   1688  CA  SER E 181      28.362 -35.465  30.543  1.00 55.10           C  
ATOM   1689  CA  ILE E 182      24.873 -36.537  29.788  1.00163.94           C  
ATOM   1690  CA  ASN E 183      23.077 -35.646  26.647  1.00118.88           C  
ATOM   1691  CA  ARG E 184      19.961 -36.475  24.704  1.00360.37           C  
ATOM   1692  CA  GLY E 185      20.401 -40.236  24.090  1.00180.64           C  
ATOM   1693  CA  ASN E 186      21.469 -40.797  27.692  1.00 91.73           C  
ATOM   1694  CA  ALA E 187      18.049 -41.374  29.204  1.00106.01           C  
ATOM   1695  CA  GLY E 188      17.533 -44.826  30.600  1.00 30.88           C  
ATOM   1696  CA  GLY E 189      21.283 -45.204  30.660  1.00 25.14           C  
ATOM   1697  CA  ALA E 190      23.296 -46.207  33.652  1.00 44.02           C  
ATOM   1698  CA  LEU E 191      25.292 -44.221  36.142  1.00 93.12           C  
ATOM   1699  CA  LEU E 192      27.915 -46.456  37.611  1.00 55.62           C  
ATOM   1700  CA  ASN E 193      30.303 -46.297  40.495  1.00 54.82           C  
ATOM   1701  CA  LEU E 194      33.933 -47.282  40.260  1.00 90.19           C  
ATOM   1702  CA  ASN E 195      32.856 -50.808  41.079  1.00 44.05           C  
ATOM   1703  CA  GLY E 196      30.747 -50.780  37.971  1.00 25.07           C  
ATOM   1704  CA  GLU E 197      27.658 -51.114  40.120  1.00 41.83           C  
ATOM   1705  CA  LEU E 198      24.540 -49.200  39.167  1.00 59.71           C  
ATOM   1706  CA  ILE E 199      24.084 -46.039  41.215  1.00104.32           C  
ATOM   1707  CA  GLY E 200      21.123 -44.741  39.233  1.00 25.08           C  
ATOM   1708  CA  ILE E 201      19.477 -44.305  35.858  1.00 50.01           C  
ATOM   1709  CA  ASN E 202      20.145 -41.063  34.008  1.00 94.12           C  
ATOM   1710  CA  THR E 203      16.782 -39.364  33.659  1.00 90.81           C  
ATOM   1711  CA  ALA E 204      17.368 -35.765  32.652  1.00 59.33           C  
ATOM   1712  CA  ILE E 205      19.573 -32.725  32.391  1.00 65.99           C  
ATOM   1713  CA  LEU E 206      19.368 -29.007  32.888  1.00 52.37           C  
ATOM   1714  CA  ALA E 207      20.888 -27.237  29.957  1.00 41.92           C  
ATOM   1715  CA  PRO E 208      19.985 -23.992  28.407  1.00 67.71           C  
ATOM   1716  CA  GLY E 209      21.734 -25.026  25.209  1.00 33.52           C  
ATOM   1717  CA  GLY E 210      20.138 -28.412  25.060  1.00 23.93           C  
ATOM   1718  CA  GLY E 211      23.649 -29.720  25.467  1.00 24.31           C  
ATOM   1719  CA  SER E 212      25.298 -30.988  28.614  1.00 60.09           C  
ATOM   1720  CA  VAL E 213      26.016 -28.138  31.019  1.00 60.43           C  
ATOM   1721  CA  GLY E 214      27.467 -30.542  33.516  1.00 37.06           C  
ATOM   1722  CA  ILE E 215      24.257 -30.727  35.467  1.00 52.90           C  
ATOM   1723  CA  GLY E 216      22.614 -34.094  35.047  1.00 21.46           C  
ATOM   1724  CA  PHE E 217      20.093 -35.962  37.126  1.00 43.45           C  
ATOM   1725  CA  ALA E 218      19.537 -39.652  37.643  1.00 35.79           C  
ATOM   1726  CA  ILE E 219      17.059 -41.693  39.592  1.00120.85           C  
ATOM   1727  CA  PRO E 220      18.793 -43.560  42.283  1.00 84.20           C  
ATOM   1728  CA  SER E 221      19.477 -47.260  41.925  1.00 39.80           C  
ATOM   1729  CA  ASN E 222      17.574 -47.977  45.049  1.00 60.70           C  
ATOM   1730  CA  MET E 223      14.955 -46.151  43.213  1.00104.13           C  
ATOM   1731  CA  ALA E 224      14.929 -48.142  40.052  1.00 48.56           C  
ATOM   1732  CA  ARG E 225      15.618 -51.420  41.733  1.00115.90           C  
ATOM   1733  CA  THR E 226      12.653 -51.825  43.958  1.00 67.70           C  
ATOM   1734  CA  LEU E 227      10.399 -49.970  41.501  1.00117.07           C  
ATOM   1735  CA  ALA E 228      11.545 -52.343  38.827  1.00 45.06           C  
ATOM   1736  CA  GLN E 229      11.097 -55.242  41.149  1.00144.78           C  
ATOM   1737  CA  GLN E 230       7.391 -55.135  41.538  1.00118.46           C  
ATOM   1738  CA  LEU E 231       7.073 -54.329  37.889  1.00 54.52           C  
ATOM   1739  CA  ILE E 232       8.037 -57.923  37.575  1.00125.38           C  
ATOM   1740  CA  ASP E 233       6.787 -58.821  41.077  1.00168.75           C  
ATOM   1741  CA  PHE E 234       4.902 -58.157  43.241  1.00179.12           C  
ATOM   1742  CA  GLY E 235       3.284 -55.828  40.822  1.00 39.93           C  
ATOM   1743  CA  GLU E 236       0.657 -54.684  43.200  1.00 95.31           C  
ATOM   1744  CA  ILE E 237      -1.469 -52.222  41.331  1.00 86.60           C  
ATOM   1745  CA  LYS E 238      -1.046 -49.771  44.123  1.00215.22           C  
ATOM   1746  CA  ARG E 239       0.620 -47.615  44.719  1.00219.39           C  
ATOM   1747  CA  GLY E 240       1.833 -48.128  41.191  1.00 47.71           C  
ATOM   1748  CA  LEU E 241       3.318 -44.745  41.696  1.00185.49           C  
ATOM   1749  CA  LEU E 242       0.973 -42.085  42.886  1.00 97.98           C  
ATOM   1750  CA  GLY E 243       0.298 -40.326  39.612  1.00 53.34           C  
ATOM   1751  CA  ILE E 244       0.891 -36.758  40.642  1.00188.51           C  
ATOM   1752  CA  LYS E 245       2.990 -33.753  39.721  1.00118.83           C  
ATOM   1753  CA  GLY E 246       4.757 -31.548  42.159  1.00 32.17           C  
ATOM   1754  CA  THR E 247       7.782 -29.453  42.832  1.00110.59           C  
ATOM   1755  CA  GLU E 248       9.687 -27.783  45.623  1.00 51.32           C  
ATOM   1756  CA  MET E 249       8.016 -25.519  48.088  1.00146.17           C  
ATOM   1757  CA  SER E 250       6.826 -22.485  46.204  1.00 36.64           C  
ATOM   1758  CA  ALA E 251       7.972 -19.060  47.237  1.00 37.97           C  
ATOM   1759  CA  ASP E 252       4.467 -17.653  47.208  1.00 49.62           C  
ATOM   1760  CA  ILE E 253       2.711 -20.322  49.193  1.00 66.93           C  
ATOM   1761  CA  ALA E 254       5.527 -21.174  51.532  1.00 57.82           C  
ATOM   1762  CA  LYS E 255       6.476 -17.839  52.845  1.00119.58           C  
ATOM   1763  CA  ALA E 256       3.145 -16.168  52.904  1.00 68.32           C  
ATOM   1764  CA  PHE E 257       0.776 -18.492  54.622  1.00181.33           C  
ATOM   1765  CA  ASN E 258       3.509 -20.283  56.281  1.00185.18           C  
ATOM   1766  CA  LEU E 259       3.216 -23.945  55.858  1.00175.34           C  
ATOM   1767  CA  ASP E 260       3.004 -25.920  59.053  1.00 63.85           C  
ATOM   1768  CA  VAL E 261       5.699 -28.231  57.800  1.00109.92           C  
ATOM   1769  CA  GLN E 262       8.712 -26.215  56.827  1.00 96.87           C  
ATOM   1770  CA  ARG E 263       8.699 -27.730  53.423  1.00100.35           C  
ATOM   1771  CA  GLY E 264       7.574 -30.769  51.603  1.00 23.96           C  
ATOM   1772  CA  ALA E 265       6.747 -32.134  48.251  1.00 40.50           C  
ATOM   1773  CA  PHE E 266       4.043 -29.882  47.089  1.00128.28           C  
ATOM   1774  CA  VAL E 267       1.614 -31.062  44.548  1.00 73.39           C  
ATOM   1775  CA  SER E 268       0.228 -28.718  41.950  1.00105.20           C  
ATOM   1776  CA  GLU E 269      -1.824 -31.319  40.192  1.00110.15           C  
ATOM   1777  CA  VAL E 270      -4.156 -34.267  40.495  1.00101.50           C  
ATOM   1778  CA  LEU E 271      -3.967 -36.999  37.889  1.00 91.33           C  
ATOM   1779  CA  PRO E 272      -7.112 -38.495  36.602  1.00 67.45           C  
ATOM   1780  CA  GLY E 273      -7.840 -42.107  37.451  1.00 24.49           C  
ATOM   1781  CA  SER E 274      -4.577 -41.698  39.209  1.00 41.75           C  
ATOM   1782  CA  GLY E 275      -3.480 -43.222  42.399  1.00 31.34           C  
ATOM   1783  CA  SER E 276      -3.418 -39.875  44.003  1.00 48.29           C  
ATOM   1784  CA  ALA E 277      -6.858 -39.230  42.674  1.00 62.53           C  
ATOM   1785  CA  LYS E 278      -8.678 -42.057  44.317  1.00110.81           C  
ATOM   1786  CA  ALA E 279      -6.497 -41.898  47.370  1.00 42.72           C  
ATOM   1787  CA  GLY E 280      -8.032 -38.529  47.585  1.00 41.85           C  
ATOM   1788  CA  VAL E 281      -4.832 -36.579  47.502  1.00 74.67           C  
ATOM   1789  CA  LYS E 282      -5.460 -33.463  45.660  1.00169.97           C  
ATOM   1790  CA  ALA E 283      -3.695 -30.343  44.608  1.00116.67           C  
ATOM   1791  CA  GLY E 284      -2.224 -27.733  46.795  1.00 47.83           C  
ATOM   1792  CA  ASP E 285      -1.201 -30.746  48.788  1.00100.09           C  
ATOM   1793  CA  ILE E 286       1.852 -30.689  50.815  1.00125.06           C  
ATOM   1794  CA  ILE E 287       3.342 -34.112  51.252  1.00 61.21           C  
ATOM   1795  CA  THR E 288       5.055 -33.944  54.602  1.00 54.49           C  
ATOM   1796  CA  SER E 289       6.075 -37.506  54.965  1.00 97.15           C  
ATOM   1797  CA  LEU E 290       5.993 -40.944  53.519  1.00 72.48           C  
ATOM   1798  CA  ASN E 291       5.534 -43.886  55.810  1.00179.37           C  
ATOM   1799  CA  GLY E 292       6.380 -43.769  59.511  1.00 52.58           C  
ATOM   1800  CA  LYS E 293       9.681 -41.997  59.061  1.00 70.35           C  
ATOM   1801  CA  PRO E 294       9.644 -38.392  58.155  1.00 61.69           C  
ATOM   1802  CA  LEU E 295       9.930 -37.271  54.557  1.00121.34           C  
ATOM   1803  CA  ASN E 296      12.320 -34.605  53.413  1.00 67.98           C  
ATOM   1804  CA  SER E 297      11.923 -32.337  50.457  1.00 46.44           C  
ATOM   1805  CA  PHE E 298      10.304 -33.216  47.201  1.00 73.84           C  
ATOM   1806  CA  ALA E 299      13.708 -34.605  46.500  1.00 45.17           C  
ATOM   1807  CA  GLU E 300      13.629 -37.142  49.240  1.00 92.04           C  
ATOM   1808  CA  LEU E 301      10.168 -37.991  48.055  1.00 71.39           C  
ATOM   1809  CA  ARG E 302      11.081 -39.665  44.872  1.00193.02           C  
ATOM   1810  CA  SER E 303      14.168 -40.976  46.475  1.00 56.63           C  
ATOM   1811  CA  ARG E 304      12.214 -43.237  48.644  1.00253.62           C  
ATOM   1812  CA  ILE E 305       9.276 -43.787  46.328  1.00127.75           C  
ATOM   1813  CA  ALA E 306      11.326 -44.141  43.251  1.00 65.24           C  
ATOM   1814  CA  THR E 307      13.186 -46.519  45.459  1.00 61.19           C  
ATOM   1815  CA  THR E 308      10.123 -48.377  46.541  1.00134.28           C  
ATOM   1816  CA  GLU E 309       8.178 -50.964  44.625  1.00 91.19           C  
ATOM   1817  CA  PRO E 310       5.706 -49.388  42.371  1.00181.31           C  
ATOM   1818  CA  GLY E 311       3.563 -50.959  43.679  1.00124.29           C  
ATOM   1819  CA  THR E 312       3.964 -51.150  47.398  1.00 56.14           C  
ATOM   1820  CA  LYS E 313       1.018 -49.980  49.371  1.00118.97           C  
ATOM   1821  CA  VAL E 314       2.198 -46.994  51.316  1.00 50.85           C  
ATOM   1822  CA  LYS E 315       0.763 -44.266  53.500  1.00116.40           C  
ATOM   1823  CA  LEU E 316       1.374 -40.623  52.800  1.00111.79           C  
ATOM   1824  CA  GLY E 317       1.293 -37.736  55.172  1.00 47.92           C  
ATOM   1825  CA  LEU E 318       0.302 -34.422  53.813  1.00131.88           C  
ATOM   1826  CA  LEU E 319      -0.877 -31.184  55.053  1.00115.36           C  
ATOM   1827  CA  ARG E 320      -3.944 -29.779  53.742  1.00224.68           C  
ATOM   1828  CA  ASN E 321      -5.532 -26.690  55.221  1.00208.84           C  
ATOM   1829  CA  GLY E 322      -3.036 -26.706  57.905  1.00 49.86           C  
ATOM   1830  CA  LYS E 323      -4.443 -29.908  59.064  1.00192.41           C  
ATOM   1831  CA  PRO E 324      -3.187 -33.355  59.071  1.00124.73           C  
ATOM   1832  CA  LEU E 325      -4.254 -36.634  57.530  1.00232.21           C  
ATOM   1833  CA  GLU E 326      -3.013 -39.962  56.612  1.00107.87           C  
ATOM   1834  CA  VAL E 327      -4.140 -41.689  53.500  1.00 64.64           C  
ATOM   1835  CA  GLU E 328      -3.226 -44.924  51.865  1.00 46.20           C  
ATOM   1836  CA  VAL E 329      -1.887 -44.482  48.391  1.00113.19           C  
ATOM   1837  CA  SER E 340     -26.318 -44.842  22.379  1.00 56.17           C  
ATOM   1838  CA  ALA E 341     -25.944 -44.365  18.639  1.00 77.21           C  
ATOM   1839  CA  GLU E 342     -24.122 -41.074  18.925  1.00 48.24           C  
ATOM   1840  CA  MET E 343     -20.684 -42.316  19.678  1.00 45.67           C  
ATOM   1841  CA  ILE E 344     -20.688 -44.809  16.880  1.00 96.76           C  
ATOM   1842  CA  THR E 345     -22.457 -42.466  14.561  1.00 66.94           C  
ATOM   1843  CA  PRO E 346     -21.827 -38.796  14.535  1.00241.71           C  
ATOM   1844  CA  ALA E 347     -24.270 -36.365  16.094  1.00 74.10           C  
ATOM   1845  CA  LEU E 348     -27.025 -38.894  15.419  1.00 97.81           C  
ATOM   1846  CA  GLU E 349     -28.814 -38.952  18.726  1.00141.45           C  
ATOM   1847  CA  GLY E 350     -30.848 -42.055  19.113  1.00 30.03           C  
ATOM   1848  CA  ALA E 351     -31.265 -45.500  20.537  1.00 38.26           C  
ATOM   1849  CA  THR E 352     -28.463 -46.853  22.632  1.00 48.46           C  
ATOM   1850  CA  LEU E 353     -26.297 -49.557  21.214  1.00 59.46           C  
ATOM   1851  CA  SER E 354     -24.701 -52.565  22.824  1.00 33.22           C  
ATOM   1852  CA  ASP E 355     -22.152 -54.962  21.431  1.00 36.49           C  
ATOM   1853  CA  GLY E 356     -22.321 -58.682  21.356  1.00 46.07           C  
ATOM   1854  CA  GLN E 357     -25.371 -60.591  20.330  1.00172.04           C  
ATOM   1855  CA  LEU E 358     -25.345 -60.498  23.969  1.00198.11           C  
ATOM   1856  CA  LYS E 359     -28.098 -63.073  24.260  1.00170.45           C  
ATOM   1857  CA  ASP E 360     -26.754 -65.409  21.591  1.00133.94           C  
ATOM   1858  CA  GLY E 361     -23.710 -65.563  19.348  1.00 31.50           C  
ATOM   1859  CA  GLY E 362     -22.883 -62.085  18.165  1.00 39.50           C  
ATOM   1860  CA  LYS E 363     -25.074 -61.446  15.187  1.00115.95           C  
ATOM   1861  CA  GLY E 364     -24.023 -57.899  15.628  1.00 33.37           C  
ATOM   1862  CA  ILE E 365     -24.591 -54.747  17.616  1.00 60.51           C  
ATOM   1863  CA  LYS E 366     -27.919 -54.401  19.313  1.00 52.01           C  
ATOM   1864  CA  ILE E 367     -29.814 -51.208  19.701  1.00 61.53           C  
ATOM   1865  CA  ASP E 368     -31.092 -51.117  23.242  1.00 56.70           C  
ATOM   1866  CA  GLU E 369     -33.910 -48.657  23.035  1.00 85.03           C  
ATOM   1867  CA  VAL E 370     -35.234 -45.973  20.770  1.00126.83           C  
ATOM   1868  CA  VAL E 371     -35.195 -42.392  22.009  1.00180.57           C  
ATOM   1869  CA  LYS E 372     -37.528 -41.956  18.994  1.00238.61           C  
ATOM   1870  CA  GLY E 373     -37.772 -38.195  19.142  1.00 39.09           C  
ATOM   1871  CA  SER E 374     -34.075 -38.520  18.211  1.00111.48           C  
ATOM   1872  CA  PRO E 375     -32.766 -38.601  14.749  1.00 81.24           C  
ATOM   1873  CA  ALA E 376     -31.480 -42.134  15.087  1.00 52.30           C  
ATOM   1874  CA  ALA E 377     -35.177 -42.781  15.307  1.00 48.76           C  
ATOM   1875  CA  GLN E 378     -35.976 -40.712  12.243  1.00 53.77           C  
ATOM   1876  CA  ALA E 379     -34.145 -42.864   9.703  1.00 56.92           C  
ATOM   1877  CA  GLY E 380     -35.669 -46.176  10.652  1.00 61.49           C  
ATOM   1878  CA  LEU E 381     -33.807 -47.459  13.643  1.00 61.72           C  
ATOM   1879  CA  GLN E 382     -36.196 -49.134  16.044  1.00 62.97           C  
ATOM   1880  CA  LYS E 383     -35.183 -50.976  19.156  1.00144.09           C  
ATOM   1881  CA  ASP E 384     -34.353 -54.671  19.251  1.00 82.62           C  
ATOM   1882  CA  ASP E 385     -32.763 -54.444  15.856  1.00 48.04           C  
ATOM   1883  CA  VAL E 386     -29.511 -56.238  15.437  1.00129.85           C  
ATOM   1884  CA  ILE E 387     -27.044 -54.800  13.023  1.00 58.60           C  
ATOM   1885  CA  ILE E 388     -25.536 -57.791  11.303  1.00112.42           C  
ATOM   1886  CA  GLY E 389     -23.072 -55.752   9.298  1.00 55.05           C  
ATOM   1887  CA  VAL E 390     -22.407 -52.538   7.418  1.00 71.70           C  
ATOM   1888  CA  ASN E 391     -21.640 -52.010   3.756  1.00 89.55           C  
ATOM   1889  CA  ARG E 392     -21.240 -55.624   2.767  1.00165.44           C  
ATOM   1890  CA  ASP E 393     -19.181 -56.260   5.801  1.00143.83           C  
ATOM   1891  CA  ARG E 394     -20.241 -58.239   8.786  1.00 96.75           C  
ATOM   1892  CA  VAL E 395     -20.353 -56.473  12.092  1.00 45.20           C  
ATOM   1893  CA  ASN E 396     -19.663 -58.810  14.972  1.00 47.20           C  
ATOM   1894  CA  SER E 397     -19.530 -56.010  17.487  1.00 38.62           C  
ATOM   1895  CA  ILE E 398     -19.176 -52.270  17.889  1.00 42.86           C  
ATOM   1896  CA  ALA E 399     -15.496 -52.251  17.123  1.00 25.31           C  
ATOM   1897  CA  GLU E 400     -15.998 -53.803  13.728  1.00 41.60           C  
ATOM   1898  CA  MET E 401     -18.888 -51.524  12.958  1.00 35.15           C  
ATOM   1899  CA  ARG E 402     -16.699 -48.622  13.847  1.00199.41           C  
ATOM   1900  CA  LYS E 403     -14.187 -49.972  11.376  1.00130.19           C  
ATOM   1901  CA  VAL E 404     -16.612 -49.745   8.490  1.00 49.40           C  
ATOM   1902  CA  LEU E 405     -17.321 -46.218   9.620  1.00 68.35           C  
ATOM   1903  CA  ALA E 406     -13.622 -45.572   9.660  1.00 34.29           C  
ATOM   1904  CA  ALA E 407     -13.781 -45.838   5.902  1.00 31.29           C  
ATOM   1905  CA  LYS E 408     -16.457 -43.188   6.183  1.00104.86           C  
ATOM   1906  CA  PRO E 409     -18.193 -44.162   3.036  1.00146.80           C  
ATOM   1907  CA  ALA E 410     -20.635 -41.525   1.887  1.00 32.45           C  
ATOM   1908  CA  ILE E 411     -23.088 -44.398   1.701  1.00 83.72           C  
ATOM   1909  CA  ILE E 412     -23.564 -46.412   4.836  1.00 49.30           C  
ATOM   1910  CA  ALA E 413     -25.841 -49.360   4.631  1.00 57.76           C  
ATOM   1911  CA  LEU E 414     -27.001 -51.031   7.793  1.00134.01           C  
ATOM   1912  CA  GLN E 415     -28.670 -54.378   7.581  1.00143.26           C  
ATOM   1913  CA  ILE E 416     -30.255 -55.352  10.719  1.00 90.90           C  
ATOM   1914  CA  VAL E 417     -32.488 -58.211  11.487  1.00 44.94           C  
ATOM   1915  CA  ARG E 418     -35.806 -57.250  12.927  1.00 74.75           C  
ATOM   1916  CA  GLY E 419     -38.106 -59.936  14.120  1.00 19.49           C  
ATOM   1917  CA  ASN E 420     -37.526 -62.841  11.869  1.00 49.04           C  
ATOM   1918  CA  GLU E 421     -36.721 -60.837   8.804  1.00 84.43           C  
ATOM   1919  CA  SER E 422     -33.940 -58.924   7.176  1.00 90.40           C  
ATOM   1920  CA  ILE E 423     -33.936 -55.181   7.372  1.00 76.80           C  
ATOM   1921  CA  TYR E 424     -31.804 -52.597   5.777  1.00165.11           C  
ATOM   1922  CA  LEU E 425     -31.083 -49.268   7.224  1.00 94.61           C  
ATOM   1923  CA  LEU E 426     -29.020 -46.470   6.012  1.00233.72           C  
ATOM   1924  CA  MET E 427     -27.450 -43.125   6.482  1.00 64.42           C  
TER    1925      MET E 427                                                      
ATOM   1926  CA  PRO F  11      44.868 -37.994  45.919  1.00 77.86           C  
ATOM   1927  CA  LEU F  12      46.502 -35.862  43.276  1.00 93.86           C  
ATOM   1928  CA  PRO F  13      48.986 -37.362  40.957  1.00154.00           C  
ATOM   1929  CA  SER F  14      49.462 -34.510  40.830  1.00157.31           C  
ATOM   1930  CA  LEU F  15      49.149 -33.415  37.206  1.00107.45           C  
ATOM   1931  CA  ALA F  16      51.430 -30.443  37.676  1.00 43.16           C  
ATOM   1932  CA  PRO F  17      54.611 -32.337  38.149  1.00 73.17           C  
ATOM   1933  CA  MET F  18      54.092 -34.304  34.961  1.00134.26           C  
ATOM   1934  CA  LEU F  19      52.909 -31.200  33.206  1.00163.42           C  
ATOM   1935  CA  GLU F  20      55.883 -29.076  34.055  1.00 61.76           C  
ATOM   1936  CA  LYS F  21      58.350 -31.171  32.167  1.00164.91           C  
ATOM   1937  CA  VAL F  22      56.081 -31.946  29.199  1.00110.29           C  
ATOM   1938  CA  LEU F  23      54.545 -28.550  28.506  1.00125.86           C  
ATOM   1939  CA  PRO F  24      57.463 -26.955  26.791  1.00 66.21           C  
ATOM   1940  CA  ALA F  25      57.104 -29.650  24.152  1.00 36.01           C  
ATOM   1941  CA  VAL F  26      53.735 -28.347  23.053  1.00115.36           C  
ATOM   1942  CA  VAL F  27      53.846 -25.224  20.991  1.00127.57           C  
ATOM   1943  CA  SER F  28      51.474 -22.779  19.441  1.00 99.42           C  
ATOM   1944  CA  VAL F  29      51.602 -22.388  15.740  1.00109.63           C  
ATOM   1945  CA  ARG F  30      50.853 -19.128  14.059  1.00 92.06           C  
ATOM   1946  CA  VAL F  31      50.172 -18.828  10.402  1.00 44.35           C  
ATOM   1947  CA  GLU F  32      49.580 -16.124   7.875  1.00 70.07           C  
ATOM   1948  CA  GLY F  33      48.776 -16.482   4.252  1.00 30.20           C  
ATOM   1949  CA  THR F  34      46.469 -15.971   1.329  1.00107.28           C  
ATOM   1950  CA  ALA F  35      44.060 -13.360  -1.358  1.00 18.22           C  
ATOM   1951  CA  GLN F  59      43.269 -11.305   1.691  1.00 69.33           C  
ATOM   1952  CA  PRO F  60      45.630 -11.850   4.507  1.00 66.85           C  
ATOM   1953  CA  PHE F  61      44.490 -13.951   7.388  1.00 51.45           C  
ATOM   1954  CA  GLU F  62      46.073 -15.004  10.611  1.00 29.59           C  
ATOM   1955  CA  GLY F  63      45.311 -18.346  12.123  1.00 22.24           C  
ATOM   1956  CA  LEU F  64      46.282 -19.927  15.386  1.00 86.77           C  
ATOM   1957  CA  GLY F  65      46.786 -23.575  16.147  1.00 23.24           C  
ATOM   1958  CA  SER F  66      49.088 -25.796  18.130  1.00 79.74           C  
ATOM   1959  CA  GLY F  67      51.755 -28.354  17.448  1.00 17.49           C  
ATOM   1960  CA  VAL F  68      53.996 -30.788  19.242  1.00 40.23           C  
ATOM   1961  CA  ILE F  69      57.741 -31.027  19.038  1.00 50.06           C  
ATOM   1962  CA  ILE F  70      58.634 -34.548  17.994  1.00 89.35           C  
ATOM   1963  CA  ASN F  71      62.367 -34.001  17.633  1.00169.36           C  
ATOM   1964  CA  ALA F  72      64.125 -31.404  19.657  1.00 41.90           C  
ATOM   1965  CA  SER F  73      67.309 -31.722  17.698  1.00 42.97           C  
ATOM   1966  CA  LYS F  74      65.782 -31.538  14.276  1.00 91.47           C  
ATOM   1967  CA  GLY F  75      63.062 -29.202  15.393  1.00 28.46           C  
ATOM   1968  CA  TYR F  76      60.290 -31.256  13.855  1.00 78.35           C  
ATOM   1969  CA  VAL F  77      56.832 -30.268  14.978  1.00 47.19           C  
ATOM   1970  CA  LEU F  78      53.677 -32.193  14.218  1.00 55.40           C  
ATOM   1971  CA  THR F  79      50.514 -30.316  13.479  1.00 48.05           C  
ATOM   1972  CA  ASN F  80      47.260 -30.711  11.679  1.00 64.79           C  
ATOM   1973  CA  ASN F  81      47.344 -30.098   7.977  1.00 47.42           C  
ATOM   1974  CA  HIS F  82      44.348 -27.837   8.137  1.00 51.68           C  
ATOM   1975  CA  VAL F  83      46.126 -25.496  10.453  1.00 44.43           C  
ATOM   1976  CA  ILE F  84      49.067 -25.261   8.031  1.00183.94           C  
ATOM   1977  CA  ASN F  85      47.314 -25.597   4.697  1.00 77.07           C  
ATOM   1978  CA  GLN F  86      46.780 -21.961   3.778  1.00 65.19           C  
ATOM   1979  CA  ALA F  87      49.895 -20.662   5.516  1.00 68.63           C  
ATOM   1980  CA  GLN F  88      52.379 -18.761   3.423  1.00 56.58           C  
ATOM   1981  CA  LYS F  89      54.496 -18.245   6.507  1.00 33.55           C  
ATOM   1982  CA  ILE F  90      54.521 -20.185   9.725  1.00 85.29           C  
ATOM   1983  CA  SER F  91      55.886 -19.267  13.098  1.00 31.84           C  
ATOM   1984  CA  ILE F  92      56.094 -21.316  16.232  1.00 72.35           C  
ATOM   1985  CA  GLN F  93      55.952 -19.947  19.720  1.00122.96           C  
ATOM   1986  CA  LEU F  94      57.220 -21.687  22.805  1.00 48.12           C  
ATOM   1987  CA  ASN F  95      55.502 -21.369  26.148  1.00 38.46           C  
ATOM   1988  CA  ASP F  96      58.526 -19.414  27.290  1.00 50.50           C  
ATOM   1989  CA  GLY F  97      57.775 -16.734  24.737  1.00 29.47           C  
ATOM   1990  CA  ARG F  98      60.568 -17.556  22.338  1.00 97.38           C  
ATOM   1991  CA  GLU F  99      59.474 -17.705  18.740  1.00 43.91           C  
ATOM   1992  CA  PHE F 100      60.893 -19.330  15.654  1.00 42.56           C  
ATOM   1993  CA  ASP F 101      60.081 -19.586  11.988  1.00 27.50           C  
ATOM   1994  CA  ALA F 102      59.113 -22.911  10.529  1.00 28.67           C  
ATOM   1995  CA  LYS F 103      58.898 -24.493   7.119  1.00 52.86           C  
ATOM   1996  CA  LEU F 104      56.501 -27.168   6.053  1.00120.02           C  
ATOM   1997  CA  ILE F 105      58.320 -30.434   5.633  1.00142.62           C  
ATOM   1998  CA  GLY F 106      55.328 -32.233   4.239  1.00 31.29           C  
ATOM   1999  CA  SER F 107      51.755 -33.041   5.019  1.00 55.82           C  
ATOM   2000  CA  ASP F 108      48.793 -34.938   3.776  1.00106.69           C  
ATOM   2001  CA  ASP F 109      45.137 -34.064   3.425  1.00 64.78           C  
ATOM   2002  CA  GLN F 110      43.419 -37.316   4.114  1.00142.79           C  
ATOM   2003  CA  SER F 111      44.798 -38.054   7.559  1.00 66.01           C  
ATOM   2004  CA  ASP F 112      45.266 -34.338   8.178  1.00 71.93           C  
ATOM   2005  CA  ILE F 113      48.822 -34.727   9.459  1.00100.84           C  
ATOM   2006  CA  ALA F 114      51.532 -32.221   8.684  1.00 34.74           C  
ATOM   2007  CA  LEU F 115      55.161 -31.969   9.678  1.00102.32           C  
ATOM   2008  CA  LEU F 116      56.931 -28.684  10.228  1.00 54.63           C  
ATOM   2009  CA  GLN F 117      60.557 -27.926  10.871  1.00 41.97           C  
ATOM   2010  CA  ILE F 118      61.774 -25.116  13.060  1.00106.17           C  
ATOM   2011  CA  GLN F 119      64.641 -23.119  11.725  1.00 99.34           C  
ATOM   2012  CA  ASN F 120      67.505 -22.784  14.193  1.00127.39           C  
ATOM   2013  CA  PRO F 121      65.607 -24.721  16.774  1.00107.58           C  
ATOM   2014  CA  SER F 122      67.983 -24.325  19.770  1.00248.46           C  
ATOM   2015  CA  LYS F 123      67.201 -25.696  23.233  1.00 77.99           C  
ATOM   2016  CA  LEU F 124      63.928 -27.405  22.570  1.00 87.33           C  
ATOM   2017  CA  THR F 125      62.125 -30.059  24.523  1.00 98.76           C  
ATOM   2018  CA  GLN F 126      60.672 -33.124  22.866  1.00131.20           C  
ATOM   2019  CA  ILE F 127      57.614 -35.104  23.705  1.00 70.11           C  
ATOM   2020  CA  ALA F 128      57.753 -38.845  24.105  1.00 36.66           C  
ATOM   2021  CA  ILE F 129      55.380 -40.909  22.019  1.00103.71           C  
ATOM   2022  CA  ALA F 130      53.166 -43.547  23.579  1.00 34.70           C  
ATOM   2023  CA  ASP F 131      51.684 -46.554  21.847  1.00 42.54           C  
ATOM   2024  CA  SER F 132      48.171 -45.596  20.832  1.00 49.90           C  
ATOM   2025  CA  ASP F 133      47.096 -49.138  20.244  1.00126.26           C  
ATOM   2026  CA  LYS F 134      47.563 -49.793  23.938  1.00 75.96           C  
ATOM   2027  CA  LEU F 135      45.011 -47.148  24.890  1.00 60.64           C  
ATOM   2028  CA  ARG F 136      41.781 -48.342  26.389  1.00159.61           C  
ATOM   2029  CA  VAL F 137      38.633 -46.480  27.233  1.00 86.27           C  
ATOM   2030  CA  GLY F 138      38.835 -44.943  30.641  1.00 32.77           C  
ATOM   2031  CA  ASP F 139      42.447 -43.959  30.408  1.00 39.95           C  
ATOM   2032  CA  PHE F 140      43.176 -40.448  31.568  1.00 57.67           C  
ATOM   2033  CA  ALA F 141      44.135 -37.858  29.032  1.00 29.76           C  
ATOM   2034  CA  VAL F 142      45.278 -34.264  29.097  1.00 38.88           C  
ATOM   2035  CA  ALA F 143      44.930 -31.947  26.164  1.00 31.20           C  
ATOM   2036  CA  VAL F 144      47.282 -29.089  25.596  1.00103.90           C  
ATOM   2037  CA  GLY F 145      46.935 -26.420  22.964  1.00 23.82           C  
ATOM   2038  CA  ASN F 146      45.861 -22.864  22.551  1.00 69.61           C  
ATOM   2039  CA  PRO F 147      42.178 -22.450  22.634  1.00 69.09           C  
ATOM   2040  CA  PHE F 148      40.974 -19.101  21.383  1.00 65.23           C  
ATOM   2041  CA  GLY F 149      44.623 -18.187  21.123  1.00 26.23           C  
ATOM   2042  CA  LEU F 150      44.591 -17.555  24.845  1.00 55.70           C  
ATOM   2043  CA  GLY F 151      47.952 -19.205  25.322  1.00 29.60           C  
ATOM   2044  CA  GLN F 152      49.045 -22.644  26.369  1.00 50.76           C  
ATOM   2045  CA  THR F 153      46.102 -24.261  28.085  1.00 36.36           C  
ATOM   2046  CA  ALA F 154      45.764 -27.688  29.586  1.00 32.28           C  
ATOM   2047  CA  THR F 155      42.517 -29.533  29.983  1.00107.12           C  
ATOM   2048  CA  SER F 156      41.825 -32.920  31.489  1.00 34.87           C  
ATOM   2049  CA  GLY F 157      39.537 -35.811  30.648  1.00 20.80           C  
ATOM   2050  CA  ILE F 158      39.504 -39.517  29.850  1.00 95.78           C  
ATOM   2051  CA  VAL F 159      39.559 -41.445  26.614  1.00129.38           C  
ATOM   2052  CA  SER F 160      35.935 -41.794  25.737  1.00 50.38           C  
ATOM   2053  CA  ALA F 161      36.351 -44.041  22.741  1.00 45.20           C  
ATOM   2054  CA  LEU F 162      38.757 -45.233  20.110  1.00 98.71           C  
ATOM   2055  CA  GLY F 163      38.636 -46.347  16.526  1.00 33.10           C  
ATOM   2056  CA  ARG F 164      35.927 -44.008  15.575  1.00102.57           C  
ATOM   2057  CA  SER F 165      35.026 -42.673  12.233  1.00158.88           C  
ATOM   2058  CA  GLY F 166      32.414 -41.992   9.678  1.00 40.58           C  
ATOM   2059  CA  LEU F 167      32.520 -38.502  11.115  1.00 55.07           C  
ATOM   2060  CA  ASN F 168      33.431 -37.478   7.583  1.00 66.18           C  
ATOM   2061  CA  LEU F 169      35.775 -34.946   9.037  1.00 52.69           C  
ATOM   2062  CA  GLU F 170      38.736 -36.467   7.236  1.00101.99           C  
ATOM   2063  CA  GLY F 171      39.495 -38.889   4.418  1.00 40.50           C  
ATOM   2064  CA  LEU F 172      41.063 -41.351   6.777  1.00129.58           C  
ATOM   2065  CA  GLU F 173      39.742 -41.296  10.248  1.00 86.91           C  
ATOM   2066  CA  ASN F 174      40.388 -43.231  13.419  1.00100.15           C  
ATOM   2067  CA  PHE F 175      39.893 -40.719  16.044  1.00 86.20           C  
ATOM   2068  CA  ILE F 176      40.493 -41.247  19.667  1.00158.81           C  
ATOM   2069  CA  GLN F 177      37.580 -39.609  21.369  1.00 62.24           C  
ATOM   2070  CA  THR F 178      38.206 -37.515  24.439  1.00 88.55           C  
ATOM   2071  CA  ASP F 179      36.111 -35.680  27.015  1.00 67.56           C  
ATOM   2072  CA  ALA F 180      38.904 -33.186  27.597  1.00 47.48           C  
ATOM   2073  CA  SER F 181      37.817 -29.726  26.629  1.00 42.64           C  
ATOM   2074  CA  ILE F 182      38.962 -29.038  23.125  1.00 93.42           C  
ATOM   2075  CA  ASN F 183      38.076 -25.850  21.342  1.00 42.19           C  
ATOM   2076  CA  ARG F 184      39.168 -24.009  18.282  1.00 91.52           C  
ATOM   2077  CA  GLY F 185      42.875 -23.360  18.394  1.00 22.93           C  
ATOM   2078  CA  ASN F 186      43.377 -26.793  19.908  1.00 54.83           C  
ATOM   2079  CA  ALA F 187      44.132 -28.330  16.544  1.00 97.94           C  
ATOM   2080  CA  GLY F 188      47.582 -29.748  16.175  1.00 26.56           C  
ATOM   2081  CA  GLY F 189      47.806 -29.789  19.938  1.00 24.66           C  
ATOM   2082  CA  ALA F 190      48.747 -32.770  21.995  1.00 45.71           C  
ATOM   2083  CA  LEU F 191      46.711 -35.272  23.921  1.00115.92           C  
ATOM   2084  CA  LEU F 192      48.854 -36.718  26.634  1.00 54.31           C  
ATOM   2085  CA  ASN F 193      48.636 -39.599  29.030  1.00 51.35           C  
ATOM   2086  CA  LEU F 194      49.520 -39.283  32.689  1.00 87.98           C  
ATOM   2087  CA  ASN F 195      53.072 -40.114  31.715  1.00 46.99           C  
ATOM   2088  CA  GLY F 196      53.071 -37.010  29.608  1.00 26.38           C  
ATOM   2089  CA  GLU F 197      53.546 -39.150  26.530  1.00 44.45           C  
ATOM   2090  CA  LEU F 198      51.732 -38.270  23.328  1.00 68.19           C  
ATOM   2091  CA  ILE F 199      48.600 -40.339  22.783  1.00 81.59           C  
ATOM   2092  CA  GLY F 200      47.412 -38.378  19.768  1.00 38.92           C  
ATOM   2093  CA  ILE F 201      47.002 -34.999  18.129  1.00147.47           C  
ATOM   2094  CA  ASN F 202      43.748 -33.149  18.644  1.00 91.00           C  
ATOM   2095  CA  THR F 203      42.173 -32.834  15.227  1.00 89.12           C  
ATOM   2096  CA  ALA F 204      38.558 -31.799  15.701  1.00 54.19           C  
ATOM   2097  CA  ILE F 205      35.419 -31.550  17.783  1.00 62.09           C  
ATOM   2098  CA  LEU F 206      31.714 -32.210  17.475  1.00 59.59           C  
ATOM   2099  CA  ALA F 207      29.863 -29.256  18.846  1.00 42.42           C  
ATOM   2100  CA  PRO F 208      26.605 -27.773  17.840  1.00139.67           C  
ATOM   2101  CA  GLY F 209      27.566 -24.538  19.562  1.00 33.03           C  
ATOM   2102  CA  GLY F 210      31.006 -24.408  18.078  1.00 28.16           C  
ATOM   2103  CA  GLY F 211      32.172 -24.765  21.648  1.00 28.69           C  
ATOM   2104  CA  SER F 212      33.406 -27.868  23.407  1.00 55.64           C  
ATOM   2105  CA  VAL F 213      30.574 -30.326  24.007  1.00 61.80           C  
ATOM   2106  CA  GLY F 214      32.956 -32.784  25.564  1.00 35.17           C  
ATOM   2107  CA  ILE F 215      33.259 -34.750  22.376  1.00 99.73           C  
ATOM   2108  CA  GLY F 216      36.686 -34.265  20.871  1.00 22.07           C  
ATOM   2109  CA  PHE F 217      38.670 -36.331  18.438  1.00 45.07           C  
ATOM   2110  CA  ALA F 218      42.374 -36.821  18.024  1.00 35.18           C  
ATOM   2111  CA  ILE F 219      44.510 -38.711  15.590  1.00155.06           C  
ATOM   2112  CA  PRO F 220      46.273 -41.417  17.398  1.00100.96           C  
ATOM   2113  CA  SER F 221      49.936 -41.109  18.251  1.00 84.28           C  
ATOM   2114  CA  ASN F 222      50.705 -44.205  16.329  1.00 68.84           C  
ATOM   2115  CA  MET F 223      49.001 -42.343  13.609  1.00129.00           C  
ATOM   2116  CA  ALA F 224      51.030 -39.223  13.709  1.00 53.59           C  
ATOM   2117  CA  ARG F 225      54.257 -40.922  14.530  1.00121.29           C  
ATOM   2118  CA  THR F 226      54.742 -43.118  11.556  1.00 71.61           C  
ATOM   2119  CA  LEU F 227      52.975 -40.659   9.242  1.00119.49           C  
ATOM   2120  CA  ALA F 228      55.336 -38.032  10.515  1.00 51.71           C  
ATOM   2121  CA  GLN F 229      58.291 -40.275  10.179  1.00 91.84           C  
ATOM   2122  CA  GLN F 230      58.226 -40.776   6.456  1.00 96.24           C  
ATOM   2123  CA  LEU F 231      57.546 -37.106   6.111  1.00 63.06           C  
ATOM   2124  CA  ILE F 232      61.093 -36.813   7.242  1.00 91.20           C  
ATOM   2125  CA  ASP F 233      61.970 -40.364   6.041  1.00173.91           C  
ATOM   2126  CA  PHE F 234      61.316 -42.573   4.173  1.00216.72           C  
ATOM   2127  CA  GLY F 235      59.185 -40.065   2.417  1.00 42.33           C  
ATOM   2128  CA  GLU F 236      58.107 -42.420  -0.268  1.00 91.94           C  
ATOM   2129  CA  ILE F 237      55.780 -40.470  -2.473  1.00 88.02           C  
ATOM   2130  CA  LYS F 238      53.246 -43.216  -2.275  1.00232.63           C  
ATOM   2131  CA  ARG F 239      51.039 -43.853  -0.642  1.00224.51           C  
ATOM   2132  CA  GLY F 240      51.530 -40.353   0.643  1.00 52.03           C  
ATOM   2133  CA  LEU F 241      48.070 -40.883   1.984  1.00164.53           C  
ATOM   2134  CA  LEU F 242      45.543 -41.889  -0.608  1.00231.10           C  
ATOM   2135  CA  GLY F 243      43.848 -38.610  -1.228  1.00 57.01           C  
ATOM   2136  CA  ILE F 244      40.244 -39.646  -0.750  1.00 77.13           C  
ATOM   2137  CA  LYS F 245      37.170 -38.587   1.171  1.00 86.39           C  
ATOM   2138  CA  GLY F 246      34.855 -40.996   2.851  1.00 33.32           C  
ATOM   2139  CA  THR F 247      32.659 -41.703   5.798  1.00112.68           C  
ATOM   2140  CA  GLU F 248      30.826 -44.469   7.598  1.00 91.57           C  
ATOM   2141  CA  MET F 249      28.621 -46.832   5.707  1.00 57.23           C  
ATOM   2142  CA  SER F 250      25.664 -44.865   4.508  1.00 36.91           C  
ATOM   2143  CA  ALA F 251      22.216 -45.910   5.545  1.00 37.79           C  
ATOM   2144  CA  ASP F 252      20.915 -45.774   2.004  1.00 60.06           C  
ATOM   2145  CA  ILE F 253      23.606 -47.720   0.247  1.00 62.69           C  
ATOM   2146  CA  ALA F 254      24.272 -50.156   3.042  1.00 57.65           C  
ATOM   2147  CA  LYS F 255      20.844 -51.331   3.878  1.00115.19           C  
ATOM   2148  CA  ALA F 256      19.288 -51.407   0.488  1.00 69.29           C  
ATOM   2149  CA  PHE F 257      21.797 -52.936  -1.843  1.00137.00           C  
ATOM   2150  CA  ASN F 258      23.356 -54.990   0.770  1.00193.29           C  
ATOM   2151  CA  LEU F 259      27.014 -54.470   0.771  1.00183.73           C  
ATOM   2152  CA  ASP F 260      28.953 -57.691   0.555  1.00 65.16           C  
ATOM   2153  CA  VAL F 261      31.154 -56.569   3.405  1.00110.41           C  
ATOM   2154  CA  GLN F 262      29.017 -55.582   6.335  1.00 98.51           C  
ATOM   2155  CA  ARG F 263      30.651 -52.237   6.435  1.00111.81           C  
ATOM   2156  CA  GLY F 264      33.786 -50.478   5.491  1.00 24.64           C  
ATOM   2157  CA  ALA F 265      35.262 -47.145   4.772  1.00 41.89           C  
ATOM   2158  CA  PHE F 266      33.173 -45.886   1.982  1.00130.46           C  
ATOM   2159  CA  VAL F 267      34.494 -43.317  -0.362  1.00 67.26           C  
ATOM   2160  CA  SER F 268      32.249 -40.653  -1.787  1.00 59.21           C  
ATOM   2161  CA  GLU F 269      34.937 -38.953  -3.778  1.00108.28           C  
ATOM   2162  CA  VAL F 270      38.039 -39.281  -5.899  1.00116.13           C  
ATOM   2163  CA  LEU F 271      40.774 -36.726  -5.601  1.00 55.28           C  
ATOM   2164  CA  PRO F 272      42.440 -35.459  -8.672  1.00143.39           C  
ATOM   2165  CA  GLY F 273      46.059 -36.376  -9.258  1.00 25.49           C  
ATOM   2166  CA  SER F 274      45.445 -38.152  -6.043  1.00 41.77           C  
ATOM   2167  CA  GLY F 275      46.858 -41.383  -4.913  1.00 35.44           C  
ATOM   2168  CA  SER F 276      43.504 -42.960  -5.019  1.00 54.29           C  
ATOM   2169  CA  ALA F 277      43.004 -41.572  -8.458  1.00 56.07           C  
ATOM   2170  CA  LYS F 278      45.915 -43.206 -10.173  1.00159.53           C  
ATOM   2171  CA  ALA F 279      45.558 -46.310  -8.081  1.00 43.64           C  
ATOM   2172  CA  GLY F 280      42.258 -46.393  -9.759  1.00 46.95           C  
ATOM   2173  CA  VAL F 281      40.139 -46.377  -6.676  1.00 72.04           C  
ATOM   2174  CA  LYS F 282      37.158 -44.333  -7.293  1.00193.11           C  
ATOM   2175  CA  ALA F 283      33.988 -43.286  -5.709  1.00 85.94           C  
ATOM   2176  CA  GLY F 284      31.253 -45.412  -4.366  1.00 38.79           C  
ATOM   2177  CA  ASP F 285      34.189 -47.474  -3.190  1.00 98.26           C  
ATOM   2178  CA  ILE F 286      33.939 -49.571  -0.226  1.00145.50           C  
ATOM   2179  CA  ILE F 287      37.297 -50.142   1.383  1.00 64.42           C  
ATOM   2180  CA  THR F 288      36.980 -53.495   3.050  1.00 57.83           C  
ATOM   2181  CA  SER F 289      40.487 -53.968   4.171  1.00 51.71           C  
ATOM   2182  CA  LEU F 290      43.948 -52.554   4.282  1.00103.17           C  
ATOM   2183  CA  ASN F 291      46.847 -54.857   4.141  1.00287.30           C  
ATOM   2184  CA  GLY F 292      46.653 -58.613   4.690  1.00 57.10           C  
ATOM   2185  CA  LYS F 293      44.821 -58.209   7.961  1.00157.38           C  
ATOM   2186  CA  PRO F 294      41.242 -57.198   7.794  1.00 65.25           C  
ATOM   2187  CA  LEU F 295      40.105 -53.610   8.044  1.00 96.22           C  
ATOM   2188  CA  ASN F 296      37.361 -52.460  10.310  1.00 69.47           C  
ATOM   2189  CA  SER F 297      35.196 -49.443   9.936  1.00 50.20           C  
ATOM   2190  CA  PHE F 298      36.220 -46.204   8.398  1.00 89.45           C  
ATOM   2191  CA  ALA F 299      37.486 -45.594  11.877  1.00 46.78           C  
ATOM   2192  CA  GLU F 300      40.012 -48.350  11.864  1.00103.32           C  
ATOM   2193  CA  LEU F 301      40.981 -47.120   8.460  1.00 69.70           C  
ATOM   2194  CA  ARG F 302      42.638 -43.951   9.517  1.00163.59           C  
ATOM   2195  CA  SER F 303      43.836 -45.655  12.609  1.00 66.33           C  
ATOM   2196  CA  ARG F 304      46.128 -47.833  10.704  1.00221.51           C  
ATOM   2197  CA  ILE F 305      46.850 -45.456   7.852  1.00 88.40           C  
ATOM   2198  CA  ALA F 306      47.138 -42.406   9.964  1.00 71.99           C  
ATOM   2199  CA  THR F 307      49.421 -44.634  11.895  1.00 66.81           C  
ATOM   2200  CA  THR F 308      51.391 -45.723   8.904  1.00135.48           C  
ATOM   2201  CA  GLU F 309      54.027 -43.767   7.063  1.00 78.19           C  
ATOM   2202  CA  PRO F 310      52.300 -41.505   4.691  1.00245.46           C  
ATOM   2203  CA  GLY F 311      54.395 -42.927   2.088  1.00195.08           C  
ATOM   2204  CA  THR F 312      54.373 -46.572   2.905  1.00 81.24           C  
ATOM   2205  CA  LYS F 313      53.277 -48.508  -0.111  1.00 91.89           C  
ATOM   2206  CA  VAL F 314      50.244 -50.523   0.802  1.00131.95           C  
ATOM   2207  CA  LYS F 315      47.501 -52.512  -0.821  1.00113.24           C  
ATOM   2208  CA  LEU F 316      43.852 -51.830  -0.305  1.00109.21           C  
ATOM   2209  CA  GLY F 317      40.896 -54.101  -0.597  1.00 46.53           C  
ATOM   2210  CA  LEU F 318      37.657 -52.641  -1.697  1.00113.79           C  
ATOM   2211  CA  LEU F 319      34.415 -53.776  -3.005  1.00112.09           C  
ATOM   2212  CA  ARG F 320      33.261 -52.351  -6.136  1.00194.42           C  
ATOM   2213  CA  ASN F 321      30.166 -53.716  -7.865  1.00205.15           C  
ATOM   2214  CA  GLY F 322      29.976 -56.456  -5.437  1.00 49.26           C  
ATOM   2215  CA  LYS F 323      33.203 -57.684  -6.717  1.00192.37           C  
ATOM   2216  CA  PRO F 324      36.606 -57.770  -5.356  1.00165.33           C  
ATOM   2217  CA  LEU F 325      39.978 -56.256  -6.262  1.00190.17           C  
ATOM   2218  CA  GLU F 326      43.256 -55.572  -4.789  1.00107.26           C  
ATOM   2219  CA  VAL F 327      45.110 -52.470  -5.795  1.00 52.40           C  
ATOM   2220  CA  GLU F 328      48.277 -50.934  -4.580  1.00 90.55           C  
ATOM   2221  CA  VAL F 329      47.952 -47.411  -3.371  1.00 60.97           C  
ATOM   2222  CA  SER F 340      49.628 -22.755 -32.128  1.00 96.71           C  
ATOM   2223  CA  ALA F 341      48.985 -19.046 -31.670  1.00 77.02           C  
ATOM   2224  CA  GLU F 342      45.787 -19.645 -29.761  1.00 54.45           C  
ATOM   2225  CA  MET F 343      47.102 -20.215 -26.341  1.00 53.00           C  
ATOM   2226  CA  ILE F 344      49.424 -17.336 -26.247  1.00152.71           C  
ATOM   2227  CA  THR F 345      47.005 -15.147 -28.094  1.00 76.85           C  
ATOM   2228  CA  PRO F 346      43.345 -15.318 -27.352  1.00160.20           C  
ATOM   2229  CA  ALA F 347      40.895 -16.991 -29.706  1.00 70.85           C  
ATOM   2230  CA  LEU F 348      43.224 -16.163 -32.591  1.00134.85           C  
ATOM   2231  CA  GLU F 349      43.627 -19.463 -34.294  1.00 80.94           C  
ATOM   2232  CA  GLY F 350      46.569 -19.524 -36.578  1.00 27.20           C  
ATOM   2233  CA  ALA F 351      50.078 -20.716 -37.098  1.00 35.62           C  
ATOM   2234  CA  THR F 352      51.576 -22.745 -34.336  1.00103.43           C  
ATOM   2235  CA  LEU F 353      54.302 -21.292 -32.228  1.00 57.09           C  
ATOM   2236  CA  SER F 354      57.468 -22.732 -30.799  1.00 34.34           C  
ATOM   2237  CA  ASP F 355      59.837 -21.261 -28.274  1.00 42.23           C  
ATOM   2238  CA  GLY F 356      63.543 -20.951 -28.539  1.00 48.50           C  
ATOM   2239  CA  GLN F 357      65.333 -19.749 -31.597  1.00164.74           C  
ATOM   2240  CA  LEU F 358      65.397 -23.385 -31.688  1.00214.55           C  
ATOM   2241  CA  LYS F 359      67.972 -23.486 -34.443  1.00136.95           C  
ATOM   2242  CA  ASP F 360      69.998 -20.470 -33.281  1.00 47.71           C  
ATOM   2243  CA  GLY F 361      70.222 -18.516 -30.064  1.00 29.88           C  
ATOM   2244  CA  GLY F 362      66.717 -17.556 -29.077  1.00 39.90           C  
ATOM   2245  CA  LYS F 363      65.928 -14.500 -31.081  1.00123.04           C  
ATOM   2246  CA  GLY F 364      62.370 -15.216 -30.121  1.00 28.87           C  
ATOM   2247  CA  ILE F 365      59.347 -17.419 -30.578  1.00 62.60           C  
ATOM   2248  CA  LYS F 366      58.970 -19.022 -33.949  1.00 51.28           C  
ATOM   2249  CA  ILE F 367      55.742 -19.590 -35.741  1.00 62.08           C  
ATOM   2250  CA  ASP F 368      55.909 -23.049 -37.191  1.00 52.23           C  
ATOM   2251  CA  GLU F 369      53.279 -22.974 -39.865  1.00 86.44           C  
ATOM   2252  CA  VAL F 370      50.453 -20.792 -41.035  1.00122.79           C  
ATOM   2253  CA  VAL F 371      46.920 -22.171 -40.931  1.00144.64           C  
ATOM   2254  CA  LYS F 372      46.261 -19.228 -43.335  1.00153.92           C  
ATOM   2255  CA  GLY F 373      42.489 -19.531 -43.385  1.00 38.59           C  
ATOM   2256  CA  SER F 374      42.848 -18.805 -39.646  1.00 45.60           C  
ATOM   2257  CA  PRO F 375      42.761 -15.360 -38.202  1.00 69.51           C  
ATOM   2258  CA  ALA F 376      46.345 -15.480 -37.031  1.00 43.79           C  
ATOM   2259  CA  ALA F 377      46.888 -15.487 -40.753  1.00 50.75           C  
ATOM   2260  CA  GLN F 378      44.546 -12.560 -41.358  1.00 57.05           C  
ATOM   2261  CA  ALA F 379      46.602  -9.934 -39.546  1.00 59.28           C  
ATOM   2262  CA  GLY F 380      49.931 -10.656 -41.171  1.00 63.28           C  
ATOM   2263  CA  LEU F 381      51.402 -13.658 -39.420  1.00 59.92           C  
ATOM   2264  CA  GLN F 382      53.327 -15.724 -41.949  1.00127.13           C  
ATOM   2265  CA  LYS F 383      55.276 -18.862 -41.158  1.00177.94           C  
ATOM   2266  CA  ASP F 384      58.989 -18.808 -40.366  1.00 77.35           C  
ATOM   2267  CA  ASP F 385      58.651 -15.457 -38.703  1.00 49.97           C  
ATOM   2268  CA  VAL F 386      60.480 -15.015 -35.460  1.00 55.25           C  
ATOM   2269  CA  ILE F 387      58.938 -12.806 -32.839  1.00128.41           C  
ATOM   2270  CA  ILE F 388      61.908 -10.939 -31.442  1.00106.75           C  
ATOM   2271  CA  GLY F 389      59.837  -9.053 -28.935  1.00 43.85           C  
ATOM   2272  CA  VAL F 390      56.583  -7.393 -28.135  1.00160.86           C  
ATOM   2273  CA  ASN F 391      55.785  -3.854 -27.087  1.00 78.94           C  
ATOM   2274  CA  ARG F 392      59.365  -2.675 -26.792  1.00158.22           C  
ATOM   2275  CA  ASP F 393      60.036  -5.821 -24.844  1.00 51.20           C  
ATOM   2276  CA  ARG F 394      62.375  -8.481 -26.053  1.00 71.90           C  
ATOM   2277  CA  VAL F 395      60.831 -11.899 -26.250  1.00 46.21           C  
ATOM   2278  CA  ASN F 396      63.351 -14.652 -25.725  1.00 58.53           C  
ATOM   2279  CA  SER F 397      60.713 -17.344 -25.484  1.00 99.96           C  
ATOM   2280  CA  ILE F 398      57.014 -17.963 -25.173  1.00 99.63           C  
ATOM   2281  CA  ALA F 399      57.052 -17.342 -21.460  1.00 30.73           C  
ATOM   2282  CA  GLU F 400      58.439 -13.862 -21.849  1.00 37.02           C  
ATOM   2283  CA  MET F 401      56.009 -13.099 -24.622  1.00 36.54           C  
ATOM   2284  CA  ARG F 402      53.239 -14.227 -22.360  1.00 92.18           C  
ATOM   2285  CA  LYS F 403      54.454 -11.730 -19.811  1.00 53.24           C  
ATOM   2286  CA  VAL F 404      53.940  -8.770 -22.084  1.00 40.01           C  
ATOM   2287  CA  LEU F 405      50.534 -10.239 -22.817  1.00101.25           C  
ATOM   2288  CA  ALA F 406      50.003 -10.340 -19.087  1.00 27.25           C  
ATOM   2289  CA  ALA F 407      49.957  -6.576 -19.169  1.00 29.81           C  
ATOM   2290  CA  LYS F 408      47.194  -6.967 -21.733  1.00103.21           C  
ATOM   2291  CA  PRO F 409      47.970  -3.711 -23.425  1.00 73.60           C  
ATOM   2292  CA  ALA F 410      45.218  -2.655 -25.795  1.00 30.84           C  
ATOM   2293  CA  ILE F 411      48.002  -2.213 -28.314  1.00 86.70           C  
ATOM   2294  CA  ILE F 412      50.171  -5.230 -28.947  1.00112.99           C  
ATOM   2295  CA  ALA F 413      53.057  -4.787 -31.275  1.00 51.55           C  
ATOM   2296  CA  LEU F 414      54.968  -7.773 -32.463  1.00121.75           C  
ATOM   2297  CA  GLN F 415      58.074  -7.323 -34.390  1.00118.59           C  
ATOM   2298  CA  ILE F 416      59.287 -10.361 -36.053  1.00117.10           C  
ATOM   2299  CA  VAL F 417      62.122 -10.880 -38.387  1.00 41.80           C  
ATOM   2300  CA  ARG F 418      61.218 -12.308 -41.724  1.00128.36           C  
ATOM   2301  CA  GLY F 419      64.013 -13.244 -44.029  1.00 22.43           C  
ATOM   2302  CA  ASN F 420      66.698 -10.693 -43.560  1.00 65.54           C  
ATOM   2303  CA  GLU F 421      64.261  -7.976 -42.707  1.00 46.95           C  
ATOM   2304  CA  SER F 422      62.487  -6.501 -39.763  1.00 47.06           C  
ATOM   2305  CA  ILE F 423      58.757  -6.964 -39.638  1.00111.69           C  
ATOM   2306  CA  TYR F 424      56.165  -5.563 -37.371  1.00169.77           C  
ATOM   2307  CA  LEU F 425      52.948  -7.217 -36.580  1.00 96.09           C  
ATOM   2308  CA  LEU F 426      50.140  -6.209 -34.421  1.00239.57           C  
ATOM   2309  CA  MET F 427      46.868  -6.836 -32.724  1.00111.94           C  
TER    2310      MET F 427                                                      
ATOM   2311  CA  PRO G  11      40.624  48.046 -45.854  1.00150.16           C  
ATOM   2312  CA  LEU G  12      38.527  45.409 -47.537  1.00100.11           C  
ATOM   2313  CA  PRO G  13      40.095  43.136 -50.010  1.00225.14           C  
ATOM   2314  CA  SER G  14      37.238  42.990 -50.584  1.00161.59           C  
ATOM   2315  CA  LEU G  15      36.233  39.359 -50.238  1.00112.51           C  
ATOM   2316  CA  ALA G  16      33.291  39.734 -52.605  1.00 43.74           C  
ATOM   2317  CA  PRO G  17      35.291  40.185 -55.718  1.00 65.49           C  
ATOM   2318  CA  MET G  18      37.152  36.966 -55.118  1.00 33.18           C  
ATOM   2319  CA  LEU G  19      33.984  35.186 -54.092  1.00 50.35           C  
ATOM   2320  CA  GLU G  20      31.996  36.074 -57.138  1.00 39.24           C  
ATOM   2321  CA  LYS G  21      34.291  34.156 -59.414  1.00 81.14           C  
ATOM   2322  CA  VAL G  22      34.874  31.183 -57.124  1.00110.57           C  
ATOM   2323  CA  LEU G  23      31.484  30.512 -55.625  1.00 79.13           C  
ATOM   2324  CA  PRO G  24      29.913  28.735 -58.531  1.00 65.78           C  
ATOM   2325  CA  ALA G  25      32.613  26.107 -58.108  1.00 32.71           C  
ATOM   2326  CA  VAL G  26      31.258  25.103 -54.725  1.00 35.56           C  
ATOM   2327  CA  VAL G  27      28.215  22.925 -54.876  1.00 94.06           C  
ATOM   2328  CA  SER G  28      25.639  21.391 -52.578  1.00 37.95           C  
ATOM   2329  CA  VAL G  29      25.323  17.641 -52.533  1.00 31.19           C  
ATOM   2330  CA  ARG G  30      22.021  15.966 -51.877  1.00 80.97           C  
ATOM   2331  CA  VAL G  31      21.731  12.323 -51.020  1.00 39.46           C  
ATOM   2332  CA  GLU G  32      19.012   9.766 -50.490  1.00 37.94           C  
ATOM   2333  CA  GLY G  33      19.405   6.219 -49.370  1.00 24.77           C  
ATOM   2334  CA  THR G  34      18.711   3.352 -47.036  1.00 98.78           C  
ATOM   2335  CA  ALA G  35      15.880   0.662 -44.598  1.00 17.74           C  
ATOM   2336  CA  GLN G  59      13.873   3.749 -43.905  1.00 78.59           C  
ATOM   2337  CA  PRO G  60      14.585   6.490 -46.311  1.00139.14           C  
ATOM   2338  CA  PHE G  61      16.685   9.428 -45.283  1.00 48.34           C  
ATOM   2339  CA  GLU G  62      17.848  12.556 -46.998  1.00 28.52           C  
ATOM   2340  CA  GLY G  63      21.172  14.133 -46.262  1.00 15.46           C  
ATOM   2341  CA  LEU G  64      22.748  17.376 -47.302  1.00 39.65           C  
ATOM   2342  CA  GLY G  65      26.391  18.170 -47.780  1.00 18.99           C  
ATOM   2343  CA  SER G  66      28.618  20.123 -50.078  1.00 36.28           C  
ATOM   2344  CA  GLY G  67      31.281  19.465 -52.654  1.00 14.36           C  
ATOM   2345  CA  VAL G  68      33.723  21.259 -54.885  1.00 32.86           C  
ATOM   2346  CA  ILE G  69      34.030  21.005 -58.619  1.00 46.33           C  
ATOM   2347  CA  ILE G  70      37.572  19.970 -59.425  1.00 86.24           C  
ATOM   2348  CA  ASN G  71      37.130  19.598 -63.170  1.00166.33           C  
ATOM   2349  CA  ALA G  72      34.521  21.517 -65.016  1.00 42.41           C  
ATOM   2350  CA  SER G  73      34.882  19.476 -68.157  1.00 42.54           C  
ATOM   2351  CA  LYS G  74      34.692  16.101 -66.504  1.00156.52           C  
ATOM   2352  CA  GLY G  75      32.302  17.258 -63.877  1.00 30.61           C  
ATOM   2353  CA  TYR G  76      34.353  15.787 -61.068  1.00 84.85           C  
ATOM   2354  CA  VAL G  77      33.284  16.933 -57.644  1.00 41.97           C  
ATOM   2355  CA  LEU G  78      35.169  16.233 -54.450  1.00 48.60           C  
ATOM   2356  CA  THR G  79      33.252  15.529 -51.298  1.00 39.22           C  
ATOM   2357  CA  ASN G  80      33.579  13.773 -48.001  1.00 57.86           C  
ATOM   2358  CA  ASN G  81      33.053  10.054 -48.018  1.00 42.96           C  
ATOM   2359  CA  HIS G  82      30.721  10.267 -45.078  1.00 54.36           C  
ATOM   2360  CA  VAL G  83      28.380  12.512 -46.959  1.00 40.85           C  
ATOM   2361  CA  ILE G  84      28.161  10.035 -49.838  1.00 72.62           C  
ATOM   2362  CA  ASN G  85      28.525   6.717 -48.067  1.00124.25           C  
ATOM   2363  CA  GLN G  86      24.873   5.810 -47.434  1.00 69.49           C  
ATOM   2364  CA  ALA G  87      23.584   7.462 -50.606  1.00 68.53           C  
ATOM   2365  CA  GLN G  88      21.666   5.340 -53.045  1.00136.98           C  
ATOM   2366  CA  LYS G  89      21.230   8.355 -55.277  1.00 30.04           C  
ATOM   2367  CA  ILE G  90      23.137  11.587 -55.369  1.00 35.40           C  
ATOM   2368  CA  SER G  91      22.249  14.956 -56.792  1.00 28.51           C  
ATOM   2369  CA  ILE G  92      24.341  18.071 -57.235  1.00 95.12           C  
ATOM   2370  CA  GLN G  93      22.936  21.570 -57.030  1.00126.68           C  
ATOM   2371  CA  LEU G  94      24.674  24.660 -58.338  1.00 46.30           C  
ATOM   2372  CA  ASN G  95      24.289  28.035 -56.714  1.00 36.48           C  
ATOM   2373  CA  ASP G  96      22.492  29.107 -59.856  1.00 49.00           C  
ATOM   2374  CA  GLY G  97      19.811  26.569 -59.077  1.00 29.84           C  
ATOM   2375  CA  ARG G  98      20.620  24.077 -61.773  1.00115.66           C  
ATOM   2376  CA  GLU G  99      20.813  20.544 -60.545  1.00102.71           C  
ATOM   2377  CA  PHE G 100      22.399  17.405 -61.891  1.00 49.72           C  
ATOM   2378  CA  ASP G 101      22.668  13.759 -60.996  1.00 28.07           C  
ATOM   2379  CA  ALA G 102      25.990  12.354 -59.938  1.00 27.33           C  
ATOM   2380  CA  LYS G 103      27.602   8.968 -59.643  1.00 54.47           C  
ATOM   2381  CA  LEU G 104      30.232   7.952 -57.157  1.00 43.87           C  
ATOM   2382  CA  ILE G 105      33.486   7.525 -58.979  1.00 80.74           C  
ATOM   2383  CA  GLY G 106      35.264   6.219 -55.897  1.00 25.09           C  
ATOM   2384  CA  SER G 107      36.125   7.094 -52.342  1.00 98.19           C  
ATOM   2385  CA  ASP G 108      37.955   5.876 -49.327  1.00105.84           C  
ATOM   2386  CA  ASP G 109      37.079   5.601 -45.671  1.00 61.56           C  
ATOM   2387  CA  GLN G 110      40.325   6.275 -43.940  1.00 88.74           C  
ATOM   2388  CA  SER G 111      40.979   9.782 -45.244  1.00128.15           C  
ATOM   2389  CA  ASP G 112      37.271  10.363 -45.872  1.00 80.80           C  
ATOM   2390  CA  ILE G 113      37.654  11.575 -49.457  1.00 95.76           C  
ATOM   2391  CA  ALA G 114      35.184  10.742 -52.194  1.00 29.92           C  
ATOM   2392  CA  LEU G 115      34.980  11.714 -55.825  1.00 98.74           C  
ATOM   2393  CA  LEU G 116      31.728  12.176 -57.684  1.00 46.00           C  
ATOM   2394  CA  GLN G 117      31.064  12.796 -61.318  1.00120.46           C  
ATOM   2395  CA  ILE G 118      28.205  14.847 -62.611  1.00 60.91           C  
ATOM   2396  CA  GLN G 119      26.288  13.496 -65.519  1.00103.75           C  
ATOM   2397  CA  ASN G 120      26.050  15.903 -68.446  1.00125.46           C  
ATOM   2398  CA  PRO G 121      27.906  18.546 -66.558  1.00106.46           C  
ATOM   2399  CA  SER G 122      27.416  21.503 -68.954  1.00202.24           C  
ATOM   2400  CA  LYS G 123      28.835  24.969 -68.248  1.00 77.71           C  
ATOM   2401  CA  LEU G 124      30.522  24.381 -64.947  1.00 88.41           C  
ATOM   2402  CA  THR G 125      33.137  26.390 -63.132  1.00115.79           C  
ATOM   2403  CA  GLN G 126      36.085  24.724 -61.514  1.00 47.17           C  
ATOM   2404  CA  ILE G 127      38.050  25.757 -58.491  1.00 96.56           C  
ATOM   2405  CA  ALA G 128      41.809  26.161 -58.554  1.00 27.53           C  
ATOM   2406  CA  ILE G 129      43.867  24.139 -56.132  1.00 94.44           C  
ATOM   2407  CA  ALA G 130      46.420  25.779 -53.871  1.00 34.40           C  
ATOM   2408  CA  ASP G 131      49.429  24.161 -52.266  1.00 47.72           C  
ATOM   2409  CA  SER G 132      48.374  23.140 -48.782  1.00 49.03           C  
ATOM   2410  CA  ASP G 133      51.904  22.679 -47.609  1.00137.67           C  
ATOM   2411  CA  LYS G 134      52.402  26.405 -48.128  1.00124.69           C  
ATOM   2412  CA  LEU G 135      49.827  27.315 -45.512  1.00108.85           C  
ATOM   2413  CA  ARG G 136      50.942  28.838 -42.250  1.00 97.50           C  
ATOM   2414  CA  VAL G 137      48.966  29.644 -39.149  1.00 39.44           C  
ATOM   2415  CA  GLY G 138      47.388  33.037 -39.423  1.00 28.92           C  
ATOM   2416  CA  ASP G 139      46.553  32.913 -43.074  1.00121.07           C  
ATOM   2417  CA  PHE G 140      43.006  33.832 -43.938  1.00 57.25           C  
ATOM   2418  CA  ALA G 141      40.503  31.245 -44.984  1.00 27.27           C  
ATOM   2419  CA  VAL G 142      36.950  31.266 -46.229  1.00 33.06           C  
ATOM   2420  CA  ALA G 143      34.648  28.322 -45.902  1.00 29.31           C  
ATOM   2421  CA  VAL G 144      31.844  27.693 -48.306  1.00105.31           C  
ATOM   2422  CA  GLY G 145      29.203  25.028 -48.007  1.00 22.30           C  
ATOM   2423  CA  ASN G 146      25.619  24.574 -47.028  1.00 60.34           C  
ATOM   2424  CA  PRO G 147      25.109  24.740 -43.364  1.00 68.53           C  
ATOM   2425  CA  PHE G 148      21.754  23.435 -42.226  1.00 70.37           C  
ATOM   2426  CA  GLY G 149      20.924  23.137 -45.888  1.00 24.42           C  
ATOM   2427  CA  LEU G 150      20.300  26.853 -45.943  1.00 51.07           C  
ATOM   2428  CA  GLY G 151      22.040  27.293 -49.258  1.00 28.52           C  
ATOM   2429  CA  GLN G 152      25.484  28.384 -50.268  1.00 43.08           C  
ATOM   2430  CA  THR G 153      26.994  30.144 -47.311  1.00 30.15           C  
ATOM   2431  CA  ALA G 154      30.398  31.679 -46.920  1.00 28.54           C  
ATOM   2432  CA  THR G 155      32.149  32.130 -43.609  1.00 30.91           C  
ATOM   2433  CA  SER G 156      35.479  33.704 -42.848  1.00 30.22           C  
ATOM   2434  CA  GLY G 157      38.273  32.897 -40.449  1.00 18.45           C  
ATOM   2435  CA  ILE G 158      41.976  32.165 -40.236  1.00 92.45           C  
ATOM   2436  CA  VAL G 159      43.988  28.986 -40.294  1.00 42.17           C  
ATOM   2437  CA  SER G 160      44.186  28.124 -36.634  1.00 86.87           C  
ATOM   2438  CA  ALA G 161      46.510  25.153 -36.918  1.00 36.80           C  
ATOM   2439  CA  LEU G 162      47.852  22.572 -39.322  1.00 90.76           C  
ATOM   2440  CA  GLY G 163      49.104  19.054 -39.134  1.00 37.27           C  
ATOM   2441  CA  ARG G 164      46.652  18.095 -36.523  1.00 95.58           C  
ATOM   2442  CA  SER G 165      45.586  14.635 -35.673  1.00113.64           C  
ATOM   2443  CA  GLY G 166      44.798  12.230 -32.924  1.00 36.76           C  
ATOM   2444  CA  LEU G 167      41.269  13.557 -33.166  1.00 48.24           C  
ATOM   2445  CA  ASN G 168      40.324   9.985 -33.971  1.00 65.01           C  
ATOM   2446  CA  LEU G 169      37.799  11.350 -36.392  1.00 50.26           C  
ATOM   2447  CA  GLU G 170      39.385   9.513 -39.310  1.00119.28           C  
ATOM   2448  CA  GLY G 171      41.879   6.747 -39.940  1.00 35.46           C  
ATOM   2449  CA  LEU G 172      44.266   9.122 -41.602  1.00124.03           C  
ATOM   2450  CA  GLU G 173      44.127  12.606 -40.356  1.00101.72           C  
ATOM   2451  CA  ASN G 174      45.967  15.824 -41.028  1.00130.90           C  
ATOM   2452  CA  PHE G 175      43.402  18.395 -40.530  1.00 88.20           C  
ATOM   2453  CA  ILE G 176      43.905  22.015 -41.176  1.00 66.36           C  
ATOM   2454  CA  GLN G 177      42.144  23.691 -38.306  1.00 51.45           C  
ATOM   2455  CA  THR G 178      40.078  26.762 -38.951  1.00113.87           C  
ATOM   2456  CA  ASP G 179      38.041  29.283 -36.976  1.00 96.16           C  
ATOM   2457  CA  ALA G 180      35.673  29.839 -39.869  1.00 42.05           C  
ATOM   2458  CA  SER G 181      32.190  28.849 -38.892  1.00 82.85           C  
ATOM   2459  CA  ILE G 182      31.620  25.295 -39.973  1.00 95.66           C  
ATOM   2460  CA  ASN G 183      28.396  23.541 -39.185  1.00 40.76           C  
ATOM   2461  CA  ARG G 184      26.559  20.462 -40.242  1.00161.24           C  
ATOM   2462  CA  GLY G 185      26.090  20.495 -43.968  1.00 24.30           C  
ATOM   2463  CA  ASN G 186      29.515  22.032 -44.405  1.00 56.91           C  
ATOM   2464  CA  ALA G 187      31.120  18.677 -45.022  1.00 96.49           C  
ATOM   2465  CA  GLY G 188      32.602  18.262 -48.448  1.00 23.98           C  
ATOM   2466  CA  GLY G 189      32.624  22.025 -48.743  1.00 22.97           C  
ATOM   2467  CA  ALA G 190      35.595  24.106 -49.650  1.00 42.70           C  
ATOM   2468  CA  LEU G 191      38.035  26.076 -47.572  1.00 93.33           C  
ATOM   2469  CA  LEU G 192      39.484  28.805 -49.701  1.00 55.54           C  
ATOM   2470  CA  ASN G 193      42.360  31.213 -49.452  1.00 53.99           C  
ATOM   2471  CA  LEU G 194      42.122  34.872 -50.366  1.00 98.86           C  
ATOM   2472  CA  ASN G 195      42.893  33.884 -53.924  1.00 48.99           C  
ATOM   2473  CA  GLY G 196      39.840  31.704 -53.954  1.00 23.63           C  
ATOM   2474  CA  GLU G 197      42.041  28.672 -54.359  1.00 41.09           C  
ATOM   2475  CA  LEU G 198      41.145  25.481 -52.534  1.00 59.42           C  
ATOM   2476  CA  ILE G 199      43.145  24.992 -49.342  1.00108.12           C  
ATOM   2477  CA  GLY G 200      41.185  21.973 -48.147  1.00 26.19           C  
ATOM   2478  CA  ILE G 201      37.826  20.268 -47.810  1.00 49.28           C  
ATOM   2479  CA  ASN G 202      35.890  20.841 -44.601  1.00 77.21           C  
ATOM   2480  CA  THR G 203      35.587  17.431 -42.976  1.00 84.36           C  
ATOM   2481  CA  ALA G 204      34.441  17.935 -39.404  1.00 58.13           C  
ATOM   2482  CA  ILE G 205      34.175  20.021 -36.273  1.00126.17           C  
ATOM   2483  CA  LEU G 206      34.579  19.720 -32.571  1.00 59.04           C  
ATOM   2484  CA  ALA G 207      31.520  21.102 -30.904  1.00 47.40           C  
ATOM   2485  CA  PRO G 208      29.892  20.085 -27.712  1.00140.78           C  
ATOM   2486  CA  GLY G 209      26.679  21.809 -28.742  1.00 29.84           C  
ATOM   2487  CA  GLY G 210      26.666  20.340 -32.181  1.00 22.71           C  
ATOM   2488  CA  GLY G 211      27.055  23.897 -33.365  1.00 23.08           C  
ATOM   2489  CA  SER G 212      30.203  25.628 -34.522  1.00 55.17           C  
ATOM   2490  CA  VAL G 213      32.552  26.275 -31.621  1.00 60.20           C  
ATOM   2491  CA  GLY G 214      35.086  27.834 -33.926  1.00 35.15           C  
ATOM   2492  CA  ILE G 215      37.107  24.663 -34.112  1.00 99.01           C  
ATOM   2493  CA  GLY G 216      36.791  23.133 -37.543  1.00 20.72           C  
ATOM   2494  CA  PHE G 217      38.950  20.705 -39.440  1.00 41.84           C  
ATOM   2495  CA  ALA G 218      39.531  20.244 -43.131  1.00 35.59           C  
ATOM   2496  CA  ILE G 219      41.553  17.844 -45.194  1.00119.86           C  
ATOM   2497  CA  PRO G 220      44.251  19.656 -46.963  1.00 90.07           C  
ATOM   2498  CA  SER G 221      43.986  20.454 -50.631  1.00 85.19           C  
ATOM   2499  CA  ASN G 222      47.107  18.561 -51.392  1.00 68.08           C  
ATOM   2500  CA  MET G 223      45.269  15.889 -49.643  1.00107.01           C  
ATOM   2501  CA  ALA G 224      42.138  15.876 -51.690  1.00 49.75           C  
ATOM   2502  CA  ARG G 225      43.913  16.666 -54.905  1.00 93.56           C  
ATOM   2503  CA  THR G 226      46.116  13.686 -55.332  1.00 65.57           C  
ATOM   2504  CA  LEU G 227      43.655  11.386 -53.562  1.00113.95           C  
ATOM   2505  CA  ALA G 228      41.045  12.576 -55.973  1.00 45.51           C  
ATOM   2506  CA  GLN G 229      43.309  12.202 -58.915  1.00 78.63           C  
ATOM   2507  CA  GLN G 230      43.833   8.496 -58.795  1.00110.82           C  
ATOM   2508  CA  LEU G 231      40.165   8.156 -58.091  1.00 53.53           C  
ATOM   2509  CA  ILE G 232      39.907   9.192 -61.669  1.00125.05           C  
ATOM   2510  CA  ASP G 233      43.424   7.923 -62.502  1.00165.82           C  
ATOM   2511  CA  PHE G 234      45.647   6.109 -61.812  1.00217.14           C  
ATOM   2512  CA  GLY G 235      43.151   4.404 -59.628  1.00 41.08           C  
ATOM   2513  CA  GLU G 236      45.582   1.819 -58.477  1.00 87.28           C  
ATOM   2514  CA  ILE G 237      43.698  -0.430 -56.142  1.00 91.56           C  
ATOM   2515  CA  LYS G 238      46.459  -0.059 -53.635  1.00231.09           C  
ATOM   2516  CA  ARG G 239      46.926   1.427 -51.412  1.00311.05           C  
ATOM   2517  CA  GLY G 240      43.438   2.758 -51.933  1.00 52.20           C  
ATOM   2518  CA  LEU G 241      43.875   4.165 -48.511  1.00190.90           C  
ATOM   2519  CA  LEU G 242      45.061   1.789 -45.876  1.00 98.14           C  
ATOM   2520  CA  GLY G 243      41.786   1.011 -44.167  1.00 49.37           C  
ATOM   2521  CA  ILE G 244      42.743   1.554 -40.549  1.00 68.32           C  
ATOM   2522  CA  LYS G 245      41.676   3.581 -37.561  1.00138.80           C  
ATOM   2523  CA  GLY G 246      44.079   5.340 -35.291  1.00 34.41           C  
ATOM   2524  CA  THR G 247      44.638   8.297 -33.064  1.00 74.82           C  
ATOM   2525  CA  GLU G 248      47.390  10.252 -31.358  1.00 53.52           C  
ATOM   2526  CA  MET G 249      49.765   8.495 -29.073  1.00 54.71           C  
ATOM   2527  CA  SER G 250      47.850   7.226 -26.106  1.00 41.82           C  
ATOM   2528  CA  ALA G 251      48.771   8.363 -22.650  1.00 41.91           C  
ATOM   2529  CA  ASP G 252      48.762   4.855 -21.293  1.00 91.94           C  
ATOM   2530  CA  ILE G 253      50.830   3.216 -23.994  1.00160.28           C  
ATOM   2531  CA  ALA G 254      53.183   6.074 -24.671  1.00 54.26           C  
ATOM   2532  CA  LYS G 255      54.230   6.941 -21.211  1.00 55.68           C  
ATOM   2533  CA  ALA G 256      54.477   3.542 -19.722  1.00 71.76           C  
ATOM   2534  CA  PHE G 257      56.319   1.305 -22.077  1.00186.32           C  
ATOM   2535  CA  ASN G 258      57.856   4.154 -23.773  1.00185.32           C  
ATOM   2536  CA  LEU G 259      57.704   3.853 -27.447  1.00142.74           C  
ATOM   2537  CA  ASP G 260      60.934   3.839 -29.298  1.00 60.14           C  
ATOM   2538  CA  VAL G 261      59.575   6.502 -31.595  1.00108.65           C  
ATOM   2539  CA  GLN G 262      58.461   9.402 -29.472  1.00100.63           C  
ATOM   2540  CA  ARG G 263      55.115   9.455 -31.146  1.00256.12           C  
ATOM   2541  CA  GLY G 264      53.455   8.260 -34.246  1.00 25.41           C  
ATOM   2542  CA  ALA G 265      50.159   7.405 -35.742  1.00 42.56           C  
ATOM   2543  CA  PHE G 266      48.970   4.646 -33.571  1.00125.96           C  
ATOM   2544  CA  VAL G 267      46.491   2.181 -34.842  1.00 66.66           C  
ATOM   2545  CA  SER G 268      43.875   0.730 -32.552  1.00104.94           C  
ATOM   2546  CA  GLU G 269      42.254  -1.375 -35.202  1.00109.39           C  
ATOM   2547  CA  VAL G 270      42.650  -3.574 -38.239  1.00 64.77           C  
ATOM   2548  CA  LEU G 271      40.069  -3.360 -40.956  1.00 59.62           C  
ATOM   2549  CA  PRO G 272      38.827  -6.515 -42.527  1.00155.09           C  
ATOM   2550  CA  GLY G 273      39.814  -7.153 -46.126  1.00 26.48           C  
ATOM   2551  CA  SER G 274      41.479  -3.851 -45.638  1.00 41.78           C  
ATOM   2552  CA  GLY G 275      44.666  -2.672 -47.093  1.00 32.55           C  
ATOM   2553  CA  SER G 276      46.232  -2.656 -43.725  1.00 46.42           C  
ATOM   2554  CA  ALA G 277      44.976  -6.123 -43.118  1.00 52.46           C  
ATOM   2555  CA  LYS G 278      46.622  -7.848 -46.016  1.00123.51           C  
ATOM   2556  CA  ALA G 279      49.669  -5.663 -45.723  1.00 42.28           C  
ATOM   2557  CA  GLY G 280      49.862  -7.259 -42.384  1.00 39.29           C  
ATOM   2558  CA  VAL G 281      49.722  -4.116 -40.356  1.00 70.64           C  
ATOM   2559  CA  LYS G 282      47.776  -4.791 -37.326  1.00124.35           C  
ATOM   2560  CA  ALA G 283      46.629  -3.137 -34.177  1.00113.40           C  
ATOM   2561  CA  GLY G 284      48.765  -1.662 -31.521  1.00 44.47           C  
ATOM   2562  CA  ASP G 285      50.800  -0.536 -34.471  1.00 96.70           C  
ATOM   2563  CA  ILE G 286      52.721   2.562 -34.330  1.00 82.38           C  
ATOM   2564  CA  ILE G 287      53.251   4.093 -37.716  1.00 54.76           C  
ATOM   2565  CA  THR G 288      56.539   5.899 -37.419  1.00 52.30           C  
ATOM   2566  CA  SER G 289      57.012   6.923 -40.961  1.00 49.35           C  
ATOM   2567  CA  LEU G 290      55.582   6.893 -44.413  1.00 67.57           C  
ATOM   2568  CA  ASN G 291      57.891   6.531 -47.356  1.00174.72           C  
ATOM   2569  CA  GLY G 292      61.573   7.457 -47.180  1.00 52.45           C  
ATOM   2570  CA  LYS G 293      61.036  10.752 -45.419  1.00 93.24           C  
ATOM   2571  CA  PRO G 294      60.100  10.642 -41.810  1.00 62.86           C  
ATOM   2572  CA  LEU G 295      56.498  10.824 -40.665  1.00124.57           C  
ATOM   2573  CA  ASN G 296      55.435  12.980 -37.794  1.00159.36           C  
ATOM   2574  CA  SER G 297      52.290  12.675 -35.761  1.00 55.25           C  
ATOM   2575  CA  PHE G 298      49.092  10.985 -36.753  1.00 89.59           C  
ATOM   2576  CA  ALA G 299      48.370  14.408 -38.092  1.00 46.79           C  
ATOM   2577  CA  GLU G 300      51.110  14.421 -40.619  1.00 92.55           C  
ATOM   2578  CA  LEU G 301      50.006  10.957 -41.494  1.00 69.32           C  
ATOM   2579  CA  ARG G 302      46.838  11.893 -43.196  1.00190.04           C  
ATOM   2580  CA  SER G 303      48.527  14.998 -44.383  1.00 68.70           C  
ATOM   2581  CA  ARG G 304      50.677  13.171 -46.749  1.00157.11           C  
ATOM   2582  CA  ILE G 305      48.399  10.198 -47.339  1.00116.08           C  
ATOM   2583  CA  ALA G 306      45.304  12.214 -47.708  1.00 61.86           C  
ATOM   2584  CA  THR G 307      47.536  14.144 -50.008  1.00 59.64           C  
ATOM   2585  CA  THR G 308      48.678  11.101 -51.894  1.00 64.35           C  
ATOM   2586  CA  GLU G 309      46.807   9.213 -54.557  1.00 84.57           C  
ATOM   2587  CA  PRO G 310      44.584   6.675 -53.060  1.00185.72           C  
ATOM   2588  CA  GLY G 311      45.915   4.586 -54.669  1.00121.31           C  
ATOM   2589  CA  THR G 312      49.629   4.968 -54.847  1.00 50.85           C  
ATOM   2590  CA  LYS G 313      51.651   2.057 -53.664  1.00 96.51           C  
ATOM   2591  CA  VAL G 314      53.501   3.195 -50.599  1.00 52.62           C  
ATOM   2592  CA  LYS G 315      55.640   1.710 -47.870  1.00 78.74           C  
ATOM   2593  CA  LEU G 316      54.925   2.281 -44.227  1.00108.12           C  
ATOM   2594  CA  GLY G 317      57.237   2.194 -41.289  1.00 46.16           C  
ATOM   2595  CA  LEU G 318      55.849   1.116 -38.010  1.00114.27           C  
ATOM   2596  CA  LEU G 319      57.048  -0.036 -34.728  1.00110.82           C  
ATOM   2597  CA  ARG G 320      55.792  -3.206 -33.500  1.00215.04           C  
ATOM   2598  CA  ASN G 321      57.257  -4.826 -30.409  1.00220.85           C  
ATOM   2599  CA  GLY G 322      59.870  -2.264 -30.285  1.00 51.17           C  
ATOM   2600  CA  LYS G 323      61.111  -3.568 -33.499  1.00121.07           C  
ATOM   2601  CA  PRO G 324      61.144  -2.247 -36.914  1.00115.36           C  
ATOM   2602  CA  LEU G 325      59.675  -3.321 -40.228  1.00239.57           C  
ATOM   2603  CA  GLU G 326      58.866  -2.046 -43.561  1.00157.50           C  
ATOM   2604  CA  VAL G 327      55.739  -3.130 -45.276  1.00125.71           C  
ATOM   2605  CA  GLU G 328      54.159  -2.273 -48.571  1.00 94.64           C  
ATOM   2606  CA  VAL G 329      50.630  -1.018 -48.310  1.00118.87           C  
ATOM   2607  CA  SER G 340      21.794 -25.197 -51.416  1.00 19.76           C  
ATOM   2608  CA  GLU G 342      22.142 -23.203 -48.254  1.00 43.81           C  
ATOM   2609  CA  MET G 343      22.826 -19.842 -49.783  1.00 39.32           C  
ATOM   2610  CA  ILE G 344      19.846 -20.055 -52.053  1.00 54.21           C  
ATOM   2611  CA  THR G 345      17.762 -21.789 -49.463  1.00 70.27           C  
ATOM   2612  CA  PRO G 346      17.945 -20.914 -45.837  1.00156.27           C  
ATOM   2613  CA  ALA G 347      19.822 -23.086 -43.377  1.00 68.52           C  
ATOM   2614  CA  LEU G 348      19.024 -26.124 -45.500  1.00 86.84           C  
ATOM   2615  CA  GLU G 349      22.403 -27.646 -46.023  1.00 75.68           C  
ATOM   2616  CA  GLY G 350      22.529 -29.981 -48.920  1.00 25.88           C  
ATOM   2617  CA  ALA G 351      23.709 -30.549 -52.430  1.00 33.01           C  
ATOM   2618  CA  THR G 352      25.537 -27.700 -54.030  1.00 99.99           C  
ATOM   2619  CA  LEU G 353      23.911 -25.816 -56.827  1.00 56.81           C  
ATOM   2620  CA  SER G 354      25.230 -24.435 -60.077  1.00 94.85           C  
ATOM   2621  CA  ASP G 355      23.745 -21.925 -62.439  1.00127.15           C  
ATOM   2622  CA  GLY G 356      23.180 -22.381 -66.114  1.00 47.79           C  
ATOM   2623  CA  GLN G 357      22.097 -25.541 -67.799  1.00156.97           C  
ATOM   2624  CA  LEU G 358      25.739 -25.425 -67.926  1.00198.89           C  
ATOM   2625  CA  LYS G 359      25.903 -28.336 -70.343  1.00100.27           C  
ATOM   2626  CA  ASP G 360      22.883 -27.279 -72.427  1.00 49.26           C  
ATOM   2627  CA  GLY G 361      20.731 -24.183 -72.688  1.00 31.22           C  
ATOM   2628  CA  GLY G 362      19.751 -23.133 -69.202  1.00 39.85           C  
ATOM   2629  CA  LYS G 363      16.907 -25.387 -68.212  1.00126.26           C  
ATOM   2630  CA  GLY G 364      17.585 -24.148 -64.759  1.00 32.63           C  
ATOM   2631  CA  ILE G 365      19.844 -24.477 -61.763  1.00 61.13           C  
ATOM   2632  CA  LYS G 366      21.727 -27.717 -61.381  1.00122.21           C  
ATOM   2633  CA  ILE G 367      22.376 -29.423 -58.112  1.00 67.83           C  
ATOM   2634  CA  ASP G 368      25.914 -30.687 -58.288  1.00 54.61           C  
ATOM   2635  CA  GLU G 369      26.005 -33.304 -55.609  1.00 86.95           C  
ATOM   2636  CA  VAL G 370      23.991 -34.489 -52.667  1.00127.02           C  
ATOM   2637  CA  VAL G 371      25.521 -34.204 -49.195  1.00183.19           C  
ATOM   2638  CA  LYS G 372      22.678 -36.662 -48.409  1.00155.10           C  
ATOM   2639  CA  GLY G 373      23.078 -36.623 -44.658  1.00 36.99           C  
ATOM   2640  CA  SER G 374      22.057 -32.969 -45.086  1.00 45.09           C  
ATOM   2641  CA  PRO G 375      18.530 -31.777 -44.974  1.00 71.44           C  
ATOM   2642  CA  ALA G 376      18.526 -30.671 -48.584  1.00 42.87           C  
ATOM   2643  CA  ALA G 377      18.776 -34.396 -49.032  1.00 46.73           C  
ATOM   2644  CA  GLN G 378      15.922 -35.169 -46.667  1.00 53.80           C  
ATOM   2645  CA  ALA G 379      13.162 -33.509 -48.687  1.00 57.23           C  
ATOM   2646  CA  GLY G 380      13.895 -35.161 -51.996  1.00 62.19           C  
ATOM   2647  CA  LEU G 381      16.760 -33.276 -53.556  1.00 58.98           C  
ATOM   2648  CA  GLN G 382      18.910 -35.746 -55.453  1.00129.89           C  
ATOM   2649  CA  LYS G 383      21.959 -34.844 -57.486  1.00153.34           C  
ATOM   2650  CA  ASP G 384      21.751 -34.188 -61.219  1.00 77.37           C  
ATOM   2651  CA  ASP G 385      18.347 -32.637 -60.831  1.00 49.79           C  
ATOM   2652  CA  VAL G 386      17.683 -29.492 -62.783  1.00 59.10           C  
ATOM   2653  CA  ILE G 387      15.334 -27.006 -61.255  1.00105.63           C  
ATOM   2654  CA  ILE G 388      13.356 -25.713 -64.186  1.00109.59           C  
ATOM   2655  CA  GLY G 389      11.436 -23.211 -62.095  1.00 47.22           C  
ATOM   2656  CA  VAL G 390       9.738 -22.473 -58.811  1.00 62.26           C  
ATOM   2657  CA  ASN G 391       6.138 -21.649 -58.007  1.00 73.50           C  
ATOM   2658  CA  ARG G 392       4.898 -21.490 -61.573  1.00155.84           C  
ATOM   2659  CA  ASP G 393       7.937 -19.404 -62.322  1.00 50.42           C  
ATOM   2660  CA  ARG G 394      10.603 -20.510 -64.722  1.00152.34           C  
ATOM   2661  CA  VAL G 395      14.067 -20.485 -63.244  1.00 47.64           C  
ATOM   2662  CA  ASN G 396      16.687 -19.923 -65.886  1.00 54.79           C  
ATOM   2663  CA  SER G 397      19.397 -19.373 -63.351  1.00 51.50           C  
ATOM   2664  CA  ILE G 398      20.179 -18.948 -59.674  1.00 38.42           C  
ATOM   2665  CA  ALA G 399      19.331 -15.283 -59.672  1.00 24.34           C  
ATOM   2666  CA  GLU G 400      15.877 -15.951 -61.014  1.00 81.33           C  
ATOM   2667  CA  MET G 401      15.305 -18.693 -58.485  1.00 31.65           C  
ATOM   2668  CA  ARG G 402      16.362 -16.288 -55.808  1.00150.04           C  
ATOM   2669  CA  LYS G 403      13.679 -13.958 -57.047  1.00123.93           C  
ATOM   2670  CA  VAL G 404      10.878 -16.397 -56.401  1.00 31.40           C  
ATOM   2671  CA  LEU G 405      12.419 -17.006 -53.009  1.00 98.35           C  
ATOM   2672  CA  ALA G 406      12.394 -13.263 -52.521  1.00 26.45           C  
ATOM   2673  CA  ALA G 407       8.630 -13.501 -52.436  1.00 30.33           C  
ATOM   2674  CA  LYS G 408       9.178 -15.969 -49.615  1.00102.52           C  
ATOM   2675  CA  PRO G 409       6.026 -17.875 -50.290  1.00 71.99           C  
ATOM   2676  CA  ALA G 410       5.139 -20.203 -47.445  1.00 33.84           C  
ATOM   2677  CA  ILE G 411       4.750 -22.805 -50.154  1.00 78.23           C  
ATOM   2678  CA  ILE G 412       7.740 -23.311 -52.384  1.00 44.58           C  
ATOM   2679  CA  ALA G 413       7.382 -25.713 -55.209  1.00 50.41           C  
ATOM   2680  CA  LEU G 414      10.407 -26.791 -57.138  1.00116.87           C  
ATOM   2681  CA  GLN G 415       9.989 -28.792 -60.210  1.00120.93           C  
ATOM   2682  CA  ILE G 416      13.090 -30.260 -61.491  1.00125.84           C  
ATOM   2683  CA  VAL G 417      13.693 -32.672 -64.251  1.00 43.88           C  
ATOM   2684  CA  ARG G 418      15.252 -35.920 -63.225  1.00 84.00           C  
ATOM   2685  CA  GLY G 419      16.342 -38.224 -65.974  1.00 20.03           C  
ATOM   2686  CA  ASN G 420      13.774 -37.930 -68.667  1.00 47.12           C  
ATOM   2687  CA  GLU G 421      10.997 -37.160 -66.243  1.00 78.65           C  
ATOM   2688  CA  SER G 422       9.300 -34.292 -64.505  1.00 49.10           C  
ATOM   2689  CA  ILE G 423       9.966 -33.987 -60.821  1.00121.39           C  
ATOM   2690  CA  TYR G 424       8.459 -31.827 -58.185  1.00169.25           C  
ATOM   2691  CA  LEU G 425      10.126 -30.861 -55.016  1.00 99.38           C  
ATOM   2692  CA  LEU G 426       9.100 -28.675 -52.214  1.00155.33           C  
ATOM   2693  CA  MET G 427       9.629 -26.854 -48.972  1.00172.22           C  
TER    2694      MET G 427                                                      
ATOM   2695  CA  PRO H  11      47.871  46.487 -40.504  1.00 86.04           C  
ATOM   2696  CA  LEU H  12      44.998  47.828 -38.523  1.00128.70           C  
ATOM   2697  CA  PRO H  13      42.864  50.360 -40.131  1.00251.14           C  
ATOM   2698  CA  SER H  14      42.492  51.006 -36.660  1.00136.76           C  
ATOM   2699  CA  LEU H  15      38.874  50.397 -35.921  1.00 79.23           C  
ATOM   2700  CA  ALA H  16      39.141  52.561 -32.847  1.00 49.47           C  
ATOM   2701  CA  PRO H  17      39.608  55.760 -34.715  1.00 68.28           C  
ATOM   2702  CA  MET H  18      36.446  55.165 -36.688  1.00 41.49           C  
ATOM   2703  CA  LEU H  19      34.633  53.981 -33.596  1.00 50.80           C  
ATOM   2704  CA  GLU H  20      35.458  56.964 -31.464  1.00 72.08           C  
ATOM   2705  CA  LYS H  21      33.476  59.309 -33.606  1.00104.60           C  
ATOM   2706  CA  VAL H  22      30.595  56.932 -34.344  1.00108.03           C  
ATOM   2707  CA  LEU H  23      29.931  55.219 -31.034  1.00113.15           C  
ATOM   2708  CA  PRO H  24      28.097  58.013 -29.329  1.00 64.78           C  
ATOM   2709  CA  ALA H  25      25.488  57.674 -32.058  1.00 30.14           C  
ATOM   2710  CA  VAL H  26      24.570  54.197 -30.896  1.00 35.45           C  
ATOM   2711  CA  VAL H  27      22.407  54.112 -27.854  1.00 96.57           C  
ATOM   2712  CA  SER H  28      20.902  51.650 -25.425  1.00 35.64           C  
ATOM   2713  CA  VAL H  29      17.164  51.507 -25.146  1.00 34.17           C  
ATOM   2714  CA  ARG H  30      15.494  50.700 -21.878  1.00 78.54           C  
ATOM   2715  CA  VAL H  31      11.894  49.681 -21.712  1.00 39.88           C  
ATOM   2716  CA  GLU H  32       9.376  49.088 -18.982  1.00 38.94           C  
ATOM   2717  CA  GLY H  33       5.839  47.986 -19.422  1.00 26.14           C  
ATOM   2718  CA  THR H  34       2.939  45.686 -18.834  1.00107.25           C  
ATOM   2719  CA  ALA H  35       0.536  43.000 -16.130  1.00 17.17           C  
ATOM   2720  CA  GLN H  59       3.640  42.432 -14.108  1.00107.42           C  
ATOM   2721  CA  PRO H  60       6.288  44.944 -14.684  1.00 71.41           C  
ATOM   2722  CA  PHE H  61       9.075  43.829 -16.934  1.00 52.55           C  
ATOM   2723  CA  GLU H  62      12.223  45.527 -18.011  1.00 25.70           C  
ATOM   2724  CA  GLY H  63      13.783  44.957 -21.364  1.00 18.17           C  
ATOM   2725  CA  LEU H  64      17.005  46.144 -22.874  1.00 49.11           C  
ATOM   2726  CA  GLY H  65      17.774  46.828 -26.486  1.00 22.14           C  
ATOM   2727  CA  SER H  66      19.713  49.274 -28.562  1.00 74.73           C  
ATOM   2728  CA  GLY H  67      18.981  52.008 -31.051  1.00 20.00           C  
ATOM   2729  CA  VAL H  68      20.734  54.409 -33.361  1.00 37.88           C  
ATOM   2730  CA  ILE H  69      20.409  58.151 -33.448  1.00 48.21           C  
ATOM   2731  CA  ILE H  70      19.285  59.067 -36.929  1.00118.08           C  
ATOM   2732  CA  ASN H  71      19.054  62.768 -36.396  1.00 59.86           C  
ATOM   2733  CA  ALA H  72      20.693  64.587 -33.571  1.00 33.35           C  
ATOM   2734  CA  SER H  73      18.592  67.691 -33.814  1.00 34.87           C  
ATOM   2735  CA  LYS H  74      15.248  65.965 -33.631  1.00131.31           C  
ATOM   2736  CA  GLY H  75      16.532  63.212 -31.460  1.00 30.34           C  
ATOM   2737  CA  TYR H  76      15.084  60.486 -33.621  1.00 71.59           C  
ATOM   2738  CA  VAL H  77      16.351  57.042 -32.785  1.00 44.02           C  
ATOM   2739  CA  LEU H  78      15.741  53.942 -34.844  1.00 49.71           C  
ATOM   2740  CA  THR H  79      15.083  50.668 -33.115  1.00 39.89           C  
ATOM   2741  CA  ASN H  80      13.405  47.355 -33.637  1.00 58.88           C  
ATOM   2742  CA  ASN H  81       9.678  47.228 -33.152  1.00 36.56           C  
ATOM   2743  CA  HIS H  82       9.956  44.185 -30.962  1.00 51.89           C  
ATOM   2744  CA  VAL H  83      12.151  45.991 -28.517  1.00 39.89           C  
ATOM   2745  CA  ILE H  84       9.600  48.793 -28.146  1.00 72.95           C  
ATOM   2746  CA  ASN H  85       6.345  46.898 -28.593  1.00 69.80           C  
ATOM   2747  CA  GLN H  86       5.453  46.189 -24.948  1.00132.29           C  
ATOM   2748  CA  ALA H  87       7.036  49.331 -23.549  1.00 68.86           C  
ATOM   2749  CA  GLN H  88       4.845  51.658 -21.560  1.00 94.27           C  
ATOM   2750  CA  LYS H  89       7.822  53.901 -20.982  1.00 32.23           C  
ATOM   2751  CA  ILE H  90      11.072  54.113 -22.847  1.00 84.35           C  
ATOM   2752  CA  SER H  91      14.377  55.571 -21.814  1.00 31.15           C  
ATOM   2753  CA  ILE H  92      17.500  56.036 -23.836  1.00 79.50           C  
ATOM   2754  CA  GLN H  93      20.989  56.088 -22.448  1.00 56.79           C  
ATOM   2755  CA  LEU H  94      24.054  57.465 -24.129  1.00 44.24           C  
ATOM   2756  CA  ASN H  95      27.432  55.841 -23.814  1.00 36.72           C  
ATOM   2757  CA  ASP H  96      28.473  58.867 -21.808  1.00 46.42           C  
ATOM   2758  CA  GLY H  97      25.912  57.944 -19.197  1.00 26.27           C  
ATOM   2759  CA  ARG H  98      23.389  60.639 -19.945  1.00 82.48           C  
ATOM   2760  CA  GLU H  99      19.827  59.375 -19.971  1.00 67.68           C  
ATOM   2761  CA  PHE H 100      16.736  60.677 -21.702  1.00 44.82           C  
ATOM   2762  CA  ASP H 101      13.096  59.761 -22.026  1.00 30.04           C  
ATOM   2763  CA  ALA H 102      11.723  58.831 -25.399  1.00 27.99           C  
ATOM   2764  CA  LYS H 103       8.348  58.520 -27.037  1.00 40.71           C  
ATOM   2765  CA  LEU H 104       7.364  56.169 -29.802  1.00 47.31           C  
ATOM   2766  CA  ILE H 105       6.877  58.147 -32.941  1.00 46.78           C  
ATOM   2767  CA  GLY H 106       5.679  55.135 -34.897  1.00 24.41           C  
ATOM   2768  CA  SER H 107       6.641  51.654 -35.965  1.00 97.66           C  
ATOM   2769  CA  ASP H 108       5.531  48.717 -38.005  1.00101.95           C  
ATOM   2770  CA  ASP H 109       5.334  45.002 -37.340  1.00 63.39           C  
ATOM   2771  CA  GLN H 110       6.149  43.485 -40.669  1.00140.53           C  
ATOM   2772  CA  SER H 111       9.546  45.066 -41.216  1.00 63.82           C  
ATOM   2773  CA  ASP H 112      10.084  45.365 -37.466  1.00 69.24           C  
ATOM   2774  CA  ILE H 113      11.162  49.021 -37.661  1.00100.28           C  
ATOM   2775  CA  ALA H 114      10.283  51.547 -34.995  1.00 29.41           C  
ATOM   2776  CA  LEU H 115      11.161  55.185 -34.588  1.00 96.81           C  
ATOM   2777  CA  LEU H 116      11.583  56.873 -31.241  1.00 46.60           C  
ATOM   2778  CA  GLN H 117      12.092  60.487 -30.357  1.00 55.15           C  
ATOM   2779  CA  ILE H 118      14.176  61.687 -27.465  1.00106.39           C  
ATOM   2780  CA  GLN H 119      12.687  64.423 -25.405  1.00 95.99           C  
ATOM   2781  CA  ASN H 120      15.023  67.351 -24.886  1.00 57.15           C  
ATOM   2782  CA  PRO H 121      17.715  65.654 -26.900  1.00110.77           C  
ATOM   2783  CA  SER H 122      20.597  68.152 -26.405  1.00246.89           C  
ATOM   2784  CA  LYS H 123      24.106  67.588 -27.741  1.00 83.31           C  
ATOM   2785  CA  LEU H 124      23.636  64.332 -29.506  1.00 75.10           C  
ATOM   2786  CA  THR H 125      25.631  62.716 -32.259  1.00 98.29           C  
ATOM   2787  CA  GLN H 126      24.104  61.345 -35.423  1.00111.88           C  
ATOM   2788  CA  ILE H 127      25.163  58.369 -37.459  1.00104.60           C  
ATOM   2789  CA  ALA H 128      25.573  58.664 -41.207  1.00 31.78           C  
ATOM   2790  CA  ILE H 129      23.732  56.193 -43.335  1.00 59.88           C  
ATOM   2791  CA  ALA H 130      25.342  54.225 -46.119  1.00 36.95           C  
ATOM   2792  CA  ASP H 131      23.753  52.746 -49.205  1.00 39.77           C  
ATOM   2793  CA  SER H 132      22.825  49.187 -48.329  1.00 37.99           C  
ATOM   2794  CA  ASP H 133      22.389  48.352 -51.958  1.00 42.20           C  
ATOM   2795  CA  LYS H 134      26.096  48.773 -52.510  1.00 80.76           C  
ATOM   2796  CA  LEU H 135      27.063  46.171 -49.934  1.00 55.58           C  
ATOM   2797  CA  ARG H 136      28.665  42.996 -51.188  1.00 96.82           C  
ATOM   2798  CA  VAL H 137      29.539  39.815 -49.381  1.00 38.59           C  
ATOM   2799  CA  GLY H 138      32.930  40.051 -47.803  1.00 25.78           C  
ATOM   2800  CA  ASP H 139      32.544  43.636 -46.735  1.00 27.36           C  
ATOM   2801  CA  PHE H 140      33.620  44.288 -43.184  1.00 53.42           C  
ATOM   2802  CA  ALA H 141      31.015  45.137 -40.619  1.00 28.83           C  
ATOM   2803  CA  VAL H 142      30.961  46.150 -36.998  1.00 32.41           C  
ATOM   2804  CA  ALA H 143      28.002  45.642 -34.744  1.00 28.20           C  
ATOM   2805  CA  VAL H 144      27.285  47.879 -31.811  1.00 33.90           C  
ATOM   2806  CA  GLY H 145      24.629  47.330 -29.210  1.00 22.20           C  
ATOM   2807  CA  ASN H 146      24.106  46.142 -25.681  1.00132.89           C  
ATOM   2808  CA  PRO H 147      24.405  42.449 -25.414  1.00151.50           C  
ATOM   2809  CA  PHE H 148      23.201  41.069 -22.115  1.00 61.72           C  
ATOM   2810  CA  GLY H 149      22.703  44.664 -21.113  1.00 24.82           C  
ATOM   2811  CA  LEU H 150      26.383  44.801 -20.394  1.00 54.37           C  
ATOM   2812  CA  GLY H 151      26.759  48.211 -21.963  1.00 30.72           C  
ATOM   2813  CA  GLN H 152      27.855  49.477 -25.326  1.00 40.32           C  
ATOM   2814  CA  THR H 153      29.714  46.662 -27.002  1.00 33.19           C  
ATOM   2815  CA  ALA H 154      31.282  46.472 -30.414  1.00 29.26           C  
ATOM   2816  CA  THR H 155      31.824  43.280 -32.348  1.00 31.66           C  
ATOM   2817  CA  SER H 156      33.449  42.775 -35.704  1.00 34.73           C  
ATOM   2818  CA  GLY H 157      32.735  40.531 -38.644  1.00 25.29           C  
ATOM   2819  CA  ILE H 158      32.037  40.493 -42.352  1.00 56.80           C  
ATOM   2820  CA  VAL H 159      28.865  40.615 -44.362  1.00 40.68           C  
ATOM   2821  CA  SER H 160      28.070  36.947 -44.797  1.00 48.28           C  
ATOM   2822  CA  ALA H 161      25.120  37.308 -47.108  1.00 48.17           C  
ATOM   2823  CA  LEU H 162      22.502  39.732 -48.263  1.00115.90           C  
ATOM   2824  CA  GLY H 163      18.986  39.607 -49.510  1.00 30.14           C  
ATOM   2825  CA  ARG H 164      18.135  36.771 -47.247  1.00152.72           C  
ATOM   2826  CA  SER H 165      14.648  35.690 -46.414  1.00 89.70           C  
ATOM   2827  CA  GLY H 166      12.330  32.891 -45.770  1.00 40.10           C  
ATOM   2828  CA  LEU H 167      13.611  33.057 -42.204  1.00116.55           C  
ATOM   2829  CA  ASN H 168       9.992  33.657 -41.305  1.00 65.40           C  
ATOM   2830  CA  LEU H 169      11.294  35.944 -38.617  1.00 55.05           C  
ATOM   2831  CA  GLU H 170       9.438  38.915 -40.044  1.00109.21           C  
ATOM   2832  CA  GLY H 171       6.651  39.644 -42.499  1.00 38.77           C  
ATOM   2833  CA  LEU H 172       9.005  41.474 -44.759  1.00127.92           C  
ATOM   2834  CA  GLU H 173      12.517  40.360 -44.656  1.00 82.77           C  
ATOM   2835  CA  ASN H 174      15.734  41.180 -46.430  1.00105.10           C  
ATOM   2836  CA  PHE H 175      18.277  40.598 -43.851  1.00 90.16           C  
ATOM   2837  CA  ILE H 176      21.887  41.331 -44.268  1.00 70.55           C  
ATOM   2838  CA  GLN H 177      23.610  38.390 -42.680  1.00 58.52           C  
ATOM   2839  CA  THR H 178      26.652  38.992 -40.556  1.00112.18           C  
ATOM   2840  CA  ASP H 179      29.200  36.935 -38.651  1.00 64.65           C  
ATOM   2841  CA  ALA H 180      29.679  39.698 -36.102  1.00 37.47           C  
ATOM   2842  CA  SER H 181      28.673  38.476 -32.702  1.00 39.04           C  
ATOM   2843  CA  ILE H 182      25.111  39.474 -32.080  1.00 92.28           C  
ATOM   2844  CA  ASN H 183      23.361  38.448 -28.921  1.00 47.80           C  
ATOM   2845  CA  ARG H 184      20.212  39.320 -27.101  1.00 61.58           C  
ATOM   2846  CA  GLY H 185      20.162  43.012 -26.366  1.00 21.86           C  
ATOM   2847  CA  ASN H 186      21.717  43.692 -29.744  1.00 55.24           C  
ATOM   2848  CA  ALA H 187      18.366  44.337 -31.348  1.00 97.00           C  
ATOM   2849  CA  GLY H 188      17.881  47.842 -32.614  1.00 24.33           C  
ATOM   2850  CA  GLY H 189      21.635  48.226 -32.586  1.00 22.33           C  
ATOM   2851  CA  ALA H 190      23.695  49.336 -35.507  1.00 45.20           C  
ATOM   2852  CA  LEU H 191      25.755  47.451 -38.020  1.00 92.52           C  
ATOM   2853  CA  LEU H 192      28.421  49.700 -39.375  1.00 60.42           C  
ATOM   2854  CA  ASN H 193      30.803  49.873 -42.288  1.00154.54           C  
ATOM   2855  CA  LEU H 194      34.477  50.632 -41.820  1.00102.36           C  
ATOM   2856  CA  ASN H 195      33.430  54.171 -42.561  1.00 59.19           C  
ATOM   2857  CA  GLY H 196      31.249  54.070 -39.491  1.00 25.20           C  
ATOM   2858  CA  GLU H 197      28.231  54.450 -41.718  1.00 57.14           C  
ATOM   2859  CA  LEU H 198      25.029  52.611 -40.864  1.00140.59           C  
ATOM   2860  CA  ILE H 199      24.666  49.496 -43.025  1.00108.90           C  
ATOM   2861  CA  GLY H 200      21.656  48.122 -41.171  1.00 29.25           C  
ATOM   2862  CA  ILE H 201      19.928  47.559 -37.854  1.00 45.48           C  
ATOM   2863  CA  ASN H 202      20.565  44.254 -36.093  1.00 81.62           C  
ATOM   2864  CA  THR H 203      17.196  42.520 -35.929  1.00 83.90           C  
ATOM   2865  CA  ALA H 204      17.760  38.889 -35.001  1.00 53.37           C  
ATOM   2866  CA  ILE H 205      19.960  35.829 -34.807  1.00100.64           C  
ATOM   2867  CA  LEU H 206      19.680  32.139 -35.452  1.00109.79           C  
ATOM   2868  CA  ALA H 207      21.178  30.246 -32.581  1.00 41.56           C  
ATOM   2869  CA  PRO H 208      20.263  26.935 -31.164  1.00 66.63           C  
ATOM   2870  CA  GLY H 209      21.925  27.830 -27.880  1.00 29.20           C  
ATOM   2871  CA  GLY H 210      20.350  31.220 -27.660  1.00 23.26           C  
ATOM   2872  CA  GLY H 211      23.872  32.528 -27.946  1.00 22.91           C  
ATOM   2873  CA  SER H 212      25.577  33.923 -31.010  1.00 54.02           C  
ATOM   2874  CA  VAL H 213      26.329  31.180 -33.516  1.00 58.58           C  
ATOM   2875  CA  GLY H 214      27.831  33.685 -35.886  1.00 34.60           C  
ATOM   2876  CA  ILE H 215      24.655  33.924 -37.901  1.00 99.97           C  
ATOM   2877  CA  GLY H 216      23.034  37.293 -37.387  1.00 20.66           C  
ATOM   2878  CA  PHE H 217      20.577  39.261 -39.447  1.00 53.70           C  
ATOM   2879  CA  ALA H 218      20.057  42.964 -39.837  1.00 33.82           C  
ATOM   2880  CA  ILE H 219      17.611  45.130 -41.700  1.00 78.39           C  
ATOM   2881  CA  PRO H 220      19.392  47.089 -44.294  1.00 84.66           C  
ATOM   2882  CA  SER H 221      20.074  50.769 -43.781  1.00 42.43           C  
ATOM   2883  CA  ASN H 222      18.212  51.663 -46.880  1.00 64.11           C  
ATOM   2884  CA  MET H 223      15.569  49.739 -45.179  1.00 97.38           C  
ATOM   2885  CA  ALA H 224      15.485  51.602 -41.937  1.00 50.57           C  
ATOM   2886  CA  ARG H 225      16.195  54.941 -43.498  1.00128.63           C  
ATOM   2887  CA  THR H 226      13.248  55.437 -45.724  1.00 66.56           C  
ATOM   2888  CA  LEU H 227      10.960  53.475 -43.393  1.00112.47           C  
ATOM   2889  CA  ALA H 228      12.068  55.734 -40.608  1.00 44.85           C  
ATOM   2890  CA  GLN H 229      11.618  58.757 -42.786  1.00161.27           C  
ATOM   2891  CA  GLN H 230       7.925  58.626 -43.248  1.00 94.48           C  
ATOM   2892  CA  LEU H 231       7.559  57.679 -39.641  1.00 53.18           C  
ATOM   2893  CA  ILE H 232       8.526  61.250 -39.144  1.00123.90           C  
ATOM   2894  CA  ASP H 233       7.329  62.298 -42.632  1.00162.59           C  
ATOM   2895  CA  PHE H 234       5.479  61.717 -44.840  1.00214.58           C  
ATOM   2896  CA  GLY H 235       3.816  59.301 -42.543  1.00 41.81           C  
ATOM   2897  CA  GLU H 236       1.241  58.240 -45.019  1.00 89.52           C  
ATOM   2898  CA  ILE H 237      -0.872  55.690 -43.270  1.00 38.48           C  
ATOM   2899  CA  LYS H 238      -0.420  53.405 -46.176  1.00193.35           C  
ATOM   2900  CA  ARG H 239       1.262  51.281 -46.909  1.00222.91           C  
ATOM   2901  CA  GLY H 240       2.398  51.601 -43.326  1.00 48.50           C  
ATOM   2902  CA  LEU H 241       3.936  48.261 -43.998  1.00186.04           C  
ATOM   2903  CA  LEU H 242       1.576  45.705 -45.360  1.00 93.94           C  
ATOM   2904  CA  GLY H 243       0.867  43.691 -42.240  1.00 51.15           C  
ATOM   2905  CA  ILE H 244       1.546  40.189 -43.492  1.00119.48           C  
ATOM   2906  CA  LYS H 245       3.561  37.155 -42.535  1.00112.30           C  
ATOM   2907  CA  GLY H 246       5.398  35.048 -45.012  1.00 33.53           C  
ATOM   2908  CA  THR H 247       8.446  33.012 -45.732  1.00111.68           C  
ATOM   2909  CA  GLU H 248      10.456  31.427 -48.512  1.00 49.97           C  
ATOM   2910  CA  MET H 249       8.830  29.349 -51.167  1.00147.45           C  
ATOM   2911  CA  SER H 250       7.605  26.203 -49.505  1.00 37.31           C  
ATOM   2912  CA  ALA H 251       8.839  22.863 -50.693  1.00 34.89           C  
ATOM   2913  CA  ASP H 252       5.376  21.378 -50.962  1.00 58.63           C  
ATOM   2914  CA  ILE H 253       3.614  24.197 -52.736  1.00 65.07           C  
ATOM   2915  CA  ALA H 254       6.506  25.155 -54.951  1.00 55.14           C  
ATOM   2916  CA  LYS H 255       7.506  21.855 -56.336  1.00100.98           C  
ATOM   2917  CA  ALA H 256       4.157  20.240 -56.692  1.00 68.25           C  
ATOM   2918  CA  PHE H 257       1.871  22.714 -58.328  1.00179.27           C  
ATOM   2919  CA  ASN H 258       4.676  24.521 -59.847  1.00189.15           C  
ATOM   2920  CA  LEU H 259       4.289  28.145 -59.232  1.00174.20           C  
ATOM   2921  CA  ASP H 260       4.240  30.285 -62.320  1.00 56.40           C  
ATOM   2922  CA  VAL H 261       6.856  32.551 -60.830  1.00115.54           C  
ATOM   2923  CA  GLN H 262       9.812  30.453 -59.848  1.00 93.97           C  
ATOM   2924  CA  ARG H 263       9.680  31.787 -56.371  1.00126.27           C  
ATOM   2925  CA  GLY H 264       8.541  34.752 -54.443  1.00 23.88           C  
ATOM   2926  CA  ALA H 265       7.589  35.962 -51.062  1.00 40.41           C  
ATOM   2927  CA  PHE H 266       4.852  33.669 -50.084  1.00128.80           C  
ATOM   2928  CA  VAL H 267       2.330  34.720 -47.563  1.00 67.22           C  
ATOM   2929  CA  SER H 268       0.874  32.215 -45.159  1.00111.23           C  
ATOM   2930  CA  GLU H 269      -1.236  34.716 -43.370  1.00144.16           C  
ATOM   2931  CA  VAL H 270      -3.531  37.710 -43.551  1.00 64.11           C  
ATOM   2932  CA  LEU H 271      -3.425  40.239 -40.773  1.00 58.64           C  
ATOM   2933  CA  PRO H 272      -6.610  41.690 -39.532  1.00 70.56           C  
ATOM   2934  CA  GLY H 273      -7.312  45.348 -40.170  1.00 24.70           C  
ATOM   2935  CA  SER H 274      -4.015  45.030 -41.870  1.00 42.16           C  
ATOM   2936  CA  GLY H 275      -2.832  46.727 -44.936  1.00 32.84           C  
ATOM   2937  CA  SER H 276      -2.715  43.492 -46.751  1.00 46.11           C  
ATOM   2938  CA  ALA H 277      -6.169  42.746 -45.567  1.00 54.94           C  
ATOM   2939  CA  LYS H 278      -7.929  45.710 -47.068  1.00120.42           C  
ATOM   2940  CA  ALA H 279      -5.674  45.674 -50.081  1.00 39.82           C  
ATOM   2941  CA  GLY H 280      -7.193  42.324 -50.509  1.00 39.79           C  
ATOM   2942  CA  VAL H 281      -4.010  40.345 -50.495  1.00 61.73           C  
ATOM   2943  CA  LYS H 282      -4.660  37.192 -48.767  1.00125.11           C  
ATOM   2944  CA  ALA H 283      -2.926  34.038 -47.919  1.00 93.19           C  
ATOM   2945  CA  GLY H 284      -1.411  31.483 -50.135  1.00 42.02           C  
ATOM   2946  CA  ASP H 285      -0.254  34.600 -51.917  1.00100.35           C  
ATOM   2947  CA  ILE H 286       2.828  34.685 -53.792  1.00 93.18           C  
ATOM   2948  CA  ILE H 287       4.288  38.125 -54.077  1.00 57.07           C  
ATOM   2949  CA  THR H 288       6.106  38.082 -57.376  1.00 63.29           C  
ATOM   2950  CA  SER H 289       7.125  41.670 -57.551  1.00 96.07           C  
ATOM   2951  CA  LEU H 290       6.947  45.022 -55.930  1.00 74.57           C  
ATOM   2952  CA  ASN H 291       6.639  48.105 -58.056  1.00181.74           C  
ATOM   2953  CA  GLY H 292       7.570  48.149 -61.737  1.00 53.21           C  
ATOM   2954  CA  LYS H 293      10.853  46.347 -61.280  1.00100.61           C  
ATOM   2955  CA  PRO H 294      10.798  42.695 -60.567  1.00 61.35           C  
ATOM   2956  CA  LEU H 295      10.958  41.387 -57.022  1.00121.49           C  
ATOM   2957  CA  ASN H 296      13.315  38.671 -55.916  1.00 69.18           C  
ATOM   2958  CA  SER H 297      12.801  36.267 -53.083  1.00 43.47           C  
ATOM   2959  CA  PHE H 298      11.073  36.980 -49.839  1.00 79.78           C  
ATOM   2960  CA  ALA H 299      14.438  38.349 -48.983  1.00 47.71           C  
ATOM   2961  CA  GLU H 300      14.437  41.018 -51.600  1.00 87.17           C  
ATOM   2962  CA  LEU H 301      10.941  41.803 -50.474  1.00 70.80           C  
ATOM   2963  CA  ARG H 302      11.752  43.333 -47.189  1.00190.40           C  
ATOM   2964  CA  SER H 303      14.858  44.711 -48.680  1.00 55.28           C  
ATOM   2965  CA  ARG H 304      13.008  47.125 -50.763  1.00172.24           C  
ATOM   2966  CA  ILE H 305       9.990  47.531 -48.510  1.00 91.81           C  
ATOM   2967  CA  ALA H 306      11.946  47.734 -45.370  1.00 72.56           C  
ATOM   2968  CA  THR H 307      13.845  50.212 -47.433  1.00 61.84           C  
ATOM   2969  CA  THR H 308      10.807  52.130 -48.490  1.00138.35           C  
ATOM   2970  CA  GLU H 309       8.823  54.592 -46.463  1.00 91.94           C  
ATOM   2971  CA  PRO H 310       6.292  52.921 -44.363  1.00182.38           C  
ATOM   2972  CA  GLY H 311       4.181  54.572 -45.610  1.00121.90           C  
ATOM   2973  CA  THR H 312       4.652  54.986 -49.305  1.00 48.07           C  
ATOM   2974  CA  LYS H 313       1.788  53.844 -51.406  1.00100.35           C  
ATOM   2975  CA  VAL H 314       3.080  51.067 -53.574  1.00 47.90           C  
ATOM   2976  CA  LYS H 315       1.673  48.350 -55.761  1.00 75.73           C  
ATOM   2977  CA  LEU H 316       2.377  44.701 -55.318  1.00 97.20           C  
ATOM   2978  CA  GLY H 317       2.372  41.935 -57.838  1.00 48.74           C  
ATOM   2979  CA  LEU H 318       1.333  38.567 -56.667  1.00116.90           C  
ATOM   2980  CA  LEU H 319       0.297  35.396 -58.103  1.00217.13           C  
ATOM   2981  CA  ARG H 320      -2.876  33.990 -57.000  1.00199.58           C  
ATOM   2982  CA  ASN H 321      -4.422  30.968 -58.703  1.00205.94           C  
ATOM   2983  CA  GLY H 322      -1.858  31.089 -61.319  1.00 48.25           C  
ATOM   2984  CA  LYS H 323      -3.213  34.357 -62.352  1.00193.67           C  
ATOM   2985  CA  PRO H 324      -1.962  37.791 -62.114  1.00165.74           C  
ATOM   2986  CA  LEU H 325      -3.096  40.970 -60.410  1.00169.58           C  
ATOM   2987  CA  GLU H 326      -1.832  44.234 -59.294  1.00120.73           C  
ATOM   2988  CA  VAL H 327      -3.099  45.755 -56.137  1.00 58.32           C  
ATOM   2989  CA  GLU H 328      -2.125  48.868 -54.387  1.00107.48           C  
ATOM   2990  CA  VAL H 329      -1.214  48.399 -50.817  1.00 60.61           C  
ATOM   2991  CA  SER H 340     -29.868  44.137 -27.004  1.00 61.25           C  
ATOM   2992  CA  ALA H 341     -29.343  43.951 -23.252  1.00 79.97           C  
ATOM   2993  CA  GLU H 342     -27.360  40.757 -23.483  1.00102.50           C  
ATOM   2994  CA  MET H 343     -24.022  42.135 -24.427  1.00106.53           C  
ATOM   2995  CA  ILE H 344     -23.913  44.699 -21.696  1.00184.63           C  
ATOM   2996  CA  THR H 345     -25.659  42.515 -19.222  1.00 75.04           C  
ATOM   2997  CA  PRO H 346     -24.783  38.902 -18.998  1.00157.15           C  
ATOM   2998  CA  ALA H 347     -27.139  36.239 -20.274  1.00 73.20           C  
ATOM   2999  CA  LEU H 348     -30.096  38.514 -19.697  1.00139.36           C  
ATOM   3000  CA  GLU H 349     -31.923  38.483 -22.957  1.00136.84           C  
ATOM   3001  CA  GLY H 350     -34.158  41.428 -23.361  1.00 29.40           C  
ATOM   3002  CA  ALA H 351     -34.814  44.721 -25.009  1.00 35.81           C  
ATOM   3003  CA  THR H 352     -32.127  46.000 -27.266  1.00101.82           C  
ATOM   3004  CA  LEU H 353     -30.055  48.913 -26.166  1.00 56.26           C  
ATOM   3005  CA  SER H 354     -28.664  51.863 -28.026  1.00 32.99           C  
ATOM   3006  CA  ASP H 355     -26.158  54.408 -26.872  1.00 44.78           C  
ATOM   3007  CA  GLY H 356     -26.466  58.114 -27.060  1.00 47.47           C  
ATOM   3008  CA  GLN H 357     -29.552  60.006 -26.085  1.00164.40           C  
ATOM   3009  CA  LEU H 358     -29.613  59.588 -29.703  1.00198.44           C  
ATOM   3010  CA  LYS H 359     -32.390  62.100 -30.137  1.00129.34           C  
ATOM   3011  CA  ASP H 360     -31.141  64.540 -27.486  1.00 46.08           C  
ATOM   3012  CA  GLY H 361     -27.901  65.012 -25.617  1.00 28.24           C  
ATOM   3013  CA  GLY H 362     -26.901  61.712 -24.099  1.00 40.53           C  
ATOM   3014  CA  LYS H 363     -29.160  61.261 -21.120  1.00 89.65           C  
ATOM   3015  CA  GLY H 364     -27.970  57.723 -21.240  1.00 33.91           C  
ATOM   3016  CA  ILE H 365     -28.421  54.366 -22.896  1.00169.95           C  
ATOM   3017  CA  LYS H 366     -31.790  53.792 -24.489  1.00 58.71           C  
ATOM   3018  CA  ILE H 367     -33.566  50.508 -24.609  1.00 63.12           C  
ATOM   3019  CA  ASP H 368     -35.073  50.205 -28.038  1.00 53.09           C  
ATOM   3020  CA  GLU H 369     -37.715  47.595 -27.529  1.00 90.55           C  
ATOM   3021  CA  VAL H 370     -38.777  44.976 -25.055  1.00112.58           C  
ATOM   3022  CA  VAL H 371     -38.630  41.327 -26.071  1.00193.55           C  
ATOM   3023  CA  LYS H 372     -40.881  41.026 -22.973  1.00181.53           C  
ATOM   3024  CA  GLY H 373     -40.885  37.256 -22.795  1.00 36.76           C  
ATOM   3025  CA  SER H 374     -37.155  37.755 -22.124  1.00 50.82           C  
ATOM   3026  CA  PRO H 375     -35.665  38.147 -18.730  1.00 75.35           C  
ATOM   3027  CA  ALA H 376     -34.592  41.720 -19.319  1.00 42.15           C  
ATOM   3028  CA  ALA H 377     -38.322  42.192 -19.387  1.00 50.35           C  
ATOM   3029  CA  GLN H 378     -38.876  40.258 -16.175  1.00 55.08           C  
ATOM   3030  CA  ALA H 379     -37.048  42.666 -13.868  1.00 58.48           C  
ATOM   3031  CA  GLY H 380     -38.755  45.844 -14.957  1.00 61.71           C  
ATOM   3032  CA  LEU H 381     -37.059  46.936 -18.133  1.00 59.74           C  
ATOM   3033  CA  GLN H 382     -39.652  48.517 -20.384  1.00127.44           C  
ATOM   3034  CA  LYS H 383     -38.956  50.058 -23.760  1.00144.73           C  
ATOM   3035  CA  ASP H 384     -38.218  53.760 -24.190  1.00 77.99           C  
ATOM   3036  CA  ASP H 385     -36.517  53.896 -20.845  1.00 51.81           C  
ATOM   3037  CA  VAL H 386     -33.318  55.864 -20.675  1.00 54.67           C  
ATOM   3038  CA  ILE H 387     -30.686  54.650 -18.305  1.00 71.64           C  
ATOM   3039  CA  ILE H 388     -29.247  57.829 -16.894  1.00 78.99           C  
ATOM   3040  CA  GLY H 389     -26.664  56.060 -14.790  1.00 43.55           C  
ATOM   3041  CA  VAL H 390     -25.825  53.043 -12.699  1.00 64.80           C  
ATOM   3042  CA  ASN H 391     -24.716  52.784  -9.097  1.00 88.73           C  
ATOM   3043  CA  ARG H 392     -24.512  56.479  -8.396  1.00159.42           C  
ATOM   3044  CA  ASP H 393     -22.606  57.037 -11.549  1.00142.79           C  
ATOM   3045  CA  ARG H 394     -23.919  58.712 -14.617  1.00116.40           C  
ATOM   3046  CA  VAL H 395     -24.078  56.685 -17.769  1.00 46.29           C  
ATOM   3047  CA  ASN H 396     -23.601  58.828 -20.830  1.00 46.93           C  
ATOM   3048  CA  SER H 397     -23.358  55.855 -23.149  1.00 98.91           C  
ATOM   3049  CA  ILE H 398     -23.006  52.113 -23.195  1.00 58.89           C  
ATOM   3050  CA  ALA H 399     -19.274  52.330 -22.720  1.00 33.77           C  
ATOM   3051  CA  GLU H 400     -19.662  54.133 -19.425  1.00 34.17           C  
ATOM   3052  CA  MET H 401     -22.399  51.759 -18.381  1.00 43.88           C  
ATOM   3053  CA  ARG H 402     -20.059  48.923 -19.137  1.00135.92           C  
ATOM   3054  CA  LYS H 403     -17.549  50.581 -16.860  1.00 96.47           C  
ATOM   3055  CA  VAL H 404     -19.826  50.398 -13.861  1.00 48.62           C  
ATOM   3056  CA  LEU H 405     -20.440  46.793 -14.764  1.00 67.42           C  
ATOM   3057  CA  ALA H 406     -16.719  46.290 -14.943  1.00 35.73           C  
ATOM   3058  CA  ALA H 407     -16.689  46.815 -11.208  1.00 32.55           C  
ATOM   3059  CA  LYS H 408     -19.253  44.047 -11.188  1.00109.00           C  
ATOM   3060  CA  PRO H 409     -20.888  45.140  -8.019  1.00 70.84           C  
ATOM   3061  CA  ALA H 410     -23.159  42.469  -6.622  1.00 30.79           C  
ATOM   3062  CA  ILE H 411     -25.763  45.195  -6.552  1.00 86.51           C  
ATOM   3063  CA  ILE H 412     -26.453  47.040  -9.743  1.00 44.10           C  
ATOM   3064  CA  ALA H 413     -28.862  49.884  -9.625  1.00 48.98           C  
ATOM   3065  CA  LEU H 414     -30.154  51.360 -12.807  1.00115.63           C  
ATOM   3066  CA  GLN H 415     -32.082  54.514 -12.760  1.00220.18           C  
ATOM   3067  CA  ILE H 416     -33.821  55.241 -15.887  1.00 92.83           C  
ATOM   3068  CA  VAL H 417     -36.255  57.903 -16.709  1.00 55.88           C  
ATOM   3069  CA  ARG H 418     -39.560  56.727 -17.993  1.00 88.68           C  
ATOM   3070  CA  GLY H 419     -42.033  59.245 -19.203  1.00 20.08           C  
ATOM   3071  CA  ASN H 420     -41.532  62.281 -17.110  1.00 45.09           C  
ATOM   3072  CA  GLU H 421     -40.536  60.390 -14.015  1.00 46.85           C  
ATOM   3073  CA  SER H 422     -37.562  58.833 -12.358  1.00 46.88           C  
ATOM   3074  CA  ILE H 423     -37.338  55.088 -12.392  1.00 81.28           C  
ATOM   3075  CA  TYR H 424     -35.078  52.689 -10.659  1.00166.33           C  
ATOM   3076  CA  LEU H 425     -34.180  49.355 -11.995  1.00100.99           C  
ATOM   3077  CA  LEU H 426     -31.940  46.709 -10.708  1.00151.27           C  
ATOM   3078  CA  MET H 427     -30.210  43.426 -10.964  1.00 59.20           C  
TER    3079      MET H 427                                                      
ATOM   3080  CA  PRO I  11      45.479  41.473 -47.797  1.00 78.85           C  
ATOM   3081  CA  LEU I  12      47.006  39.342 -45.089  1.00 95.46           C  
ATOM   3082  CA  PRO I  13      49.522  40.741 -42.743  1.00155.18           C  
ATOM   3083  CA  SER I  14      49.913  37.901 -42.677  1.00129.12           C  
ATOM   3084  CA  LEU I  15      49.505  36.692 -39.119  1.00112.85           C  
ATOM   3085  CA  ALA I  16      51.833  33.738 -39.605  1.00 42.68           C  
ATOM   3086  CA  PRO I  17      55.017  35.655 -39.941  1.00 66.44           C  
ATOM   3087  CA  MET I  18      54.403  37.448 -36.678  1.00 38.35           C  
ATOM   3088  CA  LEU I  19      53.328  34.246 -35.002  1.00 49.03           C  
ATOM   3089  CA  GLU I  20      56.326  32.245 -35.984  1.00 52.22           C  
ATOM   3090  CA  LYS I  21      58.676  34.388 -33.970  1.00 64.33           C  
ATOM   3091  CA  VAL I  22      56.370  34.934 -30.992  1.00108.73           C  
ATOM   3092  CA  LEU I  23      54.794  31.534 -30.449  1.00117.13           C  
ATOM   3093  CA  PRO I  24      57.673  29.868 -28.721  1.00 70.42           C  
ATOM   3094  CA  ALA I  25      57.299  32.478 -25.999  1.00 33.59           C  
ATOM   3095  CA  VAL I  26      53.900  31.130 -25.029  1.00111.54           C  
ATOM   3096  CA  VAL I  27      53.982  27.965 -23.029  1.00124.49           C  
ATOM   3097  CA  SER I  28      51.649  25.374 -21.625  1.00 52.79           C  
ATOM   3098  CA  VAL I  29      51.581  24.959 -17.893  1.00 32.24           C  
ATOM   3099  CA  ARG I  30      50.950  21.585 -16.356  1.00 80.32           C  
ATOM   3100  CA  VAL I  31      50.114  21.187 -12.725  1.00 40.53           C  
ATOM   3101  CA  GLU I  32      49.666  18.365 -10.272  1.00 42.91           C  
ATOM   3102  CA  GLY I  33      48.633  18.523  -6.676  1.00 26.73           C  
ATOM   3103  CA  THR I  34      46.267  17.939  -3.781  1.00138.86           C  
ATOM   3104  CA  ALA I  35      44.128  15.115  -1.172  1.00 24.65           C  
ATOM   3105  CA  GLN I  59      43.354  13.195  -4.322  1.00 83.71           C  
ATOM   3106  CA  PRO I  60      45.718  13.845  -7.104  1.00 70.08           C  
ATOM   3107  CA  PHE I  61      44.536  16.032  -9.936  1.00 47.69           C  
ATOM   3108  CA  GLU I  62      46.069  17.356 -13.091  1.00 24.17           C  
ATOM   3109  CA  GLY I  63      45.319  20.732 -14.551  1.00 17.36           C  
ATOM   3110  CA  LEU I  64      46.315  22.432 -17.752  1.00 44.91           C  
ATOM   3111  CA  GLY I  65      46.852  26.104 -18.375  1.00 21.31           C  
ATOM   3112  CA  SER I  66      49.181  28.393 -20.248  1.00 77.71           C  
ATOM   3113  CA  GLY I  67      51.814  30.955 -19.439  1.00 17.58           C  
ATOM   3114  CA  VAL I  68      54.092  33.446 -21.110  1.00 42.80           C  
ATOM   3115  CA  ILE I  69      57.829  33.675 -20.846  1.00 57.09           C  
ATOM   3116  CA  ILE I  70      58.650  37.143 -19.611  1.00 81.70           C  
ATOM   3117  CA  ASN I  71      62.372  36.761 -19.476  1.00 60.59           C  
ATOM   3118  CA  ALA I  72      64.250  34.074 -21.282  1.00 32.14           C  
ATOM   3119  CA  SER I  73      67.396  34.339 -19.262  1.00 35.20           C  
ATOM   3120  CA  LYS I  74      65.814  33.997 -15.871  1.00 84.04           C  
ATOM   3121  CA  GLY I  75      63.077  31.774 -17.157  1.00 33.15           C  
ATOM   3122  CA  TYR I  76      60.267  33.744 -15.589  1.00 71.65           C  
ATOM   3123  CA  VAL I  77      56.851  32.798 -16.828  1.00124.75           C  
ATOM   3124  CA  LEU I  78      53.666  34.683 -16.046  1.00 61.20           C  
ATOM   3125  CA  THR I  79      50.488  32.778 -15.434  1.00 43.87           C  
ATOM   3126  CA  ASN I  80      47.198  33.077 -13.664  1.00 59.85           C  
ATOM   3127  CA  ASN I  81      47.240  32.351  -9.981  1.00 49.36           C  
ATOM   3128  CA  HIS I  82      44.253  30.091 -10.287  1.00 54.88           C  
ATOM   3129  CA  VAL I  83      46.083  27.818 -12.642  1.00 44.86           C  
ATOM   3130  CA  ILE I  84      48.960  27.524 -10.181  1.00175.98           C  
ATOM   3131  CA  ASN I  85      47.209  27.742  -6.826  1.00 73.25           C  
ATOM   3132  CA  GLN I  86      46.664  24.071  -6.041  1.00 69.50           C  
ATOM   3133  CA  ALA I  87      49.798  22.840  -7.790  1.00 67.55           C  
ATOM   3134  CA  GLN I  88      52.253  20.862  -5.729  1.00 59.05           C  
ATOM   3135  CA  LYS I  89      54.426  20.485  -8.786  1.00 31.89           C  
ATOM   3136  CA  ILE I  90      54.489  22.542 -11.920  1.00 41.25           C  
ATOM   3137  CA  SER I  91      55.892  21.750 -15.314  1.00 74.91           C  
ATOM   3138  CA  ILE I  92      56.203  23.922 -18.373  1.00 91.04           C  
ATOM   3139  CA  GLN I  93      56.115  22.649 -21.921  1.00145.23           C  
ATOM   3140  CA  LEU I  94      57.405  24.498 -24.911  1.00 50.95           C  
ATOM   3141  CA  ASN I  95      55.809  24.284 -28.331  1.00110.29           C  
ATOM   3142  CA  ASP I  96      58.875  22.393 -29.383  1.00 58.55           C  
ATOM   3143  CA  GLY I  97      58.033  19.626 -26.967  1.00 28.72           C  
ATOM   3144  CA  ARG I  98      60.753  20.333 -24.456  1.00 89.12           C  
ATOM   3145  CA  GLU I  99      59.566  20.323 -20.882  1.00 40.53           C  
ATOM   3146  CA  PHE I 100      60.881  21.951 -17.751  1.00 59.48           C  
ATOM   3147  CA  ASP I 101      60.238  22.064 -14.025  1.00133.80           C  
ATOM   3148  CA  ALA I 102      59.007  25.330 -12.581  1.00 39.98           C  
ATOM   3149  CA  LYS I 103      58.802  26.836  -9.117  1.00117.23           C  
ATOM   3150  CA  LEU I 104      56.362  29.440  -7.941  1.00 60.49           C  
ATOM   3151  CA  ILE I 105      58.185  32.688  -7.435  1.00135.45           C  
ATOM   3152  CA  GLY I 106      55.132  34.388  -6.042  1.00 28.42           C  
ATOM   3153  CA  SER I 107      51.594  35.291  -6.901  1.00100.25           C  
ATOM   3154  CA  ASP I 108      48.589  37.056  -5.579  1.00 94.49           C  
ATOM   3155  CA  ASP I 109      44.928  36.180  -5.385  1.00 60.65           C  
ATOM   3156  CA  GLN I 110      43.203  39.455  -5.905  1.00 80.29           C  
ATOM   3157  CA  SER I 111      44.636  40.295  -9.337  1.00 67.55           C  
ATOM   3158  CA  ASP I 112      45.118  36.595 -10.087  1.00 73.69           C  
ATOM   3159  CA  ILE I 113      48.693  37.003 -11.293  1.00 59.84           C  
ATOM   3160  CA  ALA I 114      51.426  34.502 -10.554  1.00 35.12           C  
ATOM   3161  CA  LEU I 115      55.070  34.335 -11.504  1.00102.75           C  
ATOM   3162  CA  LEU I 116      56.857  31.081 -12.166  1.00 57.51           C  
ATOM   3163  CA  GLN I 117      60.504  30.337 -12.716  1.00 46.49           C  
ATOM   3164  CA  ILE I 118      61.724  27.582 -14.928  1.00 65.59           C  
ATOM   3165  CA  GLN I 119      64.554  25.511 -13.617  1.00133.21           C  
ATOM   3166  CA  ASN I 120      67.519  25.373 -15.971  1.00 58.70           C  
ATOM   3167  CA  PRO I 121      65.687  27.350 -18.590  1.00105.12           C  
ATOM   3168  CA  SER I 122      68.088  26.999 -21.566  1.00195.10           C  
ATOM   3169  CA  LYS I 123      67.366  28.470 -25.003  1.00 74.43           C  
ATOM   3170  CA  LEU I 124      64.119  30.215 -24.298  1.00 86.69           C  
ATOM   3171  CA  THR I 125      62.325  32.881 -26.250  1.00 96.21           C  
ATOM   3172  CA  GLN I 126      60.809  35.849 -24.506  1.00 40.62           C  
ATOM   3173  CA  ILE I 127      57.772  37.912 -25.336  1.00 98.87           C  
ATOM   3174  CA  ALA I 128      57.917  41.666 -25.641  1.00 31.90           C  
ATOM   3175  CA  ILE I 129      55.449  43.608 -23.559  1.00 88.29           C  
ATOM   3176  CA  ALA I 130      53.288  46.338 -25.030  1.00 34.91           C  
ATOM   3177  CA  ASP I 131      51.764  49.277 -23.216  1.00 35.06           C  
ATOM   3178  CA  SER I 132      48.223  48.298 -22.293  1.00 42.38           C  
ATOM   3179  CA  ASP I 133      47.276  51.872 -21.653  1.00 32.54           C  
ATOM   3180  CA  LYS I 134      47.768  52.518 -25.347  1.00 47.04           C  
ATOM   3181  CA  LEU I 135      45.167  49.963 -26.350  1.00 58.61           C  
ATOM   3182  CA  ARG I 136      41.982  51.221 -27.899  1.00101.89           C  
ATOM   3183  CA  VAL I 137      38.874  49.339 -28.796  1.00 82.89           C  
ATOM   3184  CA  GLY I 138      39.133  47.955 -32.263  1.00 34.08           C  
ATOM   3185  CA  ASP I 139      42.741  46.959 -31.991  1.00 43.33           C  
ATOM   3186  CA  PHE I 140      43.454  43.496 -33.284  1.00 59.15           C  
ATOM   3187  CA  ALA I 141      44.404  40.813 -30.840  1.00 28.39           C  
ATOM   3188  CA  VAL I 142      45.546  37.228 -30.999  1.00 35.31           C  
ATOM   3189  CA  ALA I 143      45.159  34.815 -28.154  1.00 32.44           C  
ATOM   3190  CA  VAL I 144      47.501  31.940 -27.646  1.00104.78           C  
ATOM   3191  CA  GLY I 145      47.101  29.189 -25.108  1.00 24.87           C  
ATOM   3192  CA  ASN I 146      46.045  25.597 -24.764  1.00133.76           C  
ATOM   3193  CA  PRO I 147      42.357  25.203 -25.018  1.00 78.32           C  
ATOM   3194  CA  PHE I 148      41.148  21.817 -23.847  1.00 64.21           C  
ATOM   3195  CA  GLY I 149      44.798  20.911 -23.593  1.00 22.95           C  
ATOM   3196  CA  LEU I 150      44.898  20.412 -27.342  1.00 83.98           C  
ATOM   3197  CA  GLY I 151      48.239  22.111 -27.705  1.00 35.46           C  
ATOM   3198  CA  GLN I 152      49.287  25.593 -28.577  1.00113.53           C  
ATOM   3199  CA  THR I 153      46.414  27.191 -30.338  1.00112.66           C  
ATOM   3200  CA  ALA I 154      46.058  30.673 -31.716  1.00 31.91           C  
ATOM   3201  CA  THR I 155      42.803  32.546 -32.091  1.00 30.41           C  
ATOM   3202  CA  SER I 156      42.153  35.966 -33.524  1.00 30.53           C  
ATOM   3203  CA  GLY I 157      39.856  38.808 -32.592  1.00 26.82           C  
ATOM   3204  CA  ILE I 158      39.711  42.476 -31.681  1.00 59.80           C  
ATOM   3205  CA  VAL I 159      39.831  44.327 -28.408  1.00 39.93           C  
ATOM   3206  CA  SER I 160      36.169  44.601 -27.543  1.00 45.14           C  
ATOM   3207  CA  ALA I 161      36.490  46.753 -24.468  1.00 41.45           C  
ATOM   3208  CA  LEU I 162      38.832  47.877 -21.755  1.00 90.41           C  
ATOM   3209  CA  GLY I 163      38.576  48.916 -18.178  1.00 38.44           C  
ATOM   3210  CA  ARG I 164      35.880  46.465 -17.380  1.00 85.56           C  
ATOM   3211  CA  SER I 165      34.874  45.218 -13.983  1.00 87.97           C  
ATOM   3212  CA  GLY I 166      32.194  44.282 -11.602  1.00 36.28           C  
ATOM   3213  CA  LEU I 167      32.459  40.845 -13.136  1.00 48.98           C  
ATOM   3214  CA  ASN I 168      33.226  39.692  -9.616  1.00 63.98           C  
ATOM   3215  CA  LEU I 169      35.633  37.228 -11.098  1.00 50.46           C  
ATOM   3216  CA  GLU I 170      38.554  38.700  -9.204  1.00110.19           C  
ATOM   3217  CA  GLY I 171      39.211  41.017  -6.289  1.00 36.84           C  
ATOM   3218  CA  LEU I 172      40.876  43.534  -8.513  1.00122.33           C  
ATOM   3219  CA  GLU I 173      39.673  43.587 -11.995  1.00 79.78           C  
ATOM   3220  CA  ASN I 174      40.343  45.578 -15.090  1.00138.89           C  
ATOM   3221  CA  PHE I 175      39.860  43.191 -17.832  1.00 88.78           C  
ATOM   3222  CA  ILE I 176      40.569  43.859 -21.417  1.00 69.16           C  
ATOM   3223  CA  GLN I 177      37.690  42.256 -23.222  1.00 56.03           C  
ATOM   3224  CA  THR I 178      38.367  40.323 -26.373  1.00118.86           C  
ATOM   3225  CA  ASP I 179      36.350  38.539 -29.043  1.00 60.71           C  
ATOM   3226  CA  ALA I 180      39.158  36.075 -29.668  1.00 35.18           C  
ATOM   3227  CA  SER I 181      38.062  32.587 -28.836  1.00 39.02           C  
ATOM   3228  CA  ILE I 182      39.139  31.790 -25.334  1.00 95.48           C  
ATOM   3229  CA  ASN I 183      38.263  28.505 -23.734  1.00 46.57           C  
ATOM   3230  CA  ARG I 184      39.269  26.625 -20.670  1.00 78.40           C  
ATOM   3231  CA  GLY I 185      42.977  25.968 -20.707  1.00 22.62           C  
ATOM   3232  CA  ASN I 186      43.510  29.441 -22.103  1.00 57.27           C  
ATOM   3233  CA  ALA I 187      44.158  30.893 -18.684  1.00 97.26           C  
ATOM   3234  CA  GLY I 188      47.615  32.283 -18.191  1.00 23.87           C  
ATOM   3235  CA  GLY I 189      47.911  32.456 -21.947  1.00 23.70           C  
ATOM   3236  CA  ALA I 190      48.890  35.505 -23.887  1.00 45.81           C  
ATOM   3237  CA  LEU I 191      46.878  38.063 -25.765  1.00114.80           C  
ATOM   3238  CA  LEU I 192      49.074  39.621 -28.376  1.00 52.82           C  
ATOM   3239  CA  ASN I 193      48.889  42.563 -30.704  1.00 53.49           C  
ATOM   3240  CA  LEU I 194      49.827  42.418 -34.362  1.00 95.98           C  
ATOM   3241  CA  ASN I 195      53.382  43.135 -33.336  1.00 53.14           C  
ATOM   3242  CA  GLY I 196      53.327  39.998 -31.290  1.00 25.86           C  
ATOM   3243  CA  GLU I 197      53.734  42.072 -28.157  1.00 38.01           C  
ATOM   3244  CA  LEU I 198      51.887  41.064 -25.008  1.00 62.57           C  
ATOM   3245  CA  ILE I 199      48.731  43.091 -24.419  1.00 82.99           C  
ATOM   3246  CA  GLY I 200      47.478  41.025 -21.502  1.00 31.65           C  
ATOM   3247  CA  ILE I 201      47.071  37.599 -19.961  1.00 45.81           C  
ATOM   3248  CA  ASN I 202      43.818  35.755 -20.614  1.00 88.36           C  
ATOM   3249  CA  THR I 203      42.177  35.305 -17.236  1.00 85.16           C  
ATOM   3250  CA  ALA I 204      38.574  34.284 -17.815  1.00 52.83           C  
ATOM   3251  CA  ILE I 205      35.478  34.116 -19.964  1.00 60.38           C  
ATOM   3252  CA  LEU I 206      31.768  34.687 -19.670  1.00 53.35           C  
ATOM   3253  CA  ALA I 207      29.969  31.795 -21.225  1.00 41.56           C  
ATOM   3254  CA  PRO I 208      26.688  30.287 -20.360  1.00 65.23           C  
ATOM   3255  CA  GLY I 209      27.666  27.109 -22.176  1.00 30.68           C  
ATOM   3256  CA  GLY I 210      31.094  26.910 -20.667  1.00 24.85           C  
ATOM   3257  CA  GLY I 211      32.341  27.425 -24.185  1.00 24.23           C  
ATOM   3258  CA  SER I 212      33.597  30.618 -25.759  1.00 55.21           C  
ATOM   3259  CA  VAL I 213      30.768  33.089 -26.313  1.00 59.60           C  
ATOM   3260  CA  GLY I 214      33.168  35.608 -27.745  1.00 35.59           C  
ATOM   3261  CA  ILE I 215      33.414  37.435 -24.475  1.00 50.70           C  
ATOM   3262  CA  GLY I 216      36.813  36.914 -22.939  1.00 20.32           C  
ATOM   3263  CA  PHE I 217      38.723  38.896 -20.382  1.00 44.11           C  
ATOM   3264  CA  ALA I 218      42.415  39.399 -19.887  1.00 35.07           C  
ATOM   3265  CA  ILE I 219      44.506  41.232 -17.362  1.00 73.56           C  
ATOM   3266  CA  PRO I 220      46.301  44.009 -19.036  1.00 88.95           C  
ATOM   3267  CA  SER I 221      49.990  43.688 -19.813  1.00 42.25           C  
ATOM   3268  CA  ASN I 222      50.715  46.748 -17.815  1.00 62.53           C  
ATOM   3269  CA  MET I 223      48.943  44.826 -15.221  1.00101.01           C  
ATOM   3270  CA  ALA I 224      50.966  41.681 -15.373  1.00 50.17           C  
ATOM   3271  CA  ARG I 225      54.198  43.459 -16.086  1.00 87.65           C  
ATOM   3272  CA  THR I 226      54.620  45.544 -13.019  1.00 64.36           C  
ATOM   3273  CA  LEU I 227      52.826  42.987 -10.843  1.00143.25           C  
ATOM   3274  CA  ALA I 228      55.228  40.407 -12.137  1.00 53.20           C  
ATOM   3275  CA  GLN I 229      58.177  42.645 -11.729  1.00 82.52           C  
ATOM   3276  CA  GLN I 230      58.099  43.046  -8.016  1.00121.07           C  
ATOM   3277  CA  LEU I 231      57.377  39.373  -7.774  1.00 61.61           C  
ATOM   3278  CA  ILE I 232      60.948  39.099  -8.858  1.00 88.64           C  
ATOM   3279  CA  ASP I 233      61.824  42.604  -7.538  1.00168.34           C  
ATOM   3280  CA  PHE I 234      61.156  44.731  -5.593  1.00176.71           C  
ATOM   3281  CA  GLY I 235      58.947  42.211  -3.963  1.00 41.18           C  
ATOM   3282  CA  GLU I 236      57.838  44.450  -1.213  1.00102.65           C  
ATOM   3283  CA  ILE I 237      55.462  42.400   0.845  1.00 42.86           C  
ATOM   3284  CA  LYS I 238      53.029  45.223   0.732  1.00159.95           C  
ATOM   3285  CA  ARG I 239      50.771  45.857  -0.837  1.00225.46           C  
ATOM   3286  CA  GLY I 240      51.256  42.382  -2.230  1.00 51.31           C  
ATOM   3287  CA  LEU I 241      47.835  42.926  -3.645  1.00163.40           C  
ATOM   3288  CA  LEU I 242      45.164  43.872  -1.167  1.00160.86           C  
ATOM   3289  CA  GLY I 243      43.494  40.571  -0.580  1.00 57.77           C  
ATOM   3290  CA  ILE I 244      39.884  41.598  -1.079  1.00 74.99           C  
ATOM   3291  CA  LYS I 245      36.848  40.627  -3.106  1.00110.73           C  
ATOM   3292  CA  GLY I 246      34.559  43.092  -4.749  1.00 31.24           C  
ATOM   3293  CA  THR I 247      32.394  43.874  -7.709  1.00111.00           C  
ATOM   3294  CA  GLU I 248      30.632  46.737  -9.421  1.00 52.53           C  
ATOM   3295  CA  MET I 249      28.310  48.966  -7.510  1.00 58.13           C  
ATOM   3296  CA  SER I 250      25.345  46.962  -6.386  1.00 35.53           C  
ATOM   3297  CA  ALA I 251      21.874  47.987  -7.380  1.00 37.82           C  
ATOM   3298  CA  ASP I 252      20.537  47.863  -3.850  1.00 51.20           C  
ATOM   3299  CA  ILE I 253      23.334  49.713  -2.146  1.00169.74           C  
ATOM   3300  CA  ALA I 254      23.926  52.267  -4.809  1.00 59.12           C  
ATOM   3301  CA  LYS I 255      20.488  53.364  -5.606  1.00141.94           C  
ATOM   3302  CA  ALA I 256      18.982  53.347  -2.185  1.00 69.85           C  
ATOM   3303  CA  PHE I 257      21.345  55.017   0.179  1.00184.58           C  
ATOM   3304  CA  ASN I 258      23.026  56.800  -2.534  1.00188.58           C  
ATOM   3305  CA  LEU I 259      26.705  56.601  -2.330  1.00149.43           C  
ATOM   3306  CA  ASP I 260      28.593  59.804  -2.093  1.00 71.37           C  
ATOM   3307  CA  VAL I 261      30.828  58.570  -4.876  1.00137.90           C  
ATOM   3308  CA  GLN I 262      28.737  57.761  -7.873  1.00107.01           C  
ATOM   3309  CA  ARG I 263      30.365  54.395  -8.131  1.00227.33           C  
ATOM   3310  CA  GLY I 264      33.486  52.639  -7.118  1.00 26.45           C  
ATOM   3311  CA  ALA I 265      34.968  49.288  -6.481  1.00 44.93           C  
ATOM   3312  CA  PHE I 266      32.827  47.942  -3.773  1.00140.37           C  
ATOM   3313  CA  VAL I 267      34.170  45.399  -1.415  1.00137.23           C  
ATOM   3314  CA  SER I 268      31.906  42.647  -0.170  1.00 66.33           C  
ATOM   3315  CA  GLU I 269      34.562  40.896   1.812  1.00115.02           C  
ATOM   3316  CA  VAL I 270      37.607  41.117   4.016  1.00105.38           C  
ATOM   3317  CA  LEU I 271      40.408  38.602   3.641  1.00108.47           C  
ATOM   3318  CA  PRO I 272      41.815  37.193   6.781  1.00186.62           C  
ATOM   3319  CA  GLY I 273      45.548  37.908   7.151  1.00133.95           C  
ATOM   3320  CA  SER I 274      45.080  39.921   4.051  1.00130.37           C  
ATOM   3321  CA  GLY I 275      46.464  43.268   3.246  1.00 37.59           C  
ATOM   3322  CA  SER I 276      43.112  44.868   3.259  1.00 54.15           C  
ATOM   3323  CA  ALA I 277      42.604  43.366   6.645  1.00 64.18           C  
ATOM   3324  CA  LYS I 278      45.477  44.992   8.416  1.00182.34           C  
ATOM   3325  CA  ALA I 279      45.115  48.163   6.432  1.00 50.58           C  
ATOM   3326  CA  GLY I 280      41.797  48.171   8.077  1.00 44.07           C  
ATOM   3327  CA  VAL I 281      39.728  48.196   4.952  1.00 66.42           C  
ATOM   3328  CA  LYS I 282      36.748  46.158   5.569  1.00140.15           C  
ATOM   3329  CA  ALA I 283      33.604  45.201   3.861  1.00 96.75           C  
ATOM   3330  CA  GLY I 284      30.880  47.367   2.587  1.00 39.65           C  
ATOM   3331  CA  ASP I 285      33.832  49.424   1.481  1.00102.57           C  
ATOM   3332  CA  ILE I 286      33.610  51.575  -1.444  1.00 96.15           C  
ATOM   3333  CA  ILE I 287      36.970  52.191  -2.990  1.00 65.24           C  
ATOM   3334  CA  THR I 288      36.640  55.572  -4.588  1.00132.86           C  
ATOM   3335  CA  SER I 289      40.167  56.125  -5.661  1.00 99.37           C  
ATOM   3336  CA  LEU I 290      43.626  54.712  -5.747  1.00 89.06           C  
ATOM   3337  CA  ASN I 291      46.553  57.031  -5.302  1.00182.24           C  
ATOM   3338  CA  GLY I 292      46.352  60.768  -5.967  1.00 52.66           C  
ATOM   3339  CA  LYS I 293      44.470  60.457  -9.216  1.00 70.39           C  
ATOM   3340  CA  PRO I 294      40.897  59.448  -9.107  1.00137.20           C  
ATOM   3341  CA  LEU I 295      39.825  55.859  -9.507  1.00 95.97           C  
ATOM   3342  CA  ASN I 296      37.166  54.716 -11.878  1.00 73.52           C  
ATOM   3343  CA  SER I 297      34.996  51.697 -11.538  1.00 53.33           C  
ATOM   3344  CA  PHE I 298      36.017  48.396 -10.120  1.00 74.56           C  
ATOM   3345  CA  ALA I 299      37.376  47.921 -13.587  1.00 48.78           C  
ATOM   3346  CA  GLU I 300      39.878  50.689 -13.434  1.00102.67           C  
ATOM   3347  CA  LEU I 301      40.779  49.368 -10.047  1.00 73.46           C  
ATOM   3348  CA  ARG I 302      42.518  46.259 -11.143  1.00195.19           C  
ATOM   3349  CA  SER I 303      43.717  48.014 -14.196  1.00 58.53           C  
ATOM   3350  CA  ARG I 304      45.967  50.165 -12.191  1.00264.55           C  
ATOM   3351  CA  ILE I 305      46.646  47.719  -9.389  1.00 88.58           C  
ATOM   3352  CA  ALA I 306      47.008  44.726 -11.553  1.00 73.28           C  
ATOM   3353  CA  THR I 307      49.296  47.036 -13.391  1.00 62.28           C  
ATOM   3354  CA  THR I 308      51.232  48.012 -10.324  1.00143.32           C  
ATOM   3355  CA  GLU I 309      53.856  46.057  -8.531  1.00 93.40           C  
ATOM   3356  CA  PRO I 310      52.379  43.716  -6.100  1.00186.96           C  
ATOM   3357  CA  GLY I 311      54.005  44.973  -3.960  1.00125.21           C  
ATOM   3358  CA  THR I 312      54.104  48.710  -4.236  1.00 61.31           C  
ATOM   3359  CA  LYS I 313      52.930  50.554  -1.210  1.00 92.93           C  
ATOM   3360  CA  VAL I 314      49.856  52.489  -2.189  1.00 64.14           C  
ATOM   3361  CA  LYS I 315      47.143  54.510  -0.529  1.00194.36           C  
ATOM   3362  CA  LEU I 316      43.498  53.872  -1.107  1.00 93.23           C  
ATOM   3363  CA  GLY I 317      40.522  56.142  -0.858  1.00 46.96           C  
ATOM   3364  CA  LEU I 318      37.280  54.623   0.168  1.00135.02           C  
ATOM   3365  CA  LEU I 319      33.967  55.764   1.387  1.00183.21           C  
ATOM   3366  CA  ARG I 320      32.767  54.241   4.454  1.00256.03           C  
ATOM   3367  CA  ASN I 321      29.769  55.736   6.233  1.00189.25           C  
ATOM   3368  CA  GLY I 322      29.506  58.354   3.835  1.00 63.39           C  
ATOM   3369  CA  LYS I 323      32.694  59.478   5.286  1.00129.36           C  
ATOM   3370  CA  PRO I 324      36.116  59.643   3.931  1.00165.81           C  
ATOM   3371  CA  LEU I 325      39.493  58.162   4.828  1.00173.41           C  
ATOM   3372  CA  GLU I 326      42.836  57.544   3.420  1.00116.85           C  
ATOM   3373  CA  VAL I 327      44.583  54.361   4.309  1.00119.78           C  
ATOM   3374  CA  GLU I 328      47.831  52.820   3.211  1.00 88.09           C  
ATOM   3375  CA  VAL I 329      47.428  49.392   1.761  1.00113.76           C  
ATOM   3376  CA  SER I 340      48.734  25.972  29.056  1.00103.85           C  
ATOM   3377  CA  ALA I 341      48.117  22.256  28.621  1.00 79.11           C  
ATOM   3378  CA  GLU I 342      44.894  22.793  26.747  1.00 52.49           C  
ATOM   3379  CA  MET I 343      46.286  23.441  23.345  1.00 49.65           C  
ATOM   3380  CA  ILE I 344      48.566  20.483  23.320  1.00124.85           C  
ATOM   3381  CA  THR I 345      46.097  18.321  25.165  1.00166.01           C  
ATOM   3382  CA  PRO I 346      42.495  18.511  24.285  1.00168.29           C  
ATOM   3383  CA  ALA I 347      40.071  20.070  26.736  1.00 82.03           C  
ATOM   3384  CA  LEU I 348      42.380  19.306  29.632  1.00147.85           C  
ATOM   3385  CA  GLU I 349      42.772  22.618  31.319  1.00 91.40           C  
ATOM   3386  CA  GLY I 350      45.752  22.751  33.550  1.00 28.48           C  
ATOM   3387  CA  ALA I 351      49.256  23.976  34.024  1.00 39.63           C  
ATOM   3388  CA  THR I 352      50.768  26.035  31.279  1.00 51.31           C  
ATOM   3389  CA  LEU I 353      53.431  24.518  29.129  1.00 69.24           C  
ATOM   3390  CA  SER I 354      56.546  26.025  27.659  1.00 34.97           C  
ATOM   3391  CA  ASP I 355      58.908  24.592  25.103  1.00 40.36           C  
ATOM   3392  CA  GLY I 356      62.617  24.294  25.345  1.00 45.72           C  
ATOM   3393  CA  GLN I 357      64.477  23.127  28.392  1.00159.43           C  
ATOM   3394  CA  LEU I 358      64.393  26.774  28.523  1.00197.98           C  
ATOM   3395  CA  LYS I 359      67.042  26.910  31.214  1.00122.74           C  
ATOM   3396  CA  ASP I 360      69.196  24.068  29.870  1.00 54.56           C  
ATOM   3397  CA  GLY I 361      69.339  21.999  26.715  1.00 29.52           C  
ATOM   3398  CA  GLY I 362      65.828  20.950  25.843  1.00 39.11           C  
ATOM   3399  CA  LYS I 363      65.035  17.958  27.974  1.00127.15           C  
ATOM   3400  CA  GLY I 364      61.511  18.572  26.914  1.00 32.07           C  
ATOM   3401  CA  ILE I 365      58.493  20.760  27.444  1.00121.63           C  
ATOM   3402  CA  LYS I 366      58.126  22.320  30.830  1.00 52.36           C  
ATOM   3403  CA  ILE I 367      54.926  22.888  32.675  1.00 63.28           C  
ATOM   3404  CA  ASP I 368      55.020  26.392  34.029  1.00 55.23           C  
ATOM   3405  CA  GLU I 369      52.457  26.279  36.763  1.00 83.49           C  
ATOM   3406  CA  VAL I 370      49.634  24.106  37.935  1.00119.58           C  
ATOM   3407  CA  VAL I 371      46.107  25.512  37.971  1.00181.95           C  
ATOM   3408  CA  LYS I 372      45.470  22.499  40.276  1.00178.36           C  
ATOM   3409  CA  GLY I 373      41.701  22.787  40.337  1.00 35.88           C  
ATOM   3410  CA  SER I 374      42.061  21.993  36.620  1.00 46.26           C  
ATOM   3411  CA  PRO I 375      42.014  18.525  35.255  1.00 73.07           C  
ATOM   3412  CA  ALA I 376      45.587  18.702  34.048  1.00 43.09           C  
ATOM   3413  CA  ALA I 377      46.171  18.778  37.766  1.00 51.06           C  
ATOM   3414  CA  GLN I 378      43.887  15.838  38.430  1.00 53.83           C  
ATOM   3415  CA  ALA I 379      45.959  13.237  36.591  1.00 66.24           C  
ATOM   3416  CA  GLY I 380      49.283  13.973  38.213  1.00 63.06           C  
ATOM   3417  CA  LEU I 381      50.747  16.945  36.434  1.00 57.83           C  
ATOM   3418  CA  GLN I 382      52.508  19.193  38.896  1.00 62.81           C  
ATOM   3419  CA  LYS I 383      54.543  22.235  38.040  1.00139.39           C  
ATOM   3420  CA  ASP I 384      58.250  22.167  37.277  1.00 77.39           C  
ATOM   3421  CA  ASP I 385      57.902  18.830  35.584  1.00 45.16           C  
ATOM   3422  CA  VAL I 386      59.762  18.375  32.340  1.00 58.28           C  
ATOM   3423  CA  ILE I 387      58.235  16.073  29.823  1.00105.72           C  
ATOM   3424  CA  ILE I 388      61.176  14.269  28.310  1.00110.08           C  
ATOM   3425  CA  GLY I 389      59.064  12.390  25.802  1.00 46.89           C  
ATOM   3426  CA  VAL I 390      55.817  10.620  25.096  1.00 62.77           C  
ATOM   3427  CA  ASN I 391      55.114   7.044  24.134  1.00 83.12           C  
ATOM   3428  CA  ARG I 392      58.698   5.914  23.823  1.00160.88           C  
ATOM   3429  CA  ASP I 393      59.283   9.058  21.832  1.00 51.39           C  
ATOM   3430  CA  ARG I 394      61.575  11.790  22.976  1.00100.58           C  
ATOM   3431  CA  VAL I 395      59.995  15.198  23.137  1.00 43.81           C  
ATOM   3432  CA  ASN I 396      62.477  17.972  22.523  1.00 47.43           C  
ATOM   3433  CA  SER I 397      59.804  20.620  22.412  1.00 38.04           C  
ATOM   3434  CA  ILE I 398      56.092  21.196  22.036  1.00 41.74           C  
ATOM   3435  CA  ALA I 399      56.044  20.537  18.332  1.00 23.94           C  
ATOM   3436  CA  GLU I 400      57.480  17.079  18.755  1.00 38.31           C  
ATOM   3437  CA  MET I 401      55.121  16.344  21.603  1.00 40.61           C  
ATOM   3438  CA  ARG I 402      52.312  17.357  19.327  1.00153.63           C  
ATOM   3439  CA  LYS I 403      53.595  14.846  16.829  1.00 88.32           C  
ATOM   3440  CA  VAL I 404      53.139  11.907  19.148  1.00 32.02           C  
ATOM   3441  CA  LEU I 405      49.712  13.307  19.905  1.00 97.47           C  
ATOM   3442  CA  ALA I 406      49.111  13.397  16.181  1.00 30.99           C  
ATOM   3443  CA  ALA I 407      49.203   9.627  16.254  1.00 33.19           C  
ATOM   3444  CA  LYS I 408      46.403   9.963  18.770  1.00150.23           C  
ATOM   3445  CA  PRO I 409      47.280   6.784  20.572  1.00 69.80           C  
ATOM   3446  CA  ALA I 410      44.546   5.707  22.949  1.00 30.15           C  
ATOM   3447  CA  ILE I 411      47.351   5.342  25.456  1.00 79.14           C  
ATOM   3448  CA  ILE I 412      49.499   8.373  26.028  1.00 42.71           C  
ATOM   3449  CA  ALA I 413      52.394   8.021  28.352  1.00 54.26           C  
ATOM   3450  CA  LEU I 414      54.272  11.059  29.474  1.00121.33           C  
ATOM   3451  CA  GLN I 415      57.400  10.644  31.384  1.00129.62           C  
ATOM   3452  CA  ILE I 416      58.630  13.718  32.963  1.00122.22           C  
ATOM   3453  CA  VAL I 417      61.465  14.282  35.291  1.00 46.51           C  
ATOM   3454  CA  ARG I 418      60.540  15.737  38.609  1.00 97.74           C  
ATOM   3455  CA  GLY I 419      63.289  16.767  40.919  1.00 23.88           C  
ATOM   3456  CA  ASN I 420      66.024  14.317  40.390  1.00 97.48           C  
ATOM   3457  CA  GLU I 421      63.823  11.387  39.545  1.00100.42           C  
ATOM   3458  CA  SER I 422      61.866   9.904  36.711  1.00 46.47           C  
ATOM   3459  CA  ILE I 423      58.139  10.325  36.593  1.00101.92           C  
ATOM   3460  CA  TYR I 424      55.507   8.929  34.340  1.00169.15           C  
ATOM   3461  CA  LEU I 425      52.312  10.639  33.531  1.00126.88           C  
ATOM   3462  CA  LEU I 426      49.508   9.427  31.519  1.00212.12           C  
ATOM   3463  CA  MET I 427      46.183  10.060  29.899  1.00 66.92           C  
TER    3464      MET I 427                                                      
ATOM   3465  CA  PRO J  11     -37.084 -44.707 -46.638  1.00 84.96           C  
ATOM   3466  CA  LEU J  12     -35.195 -41.851 -48.214  1.00 89.44           C  
ATOM   3467  CA  PRO J  13     -36.951 -39.539 -50.528  1.00152.48           C  
ATOM   3468  CA  SER J  14     -34.155 -39.218 -51.094  1.00117.26           C  
ATOM   3469  CA  LEU J  15     -33.159 -35.578 -50.798  1.00153.19           C  
ATOM   3470  CA  ALA J  16     -30.324 -35.786 -53.247  1.00 44.36           C  
ATOM   3471  CA  PRO J  17     -32.447 -36.206 -56.284  1.00 68.84           C  
ATOM   3472  CA  MET J  18     -34.502 -33.141 -55.480  1.00 35.30           C  
ATOM   3473  CA  LEU J  19     -31.421 -31.224 -54.482  1.00 55.29           C  
ATOM   3474  CA  GLU J  20     -29.481 -31.908 -57.630  1.00 71.89           C  
ATOM   3475  CA  LYS J  21     -31.896 -29.991 -59.779  1.00 63.96           C  
ATOM   3476  CA  VAL J  22     -32.558 -27.160 -57.314  1.00105.85           C  
ATOM   3477  CA  LEU J  23     -29.113 -26.427 -55.911  1.00115.93           C  
ATOM   3478  CA  PRO J  24     -27.753 -24.451 -58.800  1.00133.12           C  
ATOM   3479  CA  ALA J  25     -30.525 -21.947 -58.166  1.00 29.67           C  
ATOM   3480  CA  VAL J  26     -29.090 -21.045 -54.790  1.00 36.03           C  
ATOM   3481  CA  VAL J  27     -26.134 -18.760 -54.935  1.00 96.62           C  
ATOM   3482  CA  SER J  28     -23.498 -17.252 -52.685  1.00 48.46           C  
ATOM   3483  CA  VAL J  29     -23.370 -13.500 -52.470  1.00 35.93           C  
ATOM   3484  CA  ARG J  30     -20.069 -11.783 -51.930  1.00 82.94           C  
ATOM   3485  CA  VAL J  31     -19.877  -8.204 -50.827  1.00 38.54           C  
ATOM   3486  CA  GLU J  32     -17.140  -5.678 -50.338  1.00 45.37           C  
ATOM   3487  CA  GLY J  33     -17.470  -2.202 -48.987  1.00 24.88           C  
ATOM   3488  CA  THR J  34     -16.676   0.368 -46.354  1.00111.25           C  
ATOM   3489  CA  ALA J  35     -13.661   2.710 -43.816  1.00 21.42           C  
ATOM   3490  CA  GLN J  59     -11.489  -0.347 -43.685  1.00 83.91           C  
ATOM   3491  CA  PRO J  60     -12.316  -2.772 -46.376  1.00 78.25           C  
ATOM   3492  CA  PHE J  61     -14.523  -5.630 -45.349  1.00 57.58           C  
ATOM   3493  CA  GLU J  62     -15.753  -8.688 -47.096  1.00 33.57           C  
ATOM   3494  CA  GLY J  63     -19.070 -10.189 -46.213  1.00 25.42           C  
ATOM   3495  CA  LEU J  64     -20.634 -13.391 -47.343  1.00 51.78           C  
ATOM   3496  CA  GLY J  65     -24.270 -14.248 -47.709  1.00 23.88           C  
ATOM   3497  CA  SER J  66     -26.510 -16.195 -50.009  1.00 76.21           C  
ATOM   3498  CA  GLY J  67     -29.233 -15.488 -52.495  1.00 16.39           C  
ATOM   3499  CA  VAL J  68     -31.681 -17.274 -54.723  1.00 34.49           C  
ATOM   3500  CA  ILE J  69     -32.106 -16.937 -58.454  1.00104.12           C  
ATOM   3501  CA  ILE J  70     -35.698 -15.915 -59.031  1.00 84.27           C  
ATOM   3502  CA  ASN J  71     -35.472 -15.591 -62.753  1.00 61.88           C  
ATOM   3503  CA  ALA J  72     -32.763 -17.111 -64.827  1.00 34.21           C  
ATOM   3504  CA  SER J  73     -33.301 -14.971 -67.856  1.00 36.86           C  
ATOM   3505  CA  LYS J  74     -33.079 -11.622 -66.179  1.00109.63           C  
ATOM   3506  CA  GLY J  75     -30.678 -12.851 -63.572  1.00 29.37           C  
ATOM   3507  CA  TYR J  76     -32.657 -11.542 -60.645  1.00 68.89           C  
ATOM   3508  CA  VAL J  77     -31.471 -12.824 -57.303  1.00 43.50           C  
ATOM   3509  CA  LEU J  78     -33.262 -12.317 -54.025  1.00 53.97           C  
ATOM   3510  CA  THR J  79     -31.281 -11.671 -50.900  1.00 49.76           C  
ATOM   3511  CA  ASN J  80     -31.589 -10.064 -47.530  1.00 60.78           C  
ATOM   3512  CA  ASN J  81     -31.174  -6.329 -47.402  1.00 47.49           C  
ATOM   3513  CA  HIS J  82     -28.732  -6.575 -44.557  1.00 54.28           C  
ATOM   3514  CA  VAL J  83     -26.374  -8.694 -46.562  1.00 44.42           C  
ATOM   3515  CA  ILE J  84     -26.332  -6.088 -49.343  1.00180.13           C  
ATOM   3516  CA  ASN J  85     -26.624  -2.930 -47.295  1.00 76.56           C  
ATOM   3517  CA  GLN J  86     -22.941  -2.040 -46.786  1.00 83.17           C  
ATOM   3518  CA  ALA J  87     -21.731  -3.419 -50.115  1.00 71.75           C  
ATOM   3519  CA  GLN J  88     -19.942  -1.130 -52.508  1.00 61.14           C  
ATOM   3520  CA  LYS J  89     -19.602  -4.002 -54.928  1.00 29.39           C  
ATOM   3521  CA  ILE J  90     -21.429  -7.275 -55.113  1.00 37.68           C  
ATOM   3522  CA  SER J  91     -20.477 -10.546 -56.715  1.00 29.25           C  
ATOM   3523  CA  ILE J  92     -22.480 -13.705 -57.218  1.00 96.52           C  
ATOM   3524  CA  GLN J  93     -20.958 -17.160 -57.213  1.00113.31           C  
ATOM   3525  CA  LEU J  94     -22.641 -20.236 -58.601  1.00 45.71           C  
ATOM   3526  CA  ASN J  95     -22.136 -23.668 -57.135  1.00 39.43           C  
ATOM   3527  CA  ASP J  96     -20.354 -24.552 -60.349  1.00 44.56           C  
ATOM   3528  CA  GLY J  97     -17.720 -21.972 -59.534  1.00 25.63           C  
ATOM   3529  CA  ARG J  98     -18.719 -19.399 -62.098  1.00102.70           C  
ATOM   3530  CA  GLU J  99     -18.910 -15.889 -60.749  1.00 41.75           C  
ATOM   3531  CA  PHE J 100     -20.731 -12.791 -61.870  1.00 49.73           C  
ATOM   3532  CA  ASP J 101     -21.087  -9.139 -60.957  1.00122.71           C  
ATOM   3533  CA  ALA J 102     -24.395  -7.928 -59.590  1.00 35.03           C  
ATOM   3534  CA  LYS J 103     -26.088  -4.598 -59.076  1.00 58.79           C  
ATOM   3535  CA  LEU J 104     -28.663  -3.808 -56.468  1.00 56.49           C  
ATOM   3536  CA  ILE J 105     -32.000  -3.346 -58.139  1.00 94.52           C  
ATOM   3537  CA  GLY J 106     -33.749  -2.263 -55.002  1.00 27.37           C  
ATOM   3538  CA  SER J 107     -34.500  -3.334 -51.493  1.00102.72           C  
ATOM   3539  CA  ASP J 108     -36.344  -2.336 -48.406  1.00 90.21           C  
ATOM   3540  CA  ASP J 109     -35.322  -2.154 -44.805  1.00100.02           C  
ATOM   3541  CA  GLN J 110     -38.494  -2.989 -42.994  1.00 99.44           C  
ATOM   3542  CA  SER J 111     -39.069  -6.441 -44.536  1.00 61.00           C  
ATOM   3543  CA  ASP J 112     -35.338  -6.862 -45.175  1.00 72.52           C  
ATOM   3544  CA  ILE J 113     -35.792  -7.969 -48.783  1.00 98.98           C  
ATOM   3545  CA  ALA J 114     -33.438  -6.915 -51.535  1.00 37.12           C  
ATOM   3546  CA  LEU J 115     -33.281  -7.709 -55.221  1.00114.36           C  
ATOM   3547  CA  LEU J 116     -30.037  -8.046 -57.157  1.00107.65           C  
ATOM   3548  CA  GLN J 117     -29.450  -8.417 -60.859  1.00 43.43           C  
ATOM   3549  CA  ILE J 118     -26.587 -10.403 -62.281  1.00 89.34           C  
ATOM   3550  CA  GLN J 119     -24.742  -8.798 -65.109  1.00137.86           C  
ATOM   3551  CA  ASN J 120     -24.760 -10.956 -68.238  1.00 65.07           C  
ATOM   3552  CA  PRO J 121     -26.292 -13.864 -66.414  1.00105.23           C  
ATOM   3553  CA  SER J 122     -25.899 -16.689 -68.987  1.00194.61           C  
ATOM   3554  CA  LYS J 123     -27.103 -20.248 -68.360  1.00 75.94           C  
ATOM   3555  CA  LEU J 124     -28.704 -19.835 -64.988  1.00 86.95           C  
ATOM   3556  CA  THR J 125     -31.193 -22.021 -63.200  1.00 96.03           C  
ATOM   3557  CA  GLN J 126     -34.131 -20.547 -61.376  1.00 44.17           C  
ATOM   3558  CA  ILE J 127     -35.974 -21.787 -58.358  1.00 98.94           C  
ATOM   3559  CA  ALA J 128     -39.718 -22.328 -58.350  1.00 32.73           C  
ATOM   3560  CA  ILE J 129     -41.680 -20.589 -55.678  1.00 56.29           C  
ATOM   3561  CA  ALA J 130     -44.220 -22.318 -53.490  1.00 38.31           C  
ATOM   3562  CA  ASP J 131     -47.209 -20.821 -51.742  1.00 33.68           C  
ATOM   3563  CA  SER J 132     -46.078 -19.972 -48.241  1.00 39.31           C  
ATOM   3564  CA  ASP J 133     -49.630 -19.626 -47.076  1.00 30.94           C  
ATOM   3565  CA  LYS J 134     -50.082 -23.347 -47.558  1.00 49.35           C  
ATOM   3566  CA  LEU J 135     -47.262 -24.263 -45.199  1.00 56.66           C  
ATOM   3567  CA  ARG J 136     -48.190 -25.971 -41.975  1.00173.44           C  
ATOM   3568  CA  VAL J 137     -46.069 -26.868 -39.005  1.00 83.13           C  
ATOM   3569  CA  GLY J 138     -44.396 -30.198 -39.438  1.00 21.72           C  
ATOM   3570  CA  ASP J 139     -43.667 -29.747 -43.098  1.00 27.28           C  
ATOM   3571  CA  PHE J 140     -40.130 -30.642 -44.034  1.00 52.14           C  
ATOM   3572  CA  ALA J 141     -37.749 -27.922 -45.044  1.00 27.70           C  
ATOM   3573  CA  VAL J 142     -34.236 -27.753 -46.372  1.00 33.37           C  
ATOM   3574  CA  ALA J 143     -32.053 -24.726 -46.014  1.00 27.73           C  
ATOM   3575  CA  VAL J 144     -29.344 -23.893 -48.469  1.00 33.40           C  
ATOM   3576  CA  GLY J 145     -26.808 -21.153 -48.101  1.00 22.59           C  
ATOM   3577  CA  ASN J 146     -23.207 -20.541 -47.227  1.00123.89           C  
ATOM   3578  CA  PRO J 147     -22.611 -20.910 -43.579  1.00 73.22           C  
ATOM   3579  CA  PHE J 148     -19.271 -19.526 -42.481  1.00 70.12           C  
ATOM   3580  CA  GLY J 149     -18.545 -19.056 -46.144  1.00 24.59           C  
ATOM   3581  CA  LEU J 150     -17.728 -22.717 -46.425  1.00 84.32           C  
ATOM   3582  CA  GLY J 151     -19.586 -23.067 -49.681  1.00 27.89           C  
ATOM   3583  CA  GLN J 152     -23.014 -24.257 -50.652  1.00 36.31           C  
ATOM   3584  CA  THR J 153     -24.369 -26.170 -47.709  1.00 32.29           C  
ATOM   3585  CA  ALA J 154     -27.690 -27.860 -47.266  1.00 32.85           C  
ATOM   3586  CA  THR J 155     -29.335 -28.517 -43.932  1.00116.32           C  
ATOM   3587  CA  SER J 156     -32.568 -30.235 -43.167  1.00 87.42           C  
ATOM   3588  CA  GLY J 157     -35.316 -29.630 -40.666  1.00 30.54           C  
ATOM   3589  CA  ILE J 158     -39.038 -29.057 -40.308  1.00 58.99           C  
ATOM   3590  CA  VAL J 159     -41.175 -25.958 -40.212  1.00 43.83           C  
ATOM   3591  CA  SER J 160     -41.326 -25.233 -36.511  1.00 44.16           C  
ATOM   3592  CA  ALA J 161     -43.768 -22.363 -36.625  1.00 37.99           C  
ATOM   3593  CA  LEU J 162     -45.255 -19.733 -38.869  1.00 90.57           C  
ATOM   3594  CA  GLY J 163     -46.548 -16.236 -38.548  1.00 29.11           C  
ATOM   3595  CA  ARG J 164     -44.121 -15.343 -35.884  1.00 66.45           C  
ATOM   3596  CA  SER J 165     -43.241 -11.861 -34.826  1.00 87.29           C  
ATOM   3597  CA  GLY J 166     -42.440  -9.504 -32.096  1.00 37.35           C  
ATOM   3598  CA  LEU J 167     -38.879 -10.694 -32.526  1.00 48.90           C  
ATOM   3599  CA  ASN J 168     -38.108  -7.057 -33.184  1.00 61.44           C  
ATOM   3600  CA  LEU J 169     -35.600  -8.226 -35.721  1.00 48.14           C  
ATOM   3601  CA  GLU J 170     -37.321  -6.350 -38.506  1.00 97.46           C  
ATOM   3602  CA  GLY J 171     -39.950  -3.674 -38.984  1.00 36.22           C  
ATOM   3603  CA  LEU J 172     -42.280  -6.084 -40.680  1.00123.48           C  
ATOM   3604  CA  GLU J 173     -41.977  -9.604 -39.585  1.00 78.86           C  
ATOM   3605  CA  ASN J 174     -43.724 -12.870 -40.292  1.00103.17           C  
ATOM   3606  CA  PHE J 175     -41.031 -15.341 -40.022  1.00 83.24           C  
ATOM   3607  CA  ILE J 176     -41.393 -18.958 -40.759  1.00153.27           C  
ATOM   3608  CA  GLN J 177     -39.491 -20.683 -38.029  1.00 60.63           C  
ATOM   3609  CA  THR J 178     -37.308 -23.618 -38.890  1.00119.91           C  
ATOM   3610  CA  ASP J 179     -35.183 -26.192 -37.075  1.00 63.40           C  
ATOM   3611  CA  ALA J 180     -32.827 -26.501 -40.020  1.00 37.61           C  
ATOM   3612  CA  SER J 181     -29.368 -25.414 -39.074  1.00 40.29           C  
ATOM   3613  CA  ILE J 182     -28.980 -21.816 -40.037  1.00 93.23           C  
ATOM   3614  CA  ASN J 183     -25.814 -19.961 -39.264  1.00 45.14           C  
ATOM   3615  CA  ARG J 184     -24.137 -16.768 -40.246  1.00 95.71           C  
ATOM   3616  CA  GLY J 185     -23.747 -16.674 -43.985  1.00 22.50           C  
ATOM   3617  CA  ASN J 186     -27.134 -18.308 -44.380  1.00 52.39           C  
ATOM   3618  CA  ALA J 187     -28.851 -14.978 -44.851  1.00 97.00           C  
ATOM   3619  CA  GLY J 188     -30.467 -14.506 -48.197  1.00 26.68           C  
ATOM   3620  CA  GLY J 189     -30.350 -18.250 -48.638  1.00 23.85           C  
ATOM   3621  CA  ALA J 190     -33.284 -20.390 -49.532  1.00 43.53           C  
ATOM   3622  CA  LEU J 191     -35.570 -22.553 -47.480  1.00113.99           C  
ATOM   3623  CA  LEU J 192     -36.997 -25.246 -49.661  1.00 59.28           C  
ATOM   3624  CA  ASN J 193     -39.821 -27.738 -49.598  1.00150.06           C  
ATOM   3625  CA  LEU J 194     -39.250 -31.372 -50.477  1.00 89.23           C  
ATOM   3626  CA  ASN J 195     -40.361 -30.324 -53.929  1.00 58.79           C  
ATOM   3627  CA  GLY J 196     -37.385 -28.019 -54.038  1.00 24.17           C  
ATOM   3628  CA  GLU J 197     -39.721 -25.065 -54.213  1.00102.90           C  
ATOM   3629  CA  LEU J 198     -38.877 -21.884 -52.332  1.00 66.14           C  
ATOM   3630  CA  ILE J 199     -40.768 -21.599 -49.055  1.00 80.99           C  
ATOM   3631  CA  GLY J 200     -38.883 -18.557 -47.800  1.00 31.79           C  
ATOM   3632  CA  ILE J 201     -35.598 -16.683 -47.499  1.00107.25           C  
ATOM   3633  CA  ASN J 202     -33.553 -17.327 -44.357  1.00 87.24           C  
ATOM   3634  CA  THR J 203     -33.322 -13.972 -42.615  1.00 85.29           C  
ATOM   3635  CA  ALA J 204     -32.097 -14.546 -39.083  1.00 53.04           C  
ATOM   3636  CA  ILE J 205     -31.559 -16.758 -36.086  1.00 59.80           C  
ATOM   3637  CA  LEU J 206     -31.951 -16.636 -32.349  1.00 54.65           C  
ATOM   3638  CA  ALA J 207     -28.785 -17.935 -30.806  1.00 41.46           C  
ATOM   3639  CA  PRO J 208     -27.126 -17.019 -27.610  1.00 66.55           C  
ATOM   3640  CA  GLY J 209     -23.856 -18.530 -28.790  1.00 30.15           C  
ATOM   3641  CA  GLY J 210     -24.005 -16.959 -32.184  1.00 24.47           C  
ATOM   3642  CA  GLY J 211     -24.275 -20.487 -33.493  1.00 26.23           C  
ATOM   3643  CA  SER J 212     -27.406 -22.262 -34.614  1.00103.23           C  
ATOM   3644  CA  VAL J 213     -29.643 -23.133 -31.695  1.00 61.88           C  
ATOM   3645  CA  GLY J 214     -32.157 -24.697 -34.020  1.00 41.42           C  
ATOM   3646  CA  ILE J 215     -34.310 -21.615 -34.032  1.00 51.05           C  
ATOM   3647  CA  GLY J 216     -34.138 -19.929 -37.390  1.00 19.93           C  
ATOM   3648  CA  PHE J 217     -36.451 -17.523 -39.117  1.00 44.59           C  
ATOM   3649  CA  ALA J 218     -37.160 -16.952 -42.760  1.00 34.06           C  
ATOM   3650  CA  ILE J 219     -39.321 -14.557 -44.668  1.00121.54           C  
ATOM   3651  CA  PRO J 220     -41.963 -16.427 -46.450  1.00103.66           C  
ATOM   3652  CA  SER J 221     -41.780 -17.021 -50.173  1.00 42.20           C  
ATOM   3653  CA  ASN J 222     -45.001 -15.250 -50.717  1.00 67.33           C  
ATOM   3654  CA  MET J 223     -43.177 -12.554 -48.943  1.00129.65           C  
ATOM   3655  CA  ALA J 224     -40.155 -12.359 -51.085  1.00 54.15           C  
ATOM   3656  CA  ARG J 225     -41.961 -13.087 -54.278  1.00114.35           C  
ATOM   3657  CA  THR J 226     -44.342 -10.228 -54.543  1.00 71.30           C  
ATOM   3658  CA  LEU J 227     -41.924  -7.901 -52.733  1.00118.99           C  
ATOM   3659  CA  ALA J 228     -39.291  -8.850 -55.240  1.00 50.81           C  
ATOM   3660  CA  GLN J 229     -41.691  -8.457 -58.089  1.00164.63           C  
ATOM   3661  CA  GLN J 230     -42.375  -4.810 -57.689  1.00168.85           C  
ATOM   3662  CA  LEU J 231     -38.665  -4.253 -57.236  1.00135.78           C  
ATOM   3663  CA  ILE J 232     -38.384  -5.214 -60.823  1.00 89.26           C  
ATOM   3664  CA  ASP J 233     -41.962  -4.122 -61.571  1.00171.33           C  
ATOM   3665  CA  PHE J 234     -44.151  -2.343 -60.827  1.00180.18           C  
ATOM   3666  CA  GLY J 235     -41.770  -0.635 -58.526  1.00 42.56           C  
ATOM   3667  CA  GLU J 236     -44.345   1.731 -57.243  1.00100.00           C  
ATOM   3668  CA  ILE J 237     -42.535   4.001 -54.876  1.00 39.82           C  
ATOM   3669  CA  LYS J 238     -45.141   3.384 -52.294  1.00202.01           C  
ATOM   3670  CA  ARG J 239     -45.612   1.669 -50.114  1.00219.59           C  
ATOM   3671  CA  GLY J 240     -42.026   0.687 -50.791  1.00 49.75           C  
ATOM   3672  CA  LEU J 241     -42.341  -0.901 -47.429  1.00184.45           C  
ATOM   3673  CA  LEU J 242     -43.523   1.327 -44.665  1.00 94.42           C  
ATOM   3674  CA  GLY J 243     -40.226   2.228 -43.058  1.00 51.70           C  
ATOM   3675  CA  ILE J 244     -41.061   1.504 -39.466  1.00189.96           C  
ATOM   3676  CA  LYS J 245     -39.874  -0.556 -36.524  1.00 87.59           C  
ATOM   3677  CA  GLY J 246     -42.108  -2.524 -34.265  1.00 32.91           C  
ATOM   3678  CA  THR J 247     -42.489  -5.599 -32.178  1.00111.70           C  
ATOM   3679  CA  GLU J 248     -45.043  -7.713 -30.377  1.00 44.60           C  
ATOM   3680  CA  MET J 249     -47.484  -6.183 -27.989  1.00 54.25           C  
ATOM   3681  CA  SER J 250     -45.514  -4.968 -25.030  1.00 33.52           C  
ATOM   3682  CA  ALA J 251     -46.260  -6.213 -21.569  1.00 35.88           C  
ATOM   3683  CA  ASP J 252     -46.479  -2.751 -20.085  1.00 48.94           C  
ATOM   3684  CA  ILE J 253     -48.634  -1.123 -22.698  1.00 57.21           C  
ATOM   3685  CA  ALA J 254     -50.872  -4.057 -23.429  1.00 55.41           C  
ATOM   3686  CA  LYS J 255     -51.865  -5.132 -20.019  1.00 96.70           C  
ATOM   3687  CA  ALA J 256     -52.096  -1.809 -18.322  1.00 69.74           C  
ATOM   3688  CA  PHE J 257     -53.999   0.505 -20.557  1.00188.26           C  
ATOM   3689  CA  ASN J 258     -55.582  -2.298 -22.295  1.00188.31           C  
ATOM   3690  CA  LEU J 259     -55.513  -1.981 -25.988  1.00151.39           C  
ATOM   3691  CA  ASP J 260     -58.810  -1.914 -27.717  1.00 82.59           C  
ATOM   3692  CA  VAL J 261     -57.433  -4.430 -30.172  1.00110.35           C  
ATOM   3693  CA  GLN J 262     -56.208  -7.421 -28.249  1.00 54.16           C  
ATOM   3694  CA  ARG J 263     -52.897  -7.155 -29.946  1.00130.61           C  
ATOM   3695  CA  GLY J 264     -51.310  -5.923 -33.069  1.00 22.76           C  
ATOM   3696  CA  ALA J 265     -48.086  -4.869 -34.583  1.00 40.71           C  
ATOM   3697  CA  PHE J 266     -46.963  -2.145 -32.339  1.00133.09           C  
ATOM   3698  CA  VAL J 267     -44.640   0.448 -33.601  1.00 74.85           C  
ATOM   3699  CA  SER J 268     -42.012   1.965 -31.373  1.00110.96           C  
ATOM   3700  CA  GLU J 269     -40.568   4.257 -33.978  1.00130.72           C  
ATOM   3701  CA  VAL J 270     -41.127   6.527 -36.920  1.00107.34           C  
ATOM   3702  CA  LEU J 271     -38.625   6.554 -39.712  1.00101.51           C  
ATOM   3703  CA  PRO J 272     -37.597   9.765 -41.253  1.00 70.90           C  
ATOM   3704  CA  GLY J 273     -38.690  10.465 -44.796  1.00 23.72           C  
ATOM   3705  CA  SER J 274     -40.184   7.072 -44.394  1.00 88.20           C  
ATOM   3706  CA  GLY J 275     -43.390   5.821 -45.745  1.00 34.87           C  
ATOM   3707  CA  SER J 276     -44.858   5.629 -42.344  1.00 51.44           C  
ATOM   3708  CA  ALA J 277     -43.713   9.136 -41.706  1.00 53.54           C  
ATOM   3709  CA  LYS J 278     -45.563  10.854 -44.492  1.00119.44           C  
ATOM   3710  CA  ALA J 279     -48.492   8.529 -44.137  1.00 42.22           C  
ATOM   3711  CA  GLY J 280     -48.622  10.018 -40.749  1.00 39.58           C  
ATOM   3712  CA  VAL J 281     -48.313   6.816 -38.835  1.00 64.61           C  
ATOM   3713  CA  LYS J 282     -46.285   7.470 -35.875  1.00123.03           C  
ATOM   3714  CA  ALA J 283     -45.022   5.774 -32.833  1.00 87.81           C  
ATOM   3715  CA  GLY J 284     -46.931   4.097 -30.118  1.00 39.47           C  
ATOM   3716  CA  ASP J 285     -48.997   2.922 -33.054  1.00100.13           C  
ATOM   3717  CA  ILE J 286     -50.962  -0.172 -32.925  1.00169.20           C  
ATOM   3718  CA  ILE J 287     -51.376  -1.613 -36.360  1.00 70.30           C  
ATOM   3719  CA  THR J 288     -54.597  -3.534 -36.045  1.00 62.07           C  
ATOM   3720  CA  SER J 289     -55.091  -4.496 -39.599  1.00 51.82           C  
ATOM   3721  CA  LEU J 290     -53.798  -4.287 -43.107  1.00 85.48           C  
ATOM   3722  CA  ASN J 291     -56.271  -4.129 -45.932  1.00258.76           C  
ATOM   3723  CA  GLY J 292     -59.939  -4.948 -45.632  1.00 61.08           C  
ATOM   3724  CA  LYS J 293     -59.075  -8.311 -44.132  1.00 89.53           C  
ATOM   3725  CA  PRO J 294     -58.047  -8.349 -40.529  1.00141.48           C  
ATOM   3726  CA  LEU J 295     -54.413  -8.373 -39.494  1.00126.44           C  
ATOM   3727  CA  ASN J 296     -53.185 -10.551 -36.720  1.00158.36           C  
ATOM   3728  CA  SER J 297     -49.995 -10.199 -34.775  1.00 53.88           C  
ATOM   3729  CA  PHE J 298     -46.893  -8.342 -35.759  1.00 74.93           C  
ATOM   3730  CA  ALA J 299     -46.072 -11.671 -37.234  1.00 47.39           C  
ATOM   3731  CA  GLU J 300     -48.880 -11.687 -39.694  1.00 92.51           C  
ATOM   3732  CA  LEU J 301     -47.928  -8.154 -40.489  1.00 72.93           C  
ATOM   3733  CA  ARG J 302     -44.771  -8.878 -42.327  1.00169.27           C  
ATOM   3734  CA  SER J 303     -46.262 -12.024 -43.624  1.00 57.19           C  
ATOM   3735  CA  ARG J 304     -48.659 -10.158 -45.736  1.00251.62           C  
ATOM   3736  CA  ILE J 305     -46.563  -7.079 -46.321  1.00127.36           C  
ATOM   3737  CA  ALA J 306     -43.417  -8.942 -46.898  1.00 71.90           C  
ATOM   3738  CA  THR J 307     -45.524 -10.936 -49.220  1.00164.46           C  
ATOM   3739  CA  THR J 308     -46.929  -7.903 -50.935  1.00 71.66           C  
ATOM   3740  CA  GLU J 309     -45.151  -5.843 -53.545  1.00103.77           C  
ATOM   3741  CA  PRO J 310     -43.076  -3.243 -51.996  1.00213.84           C  
ATOM   3742  CA  GLY J 311     -44.489  -1.174 -53.556  1.00130.14           C  
ATOM   3743  CA  THR J 312     -48.185  -1.679 -53.703  1.00 51.54           C  
ATOM   3744  CA  LYS J 313     -50.367   1.006 -52.283  1.00138.53           C  
ATOM   3745  CA  VAL J 314     -52.132  -0.305 -49.251  1.00 51.10           C  
ATOM   3746  CA  LYS J 315     -54.186   1.003 -46.363  1.00 66.46           C  
ATOM   3747  CA  LEU J 316     -53.362   0.349 -42.764  1.00101.45           C  
ATOM   3748  CA  GLY J 317     -55.596   0.243 -39.762  1.00 46.60           C  
ATOM   3749  CA  LEU J 318     -54.140   1.280 -36.508  1.00108.46           C  
ATOM   3750  CA  LEU J 319     -55.207   2.241 -33.122  1.00114.52           C  
ATOM   3751  CA  ARG J 320     -54.039   5.427 -31.840  1.00196.69           C  
ATOM   3752  CA  ASN J 321     -55.465   6.861 -28.613  1.00209.69           C  
ATOM   3753  CA  GLY J 322     -58.000   4.215 -28.501  1.00 50.33           C  
ATOM   3754  CA  LYS J 323     -59.402   5.588 -31.611  1.00135.43           C  
ATOM   3755  CA  PRO J 324     -59.496   4.436 -35.093  1.00161.91           C  
ATOM   3756  CA  LEU J 325     -58.186   5.667 -38.431  1.00173.57           C  
ATOM   3757  CA  GLU J 326     -57.509   4.486 -41.859  1.00123.79           C  
ATOM   3758  CA  VAL J 327     -54.441   5.745 -43.586  1.00118.48           C  
ATOM   3759  CA  GLU J 328     -52.915   4.957 -46.931  1.00 43.39           C  
ATOM   3760  CA  VAL J 329     -49.314   3.947 -46.826  1.00 55.80           C  
ATOM   3761  CA  SER J 340     -22.478  31.889 -51.166  1.00 60.44           C  
ATOM   3762  CA  ALA J 341     -18.772  31.433 -50.527  1.00 78.29           C  
ATOM   3763  CA  GLU J 342     -19.255  29.282 -47.475  1.00116.79           C  
ATOM   3764  CA  MET J 343     -19.977  25.979 -49.049  1.00 80.55           C  
ATOM   3765  CA  ILE J 344     -17.073  26.209 -51.400  1.00 99.72           C  
ATOM   3766  CA  THR J 345     -14.872  27.719 -48.775  1.00 68.18           C  
ATOM   3767  CA  PRO J 346     -15.051  26.653 -45.211  1.00158.59           C  
ATOM   3768  CA  ALA J 347     -16.689  28.818 -42.587  1.00 73.18           C  
ATOM   3769  CA  LEU J 348     -15.957  31.907 -44.636  1.00138.71           C  
ATOM   3770  CA  GLU J 349     -19.261  33.636 -44.906  1.00140.28           C  
ATOM   3771  CA  GLY J 350     -19.337  36.074 -47.715  1.00 28.70           C  
ATOM   3772  CA  ALA J 351     -20.514  36.899 -51.168  1.00 33.99           C  
ATOM   3773  CA  THR J 352     -22.503  34.258 -52.916  1.00102.15           C  
ATOM   3774  CA  LEU J 353     -20.998  32.397 -55.801  1.00 58.75           C  
ATOM   3775  CA  SER J 354     -22.392  31.194 -59.094  1.00 42.88           C  
ATOM   3776  CA  ASP J 355     -20.872  28.971 -61.750  1.00 44.12           C  
ATOM   3777  CA  GLY J 356     -20.540  29.569 -65.491  1.00 62.62           C  
ATOM   3778  CA  GLN J 357     -19.321  32.853 -66.819  1.00193.94           C  
ATOM   3779  CA  LEU J 358     -22.784  33.414 -66.511  1.00316.28           C  
ATOM   3780  CA  LYS J 359     -23.639  33.950 -70.024  1.00147.62           C  
ATOM   3781  CA  ASP J 360     -20.265  33.766 -71.609  1.00 48.34           C  
ATOM   3782  CA  GLY J 361     -17.809  30.981 -71.844  1.00 31.12           C  
ATOM   3783  CA  GLY J 362     -17.029  30.117 -68.302  1.00 39.35           C  
ATOM   3784  CA  LYS J 363     -14.129  32.281 -67.359  1.00127.58           C  
ATOM   3785  CA  GLY J 364     -14.800  30.990 -63.894  1.00 29.80           C  
ATOM   3786  CA  ILE J 365     -17.115  31.193 -60.946  1.00 85.53           C  
ATOM   3787  CA  LYS J 366     -18.713  34.523 -60.262  1.00 61.18           C  
ATOM   3788  CA  ILE J 367     -19.325  36.051 -56.902  1.00 62.61           C  
ATOM   3789  CA  ASP J 368     -22.793  37.507 -56.974  1.00 57.49           C  
ATOM   3790  CA  GLU J 369     -22.760  39.941 -54.129  1.00 84.44           C  
ATOM   3791  CA  VAL J 370     -20.623  40.829 -51.179  1.00118.18           C  
ATOM   3792  CA  VAL J 371     -22.098  40.544 -47.698  1.00181.22           C  
ATOM   3793  CA  LYS J 372     -19.094  42.762 -46.766  1.00147.35           C  
ATOM   3794  CA  GLY J 373     -19.486  42.470 -43.020  1.00 35.49           C  
ATOM   3795  CA  SER J 374     -18.669  38.804 -43.700  1.00 48.56           C  
ATOM   3796  CA  PRO J 375     -15.204  37.432 -43.735  1.00 78.40           C  
ATOM   3797  CA  ALA J 376     -15.298  36.585 -47.416  1.00 42.27           C  
ATOM   3798  CA  ALA J 377     -15.410  40.337 -47.660  1.00 48.31           C  
ATOM   3799  CA  GLN J 378     -12.498  40.856 -45.301  1.00 55.11           C  
ATOM   3800  CA  ALA J 379      -9.840  39.195 -47.454  1.00 58.61           C  
ATOM   3801  CA  GLY J 380     -10.539  41.071 -50.648  1.00 62.06           C  
ATOM   3802  CA  LEU J 381     -13.458  39.424 -52.329  1.00 60.80           C  
ATOM   3803  CA  GLN J 382     -15.669  42.047 -53.890  1.00 49.28           C  
ATOM   3804  CA  LYS J 383     -18.680  41.391 -56.038  1.00165.75           C  
ATOM   3805  CA  ASP J 384     -18.555  40.955 -59.803  1.00 87.93           C  
ATOM   3806  CA  ASP J 385     -15.212  39.275 -59.573  1.00 50.47           C  
ATOM   3807  CA  VAL J 386     -14.727  36.127 -61.528  1.00 65.32           C  
ATOM   3808  CA  ILE J 387     -12.329  33.523 -60.361  1.00177.78           C  
ATOM   3809  CA  ILE J 388     -10.498  32.287 -63.367  1.00122.21           C  
ATOM   3810  CA  GLY J 389      -8.724  29.593 -61.405  1.00 54.78           C  
ATOM   3811  CA  VAL J 390      -7.016  28.597 -58.199  1.00 66.82           C  
ATOM   3812  CA  ASN J 391      -3.436  27.616 -57.516  1.00 80.15           C  
ATOM   3813  CA  ARG J 392      -2.246  27.586 -61.073  1.00161.90           C  
ATOM   3814  CA  ASP J 393      -5.363  25.645 -61.890  1.00 55.05           C  
ATOM   3815  CA  ARG J 394      -8.050  26.955 -64.175  1.00151.13           C  
ATOM   3816  CA  VAL J 395     -11.482  27.062 -62.619  1.00 51.54           C  
ATOM   3817  CA  ASN J 396     -14.179  26.699 -65.224  1.00 50.04           C  
ATOM   3818  CA  SER J 397     -16.904  26.273 -62.663  1.00 44.09           C  
ATOM   3819  CA  ILE J 398     -17.606  25.590 -59.018  1.00 39.12           C  
ATOM   3820  CA  ALA J 399     -16.922  21.913 -59.289  1.00 26.71           C  
ATOM   3821  CA  GLU J 400     -13.436  22.471 -60.615  1.00 29.64           C  
ATOM   3822  CA  MET J 401     -12.711  25.059 -57.981  1.00 40.25           C  
ATOM   3823  CA  ARG J 402     -13.821  22.527 -55.447  1.00104.10           C  
ATOM   3824  CA  LYS J 403     -11.257  20.113 -56.774  1.00 95.32           C  
ATOM   3825  CA  VAL J 404      -8.381  22.463 -56.146  1.00100.31           C  
ATOM   3826  CA  LEU J 405      -9.789  22.907 -52.678  1.00104.03           C  
ATOM   3827  CA  ALA J 406      -9.924  19.153 -52.367  1.00 32.23           C  
ATOM   3828  CA  ALA J 407      -6.151  19.199 -52.345  1.00 30.23           C  
ATOM   3829  CA  LYS J 408      -6.577  21.622 -49.479  1.00102.57           C  
ATOM   3830  CA  PRO J 409      -3.304  23.346 -49.991  1.00 71.18           C  
ATOM   3831  CA  ALA J 410      -2.333  25.522 -47.057  1.00 32.51           C  
ATOM   3832  CA  ILE J 411      -1.856  28.225 -49.660  1.00144.29           C  
ATOM   3833  CA  ILE J 412      -4.854  28.978 -51.802  1.00 45.62           C  
ATOM   3834  CA  ALA J 413      -4.470  31.546 -54.478  1.00 49.40           C  
ATOM   3835  CA  LEU J 414      -7.464  32.848 -56.312  1.00119.33           C  
ATOM   3836  CA  GLN J 415      -7.016  35.013 -59.281  1.00149.32           C  
ATOM   3837  CA  ILE J 416     -10.083  36.760 -60.298  1.00107.28           C  
ATOM   3838  CA  VAL J 417     -10.605  39.241 -63.002  1.00 50.35           C  
ATOM   3839  CA  ARG J 418     -12.066  42.500 -61.864  1.00 70.80           C  
ATOM   3840  CA  GLY J 419     -13.054  44.979 -64.482  1.00 19.60           C  
ATOM   3841  CA  ASN J 420     -10.524  44.710 -67.212  1.00 56.37           C  
ATOM   3842  CA  GLU J 421      -7.772  43.716 -64.853  1.00 47.24           C  
ATOM   3843  CA  SER J 422      -6.198  40.696 -63.288  1.00 49.72           C  
ATOM   3844  CA  ILE J 423      -6.700  40.238 -59.598  1.00 74.44           C  
ATOM   3845  CA  TYR J 424      -5.318  37.824 -57.133  1.00163.68           C  
ATOM   3846  CA  LEU J 425      -7.011  36.791 -53.995  1.00 94.37           C  
ATOM   3847  CA  LEU J 426      -6.026  34.428 -51.326  1.00145.14           C  
ATOM   3848  CA  MET J 427      -6.645  32.470 -48.217  1.00 59.55           C  
TER    3849      MET J 427                                                      
ATOM   3850  CA  PRO K  11     -44.237 -43.721 -41.173  1.00102.75           C  
ATOM   3851  CA  LEU K  12     -41.392 -44.993 -39.046  1.00 86.79           C  
ATOM   3852  CA  PRO K  13     -38.937 -47.277 -40.658  1.00153.06           C  
ATOM   3853  CA  SER K  14     -38.695 -47.776 -37.811  1.00158.31           C  
ATOM   3854  CA  LEU K  15     -35.072 -47.245 -36.899  1.00 73.40           C  
ATOM   3855  CA  ALA K  16     -35.227 -49.536 -33.900  1.00 46.81           C  
ATOM   3856  CA  PRO K  17     -35.528 -52.708 -35.835  1.00 72.55           C  
ATOM   3857  CA  MET K  18     -32.434 -51.852 -37.830  1.00126.32           C  
ATOM   3858  CA  LEU K  19     -30.595 -50.705 -34.751  1.00 54.24           C  
ATOM   3859  CA  GLU K  20     -31.295 -53.810 -32.768  1.00 73.24           C  
ATOM   3860  CA  LYS K  21     -29.219 -55.981 -35.022  1.00 44.66           C  
ATOM   3861  CA  VAL K  22     -26.440 -53.479 -35.732  1.00109.50           C  
ATOM   3862  CA  LEU K  23     -25.791 -51.886 -32.360  1.00114.02           C  
ATOM   3863  CA  PRO K  24     -23.785 -54.667 -30.833  1.00 63.95           C  
ATOM   3864  CA  ALA K  25     -21.246 -54.105 -33.591  1.00 30.52           C  
ATOM   3865  CA  VAL K  26     -20.458 -50.638 -32.313  1.00 35.99           C  
ATOM   3866  CA  VAL K  27     -18.217 -50.579 -29.325  1.00 99.93           C  
ATOM   3867  CA  SER K  28     -16.796 -48.166 -26.799  1.00 49.22           C  
ATOM   3868  CA  VAL K  29     -13.061 -47.897 -26.559  1.00123.86           C  
ATOM   3869  CA  ARG K  30     -11.388 -47.067 -23.330  1.00151.19           C  
ATOM   3870  CA  VAL K  31      -7.829 -45.994 -23.146  1.00 52.31           C  
ATOM   3871  CA  GLU K  32      -5.311 -45.355 -20.432  1.00 38.72           C  
ATOM   3872  CA  GLY K  33      -1.860 -43.993 -20.875  1.00 27.30           C  
ATOM   3873  CA  THR K  34       0.841 -41.531 -20.032  1.00113.96           C  
ATOM   3874  CA  ALA K  35       3.366 -39.995 -16.471  1.00 27.32           C  
ATOM   3875  CA  GLN K  59       0.182 -39.538 -14.537  1.00107.99           C  
ATOM   3876  CA  PRO K  60      -2.580 -41.710 -15.664  1.00 81.35           C  
ATOM   3877  CA  PHE K  61      -5.193 -40.262 -17.960  1.00 58.18           C  
ATOM   3878  CA  GLU K  62      -8.288 -41.935 -19.253  1.00 24.90           C  
ATOM   3879  CA  GLY K  63      -9.910 -41.324 -22.573  1.00 20.70           C  
ATOM   3880  CA  LEU K  64     -13.097 -42.621 -24.078  1.00 57.29           C  
ATOM   3881  CA  GLY K  65     -13.914 -43.182 -27.704  1.00 27.39           C  
ATOM   3882  CA  SER K  66     -15.779 -45.622 -29.875  1.00 79.11           C  
ATOM   3883  CA  GLY K  67     -14.966 -48.196 -32.485  1.00 17.04           C  
ATOM   3884  CA  VAL K  68     -16.659 -50.583 -34.854  1.00 36.65           C  
ATOM   3885  CA  ILE K  69     -16.135 -54.293 -35.105  1.00107.96           C  
ATOM   3886  CA  ILE K  70     -15.097 -55.018 -38.656  1.00115.65           C  
ATOM   3887  CA  ASN K  71     -14.684 -58.724 -38.288  1.00 60.36           C  
ATOM   3888  CA  ALA K  72     -16.195 -60.708 -35.498  1.00 31.50           C  
ATOM   3889  CA  SER K  73     -13.997 -63.719 -35.880  1.00 33.85           C  
ATOM   3890  CA  LYS K  74     -10.710 -61.901 -35.777  1.00 88.80           C  
ATOM   3891  CA  GLY K  75     -12.006 -59.270 -33.430  1.00 30.54           C  
ATOM   3892  CA  TYR K  76     -10.769 -56.376 -35.505  1.00 69.98           C  
ATOM   3893  CA  VAL K  77     -12.153 -53.049 -34.483  1.00123.27           C  
ATOM   3894  CA  LEU K  78     -11.690 -49.829 -36.403  1.00 55.36           C  
ATOM   3895  CA  THR K  79     -11.177 -46.592 -34.558  1.00 48.25           C  
ATOM   3896  CA  ASN K  80      -9.645 -43.198 -34.983  1.00 58.44           C  
ATOM   3897  CA  ASN K  81      -5.939 -42.970 -34.472  1.00 50.04           C  
ATOM   3898  CA  HIS K  82      -6.288 -40.009 -32.181  1.00 55.88           C  
ATOM   3899  CA  VAL K  83      -8.388 -41.993 -29.798  1.00 44.17           C  
ATOM   3900  CA  ILE K  84      -5.686 -44.677 -29.610  1.00181.90           C  
ATOM   3901  CA  ASN K  85      -2.540 -42.616 -29.952  1.00 78.80           C  
ATOM   3902  CA  GLN K  86      -1.646 -41.978 -26.282  1.00 72.42           C  
ATOM   3903  CA  ALA K  87      -3.016 -45.286 -25.005  1.00 67.45           C  
ATOM   3904  CA  GLN K  88      -0.711 -47.593 -23.124  1.00 55.42           C  
ATOM   3905  CA  LYS K  89      -3.563 -50.013 -22.672  1.00 30.77           C  
ATOM   3906  CA  ILE K  90      -6.821 -50.289 -24.504  1.00 39.58           C  
ATOM   3907  CA  SER K  91     -10.042 -51.944 -23.515  1.00 78.65           C  
ATOM   3908  CA  ILE K  92     -13.184 -52.489 -25.493  1.00 72.86           C  
ATOM   3909  CA  GLN K  93     -16.643 -52.655 -24.015  1.00191.31           C  
ATOM   3910  CA  LEU K  94     -19.658 -54.114 -25.696  1.00 55.89           C  
ATOM   3911  CA  ASN K  95     -23.116 -52.679 -25.261  1.00 32.92           C  
ATOM   3912  CA  ASP K  96     -23.969 -55.821 -23.358  1.00 52.33           C  
ATOM   3913  CA  GLY K  97     -21.406 -54.885 -20.756  1.00 29.56           C  
ATOM   3914  CA  ARG K  98     -18.786 -57.451 -21.563  1.00145.46           C  
ATOM   3915  CA  GLU K  99     -15.340 -56.008 -21.886  1.00102.50           C  
ATOM   3916  CA  PHE K 100     -12.135 -57.157 -23.483  1.00 49.07           C  
ATOM   3917  CA  ASP K 101      -8.576 -56.010 -23.893  1.00 30.16           C  
ATOM   3918  CA  ALA K 102      -7.285 -54.938 -27.257  1.00 32.06           C  
ATOM   3919  CA  LYS K 103      -3.954 -54.424 -28.951  1.00 87.89           C  
ATOM   3920  CA  LEU K 104      -3.176 -51.864 -31.587  1.00122.89           C  
ATOM   3921  CA  ILE K 105      -2.693 -53.668 -34.863  1.00137.28           C  
ATOM   3922  CA  GLY K 106      -1.620 -50.560 -36.691  1.00 30.57           C  
ATOM   3923  CA  SER K 107      -2.766 -47.101 -37.589  1.00105.65           C  
ATOM   3924  CA  ASP K 108      -1.793 -44.036 -39.486  1.00104.37           C  
ATOM   3925  CA  ASP K 109      -1.743 -40.357 -38.672  1.00 58.31           C  
ATOM   3926  CA  GLN K 110      -2.614 -38.725 -41.928  1.00155.16           C  
ATOM   3927  CA  SER K 111      -5.993 -40.385 -42.500  1.00 72.36           C  
ATOM   3928  CA  ASP K 112      -6.457 -40.902 -38.758  1.00 75.16           C  
ATOM   3929  CA  ILE K 113      -7.462 -44.558 -39.055  1.00 99.67           C  
ATOM   3930  CA  ALA K 114      -6.362 -47.194 -36.590  1.00 35.14           C  
ATOM   3931  CA  LEU K 115      -7.007 -50.911 -36.307  1.00 85.41           C  
ATOM   3932  CA  LEU K 116      -7.410 -52.717 -33.018  1.00 62.65           C  
ATOM   3933  CA  GLN K 117      -7.707 -56.388 -32.270  1.00 40.64           C  
ATOM   3934  CA  ILE K 118      -9.674 -57.758 -29.368  1.00 87.96           C  
ATOM   3935  CA  GLN K 119      -8.041 -60.529 -27.459  1.00 93.62           C  
ATOM   3936  CA  ASN K 120     -10.209 -63.600 -27.045  1.00 56.80           C  
ATOM   3937  CA  PRO K 121     -13.009 -61.952 -28.931  1.00107.47           C  
ATOM   3938  CA  SER K 122     -15.785 -64.583 -28.505  1.00247.22           C  
ATOM   3939  CA  LYS K 123     -19.358 -64.073 -29.703  1.00 75.93           C  
ATOM   3940  CA  LEU K 124     -18.977 -60.773 -31.448  1.00 89.45           C  
ATOM   3941  CA  THR K 125     -21.186 -59.134 -34.008  1.00 95.69           C  
ATOM   3942  CA  GLN K 126     -19.728 -57.476 -37.061  1.00 44.22           C  
ATOM   3943  CA  ILE K 127     -21.011 -54.540 -39.025  1.00100.64           C  
ATOM   3944  CA  ALA K 128     -21.486 -54.670 -42.773  1.00 33.18           C  
ATOM   3945  CA  ILE K 129     -19.679 -52.130 -44.887  1.00 98.03           C  
ATOM   3946  CA  ALA K 130     -21.517 -50.029 -47.432  1.00 36.59           C  
ATOM   3947  CA  ASP K 131     -20.131 -48.383 -50.532  1.00 54.04           C  
ATOM   3948  CA  SER K 132     -19.217 -44.844 -49.555  1.00 45.13           C  
ATOM   3949  CA  ASP K 133     -18.950 -43.652 -53.084  1.00146.13           C  
ATOM   3950  CA  LYS K 134     -22.601 -44.403 -53.692  1.00127.83           C  
ATOM   3951  CA  LEU K 135     -23.716 -41.989 -50.980  1.00 57.61           C  
ATOM   3952  CA  ARG K 136     -25.414 -38.789 -52.051  1.00119.37           C  
ATOM   3953  CA  VAL K 137     -26.471 -35.783 -50.075  1.00 82.65           C  
ATOM   3954  CA  GLY K 138     -29.826 -36.251 -48.460  1.00 22.13           C  
ATOM   3955  CA  ASP K 139     -29.260 -39.855 -47.553  1.00 32.54           C  
ATOM   3956  CA  PHE K 140     -30.179 -40.717 -44.002  1.00 52.25           C  
ATOM   3957  CA  ALA K 141     -27.467 -41.495 -41.522  1.00 34.39           C  
ATOM   3958  CA  VAL K 142     -27.319 -42.667 -37.948  1.00 44.06           C  
ATOM   3959  CA  ALA K 143     -24.349 -42.120 -35.734  1.00 31.78           C  
ATOM   3960  CA  VAL K 144     -23.479 -44.423 -32.901  1.00 36.90           C  
ATOM   3961  CA  GLY K 145     -20.779 -43.858 -30.348  1.00 28.30           C  
ATOM   3962  CA  ASN K 146     -20.280 -42.802 -26.780  1.00140.56           C  
ATOM   3963  CA  PRO K 147     -20.683 -39.116 -26.364  1.00 90.79           C  
ATOM   3964  CA  PHE K 148     -19.273 -37.833 -23.107  1.00 97.63           C  
ATOM   3965  CA  GLY K 149     -18.825 -41.447 -22.153  1.00 33.56           C  
ATOM   3966  CA  LEU K 150     -22.524 -41.663 -21.536  1.00 65.25           C  
ATOM   3967  CA  GLY K 151     -22.764 -45.081 -23.106  1.00 44.89           C  
ATOM   3968  CA  GLN K 152     -23.846 -46.277 -26.500  1.00 45.97           C  
ATOM   3969  CA  THR K 153     -25.870 -43.509 -27.991  1.00113.63           C  
ATOM   3970  CA  ALA K 154     -27.541 -43.266 -31.359  1.00 32.49           C  
ATOM   3971  CA  THR K 155     -28.242 -40.030 -33.167  1.00 33.63           C  
ATOM   3972  CA  SER K 156     -29.954 -39.465 -36.462  1.00 34.24           C  
ATOM   3973  CA  GLY K 157     -29.385 -37.077 -39.323  1.00 21.87           C  
ATOM   3974  CA  ILE K 158     -28.749 -36.889 -43.045  1.00 90.78           C  
ATOM   3975  CA  VAL K 159     -25.624 -36.761 -45.142  1.00 39.28           C  
ATOM   3976  CA  SER K 160     -25.005 -33.054 -45.422  1.00 45.82           C  
ATOM   3977  CA  ALA K 161     -22.100 -33.186 -47.826  1.00 46.96           C  
ATOM   3978  CA  LEU K 162     -19.332 -35.387 -49.098  1.00 74.07           C  
ATOM   3979  CA  GLY K 163     -15.824 -35.008 -50.365  1.00 29.44           C  
ATOM   3980  CA  ARG K 164     -15.011 -32.259 -47.973  1.00155.45           C  
ATOM   3981  CA  SER K 165     -11.586 -31.141 -47.097  1.00121.78           C  
ATOM   3982  CA  GLY K 166      -9.352 -28.225 -46.427  1.00 36.38           C  
ATOM   3983  CA  LEU K 167     -10.584 -28.509 -42.864  1.00 54.92           C  
ATOM   3984  CA  ASN K 168      -6.944 -29.064 -41.997  1.00 65.12           C  
ATOM   3985  CA  LEU K 169      -8.074 -31.511 -39.381  1.00 51.19           C  
ATOM   3986  CA  GLU K 170      -6.075 -34.307 -40.973  1.00113.40           C  
ATOM   3987  CA  GLY K 171      -3.337 -34.806 -43.533  1.00 37.40           C  
ATOM   3988  CA  LEU K 172      -5.698 -36.604 -45.820  1.00139.38           C  
ATOM   3989  CA  GLU K 173      -9.261 -35.652 -45.613  1.00 96.88           C  
ATOM   3990  CA  ASN K 174     -12.450 -36.540 -47.413  1.00 99.18           C  
ATOM   3991  CA  PHE K 175     -14.991 -36.242 -44.785  1.00 82.37           C  
ATOM   3992  CA  ILE K 176     -18.581 -37.131 -45.165  1.00 71.78           C  
ATOM   3993  CA  GLN K 177     -20.429 -34.352 -43.425  1.00 57.59           C  
ATOM   3994  CA  THR K 178     -23.412 -35.186 -41.299  1.00111.97           C  
ATOM   3995  CA  ASP K 179     -26.026 -33.348 -39.255  1.00 60.41           C  
ATOM   3996  CA  ALA K 180     -26.312 -36.220 -36.806  1.00 39.75           C  
ATOM   3997  CA  SER K 181     -25.318 -35.100 -33.371  1.00 88.36           C  
ATOM   3998  CA  ILE K 182     -21.681 -35.929 -32.876  1.00102.22           C  
ATOM   3999  CA  ASN K 183     -19.868 -35.036 -29.716  1.00 87.84           C  
ATOM   4000  CA  ARG K 184     -16.663 -35.711 -27.860  1.00367.21           C  
ATOM   4001  CA  GLY K 185     -16.883 -39.494 -27.266  1.00179.80           C  
ATOM   4002  CA  ASN K 186     -18.085 -40.109 -30.816  1.00 88.70           C  
ATOM   4003  CA  ALA K 187     -14.673 -40.524 -32.431  1.00 54.59           C  
ATOM   4004  CA  GLY K 188     -14.091 -43.946 -33.891  1.00 30.75           C  
ATOM   4005  CA  GLY K 189     -17.824 -44.488 -33.811  1.00 25.20           C  
ATOM   4006  CA  ALA K 190     -19.887 -45.566 -36.736  1.00 48.27           C  
ATOM   4007  CA  LEU K 191     -22.075 -43.679 -39.138  1.00 96.68           C  
ATOM   4008  CA  LEU K 192     -24.658 -46.009 -40.523  1.00 64.62           C  
ATOM   4009  CA  ASN K 193     -27.151 -45.931 -43.341  1.00 72.86           C  
ATOM   4010  CA  LEU K 194     -30.806 -46.953 -43.012  1.00130.94           C  
ATOM   4011  CA  ASN K 195     -29.508 -50.371 -43.554  1.00215.64           C  
ATOM   4012  CA  GLY K 196     -27.210 -51.211 -40.757  1.00211.21           C  
ATOM   4013  CA  GLU K 197     -24.272 -50.654 -43.065  1.00 80.39           C  
ATOM   4014  CA  LEU K 198     -21.212 -48.614 -42.195  1.00 66.78           C  
ATOM   4015  CA  ILE K 199     -20.975 -45.429 -44.243  1.00 83.02           C  
ATOM   4016  CA  GLY K 200     -17.996 -44.024 -42.380  1.00 32.90           C  
ATOM   4017  CA  ILE K 201     -16.241 -43.519 -39.070  1.00 53.33           C  
ATOM   4018  CA  ASN K 202     -16.997 -40.328 -37.153  1.00 84.04           C  
ATOM   4019  CA  THR K 203     -13.700 -38.466 -36.967  1.00 88.26           C  
ATOM   4020  CA  ALA K 204     -14.401 -34.900 -35.914  1.00 64.98           C  
ATOM   4021  CA  ILE K 205     -16.715 -31.961 -35.559  1.00117.09           C  
ATOM   4022  CA  LEU K 206     -16.659 -28.256 -36.124  1.00 67.15           C  
ATOM   4023  CA  ALA K 207     -18.116 -26.520 -33.152  1.00 72.33           C  
ATOM   4024  CA  PRO K 208     -17.323 -23.235 -31.539  1.00214.17           C  
ATOM   4025  CA  GLY K 209     -18.993 -24.384 -28.370  1.00243.19           C  
ATOM   4026  CA  GLY K 210     -17.221 -27.713 -27.885  1.00144.80           C  
ATOM   4027  CA  GLY K 211     -20.687 -29.263 -28.348  1.00 64.94           C  
ATOM   4028  CA  SER K 212     -22.307 -30.476 -31.558  1.00 67.86           C  
ATOM   4029  CA  VAL K 213     -23.316 -27.697 -33.940  1.00148.61           C  
ATOM   4030  CA  GLY K 214     -24.748 -30.161 -36.380  1.00 43.22           C  
ATOM   4031  CA  ILE K 215     -21.599 -30.161 -38.459  1.00101.06           C  
ATOM   4032  CA  GLY K 216     -19.801 -33.456 -38.113  1.00 21.65           C  
ATOM   4033  CA  PHE K 217     -17.289 -35.219 -40.297  1.00 44.70           C  
ATOM   4034  CA  ALA K 218     -16.581 -38.879 -40.831  1.00 36.25           C  
ATOM   4035  CA  ILE K 219     -14.080 -40.808 -42.868  1.00118.47           C  
ATOM   4036  CA  PRO K 220     -15.837 -42.736 -45.507  1.00 85.23           C  
ATOM   4037  CA  SER K 221     -16.335 -46.465 -45.141  1.00 42.50           C  
ATOM   4038  CA  ASN K 222     -14.509 -47.118 -48.324  1.00 66.24           C  
ATOM   4039  CA  MET K 223     -11.911 -45.166 -46.592  1.00100.57           C  
ATOM   4040  CA  ALA K 224     -11.679 -47.142 -43.427  1.00 49.44           C  
ATOM   4041  CA  ARG K 225     -12.276 -50.447 -45.088  1.00119.57           C  
ATOM   4042  CA  THR K 226      -9.354 -50.711 -47.382  1.00 64.07           C  
ATOM   4043  CA  LEU K 227      -7.114 -48.750 -45.010  1.00117.19           C  
ATOM   4044  CA  ALA K 228      -8.068 -51.185 -42.308  1.00 46.85           C  
ATOM   4045  CA  GLN K 229      -7.556 -54.043 -44.678  1.00149.17           C  
ATOM   4046  CA  GLN K 230      -3.877 -53.773 -45.169  1.00121.93           C  
ATOM   4047  CA  LEU K 231      -3.455 -52.982 -41.528  1.00 63.02           C  
ATOM   4048  CA  ILE K 232      -4.305 -56.599 -41.158  1.00 92.65           C  
ATOM   4049  CA  ASP K 233      -3.064 -57.411 -44.689  1.00164.10           C  
ATOM   4050  CA  PHE K 234      -1.251 -56.669 -46.889  1.00219.47           C  
ATOM   4051  CA  GLY K 235       0.302 -54.268 -44.515  1.00 43.66           C  
ATOM   4052  CA  GLU K 236       2.735 -53.009 -47.047  1.00 93.85           C  
ATOM   4053  CA  ILE K 237       4.809 -50.459 -45.242  1.00 76.66           C  
ATOM   4054  CA  LYS K 238       4.231 -48.062 -48.063  1.00219.23           C  
ATOM   4055  CA  ARG K 239       2.443 -45.996 -48.592  1.00198.07           C  
ATOM   4056  CA  GLY K 240       1.373 -46.534 -45.007  1.00 51.32           C  
ATOM   4057  CA  LEU K 241      -0.281 -43.233 -45.476  1.00165.73           C  
ATOM   4058  CA  LEU K 242       1.931 -40.494 -46.725  1.00 96.70           C  
ATOM   4059  CA  GLY K 243       2.694 -38.664 -43.505  1.00 47.85           C  
ATOM   4060  CA  ILE K 244       1.784 -35.158 -44.609  1.00 85.55           C  
ATOM   4061  CA  LYS K 245      -0.335 -32.272 -43.491  1.00115.69           C  
ATOM   4062  CA  GLY K 246      -2.273 -30.086 -45.825  1.00 30.68           C  
ATOM   4063  CA  THR K 247      -5.423 -28.142 -46.390  1.00110.97           C  
ATOM   4064  CA  GLU K 248      -7.504 -26.564 -49.113  1.00 54.26           C  
ATOM   4065  CA  MET K 249      -5.953 -24.229 -51.592  1.00 52.89           C  
ATOM   4066  CA  SER K 250      -4.965 -21.152 -49.718  1.00 82.43           C  
ATOM   4067  CA  ALA K 251      -6.231 -17.804 -50.845  1.00 36.27           C  
ATOM   4068  CA  ASP K 252      -2.779 -16.290 -50.853  1.00 57.58           C  
ATOM   4069  CA  ILE K 253      -0.951 -18.835 -52.957  1.00 62.60           C  
ATOM   4070  CA  ALA K 254      -3.828 -19.773 -55.196  1.00 55.40           C  
ATOM   4071  CA  LYS K 255      -4.968 -16.403 -56.244  1.00111.22           C  
ATOM   4072  CA  ALA K 256      -1.671 -14.690 -56.630  1.00 70.71           C  
ATOM   4073  CA  PHE K 257       0.671 -16.963 -58.454  1.00181.58           C  
ATOM   4074  CA  ASN K 258      -2.072 -18.813 -60.015  1.00184.32           C  
ATOM   4075  CA  LEU K 259      -1.621 -22.460 -59.601  1.00175.96           C  
ATOM   4076  CA  ASP K 260      -1.504 -24.416 -62.809  1.00 62.28           C  
ATOM   4077  CA  VAL K 261      -4.076 -26.808 -61.445  1.00110.92           C  
ATOM   4078  CA  GLN K 262      -7.066 -24.857 -60.286  1.00100.97           C  
ATOM   4079  CA  ARG K 263      -6.847 -26.436 -56.913  1.00126.67           C  
ATOM   4080  CA  GLY K 264      -5.520 -29.436 -55.164  1.00 23.50           C  
ATOM   4081  CA  ALA K 265      -4.495 -30.784 -51.858  1.00 43.52           C  
ATOM   4082  CA  PHE K 266      -1.818 -28.453 -50.804  1.00127.32           C  
ATOM   4083  CA  VAL K 267       0.777 -29.522 -48.368  1.00 69.05           C  
ATOM   4084  CA  SER K 268       2.145 -27.095 -45.834  1.00108.25           C  
ATOM   4085  CA  GLU K 269       4.453 -29.576 -44.214  1.00111.15           C  
ATOM   4086  CA  VAL K 270       6.818 -32.467 -44.621  1.00108.07           C  
ATOM   4087  CA  LEU K 271       6.884 -35.116 -41.970  1.00102.32           C  
ATOM   4088  CA  PRO K 272      10.114 -36.533 -40.814  1.00146.13           C  
ATOM   4089  CA  GLY K 273      10.937 -40.096 -41.728  1.00 22.95           C  
ATOM   4090  CA  SER K 274       7.563 -39.867 -43.302  1.00 86.98           C  
ATOM   4091  CA  GLY K 275       6.415 -41.404 -46.464  1.00 34.40           C  
ATOM   4092  CA  SER K 276       6.164 -38.081 -48.092  1.00 47.72           C  
ATOM   4093  CA  ALA K 277       9.631 -37.295 -46.920  1.00 53.58           C  
ATOM   4094  CA  LYS K 278      11.460 -40.114 -48.602  1.00149.92           C  
ATOM   4095  CA  ALA K 279       9.169 -39.981 -51.581  1.00 41.46           C  
ATOM   4096  CA  GLY K 280      10.570 -36.564 -51.851  1.00 40.07           C  
ATOM   4097  CA  VAL K 281       7.304 -34.728 -51.684  1.00 63.92           C  
ATOM   4098  CA  LYS K 282       7.868 -31.649 -49.805  1.00136.27           C  
ATOM   4099  CA  ALA K 283       6.059 -28.599 -48.723  1.00 94.17           C  
ATOM   4100  CA  GLY K 284       4.381 -26.042 -50.826  1.00 40.11           C  
ATOM   4101  CA  ASP K 285       3.335 -29.120 -52.736  1.00103.41           C  
ATOM   4102  CA  ILE K 286       0.222 -29.131 -54.641  1.00159.46           C  
ATOM   4103  CA  ILE K 287      -1.161 -32.618 -55.013  1.00 73.57           C  
ATOM   4104  CA  THR K 288      -2.986 -32.503 -58.285  1.00140.36           C  
ATOM   4105  CA  SER K 289      -3.908 -36.097 -58.624  1.00103.44           C  
ATOM   4106  CA  LEU K 290      -3.611 -39.528 -57.174  1.00 77.56           C  
ATOM   4107  CA  ASN K 291      -3.107 -42.438 -59.498  1.00185.55           C  
ATOM   4108  CA  GLY K 292      -4.232 -42.383 -63.115  1.00 55.52           C  
ATOM   4109  CA  LYS K 293      -7.557 -40.735 -62.505  1.00135.94           C  
ATOM   4110  CA  PRO K 294      -7.598 -37.103 -61.666  1.00 65.23           C  
ATOM   4111  CA  LEU K 295      -7.742 -36.001 -58.052  1.00123.83           C  
ATOM   4112  CA  ASN K 296     -10.201 -33.447 -56.802  1.00 69.65           C  
ATOM   4113  CA  SER K 297      -9.751 -31.169 -53.869  1.00 90.71           C  
ATOM   4114  CA  PHE K 298      -7.956 -32.016 -50.700  1.00103.70           C  
ATOM   4115  CA  ALA K 299     -11.279 -33.537 -49.856  1.00 49.70           C  
ATOM   4116  CA  GLU K 300     -11.224 -36.086 -52.577  1.00 93.32           C  
ATOM   4117  CA  LEU K 301      -7.688 -36.782 -51.601  1.00156.88           C  
ATOM   4118  CA  ARG K 302      -8.391 -38.465 -48.330  1.00165.78           C  
ATOM   4119  CA  SER K 303     -11.467 -39.926 -49.850  1.00 59.72           C  
ATOM   4120  CA  ARG K 304      -9.489 -42.107 -52.079  1.00248.55           C  
ATOM   4121  CA  ILE K 305      -6.462 -42.504 -49.858  1.00 93.20           C  
ATOM   4122  CA  ALA K 306      -8.379 -42.979 -46.728  1.00 69.56           C  
ATOM   4123  CA  THR K 307     -10.194 -45.431 -48.896  1.00 60.81           C  
ATOM   4124  CA  THR K 308      -7.097 -47.209 -50.043  1.00146.21           C  
ATOM   4125  CA  GLU K 309      -4.924 -49.654 -48.244  1.00102.77           C  
ATOM   4126  CA  PRO K 310      -2.492 -47.954 -46.043  1.00187.00           C  
ATOM   4127  CA  GLY K 311      -0.297 -49.454 -47.399  1.00129.18           C  
ATOM   4128  CA  THR K 312      -0.887 -49.686 -51.081  1.00125.97           C  
ATOM   4129  CA  LYS K 313       1.892 -48.315 -53.164  1.00114.66           C  
ATOM   4130  CA  VAL K 314       0.511 -45.476 -55.179  1.00 47.60           C  
ATOM   4131  CA  LYS K 315       1.750 -42.655 -57.362  1.00 45.49           C  
ATOM   4132  CA  LEU K 316       0.998 -39.053 -56.655  1.00105.10           C  
ATOM   4133  CA  GLY K 317       0.885 -36.166 -59.038  1.00 49.52           C  
ATOM   4134  CA  LEU K 318       1.796 -32.828 -57.683  1.00133.01           C  
ATOM   4135  CA  LEU K 319       2.726 -29.524 -59.018  1.00123.17           C  
ATOM   4136  CA  ARG K 320       5.798 -28.031 -57.860  1.00238.49           C  
ATOM   4137  CA  ASN K 321       7.254 -24.902 -59.407  1.00206.55           C  
ATOM   4138  CA  GLY K 322       4.645 -24.997 -61.977  1.00 48.75           C  
ATOM   4139  CA  LYS K 323       6.089 -28.179 -63.147  1.00123.39           C  
ATOM   4140  CA  PRO K 324       5.013 -31.665 -63.064  1.00155.17           C  
ATOM   4141  CA  LEU K 325       6.327 -34.887 -61.550  1.00199.17           C  
ATOM   4142  CA  GLU K 326       5.176 -38.262 -60.711  1.00119.09           C  
ATOM   4143  CA  VAL K 327       6.508 -39.901 -57.620  1.00 54.28           C  
ATOM   4144  CA  GLU K 328       5.634 -43.106 -55.950  1.00 53.00           C  
ATOM   4145  CA  VAL K 329       4.834 -42.696 -52.356  1.00 61.14           C  
ATOM   4146  CA  SER K 340      32.305 -45.385 -25.463  1.00 61.82           C  
ATOM   4147  CA  ALA K 341      31.790 -44.888 -21.740  1.00 77.86           C  
ATOM   4148  CA  GLU K 342      29.903 -41.650 -22.191  1.00 53.53           C  
ATOM   4149  CA  MET K 343      26.511 -42.967 -23.022  1.00 36.66           C  
ATOM   4150  CA  ILE K 344      26.528 -45.449 -20.214  1.00109.34           C  
ATOM   4151  CA  THR K 345      28.084 -42.994 -17.860  1.00 68.09           C  
ATOM   4152  CA  PRO K 346      27.329 -39.357 -17.961  1.00156.11           C  
ATOM   4153  CA  ALA K 347      29.822 -36.886 -19.359  1.00 74.38           C  
ATOM   4154  CA  LEU K 348      32.663 -39.273 -18.589  1.00138.34           C  
ATOM   4155  CA  GLU K 349      34.522 -39.480 -21.836  1.00140.85           C  
ATOM   4156  CA  GLY K 350      36.676 -42.510 -21.994  1.00 29.74           C  
ATOM   4157  CA  ALA K 351      37.239 -45.954 -23.348  1.00 36.65           C  
ATOM   4158  CA  THR K 352      34.506 -47.340 -25.493  1.00103.72           C  
ATOM   4159  CA  LEU K 353      32.372 -50.129 -24.192  1.00 58.25           C  
ATOM   4160  CA  SER K 354      30.942 -53.205 -25.810  1.00 33.07           C  
ATOM   4161  CA  ASP K 355      28.365 -55.607 -24.483  1.00 39.97           C  
ATOM   4162  CA  GLY K 356      28.610 -59.321 -24.298  1.00 46.65           C  
ATOM   4163  CA  GLN K 357      31.645 -61.191 -23.148  1.00159.98           C  
ATOM   4164  CA  LEU K 358      31.763 -61.061 -26.784  1.00194.91           C  
ATOM   4165  CA  LYS K 359      34.553 -63.608 -26.953  1.00117.93           C  
ATOM   4166  CA  ASP K 360      33.222 -65.849 -24.172  1.00 48.35           C  
ATOM   4167  CA  GLY K 361      30.045 -66.108 -22.152  1.00 29.57           C  
ATOM   4168  CA  GLY K 362      29.082 -62.639 -21.056  1.00 40.66           C  
ATOM   4169  CA  LYS K 363      31.014 -61.988 -17.920  1.00118.39           C  
ATOM   4170  CA  GLY K 364      30.064 -58.407 -18.523  1.00 31.51           C  
ATOM   4171  CA  ILE K 365      30.619 -55.244 -20.505  1.00161.06           C  
ATOM   4172  CA  LYS K 366      33.981 -54.896 -22.128  1.00120.82           C  
ATOM   4173  CA  ILE K 367      35.834 -51.663 -22.473  1.00 65.03           C  
ATOM   4174  CA  ASP K 368      37.378 -51.668 -25.897  1.00 57.77           C  
ATOM   4175  CA  GLU K 369      40.084 -49.081 -25.621  1.00 84.92           C  
ATOM   4176  CA  VAL K 370      41.166 -46.279 -23.364  1.00158.59           C  
ATOM   4177  CA  VAL K 371      41.144 -42.737 -24.674  1.00185.36           C  
ATOM   4178  CA  LYS K 372      43.293 -42.249 -21.526  1.00240.80           C  
ATOM   4179  CA  GLY K 373      43.523 -38.492 -21.716  1.00 40.22           C  
ATOM   4180  CA  SER K 374      39.768 -38.813 -21.040  1.00 53.11           C  
ATOM   4181  CA  PRO K 375      38.231 -38.882 -17.641  1.00 80.82           C  
ATOM   4182  CA  ALA K 376      37.096 -42.475 -17.935  1.00 42.46           C  
ATOM   4183  CA  ALA K 377      40.814 -43.055 -17.933  1.00 52.16           C  
ATOM   4184  CA  GLN K 378      41.443 -40.874 -14.901  1.00 55.71           C  
ATOM   4185  CA  ALA K 379      39.464 -42.993 -12.431  1.00 64.44           C  
ATOM   4186  CA  GLY K 380      41.118 -46.301 -13.195  1.00 61.26           C  
ATOM   4187  CA  LEU K 381      39.440 -47.655 -16.278  1.00 63.30           C  
ATOM   4188  CA  GLN K 382      41.998 -49.459 -18.427  1.00146.33           C  
ATOM   4189  CA  LYS K 383      41.189 -51.263 -21.619  1.00142.90           C  
ATOM   4190  CA  ASP K 384      40.458 -54.980 -21.710  1.00 78.61           C  
ATOM   4191  CA  ASP K 385      38.708 -54.775 -18.395  1.00 50.57           C  
ATOM   4192  CA  VAL K 386      35.412 -56.509 -18.136  1.00 64.82           C  
ATOM   4193  CA  ILE K 387      32.775 -55.144 -15.870  1.00 73.93           C  
ATOM   4194  CA  ILE K 388      31.289 -58.153 -14.147  1.00111.66           C  
ATOM   4195  CA  GLY K 389      28.707 -56.094 -12.322  1.00 51.21           C  
ATOM   4196  CA  VAL K 390      27.978 -52.912 -10.497  1.00140.00           C  
ATOM   4197  CA  ASN K 391      26.878 -52.276  -6.937  1.00 92.69           C  
ATOM   4198  CA  ARG K 392      26.486 -55.897  -5.940  1.00158.22           C  
ATOM   4199  CA  ASP K 393      24.608 -56.358  -9.171  1.00 76.80           C  
ATOM   4200  CA  ARG K 394      25.836 -58.654 -11.877  1.00120.77           C  
ATOM   4201  CA  VAL K 395      26.141 -56.956 -15.224  1.00 50.95           C  
ATOM   4202  CA  ASN K 396      25.673 -59.383 -18.067  1.00 50.17           C  
ATOM   4203  CA  SER K 397      25.487 -56.665 -20.661  1.00 91.04           C  
ATOM   4204  CA  ILE K 398      25.197 -52.913 -21.138  1.00 40.87           C  
ATOM   4205  CA  ALA K 399      21.472 -52.930 -20.613  1.00 25.71           C  
ATOM   4206  CA  GLU K 400      21.820 -54.437 -17.176  1.00 32.93           C  
ATOM   4207  CA  MET K 401      24.593 -52.073 -16.258  1.00 40.01           C  
ATOM   4208  CA  ARG K 402      22.321 -49.284 -17.304  1.00139.52           C  
ATOM   4209  CA  LYS K 403      19.683 -50.470 -14.918  1.00138.53           C  
ATOM   4210  CA  VAL K 404      21.947 -50.240 -11.917  1.00102.68           C  
ATOM   4211  CA  LEU K 405      22.809 -46.783 -13.174  1.00102.96           C  
ATOM   4212  CA  ALA K 406      19.099 -46.127 -13.384  1.00 27.35           C  
ATOM   4213  CA  ALA K 407      19.040 -46.240  -9.619  1.00 29.48           C  
ATOM   4214  CA  LYS K 408      21.662 -43.521  -9.805  1.00 99.47           C  
ATOM   4215  CA  PRO K 409      23.241 -44.484  -6.549  1.00 70.38           C  
ATOM   4216  CA  ALA K 410      25.591 -41.794  -5.314  1.00 32.43           C  
ATOM   4217  CA  ILE K 411      28.059 -44.634  -4.905  1.00142.54           C  
ATOM   4218  CA  ILE K 412      28.759 -46.658  -8.001  1.00 50.53           C  
ATOM   4219  CA  ALA K 413      31.082 -49.559  -7.662  1.00 51.31           C  
ATOM   4220  CA  LEU K 414      32.321 -51.339 -10.710  1.00117.87           C  
ATOM   4221  CA  GLN K 415      34.212 -54.481 -10.344  1.00127.02           C  
ATOM   4222  CA  ILE K 416      35.895 -55.622 -13.392  1.00123.76           C  
ATOM   4223  CA  VAL K 417      38.256 -58.423 -13.962  1.00 45.18           C  
ATOM   4224  CA  ARG K 418      41.637 -57.477 -15.262  1.00 81.07           C  
ATOM   4225  CA  GLY K 419      43.882 -60.288 -16.292  1.00 20.10           C  
ATOM   4226  CA  ASN K 420      43.330 -63.080 -13.869  1.00 49.35           C  
ATOM   4227  CA  GLU K 421      42.420 -60.789 -11.042  1.00 47.91           C  
ATOM   4228  CA  SER K 422      39.521 -58.996  -9.505  1.00 48.32           C  
ATOM   4229  CA  ILE K 423      39.388 -55.277  -9.862  1.00 75.14           C  
ATOM   4230  CA  TYR K 424      37.143 -52.694  -8.421  1.00155.03           C  
ATOM   4231  CA  LEU K 425      36.439 -49.396  -9.982  1.00 96.61           C  
ATOM   4232  CA  LEU K 426      34.277 -46.588  -8.936  1.00145.27           C  
ATOM   4233  CA  MET K 427      32.691 -43.270  -9.493  1.00 92.39           C  
TER    4234      MET K 427                                                      
ATOM   4235  CA  PRO L  11     -42.319 -38.326 -48.071  1.00 69.08           C  
ATOM   4236  CA  LEU L  12     -43.885 -36.263 -45.336  1.00 87.85           C  
ATOM   4237  CA  PRO L  13     -46.292 -37.846 -42.993  1.00152.02           C  
ATOM   4238  CA  SER L  14     -46.821 -35.023 -42.838  1.00120.03           C  
ATOM   4239  CA  LEU L  15     -46.397 -33.952 -39.236  1.00113.20           C  
ATOM   4240  CA  ALA L  16     -48.818 -31.059 -39.544  1.00 42.41           C  
ATOM   4241  CA  PRO L  17     -51.959 -33.037 -39.924  1.00 73.01           C  
ATOM   4242  CA  MET L  18     -51.171 -34.948 -36.766  1.00121.98           C  
ATOM   4243  CA  LEU L  19     -50.195 -31.768 -34.978  1.00 56.34           C  
ATOM   4244  CA  GLU L  20     -53.262 -29.831 -35.842  1.00 59.26           C  
ATOM   4245  CA  LYS L  21     -55.511 -32.080 -33.856  1.00 85.83           C  
ATOM   4246  CA  VAL L  22     -53.133 -32.682 -30.932  1.00148.09           C  
ATOM   4247  CA  LEU L  23     -51.679 -29.240 -30.366  1.00 81.64           C  
ATOM   4248  CA  PRO L  24     -54.519 -27.707 -28.479  1.00 79.14           C  
ATOM   4249  CA  ALA L  25     -54.035 -30.413 -25.872  1.00 34.56           C  
ATOM   4250  CA  VAL L  26     -50.662 -29.008 -24.917  1.00 42.57           C  
ATOM   4251  CA  VAL L  27     -50.795 -25.917 -22.815  1.00 99.02           C  
ATOM   4252  CA  SER L  28     -48.490 -23.329 -21.328  1.00 85.70           C  
ATOM   4253  CA  VAL L  29     -48.380 -22.979 -17.600  1.00 40.93           C  
ATOM   4254  CA  ARG L  30     -47.864 -19.620 -15.990  1.00 96.39           C  
ATOM   4255  CA  VAL L  31     -46.795 -19.358 -12.413  1.00118.53           C  
ATOM   4256  CA  GLU L  32     -46.376 -16.643  -9.829  1.00 77.07           C  
ATOM   4257  CA  GLY L  33     -45.391 -16.953  -6.238  1.00 38.71           C  
ATOM   4258  CA  THR L  34     -43.073 -16.566  -3.292  1.00133.17           C  
ATOM   4259  CA  ALA L  35     -40.202 -14.191  -1.067  1.00 53.54           C  
ATOM   4260  CA  GLN L  59     -39.634 -12.060  -4.137  1.00183.76           C  
ATOM   4261  CA  PRO L  60     -42.315 -12.343  -6.537  1.00103.05           C  
ATOM   4262  CA  PHE L  61     -41.166 -14.431  -9.435  1.00 68.12           C  
ATOM   4263  CA  GLU L  62     -42.860 -15.445 -12.615  1.00 36.66           C  
ATOM   4264  CA  GLY L  63     -42.150 -18.744 -14.234  1.00 19.18           C  
ATOM   4265  CA  LEU L  64     -43.172 -20.295 -17.488  1.00 38.67           C  
ATOM   4266  CA  GLY L  65     -43.629 -23.956 -18.240  1.00 21.76           C  
ATOM   4267  CA  SER L  66     -45.917 -26.255 -20.146  1.00 76.85           C  
ATOM   4268  CA  GLY L  67     -48.465 -28.908 -19.377  1.00 20.00           C  
ATOM   4269  CA  VAL L  68     -50.669 -31.432 -21.085  1.00114.01           C  
ATOM   4270  CA  ILE L  69     -54.399 -31.799 -20.730  1.00110.73           C  
ATOM   4271  CA  ILE L  70     -55.052 -35.350 -19.621  1.00 95.73           C  
ATOM   4272  CA  ASN L  71     -58.788 -35.082 -19.338  1.00 60.56           C  
ATOM   4273  CA  ALA L  72     -60.789 -32.425 -21.064  1.00 31.85           C  
ATOM   4274  CA  SER L  73     -63.891 -32.866 -19.008  1.00 35.49           C  
ATOM   4275  CA  LYS L  74     -62.272 -32.532 -15.639  1.00 93.15           C  
ATOM   4276  CA  GLY L  75     -59.632 -30.180 -16.895  1.00 31.22           C  
ATOM   4277  CA  TYR L  76     -56.737 -32.105 -15.443  1.00 66.56           C  
ATOM   4278  CA  VAL L  77     -53.384 -30.972 -16.695  1.00124.06           C  
ATOM   4279  CA  LEU L  78     -50.150 -32.849 -16.151  1.00169.40           C  
ATOM   4280  CA  THR L  79     -47.000 -30.866 -15.482  1.00 48.48           C  
ATOM   4281  CA  ASN L  80     -43.645 -31.089 -13.817  1.00 62.57           C  
ATOM   4282  CA  ASN L  81     -43.586 -30.531 -10.108  1.00 45.47           C  
ATOM   4283  CA  HIS L  82     -40.694 -28.147 -10.362  1.00 53.82           C  
ATOM   4284  CA  VAL L  83     -42.644 -25.865 -12.597  1.00 44.59           C  
ATOM   4285  CA  ILE L  84     -45.522 -25.709 -10.097  1.00123.49           C  
ATOM   4286  CA  ASN L  85     -43.731 -26.080  -6.770  1.00 80.85           C  
ATOM   4287  CA  GLN L  86     -43.240 -22.445  -5.844  1.00 70.49           C  
ATOM   4288  CA  ALA L  87     -46.479 -21.291  -7.483  1.00 72.68           C  
ATOM   4289  CA  GLN L  88     -48.850 -19.347  -5.303  1.00 96.68           C  
ATOM   4290  CA  LYS L  89     -51.122 -18.907  -8.290  1.00 32.50           C  
ATOM   4291  CA  ILE L  90     -51.182 -20.792 -11.528  1.00 41.34           C  
ATOM   4292  CA  SER L  91     -52.704 -19.960 -14.855  1.00 75.80           C  
ATOM   4293  CA  ILE L  92     -53.118 -22.070 -17.946  1.00 96.68           C  
ATOM   4294  CA  GLN L  93     -53.066 -20.654 -21.432  1.00 50.70           C  
ATOM   4295  CA  LEU L  94     -54.373 -22.432 -24.476  1.00 54.70           C  
ATOM   4296  CA  ASN L  95     -52.902 -22.196 -27.931  1.00110.70           C  
ATOM   4297  CA  ASP L  96     -56.007 -20.302 -28.924  1.00 49.56           C  
ATOM   4298  CA  GLY L  97     -55.233 -17.614 -26.391  1.00 26.33           C  
ATOM   4299  CA  ARG L  98     -57.876 -18.530 -23.868  1.00 91.69           C  
ATOM   4300  CA  GLU L  99     -56.596 -18.511 -20.326  1.00 42.05           C  
ATOM   4301  CA  PHE L 100     -57.831 -20.193 -17.190  1.00 42.97           C  
ATOM   4302  CA  ASP L 101     -56.873 -20.456 -13.553  1.00 39.14           C  
ATOM   4303  CA  ALA L 102     -55.725 -23.747 -12.164  1.00 31.95           C  
ATOM   4304  CA  LYS L 103     -55.265 -25.292  -8.778  1.00 99.73           C  
ATOM   4305  CA  LEU L 104     -52.773 -27.907  -7.757  1.00 52.79           C  
ATOM   4306  CA  ILE L 105     -54.461 -31.232  -7.328  1.00133.63           C  
ATOM   4307  CA  GLY L 106     -51.310 -32.861  -6.058  1.00 28.32           C  
ATOM   4308  CA  SER L 107     -47.763 -33.639  -7.032  1.00104.34           C  
ATOM   4309  CA  ASP L 108     -44.632 -35.304  -5.862  1.00113.39           C  
ATOM   4310  CA  ASP L 109     -40.975 -34.337  -5.817  1.00 70.21           C  
ATOM   4311  CA  GLN L 110     -39.168 -37.550  -6.487  1.00152.11           C  
ATOM   4312  CA  SER L 111     -40.691 -38.357  -9.855  1.00 65.68           C  
ATOM   4313  CA  ASP L 112     -41.332 -34.664 -10.440  1.00 73.92           C  
ATOM   4314  CA  ILE L 113     -44.928 -35.115 -11.564  1.00 62.33           C  
ATOM   4315  CA  ALA L 114     -47.736 -32.751 -10.653  1.00 34.53           C  
ATOM   4316  CA  LEU L 115     -51.409 -32.646 -11.508  1.00100.09           C  
ATOM   4317  CA  LEU L 116     -53.339 -29.440 -11.989  1.00 48.29           C  
ATOM   4318  CA  GLN L 117     -57.015 -28.783 -12.478  1.00 42.16           C  
ATOM   4319  CA  ILE L 118     -58.366 -25.999 -14.614  1.00 89.96           C  
ATOM   4320  CA  GLN L 119     -61.276 -24.138 -13.164  1.00123.40           C  
ATOM   4321  CA  ASN L 120     -64.231 -23.851 -15.515  1.00 60.93           C  
ATOM   4322  CA  PRO L 121     -62.417 -25.811 -18.154  1.00103.73           C  
ATOM   4323  CA  SER L 122     -64.897 -25.462 -21.063  1.00196.27           C  
ATOM   4324  CA  LYS L 123     -64.207 -26.841 -24.543  1.00 76.61           C  
ATOM   4325  CA  LEU L 124     -60.847 -28.422 -24.007  1.00 92.25           C  
ATOM   4326  CA  THR L 125     -59.000 -30.989 -26.037  1.00119.15           C  
ATOM   4327  CA  GLN L 126     -57.455 -34.027 -24.447  1.00122.91           C  
ATOM   4328  CA  ILE L 127     -54.344 -35.867 -25.460  1.00 67.65           C  
ATOM   4329  CA  ALA L 128     -54.327 -39.610 -25.834  1.00 35.99           C  
ATOM   4330  CA  ILE L 129     -51.755 -41.539 -23.904  1.00 71.60           C  
ATOM   4331  CA  ALA L 130     -49.570 -44.186 -25.467  1.00 36.30           C  
ATOM   4332  CA  ASP L 131     -47.868 -47.122 -23.818  1.00 34.68           C  
ATOM   4333  CA  SER L 132     -44.363 -46.003 -22.963  1.00 40.78           C  
ATOM   4334  CA  ASP L 133     -43.238 -49.549 -22.458  1.00 32.05           C  
ATOM   4335  CA  LYS L 134     -43.706 -50.199 -26.158  1.00 46.64           C  
ATOM   4336  CA  LEU L 135     -41.334 -47.427 -27.172  1.00125.88           C  
ATOM   4337  CA  ARG L 136     -38.068 -48.482 -28.799  1.00115.81           C  
ATOM   4338  CA  VAL L 137     -35.011 -46.494 -29.725  1.00 37.43           C  
ATOM   4339  CA  GLY L 138     -35.389 -44.992 -33.142  1.00 24.83           C  
ATOM   4340  CA  ASP L 139     -39.037 -44.158 -32.738  1.00 25.95           C  
ATOM   4341  CA  PHE L 140     -39.956 -40.680 -33.856  1.00 42.80           C  
ATOM   4342  CA  ALA L 141     -40.922 -38.133 -31.265  1.00 33.01           C  
ATOM   4343  CA  VAL L 142     -42.176 -34.597 -31.271  1.00 96.89           C  
ATOM   4344  CA  ALA L 143     -41.850 -32.267 -28.351  1.00 31.09           C  
ATOM   4345  CA  VAL L 144     -44.271 -29.474 -27.683  1.00 34.45           C  
ATOM   4346  CA  GLY L 145     -43.936 -26.814 -25.048  1.00 21.59           C  
ATOM   4347  CA  ASN L 146     -42.977 -23.220 -24.654  1.00 63.38           C  
ATOM   4348  CA  PRO L 147     -39.321 -22.658 -24.902  1.00 68.64           C  
ATOM   4349  CA  PHE L 148     -38.199 -19.254 -23.717  1.00 73.26           C  
ATOM   4350  CA  GLY L 149     -41.866 -18.540 -23.220  1.00 25.57           C  
ATOM   4351  CA  LEU L 150     -42.050 -17.891 -26.925  1.00 55.32           C  
ATOM   4352  CA  GLY L 151     -45.346 -19.690 -27.310  1.00 28.72           C  
ATOM   4353  CA  GLN L 152     -46.320 -23.161 -28.327  1.00 46.02           C  
ATOM   4354  CA  THR L 153     -43.399 -24.645 -30.182  1.00 30.47           C  
ATOM   4355  CA  ALA L 154     -42.971 -28.058 -31.700  1.00 28.74           C  
ATOM   4356  CA  THR L 155     -39.651 -29.772 -32.222  1.00 31.23           C  
ATOM   4357  CA  SER L 156     -38.912 -33.117 -33.781  1.00 81.92           C  
ATOM   4358  CA  GLY L 157     -36.461 -35.881 -33.053  1.00 22.36           C  
ATOM   4359  CA  ILE L 158     -36.185 -39.573 -32.297  1.00 93.31           C  
ATOM   4360  CA  VAL L 159     -36.159 -41.547 -29.093  1.00 40.21           C  
ATOM   4361  CA  SER L 160     -32.480 -41.718 -28.338  1.00 86.56           C  
ATOM   4362  CA  ALA L 161     -32.658 -44.000 -25.331  1.00 36.96           C  
ATOM   4363  CA  LEU L 162     -34.945 -45.304 -22.635  1.00 87.59           C  
ATOM   4364  CA  GLY L 163     -34.677 -46.452 -19.077  1.00 28.77           C  
ATOM   4365  CA  ARG L 164     -32.001 -44.013 -18.292  1.00 86.56           C  
ATOM   4366  CA  SER L 165     -31.047 -42.856 -14.900  1.00115.01           C  
ATOM   4367  CA  GLY L 166     -28.251 -41.947 -12.599  1.00 36.17           C  
ATOM   4368  CA  LEU L 167     -28.622 -38.455 -13.994  1.00 51.95           C  
ATOM   4369  CA  ASN L 168     -29.283 -37.435 -10.419  1.00 66.86           C  
ATOM   4370  CA  LEU L 169     -31.807 -34.983 -11.737  1.00 57.18           C  
ATOM   4371  CA  GLU L 170     -34.660 -36.588  -9.848  1.00112.68           C  
ATOM   4372  CA  GLY L 171     -35.174 -39.004  -6.989  1.00 40.75           C  
ATOM   4373  CA  LEU L 172     -36.796 -41.518  -9.233  1.00132.78           C  
ATOM   4374  CA  GLU L 173     -35.719 -41.427 -12.764  1.00 94.51           C  
ATOM   4375  CA  ASN L 174     -36.402 -43.401 -15.896  1.00 97.59           C  
ATOM   4376  CA  PHE L 175     -36.094 -40.848 -18.514  1.00 91.93           C  
ATOM   4377  CA  ILE L 176     -36.841 -41.366 -22.108  1.00 64.66           C  
ATOM   4378  CA  GLN L 177     -34.031 -39.607 -23.881  1.00 54.30           C  
ATOM   4379  CA  THR L 178     -34.800 -37.569 -26.962  1.00136.58           C  
ATOM   4380  CA  ASP L 179     -32.875 -35.604 -29.552  1.00 65.42           C  
ATOM   4381  CA  ALA L 180     -35.818 -33.258 -30.016  1.00 45.10           C  
ATOM   4382  CA  SER L 181     -34.830 -29.762 -29.077  1.00 39.72           C  
ATOM   4383  CA  ILE L 182     -35.865 -29.122 -25.530  1.00 93.74           C  
ATOM   4384  CA  ASN L 183     -35.049 -25.884 -23.800  1.00 40.39           C  
ATOM   4385  CA  ARG L 184     -36.073 -24.080 -20.691  1.00 42.15           C  
ATOM   4386  CA  GLY L 185     -39.813 -23.609 -20.642  1.00 22.02           C  
ATOM   4387  CA  ASN L 186     -40.239 -27.051 -22.151  1.00 52.53           C  
ATOM   4388  CA  ALA L 187     -40.803 -28.616 -18.765  1.00 98.20           C  
ATOM   4389  CA  GLY L 188     -44.185 -30.162 -18.275  1.00 27.99           C  
ATOM   4390  CA  GLY L 189     -44.566 -30.205 -22.023  1.00 22.75           C  
ATOM   4391  CA  ALA L 190     -45.459 -33.236 -24.018  1.00 47.77           C  
ATOM   4392  CA  LEU L 191     -43.403 -35.634 -26.050  1.00 95.23           C  
ATOM   4393  CA  LEU L 192     -45.586 -37.185 -28.661  1.00 59.13           C  
ATOM   4394  CA  ASN L 193     -45.360 -40.039 -31.071  1.00 54.69           C  
ATOM   4395  CA  LEU L 194     -46.359 -39.822 -34.702  1.00 84.61           C  
ATOM   4396  CA  ASN L 195     -49.846 -40.750 -33.584  1.00 56.09           C  
ATOM   4397  CA  GLY L 196     -49.914 -37.629 -31.493  1.00 24.66           C  
ATOM   4398  CA  GLU L 197     -50.189 -39.775 -28.409  1.00 44.26           C  
ATOM   4399  CA  LEU L 198     -48.321 -38.837 -25.252  1.00142.24           C  
ATOM   4400  CA  ILE L 199     -45.065 -40.780 -24.863  1.00114.56           C  
ATOM   4401  CA  GLY L 200     -43.822 -38.774 -21.894  1.00 33.66           C  
ATOM   4402  CA  ILE L 201     -43.508 -35.390 -20.238  1.00 91.42           C  
ATOM   4403  CA  ASN L 202     -40.330 -33.427 -20.915  1.00 79.32           C  
ATOM   4404  CA  THR L 203     -38.630 -33.028 -17.564  1.00 86.04           C  
ATOM   4405  CA  ALA L 204     -35.074 -31.872 -18.167  1.00 54.41           C  
ATOM   4406  CA  ILE L 205     -32.025 -31.496 -20.359  1.00 63.18           C  
ATOM   4407  CA  LEU L 206     -28.299 -31.966 -20.124  1.00 56.23           C  
ATOM   4408  CA  ALA L 207     -26.588 -28.987 -21.613  1.00 44.13           C  
ATOM   4409  CA  PRO L 208     -23.371 -27.372 -20.711  1.00 71.92           C  
ATOM   4410  CA  GLY L 209     -24.468 -24.169 -22.402  1.00 31.92           C  
ATOM   4411  CA  GLY L 210     -27.878 -24.153 -20.835  1.00 27.65           C  
ATOM   4412  CA  GLY L 211     -29.210 -24.561 -24.335  1.00 25.38           C  
ATOM   4413  CA  SER L 212     -30.375 -27.738 -26.007  1.00 55.86           C  
ATOM   4414  CA  VAL L 213     -27.467 -30.073 -26.725  1.00 62.26           C  
ATOM   4415  CA  GLY L 214     -29.806 -32.624 -28.207  1.00 37.60           C  
ATOM   4416  CA  ILE L 215     -29.920 -34.592 -25.005  1.00 89.86           C  
ATOM   4417  CA  GLY L 216     -33.315 -34.248 -23.401  1.00 20.77           C  
ATOM   4418  CA  PHE L 217     -35.122 -36.395 -20.900  1.00 43.92           C  
ATOM   4419  CA  ALA L 218     -38.782 -37.036 -20.345  1.00 33.41           C  
ATOM   4420  CA  ILE L 219     -40.760 -39.021 -17.846  1.00 72.06           C  
ATOM   4421  CA  PRO L 220     -42.502 -41.800 -19.554  1.00 88.62           C  
ATOM   4422  CA  SER L 221     -46.191 -41.592 -20.277  1.00 87.16           C  
ATOM   4423  CA  ASN L 222     -46.840 -44.704 -18.339  1.00 65.68           C  
ATOM   4424  CA  MET L 223     -45.046 -42.815 -15.733  1.00103.73           C  
ATOM   4425  CA  ALA L 224     -47.170 -39.747 -15.714  1.00 51.58           C  
ATOM   4426  CA  ARG L 225     -50.378 -41.557 -16.360  1.00 92.48           C  
ATOM   4427  CA  THR L 226     -50.668 -43.779 -13.386  1.00 73.66           C  
ATOM   4428  CA  LEU L 227     -48.885 -41.257 -11.156  1.00119.65           C  
ATOM   4429  CA  ALA L 228     -51.382 -38.682 -12.307  1.00 50.25           C  
ATOM   4430  CA  GLN L 229     -54.148 -41.163 -11.853  1.00145.70           C  
ATOM   4431  CA  GLN L 230     -54.021 -41.528  -8.123  1.00 91.27           C  
ATOM   4432  CA  LEU L 231     -53.416 -37.840  -7.863  1.00 53.82           C  
ATOM   4433  CA  ILE L 232     -57.017 -37.689  -8.845  1.00124.48           C  
ATOM   4434  CA  ASP L 233     -57.727 -41.216  -7.542  1.00168.89           C  
ATOM   4435  CA  PHE L 234     -56.976 -43.309  -5.616  1.00188.63           C  
ATOM   4436  CA  GLY L 235     -54.731 -40.809  -4.030  1.00 42.90           C  
ATOM   4437  CA  GLU L 236     -53.454 -43.083  -1.367  1.00102.26           C  
ATOM   4438  CA  ILE L 237     -51.087 -40.998   0.655  1.00 92.45           C  
ATOM   4439  CA  LYS L 238     -48.502 -43.659   0.314  1.00201.99           C  
ATOM   4440  CA  ARG L 239     -46.302 -44.228  -1.302  1.00229.50           C  
ATOM   4441  CA  GLY L 240     -46.992 -40.771  -2.616  1.00 51.80           C  
ATOM   4442  CA  LEU L 241     -43.605 -41.142  -4.128  1.00168.13           C  
ATOM   4443  CA  LEU L 242     -40.892 -42.144  -1.752  1.00 94.02           C  
ATOM   4444  CA  GLY L 243     -39.216 -38.811  -1.204  1.00 53.14           C  
ATOM   4445  CA  ILE L 244     -35.590 -39.669  -1.804  1.00 74.08           C  
ATOM   4446  CA  LYS L 245     -32.643 -38.618  -3.915  1.00 88.42           C  
ATOM   4447  CA  GLY L 246     -30.411 -41.030  -5.696  1.00 35.01           C  
ATOM   4448  CA  THR L 247     -28.316 -41.689  -8.720  1.00115.09           C  
ATOM   4449  CA  GLU L 248     -26.446 -44.363 -10.634  1.00105.66           C  
ATOM   4450  CA  MET L 249     -24.147 -46.737  -8.872  1.00 58.07           C  
ATOM   4451  CA  SER L 250     -21.178 -44.673  -7.918  1.00 85.16           C  
ATOM   4452  CA  ALA L 251     -17.712 -45.660  -8.968  1.00 39.17           C  
ATOM   4453  CA  ASP L 252     -16.278 -45.499  -5.487  1.00 50.44           C  
ATOM   4454  CA  ILE L 253     -18.848 -47.542  -3.650  1.00 60.89           C  
ATOM   4455  CA  ALA L 254     -19.608 -49.982  -6.403  1.00 55.53           C  
ATOM   4456  CA  LYS L 255     -16.194 -51.037  -7.388  1.00154.95           C  
ATOM   4457  CA  ALA L 256     -14.492 -51.107  -4.058  1.00 70.78           C  
ATOM   4458  CA  PHE L 257     -16.851 -52.697  -1.606  1.00138.51           C  
ATOM   4459  CA  ASN L 258     -18.511 -54.615  -4.238  1.00186.82           C  
ATOM   4460  CA  LEU L 259     -22.178 -54.416  -3.878  1.00146.11           C  
ATOM   4461  CA  ASP L 260     -24.015 -57.642  -3.575  1.00 67.45           C  
ATOM   4462  CA  VAL L 261     -26.377 -56.459  -6.265  1.00105.34           C  
ATOM   4463  CA  GLN L 262     -24.437 -55.541  -9.341  1.00 55.13           C  
ATOM   4464  CA  ARG L 263     -26.134 -52.224  -9.482  1.00142.86           C  
ATOM   4465  CA  GLY L 264     -29.207 -50.485  -8.313  1.00 25.09           C  
ATOM   4466  CA  ALA L 265     -30.746 -47.192  -7.531  1.00 41.57           C  
ATOM   4467  CA  PHE L 266     -28.521 -45.842  -4.892  1.00128.24           C  
ATOM   4468  CA  VAL L 267     -29.779 -43.284  -2.499  1.00 66.63           C  
ATOM   4469  CA  SER L 268     -27.523 -40.533  -1.252  1.00 60.50           C  
ATOM   4470  CA  GLU L 269     -30.123 -38.882   0.893  1.00104.83           C  
ATOM   4471  CA  VAL L 270     -33.107 -39.207   3.173  1.00100.91           C  
ATOM   4472  CA  LEU L 271     -35.951 -36.730   2.954  1.00 93.51           C  
ATOM   4473  CA  PRO L 272     -37.494 -35.439   6.069  1.00 69.26           C  
ATOM   4474  CA  GLY L 273     -41.061 -36.431   6.853  1.00 26.20           C  
ATOM   4475  CA  SER L 274     -40.582 -38.281   3.653  1.00 44.82           C  
ATOM   4476  CA  GLY L 275     -41.967 -41.567   2.673  1.00 32.41           C  
ATOM   4477  CA  SER L 276     -38.553 -43.029   2.616  1.00 44.91           C  
ATOM   4478  CA  ALA L 277     -37.938 -41.562   5.996  1.00 56.00           C  
ATOM   4479  CA  LYS L 278     -40.679 -43.282   7.905  1.00159.88           C  
ATOM   4480  CA  ALA L 279     -40.351 -46.380   5.799  1.00 41.05           C  
ATOM   4481  CA  GLY L 280     -36.966 -46.374   7.301  1.00 39.86           C  
ATOM   4482  CA  VAL L 281     -35.024 -46.335   4.102  1.00 67.22           C  
ATOM   4483  CA  LYS L 282     -32.038 -44.262   4.586  1.00123.57           C  
ATOM   4484  CA  ALA L 283     -28.982 -43.150   2.750  1.00114.97           C  
ATOM   4485  CA  GLY L 284     -26.291 -45.276   1.329  1.00 47.03           C  
ATOM   4486  CA  ASP L 285     -29.215 -47.440   0.394  1.00 97.42           C  
ATOM   4487  CA  ILE L 286     -29.121 -49.502  -2.613  1.00 84.14           C  
ATOM   4488  CA  ILE L 287     -32.541 -50.173  -4.012  1.00 56.59           C  
ATOM   4489  CA  THR L 288     -32.213 -53.530  -5.668  1.00 53.05           C  
ATOM   4490  CA  SER L 289     -35.759 -54.105  -6.587  1.00 53.16           C  
ATOM   4491  CA  LEU L 290     -39.254 -52.788  -6.531  1.00 74.75           C  
ATOM   4492  CA  ASN L 291     -42.102 -55.185  -5.997  1.00180.76           C  
ATOM   4493  CA  GLY L 292     -41.836 -58.900  -6.762  1.00 52.67           C  
ATOM   4494  CA  LYS L 293     -40.203 -58.443 -10.136  1.00 79.41           C  
ATOM   4495  CA  PRO L 294     -36.625 -57.388 -10.132  1.00137.49           C  
ATOM   4496  CA  LEU L 295     -35.609 -53.777 -10.506  1.00 96.94           C  
ATOM   4497  CA  ASN L 296     -33.006 -52.573 -12.908  1.00 70.12           C  
ATOM   4498  CA  SER L 297     -30.908 -49.488 -12.683  1.00 51.05           C  
ATOM   4499  CA  PHE L 298     -31.909 -46.255 -11.097  1.00 92.65           C  
ATOM   4500  CA  ALA L 299     -33.372 -45.686 -14.503  1.00 46.30           C  
ATOM   4501  CA  GLU L 300     -35.806 -48.522 -14.361  1.00105.04           C  
ATOM   4502  CA  LEU L 301     -36.643 -47.313 -10.912  1.00 72.20           C  
ATOM   4503  CA  ARG L 302     -38.451 -44.220 -11.891  1.00189.06           C  
ATOM   4504  CA  SER L 303     -39.751 -45.904 -14.944  1.00 60.71           C  
ATOM   4505  CA  ARG L 304     -41.864 -48.160 -12.912  1.00256.76           C  
ATOM   4506  CA  ILE L 305     -42.477 -45.861 -10.008  1.00146.54           C  
ATOM   4507  CA  ALA L 306     -43.005 -42.819 -12.091  1.00 67.63           C  
ATOM   4508  CA  THR L 307     -45.334 -45.052 -13.961  1.00162.67           C  
ATOM   4509  CA  THR L 308     -47.061 -46.265 -10.846  1.00 70.34           C  
ATOM   4510  CA  GLU L 309     -49.718 -44.424  -8.896  1.00 82.49           C  
ATOM   4511  CA  PRO L 310     -48.220 -42.079  -6.463  1.00182.89           C  
ATOM   4512  CA  GLY L 311     -49.727 -43.397  -4.294  1.00124.42           C  
ATOM   4513  CA  THR L 312     -49.755 -47.128  -4.598  1.00 52.24           C  
ATOM   4514  CA  LYS L 313     -48.458 -48.990  -1.627  1.00124.20           C  
ATOM   4515  CA  VAL L 314     -45.363 -50.803  -2.728  1.00 48.06           C  
ATOM   4516  CA  LYS L 315     -42.529 -52.743  -1.183  1.00 59.56           C  
ATOM   4517  CA  LEU L 316     -38.931 -52.001  -1.936  1.00101.28           C  
ATOM   4518  CA  GLY L 317     -35.920 -54.205  -1.807  1.00 46.72           C  
ATOM   4519  CA  LEU L 318     -32.667 -52.649  -0.894  1.00112.87           C  
ATOM   4520  CA  LEU L 319     -29.324 -53.680   0.230  1.00109.55           C  
ATOM   4521  CA  ARG L 320     -28.001 -52.223   3.280  1.00213.85           C  
ATOM   4522  CA  ASN L 321     -24.943 -53.779   4.908  1.00192.44           C  
ATOM   4523  CA  GLY L 322     -24.721 -56.293   2.412  1.00 64.39           C  
ATOM   4524  CA  LYS L 323     -27.835 -57.527   3.973  1.00120.57           C  
ATOM   4525  CA  PRO L 324     -31.277 -57.728   2.725  1.00117.64           C  
ATOM   4526  CA  LEU L 325     -34.612 -56.320   3.797  1.00226.71           C  
ATOM   4527  CA  GLU L 326     -38.016 -55.633   2.590  1.00110.34           C  
ATOM   4528  CA  VAL L 327     -39.850 -52.544   3.611  1.00 59.96           C  
ATOM   4529  CA  GLU L 328     -43.169 -51.119   2.651  1.00 44.96           C  
ATOM   4530  CA  VAL L 329     -43.000 -47.642   1.278  1.00 57.90           C  
ATOM   4531  CA  SER L 340     -45.239 -23.000  30.208  1.00 95.15           C  
ATOM   4532  CA  ALA L 341     -44.745 -19.281  29.687  1.00 80.71           C  
ATOM   4533  CA  GLU L 342     -41.555 -19.708  27.713  1.00 55.31           C  
ATOM   4534  CA  MET L 343     -42.927 -20.561  24.350  1.00109.65           C  
ATOM   4535  CA  ILE L 344     -45.351 -17.708  24.305  1.00 94.36           C  
ATOM   4536  CA  THR L 345     -42.884 -15.479  26.059  1.00158.30           C  
ATOM   4537  CA  PRO L 346     -39.278 -15.402  25.139  1.00250.24           C  
ATOM   4538  CA  ALA L 347     -36.776 -16.982  27.490  1.00 74.80           C  
ATOM   4539  CA  LEU L 348     -39.019 -16.137  30.427  1.00 92.49           C  
ATOM   4540  CA  GLU L 349     -39.300 -19.429  32.185  1.00 77.14           C  
ATOM   4541  CA  GLY L 350     -42.190 -19.614  34.522  1.00 27.48           C  
ATOM   4542  CA  ALA L 351     -45.628 -20.947  35.146  1.00 39.03           C  
ATOM   4543  CA  THR L 352     -47.142 -23.059  32.451  1.00104.13           C  
ATOM   4544  CA  LEU L 353     -49.906 -21.696  30.326  1.00 59.81           C  
ATOM   4545  CA  SER L 354     -53.056 -23.279  29.032  1.00 41.72           C  
ATOM   4546  CA  ASP L 355     -55.586 -22.123  26.491  1.00135.40           C  
ATOM   4547  CA  GLY L 356     -59.373 -21.824  26.855  1.00 63.84           C  
ATOM   4548  CA  GLN L 357     -60.980 -20.692  30.034  1.00198.58           C  
ATOM   4549  CA  LEU L 358     -60.513 -24.198  30.416  1.00243.06           C  
ATOM   4550  CA  LYS L 359     -63.966 -25.231  30.983  1.00207.31           C  
ATOM   4551  CA  ASP L 360     -65.712 -21.947  30.790  1.00 49.95           C  
ATOM   4552  CA  GLY L 361     -65.965 -19.460  28.025  1.00 28.28           C  
ATOM   4553  CA  GLY L 362     -62.451 -18.443  27.279  1.00 37.02           C  
ATOM   4554  CA  LYS L 363     -61.717 -15.485  29.471  1.00152.96           C  
ATOM   4555  CA  GLY L 364     -58.223 -15.993  28.266  1.00 35.06           C  
ATOM   4556  CA  ILE L 365     -55.106 -18.043  28.763  1.00 67.47           C  
ATOM   4557  CA  LYS L 366     -54.658 -19.605  32.144  1.00 73.65           C  
ATOM   4558  CA  ILE L 367     -51.385 -19.983  33.888  1.00186.62           C  
ATOM   4559  CA  ASP L 368     -51.411 -23.436  35.377  1.00 59.85           C  
ATOM   4560  CA  GLU L 369     -48.699 -23.322  37.954  1.00 93.61           C  
ATOM   4561  CA  VAL L 370     -45.951 -21.016  39.053  1.00127.23           C  
ATOM   4562  CA  VAL L 371     -42.373 -22.298  38.980  1.00183.59           C  
ATOM   4563  CA  LYS L 372     -41.732 -19.242  41.231  1.00171.38           C  
ATOM   4564  CA  GLY L 373     -37.957 -19.442  41.197  1.00 35.87           C  
ATOM   4565  CA  SER L 374     -38.433 -18.711  37.479  1.00 46.47           C  
ATOM   4566  CA  PRO L 375     -38.525 -15.265  36.063  1.00 70.14           C  
ATOM   4567  CA  ALA L 376     -42.123 -15.562  34.964  1.00 42.12           C  
ATOM   4568  CA  ALA L 377     -42.619 -15.606  38.696  1.00 49.54           C  
ATOM   4569  CA  GLN L 378     -40.425 -12.597  39.352  1.00 56.21           C  
ATOM   4570  CA  ALA L 379     -42.546 -10.047  37.490  1.00 57.76           C  
ATOM   4571  CA  GLY L 380     -45.834 -10.855  39.157  1.00 63.79           C  
ATOM   4572  CA  LEU L 381     -47.274 -13.876  37.444  1.00 66.58           C  
ATOM   4573  CA  GLN L 382     -48.937 -16.112  39.973  1.00 55.48           C  
ATOM   4574  CA  LYS L 383     -50.876 -19.249  39.253  1.00143.53           C  
ATOM   4575  CA  ASP L 384     -54.616 -19.291  38.604  1.00 82.78           C  
ATOM   4576  CA  ASP L 385     -54.430 -15.988  36.838  1.00 53.16           C  
ATOM   4577  CA  VAL L 386     -56.346 -15.644  33.649  1.00132.46           C  
ATOM   4578  CA  ILE L 387     -54.934 -13.367  31.040  1.00 64.88           C  
ATOM   4579  CA  ILE L 388     -57.936 -11.647  29.568  1.00112.57           C  
ATOM   4580  CA  GLY L 389     -55.917  -9.786  26.977  1.00 47.85           C  
ATOM   4581  CA  VAL L 390     -52.726  -7.967  26.156  1.00 61.83           C  
ATOM   4582  CA  ASN L 391     -52.100  -4.405  25.091  1.00 80.65           C  
ATOM   4583  CA  ARG L 392     -55.725  -3.353  24.844  1.00157.77           C  
ATOM   4584  CA  ASP L 393     -56.302  -6.546  22.939  1.00 53.24           C  
ATOM   4585  CA  ARG L 394     -58.508  -9.277  24.238  1.00119.38           C  
ATOM   4586  CA  VAL L 395     -56.882 -12.655  24.395  1.00 51.61           C  
ATOM   4587  CA  ASN L 396     -59.350 -15.465  23.985  1.00 62.95           C  
ATOM   4588  CA  SER L 397     -56.637 -18.025  23.623  1.00 55.62           C  
ATOM   4589  CA  ILE L 398     -52.918 -18.585  23.282  1.00 41.52           C  
ATOM   4590  CA  ALA L 399     -52.985 -18.002  19.569  1.00 24.60           C  
ATOM   4591  CA  GLU L 400     -54.455 -14.556  19.964  1.00 52.70           C  
ATOM   4592  CA  MET L 401     -52.041 -13.718  22.726  1.00 34.12           C  
ATOM   4593  CA  ARG L 402     -49.312 -14.765  20.363  1.00138.50           C  
ATOM   4594  CA  LYS L 403     -50.715 -12.297  17.896  1.00102.56           C  
ATOM   4595  CA  VAL L 404     -50.202  -9.315  20.150  1.00 31.35           C  
ATOM   4596  CA  LEU L 405     -46.729 -10.627  20.834  1.00101.54           C  
ATOM   4597  CA  ALA L 406     -46.217 -10.801  17.100  1.00 32.59           C  
ATOM   4598  CA  ALA L 407     -46.355  -7.030  17.087  1.00 31.34           C  
ATOM   4599  CA  LYS L 408     -43.599  -7.310  19.655  1.00 99.17           C  
ATOM   4600  CA  PRO L 409     -44.341  -4.040  21.313  1.00 74.77           C  
ATOM   4601  CA  ALA L 410     -41.578  -2.930  23.641  1.00 31.72           C  
ATOM   4602  CA  ILE L 411     -44.341  -2.527  26.188  1.00 87.36           C  
ATOM   4603  CA  ILE L 412     -46.416  -5.593  26.895  1.00106.12           C  
ATOM   4604  CA  ALA L 413     -49.287  -5.209  29.252  1.00 51.61           C  
ATOM   4605  CA  LEU L 414     -51.087  -8.238  30.512  1.00113.36           C  
ATOM   4606  CA  GLN L 415     -54.190  -7.858  32.473  1.00121.12           C  
ATOM   4607  CA  ILE L 416     -55.260 -10.922  34.179  1.00117.52           C  
ATOM   4608  CA  VAL L 417     -58.081 -11.521  36.527  1.00 45.42           C  
ATOM   4609  CA  ARG L 418     -57.010 -12.796  39.880  1.00 74.76           C  
ATOM   4610  CA  GLY L 419     -59.645 -13.780  42.330  1.00 18.68           C  
ATOM   4611  CA  ASN L 420     -62.548 -11.494  41.769  1.00 50.62           C  
ATOM   4612  CA  GLU L 421     -60.463  -8.552  40.699  1.00 53.46           C  
ATOM   4613  CA  SER L 422     -58.579  -7.066  37.830  1.00 45.62           C  
ATOM   4614  CA  ILE L 423     -54.853  -7.399  37.691  1.00 76.04           C  
ATOM   4615  CA  TYR L 424     -52.291  -5.986  35.403  1.00163.97           C  
ATOM   4616  CA  LEU L 425     -49.045  -7.589  34.590  1.00 91.14           C  
ATOM   4617  CA  LEU L 426     -46.271  -6.541  32.381  1.00145.01           C  
ATOM   4618  CA  MET L 427     -43.008  -7.048  30.641  1.00 85.17           C  
TER    4619      MET L 427                                                      
ATOM   4620  CA  LYS M   1     -29.062   8.918  10.304  1.00149.74           C  
ATOM   4621  CA  VAL M   2     -31.202   5.865  10.213  1.00 88.48           C  
ATOM   4622  CA  PHE M   3     -33.626   5.813   7.360  1.00 70.00           C  
ATOM   4623  CA  GLY M   4     -37.019   4.311   7.651  1.00 26.60           C  
ATOM   4624  CA  ARG M   5     -37.602   1.611   5.107  1.00196.86           C  
ATOM   4625  CA  CYS M   6     -39.983   3.722   3.092  1.00 33.95           C  
ATOM   4626  CA  GLU M   7     -37.934   6.826   3.617  1.00 45.06           C  
ATOM   4627  CA  LEU M   8     -34.891   5.119   2.258  1.00 40.57           C  
ATOM   4628  CA  ALA M   9     -36.813   3.756  -0.659  1.00 24.70           C  
ATOM   4629  CA  ALA M  10     -38.057   7.194  -1.493  1.00 22.96           C  
ATOM   4630  CA  ALA M  11     -34.605   8.641  -1.164  1.00 30.37           C  
ATOM   4631  CA  MET M  12     -33.105   5.932  -3.277  1.00 64.90           C  
ATOM   4632  CA  LYS M  13     -35.797   6.413  -5.864  1.00 29.34           C  
ATOM   4633  CA  ARG M  14     -35.125  10.125  -5.799  1.00 93.71           C  
ATOM   4634  CA  HIS M  15     -31.481   9.288  -6.329  1.00 76.74           C  
ATOM   4635  CA  GLY M  16     -32.433   7.206  -9.323  1.00 26.88           C  
ATOM   4636  CA  LEU M  17     -31.538   3.902  -7.732  1.00 60.09           C  
ATOM   4637  CA  ASP M  18     -34.919   2.471  -8.639  1.00104.88           C  
ATOM   4638  CA  ASN M  19     -34.418  -0.078 -11.340  1.00 50.42           C  
ATOM   4639  CA  TYR M  20     -30.866   1.082 -11.556  1.00 43.47           C  
ATOM   4640  CA  ARG M  21     -28.992  -1.507 -13.525  1.00138.91           C  
ATOM   4641  CA  GLY M  22     -32.263  -3.363 -13.486  1.00 19.43           C  
ATOM   4642  CA  TYR M  23     -32.308  -3.604  -9.746  1.00 47.86           C  
ATOM   4643  CA  SER M  24     -35.644  -2.740  -8.303  1.00 90.53           C  
ATOM   4644  CA  LEU M  25     -35.898  -0.387  -5.389  1.00 65.85           C  
ATOM   4645  CA  GLY M  26     -36.698  -3.250  -3.113  1.00 28.26           C  
ATOM   4646  CA  ASN M  27     -33.340  -4.743  -3.889  1.00 41.22           C  
ATOM   4647  CA  TRP M  28     -31.552  -1.576  -2.927  1.00 67.96           C  
ATOM   4648  CA  VAL M  29     -33.656  -1.125   0.159  1.00 33.74           C  
ATOM   4649  CA  CYS M  30     -33.050  -4.695   1.107  1.00 90.26           C  
ATOM   4650  CA  ALA M  31     -29.353  -4.345   0.529  1.00 25.23           C  
ATOM   4651  CA  ALA M  32     -29.333  -1.244   2.638  1.00 25.83           C  
ATOM   4652  CA  LYS M  33     -31.264  -3.017   5.328  1.00112.17           C  
ATOM   4653  CA  PHE M  34     -28.827  -5.853   5.648  1.00 80.34           C  
ATOM   4654  CA  GLU M  35     -25.778  -3.756   4.909  1.00 87.86           C  
ATOM   4655  CA  SER M  36     -26.296  -1.027   7.440  1.00 95.68           C  
ATOM   4656  CA  ASN M  37     -29.781  -1.477   8.793  1.00 66.03           C  
ATOM   4657  CA  PHE M  38     -30.530   1.783   7.025  1.00 69.71           C  
ATOM   4658  CA  ASN M  39     -27.974   3.613   9.076  1.00 41.10           C  
ATOM   4659  CA  THR M  40     -25.958   5.980   6.940  1.00 45.00           C  
ATOM   4660  CA  GLN M  41     -23.389   6.182   9.715  1.00 62.89           C  
ATOM   4661  CA  ALA M  42     -22.715   2.459   9.684  1.00 51.06           C  
ATOM   4662  CA  THR M  43     -19.085   1.673   9.204  1.00 47.80           C  
ATOM   4663  CA  ASN M  44     -17.601  -1.748   9.536  1.00 53.16           C  
ATOM   4664  CA  ARG M  45     -13.986  -2.571   9.363  1.00152.64           C  
ATOM   4665  CA  ASN M  46     -13.064  -5.482   7.208  1.00 63.98           C  
ATOM   4666  CA  THR M  47     -10.461  -7.999   8.211  1.00 29.58           C  
ATOM   4667  CA  ASP M  48      -8.417  -6.796   5.273  1.00 67.34           C  
ATOM   4668  CA  GLY M  49      -8.253  -3.379   6.824  1.00 37.72           C  
ATOM   4669  CA  SER M  50     -10.591  -1.878   4.332  1.00 60.68           C  
ATOM   4670  CA  THR M  51     -13.766  -0.653   5.773  1.00191.81           C  
ATOM   4671  CA  ASP M  52     -17.321  -0.552   4.569  1.00 54.44           C  
ATOM   4672  CA  TYR M  53     -19.085   2.707   4.893  1.00109.40           C  
ATOM   4673  CA  GLY M  54     -22.582   3.958   4.778  1.00 34.77           C  
ATOM   4674  CA  ILE M  55     -25.981   2.549   4.169  1.00 64.76           C  
ATOM   4675  CA  LEU M  56     -24.594   0.573   1.249  1.00149.92           C  
ATOM   4676  CA  GLN M  57     -21.491  -0.416   3.180  1.00 67.90           C  
ATOM   4677  CA  ILE M  58     -19.347   0.592   0.267  1.00 84.44           C  
ATOM   4678  CA  ASN M  59     -15.862  -0.777   0.710  1.00 67.52           C  
ATOM   4679  CA  SER M  60     -12.809   1.431   0.895  1.00106.37           C  
ATOM   4680  CA  ARG M  61     -10.862  -1.245  -0.824  1.00223.68           C  
ATOM   4681  CA  TRP M  62     -12.288  -0.411  -4.192  1.00114.07           C  
ATOM   4682  CA  TRP M  63     -14.794   2.402  -3.928  1.00118.95           C  
ATOM   4683  CA  CYS M  64     -13.822   5.212  -1.589  1.00 59.57           C  
ATOM   4684  CA  ASN M  65     -10.712   6.684  -0.105  1.00 69.46           C  
ATOM   4685  CA  ASP M  66     -10.422   6.346   3.648  1.00 98.77           C  
ATOM   4686  CA  GLY M  67      -6.658   6.899   3.437  1.00 47.31           C  
ATOM   4687  CA  ARG M  68      -6.484   3.894   5.754  1.00182.61           C  
ATOM   4688  CA  THR M  69      -6.694   1.188   3.171  1.00198.07           C  
ATOM   4689  CA  PRO M  70      -3.350   0.494   1.583  1.00278.80           C  
ATOM   4690  CA  GLY M  71      -3.507  -0.757  -2.002  1.00240.74           C  
ATOM   4691  CA  SER M  72      -7.105   0.369  -2.275  1.00140.37           C  
ATOM   4692  CA  ARG M  73      -8.547   2.404  -5.021  1.00175.10           C  
ATOM   4693  CA  ASN M  74     -11.253   4.962  -4.812  1.00 93.79           C  
ATOM   4694  CA  LEU M  75     -13.314   4.213  -7.878  1.00 60.10           C  
ATOM   4695  CA  CYS M  76     -16.103   6.394  -6.612  1.00 71.01           C  
ATOM   4696  CA  ASN M  77     -13.557   9.157  -6.198  1.00 57.66           C  
ATOM   4697  CA  ILE M  78     -15.042  10.173  -2.923  1.00128.61           C  
ATOM   4698  CA  PRO M  79     -13.825  10.204   0.599  1.00 77.18           C  
ATOM   4699  CA  CYS M  80     -15.388   7.258   2.278  1.00 94.90           C  
ATOM   4700  CA  SER M  81     -16.641   9.719   4.842  1.00 80.91           C  
ATOM   4701  CA  ALA M  82     -18.911  11.015   2.120  1.00 38.75           C  
ATOM   4702  CA  LEU M  83     -20.592   7.624   2.258  1.00 73.00           C  
ATOM   4703  CA  LEU M  84     -21.557   8.348   5.882  1.00 67.07           C  
ATOM   4704  CA  SER M  85     -23.621  11.418   5.007  1.00 46.99           C  
ATOM   4705  CA  SER M  86     -27.277  11.592   5.890  1.00 29.98           C  
ATOM   4706  CA  ASP M  87     -27.650  12.579   2.292  1.00 47.35           C  
ATOM   4707  CA  ILE M  88     -27.638   9.321   0.352  1.00156.21           C  
ATOM   4708  CA  THR M  89     -26.427  10.839  -2.910  1.00 61.28           C  
ATOM   4709  CA  ALA M  90     -22.777   9.978  -2.523  1.00 33.12           C  
ATOM   4710  CA  SER M  91     -23.613   6.437  -1.564  1.00 71.92           C  
ATOM   4711  CA  VAL M  92     -26.099   6.147  -4.388  1.00 41.98           C  
ATOM   4712  CA  ASN M  93     -23.741   7.489  -6.980  1.00 24.23           C  
ATOM   4713  CA  CYS M  94     -21.048   5.211  -5.691  1.00 31.73           C  
ATOM   4714  CA  ALA M  95     -23.521   2.356  -5.575  1.00 29.10           C  
ATOM   4715  CA  LYS M  96     -24.404   3.008  -9.158  1.00 28.43           C  
ATOM   4716  CA  LYS M  97     -20.757   2.653 -10.036  1.00114.79           C  
ATOM   4717  CA  ILE M  98     -20.493  -0.497  -7.987  1.00 39.62           C  
ATOM   4718  CA  VAL M  99     -23.563  -2.089  -9.471  1.00 93.73           C  
ATOM   4719  CA  SER M 100     -22.217  -1.220 -12.902  1.00 46.17           C  
ATOM   4720  CA  ASP M 101     -19.120  -3.185 -11.926  1.00 49.08           C  
ATOM   4721  CA  GLY M 102     -20.527  -6.163 -13.772  1.00 26.87           C  
ATOM   4722  CA  ASN M 103     -20.950  -8.144 -10.595  1.00 41.89           C  
ATOM   4723  CA  GLY M 104     -24.222  -6.354 -10.165  1.00 21.70           C  
ATOM   4724  CA  MET M 105     -25.741  -6.263  -6.709  1.00 70.25           C  
ATOM   4725  CA  ASN M 106     -23.758  -9.376  -5.915  1.00 56.91           C  
ATOM   4726  CA  ALA M 107     -21.058  -6.895  -4.993  1.00 38.56           C  
ATOM   4727  CA  TRP M 108     -23.024  -6.460  -1.817  1.00 62.63           C  
ATOM   4728  CA  VAL M 109     -22.577  -9.760  -0.050  1.00 80.53           C  
ATOM   4729  CA  ALA M 110     -25.511  -9.119   2.215  1.00 18.84           C  
ATOM   4730  CA  TRP M 111     -27.615  -8.463  -0.816  1.00 48.77           C  
ATOM   4731  CA  ARG M 112     -26.599 -11.658  -2.471  1.00112.66           C  
ATOM   4732  CA  ASN M 113     -27.095 -13.709   0.612  1.00 50.92           C  
ATOM   4733  CA  ARG M 114     -30.124 -11.971   2.053  1.00186.66           C  
ATOM   4734  CA  CYS M 115     -31.701 -10.023  -0.789  1.00 67.00           C  
ATOM   4735  CA  LYS M 116     -31.252 -12.012  -3.923  1.00 75.76           C  
ATOM   4736  CA  GLY M 117     -34.234 -14.105  -4.880  1.00 40.84           C  
ATOM   4737  CA  THR M 118     -36.265 -12.953  -1.898  1.00 87.18           C  
ATOM   4738  CA  ASP M 119     -39.290 -10.697  -1.598  1.00131.91           C  
ATOM   4739  CA  VAL M 120     -37.448  -7.562  -2.391  1.00 57.34           C  
ATOM   4740  CA  GLN M 121     -40.780  -5.953  -3.096  1.00 67.26           C  
ATOM   4741  CA  ALA M 122     -41.725  -6.314   0.515  1.00 51.75           C  
ATOM   4742  CA  TRP M 123     -39.121  -3.747   1.313  1.00 81.99           C  
ATOM   4743  CA  ILE M 124     -40.905  -1.204  -0.872  1.00156.34           C  
ATOM   4744  CA  ARG M 125     -44.463  -2.323  -0.188  1.00139.80           C  
ATOM   4745  CA  GLY M 126     -46.678   0.135   1.627  1.00 22.73           C  
ATOM   4746  CA  CYS M 127     -44.295   2.876   0.731  1.00 43.73           C  
ATOM   4747  CA  ARG M 128     -45.571   5.803  -1.203  1.00169.25           C  
ATOM   4748  CA  LEU M 129     -42.844   6.080  -3.731  1.00 38.02           C  
TER    4749      LEU M 129                                                      
ATOM   4750  CA  LYS N   1      12.223  11.058  28.754  1.00158.66           C  
ATOM   4751  CA  VAL N   2      12.471   8.286  31.219  1.00 96.98           C  
ATOM   4752  CA  PHE N   3       9.584   8.265  33.600  1.00 74.91           C  
ATOM   4753  CA  GLY N   4       9.891   7.121  37.137  1.00 26.74           C  
ATOM   4754  CA  ARG N   5       7.565   4.296  37.988  1.00194.93           C  
ATOM   4755  CA  CYS N   6       5.303   6.472  40.094  1.00 41.69           C  
ATOM   4756  CA  GLU N   7       5.609   9.353  37.711  1.00 35.74           C  
ATOM   4757  CA  LEU N   8       4.551   7.188  34.833  1.00 42.67           C  
ATOM   4758  CA  ALA N   9       1.706   5.753  36.815  1.00 25.35           C  
ATOM   4759  CA  ALA N  10       0.515   9.219  37.647  1.00 23.12           C  
ATOM   4760  CA  ALA N  11       0.778  10.306  34.067  1.00 27.86           C  
ATOM   4761  CA  MET N  12      -0.980   7.201  32.861  1.00 31.54           C  
ATOM   4762  CA  LYS N  13      -3.709   7.764  35.389  1.00 34.86           C  
ATOM   4763  CA  ARG N  14      -3.943  11.355  34.291  1.00120.80           C  
ATOM   4764  CA  HIS N  15      -4.294  10.090  30.756  1.00 83.87           C  
ATOM   4765  CA  GLY N  16      -7.084   7.819  31.912  1.00 31.40           C  
ATOM   4766  CA  LEU N  17      -5.183   4.587  31.423  1.00 53.96           C  
ATOM   4767  CA  ASP N  18      -5.981   3.515  34.954  1.00 49.03           C  
ATOM   4768  CA  ASN N  19      -8.500   0.713  34.731  1.00 51.75           C  
ATOM   4769  CA  TYR N  20      -8.687   1.365  31.033  1.00 46.74           C  
ATOM   4770  CA  ARG N  21     -10.393  -1.574  29.426  1.00121.60           C  
ATOM   4771  CA  GLY N  22     -10.248  -3.076  32.868  1.00 22.10           C  
ATOM   4772  CA  TYR N  23      -6.513  -2.922  33.032  1.00 53.26           C  
ATOM   4773  CA  SER N  24      -5.247  -1.602  36.294  1.00 32.23           C  
ATOM   4774  CA  LEU N  25      -2.604   1.069  36.274  1.00 47.32           C  
ATOM   4775  CA  GLY N  26      -0.094  -1.467  37.455  1.00 22.95           C  
ATOM   4776  CA  ASN N  27      -0.620  -3.397  34.273  1.00 33.47           C  
ATOM   4777  CA  TRP N  28       0.111  -0.371  32.160  1.00 53.62           C  
ATOM   4778  CA  VAL N  29       3.066   0.589  34.276  1.00 31.82           C  
ATOM   4779  CA  CYS N  30       4.498  -2.860  34.132  1.00 42.81           C  
ATOM   4780  CA  ALA N  31       3.896  -3.013  30.414  1.00 22.54           C  
ATOM   4781  CA  ALA N  32       5.680   0.272  30.038  1.00 24.11           C  
ATOM   4782  CA  LYS N  33       8.471  -0.970  32.214  1.00 98.01           C  
ATOM   4783  CA  PHE N  34       9.137  -4.021  30.122  1.00 76.80           C  
ATOM   4784  CA  GLU N  35       8.300  -2.374  26.831  1.00 87.67           C  
ATOM   4785  CA  SER N  36      10.527   0.630  27.095  1.00101.39           C  
ATOM   4786  CA  ASN N  37      11.866   0.802  30.621  1.00 88.99           C  
ATOM   4787  CA  PHE N  38       9.713   3.888  30.971  1.00 86.19           C  
ATOM   4788  CA  ASN N  39      11.681   5.517  28.205  1.00 47.49           C  
ATOM   4789  CA  THR N  40       9.398   7.509  25.952  1.00 45.03           C  
ATOM   4790  CA  GLN N  41      12.182   7.618  23.385  1.00 60.37           C  
ATOM   4791  CA  ALA N  42      12.541   3.857  23.125  1.00 50.93           C  
ATOM   4792  CA  THR N  43      12.185   2.548  19.622  1.00 46.08           C  
ATOM   4793  CA  ASN N  44      12.864  -0.987  18.531  1.00 48.97           C  
ATOM   4794  CA  ARG N  45      12.931  -2.295  15.008  1.00 68.00           C  
ATOM   4795  CA  ASN N  46      10.930  -5.396  14.372  1.00 54.17           C  
ATOM   4796  CA  THR N  47      12.056  -8.123  12.025  1.00 94.77           C  
ATOM   4797  CA  ASP N  48       9.148  -7.305   9.756  1.00 73.92           C  
ATOM   4798  CA  GLY N  49      10.508  -3.829   9.333  1.00 32.63           C  
ATOM   4799  CA  SER N  50       7.896  -2.256  11.496  1.00 42.70           C  
ATOM   4800  CA  THR N  51       9.158  -0.490  14.547  1.00 44.69           C  
ATOM   4801  CA  ASP N  52       7.829  -0.248  18.069  1.00 42.48           C  
ATOM   4802  CA  TYR N  53       7.845   3.221  19.440  1.00 88.28           C  
ATOM   4803  CA  GLY N  54       7.547   4.871  22.784  1.00 33.55           C  
ATOM   4804  CA  ILE N  55       6.891   3.808  26.318  1.00103.80           C  
ATOM   4805  CA  LEU N  56       4.226   1.445  25.041  1.00 92.15           C  
ATOM   4806  CA  GLN N  57       6.380   0.298  22.139  1.00 71.71           C  
ATOM   4807  CA  ILE N  58       3.430   0.747  19.847  1.00 65.59           C  
ATOM   4808  CA  ASN N  59       4.098  -0.905  16.519  1.00 62.46           C  
ATOM   4809  CA  SER N  60       4.083   1.020  13.264  1.00 52.33           C  
ATOM   4810  CA  ARG N  61       2.730  -2.033  11.563  1.00237.41           C  
ATOM   4811  CA  TRP N  62      -0.753  -1.336  12.783  1.00118.07           C  
ATOM   4812  CA  TRP N  63      -0.778   1.726  14.986  1.00123.00           C  
ATOM   4813  CA  CYS N  64       1.326   4.629  13.782  1.00 62.61           C  
ATOM   4814  CA  ASN N  65       2.895   5.930  10.637  1.00 75.03           C  
ATOM   4815  CA  ASP N  66       6.666   5.842  10.678  1.00 97.48           C  
ATOM   4816  CA  GLY N  67       6.300   5.681   6.957  1.00 47.08           C  
ATOM   4817  CA  ARG N  68       8.978   3.041   6.725  1.00232.00           C  
ATOM   4818  CA  THR N  69       6.582   0.190   7.262  1.00 87.54           C  
ATOM   4819  CA  PRO N  70       5.150  -0.743   3.894  1.00369.73           C  
ATOM   4820  CA  GLY N  71       1.654  -2.233   4.096  1.00241.20           C  
ATOM   4821  CA  SER N  72       1.303  -0.859   7.620  1.00 82.11           C  
ATOM   4822  CA  ARG N  73      -1.715   0.871   8.905  1.00138.08           C  
ATOM   4823  CA  ASN N  74      -1.836   3.917  11.094  1.00 74.47           C  
ATOM   4824  CA  LEU N  75      -4.824   3.043  13.238  1.00 59.89           C  
ATOM   4825  CA  CYS N  76      -3.846   5.569  15.855  1.00 61.46           C  
ATOM   4826  CA  ASN N  77      -3.605   8.073  13.020  1.00 62.57           C  
ATOM   4827  CA  ILE N  78      -0.471   9.538  14.434  1.00 49.27           C  
ATOM   4828  CA  PRO N  79       3.062   9.693  13.324  1.00 83.13           C  
ATOM   4829  CA  CYS N  80       4.969   7.136  15.247  1.00 94.57           C  
ATOM   4830  CA  SER N  81       7.269   9.944  16.269  1.00 82.63           C  
ATOM   4831  CA  ALA N  82       4.361  11.227  18.289  1.00 39.83           C  
ATOM   4832  CA  LEU N  83       4.725   8.065  20.344  1.00 67.19           C  
ATOM   4833  CA  LEU N  84       8.237   9.192  21.312  1.00 66.86           C  
ATOM   4834  CA  SER N  85       7.046  12.407  22.974  1.00 97.72           C  
ATOM   4835  CA  SER N  86       7.709  13.060  26.620  1.00 38.07           C  
ATOM   4836  CA  ASP N  87       4.012  13.736  26.705  1.00 55.10           C  
ATOM   4837  CA  ILE N  88       2.439  10.310  27.072  1.00185.66           C  
ATOM   4838  CA  THR N  89      -0.908  11.379  25.651  1.00 63.48           C  
ATOM   4839  CA  ALA N  90      -0.327  10.144  22.131  1.00 32.04           C  
ATOM   4840  CA  SER N  91       0.955   6.826  23.415  1.00 82.02           C  
ATOM   4841  CA  VAL N  92      -1.909   6.526  25.828  1.00 38.21           C  
ATOM   4842  CA  ASN N  93      -4.541   7.357  23.273  1.00 29.36           C  
ATOM   4843  CA  CYS N  94      -2.959   4.913  20.904  1.00 33.42           C  
ATOM   4844  CA  ALA N  95      -2.653   2.361  23.674  1.00 27.64           C  
ATOM   4845  CA  LYS N  96      -6.297   2.779  24.418  1.00 26.66           C  
ATOM   4846  CA  LYS N  97      -7.085   1.917  20.847  1.00 56.12           C  
ATOM   4847  CA  ILE N  98      -4.680  -0.986  20.927  1.00 37.03           C  
ATOM   4848  CA  VAL N  99      -6.080  -2.394  24.134  1.00 91.97           C  
ATOM   4849  CA  SER N 100      -9.542  -2.024  22.646  1.00 43.76           C  
ATOM   4850  CA  ASP N 101      -8.311  -4.165  19.763  1.00 45.68           C  
ATOM   4851  CA  GLY N 102      -9.825  -7.180  21.476  1.00 27.53           C  
ATOM   4852  CA  ASN N 103      -6.516  -8.798  22.280  1.00 37.85           C  
ATOM   4853  CA  GLY N 104      -6.377  -6.539  25.281  1.00 23.22           C  
ATOM   4854  CA  MET N 105      -2.995  -6.050  26.909  1.00 54.65           C  
ATOM   4855  CA  ASN N 106      -1.851  -9.225  25.221  1.00 55.19           C  
ATOM   4856  CA  ALA N 107      -1.122  -6.954  22.289  1.00 39.27           C  
ATOM   4857  CA  TRP N 108       1.959  -6.020  24.226  1.00 57.20           C  
ATOM   4858  CA  VAL N 109       4.034  -9.165  24.230  1.00 30.23           C  
ATOM   4859  CA  ALA N 110       6.139  -7.950  27.093  1.00 20.07           C  
ATOM   4860  CA  TRP N 111       3.008  -7.394  29.086  1.00 48.31           C  
ATOM   4861  CA  ARG N 112       1.746 -10.832  28.329  1.00 85.62           C  
ATOM   4862  CA  ASN N 113       4.956 -12.510  29.238  1.00 57.59           C  
ATOM   4863  CA  ARG N 114       6.121 -10.248  32.042  1.00113.37           C  
ATOM   4864  CA  CYS N 115       2.989  -8.492  33.266  1.00 66.61           C  
ATOM   4865  CA  LYS N 116       0.189 -10.935  32.917  1.00 82.53           C  
ATOM   4866  CA  GLY N 117      -0.805 -12.736  36.072  1.00 23.93           C  
ATOM   4867  CA  THR N 118       1.805 -10.953  38.081  1.00 93.59           C  
ATOM   4868  CA  ASP N 119       1.338  -8.706  41.036  1.00 44.25           C  
ATOM   4869  CA  VAL N 120       1.020  -5.707  38.759  1.00 42.56           C  
ATOM   4870  CA  GLN N 121      -0.101  -3.648  41.715  1.00 95.23           C  
ATOM   4871  CA  ALA N 122       3.472  -3.633  42.872  1.00 39.02           C  
ATOM   4872  CA  TRP N 123       4.225  -1.307  40.021  1.00 87.61           C  
ATOM   4873  CA  ILE N 124       1.717   1.114  41.503  1.00215.06           C  
ATOM   4874  CA  ARG N 125       3.105   0.492  45.009  1.00332.53           C  
ATOM   4875  CA  GLY N 126       3.765   3.487  47.215  1.00114.97           C  
ATOM   4876  CA  CYS N 127       3.079   5.898  44.367  1.00 85.14           C  
ATOM   4877  CA  ARG N 128       0.614   8.590  45.251  1.00 56.14           C  
ATOM   4878  CA  LEU N 129      -1.653   8.632  42.294  1.00 86.15           C  
TER    4879      LEU N 129                                                      
ATOM   4880  CA  LYS O   1      31.815  10.423 -11.660  1.00 87.53           C  
ATOM   4881  CA  VAL O   2      34.138   7.563 -12.317  1.00 35.53           C  
ATOM   4882  CA  PHE O   3      36.626   7.365  -9.520  1.00 69.31           C  
ATOM   4883  CA  GLY O   4      40.113   6.065  -9.983  1.00 26.22           C  
ATOM   4884  CA  ARG O   5      40.776   3.213  -7.675  1.00122.67           C  
ATOM   4885  CA  CYS O   6      43.171   5.177  -5.525  1.00 33.25           C  
ATOM   4886  CA  GLU O   7      40.988   8.224  -5.694  1.00 37.60           C  
ATOM   4887  CA  LEU O   8      38.026   6.268  -4.490  1.00 43.24           C  
ATOM   4888  CA  ALA O   9      40.060   4.675  -1.765  1.00 22.95           C  
ATOM   4889  CA  ALA O  10      41.138   8.077  -0.597  1.00 22.97           C  
ATOM   4890  CA  ALA O  11      37.595   9.339  -0.707  1.00 28.13           C  
ATOM   4891  CA  MET O  12      36.323   6.299   1.110  1.00 81.75           C  
ATOM   4892  CA  LYS O  13      39.059   6.704   3.671  1.00121.52           C  
ATOM   4893  CA  ARG O  14      38.213  10.346   4.089  1.00 31.72           C  
ATOM   4894  CA  HIS O  15      34.609   9.367   4.601  1.00 77.68           C  
ATOM   4895  CA  GLY O  16      35.726   6.952   7.264  1.00 31.30           C  
ATOM   4896  CA  LEU O  17      34.951   3.776   5.386  1.00 61.62           C  
ATOM   4897  CA  ASP O  18      38.450   2.485   5.972  1.00 46.88           C  
ATOM   4898  CA  ASN O  19      38.195  -0.310   8.485  1.00 47.65           C  
ATOM   4899  CA  TYR O  20      34.586   0.605   8.962  1.00 52.37           C  
ATOM   4900  CA  ARG O  21      32.938  -2.280  10.691  1.00120.13           C  
ATOM   4901  CA  GLY O  22      36.272  -3.977  10.337  1.00 20.66           C  
ATOM   4902  CA  TYR O  23      36.209  -3.854   6.596  1.00 52.44           C  
ATOM   4903  CA  SER O  24      39.456  -2.700   5.156  1.00 34.69           C  
ATOM   4904  CA  LEU O  25      39.556   0.012   2.567  1.00101.87           C  
ATOM   4905  CA  GLY O  26      40.405  -2.577  -0.037  1.00 24.11           C  
ATOM   4906  CA  ASN O  27      37.149  -4.324   0.650  1.00 34.78           C  
ATOM   4907  CA  TRP O  28      35.182  -1.172   0.034  1.00 59.10           C  
ATOM   4908  CA  VAL O  29      37.142  -0.333  -3.052  1.00 39.85           C  
ATOM   4909  CA  CYS O  30      36.766  -3.773  -4.436  1.00111.30           C  
ATOM   4910  CA  ALA O  31      33.079  -3.733  -3.654  1.00 27.09           C  
ATOM   4911  CA  ALA O  32      32.823  -0.440  -5.434  1.00 29.63           C  
ATOM   4912  CA  LYS O  33      34.772  -1.771  -8.343  1.00111.61           C  
ATOM   4913  CA  PHE O  34      32.509  -4.714  -8.897  1.00 73.39           C  
ATOM   4914  CA  GLU O  35      29.373  -2.890  -7.870  1.00 90.54           C  
ATOM   4915  CA  SER O  36      29.692   0.066 -10.166  1.00114.62           C  
ATOM   4916  CA  ASN O  37      33.211   0.012 -11.555  1.00137.93           C  
ATOM   4917  CA  PHE O  38      33.779   3.123  -9.483  1.00 74.57           C  
ATOM   4918  CA  ASN O  39      31.046   4.875 -11.390  1.00 45.61           C  
ATOM   4919  CA  THR O  40      29.032   6.876  -8.936  1.00111.29           C  
ATOM   4920  CA  GLN O  41      26.304   7.357 -11.517  1.00111.10           C  
ATOM   4921  CA  ALA O  42      25.873   3.621 -12.010  1.00 57.50           C  
ATOM   4922  CA  THR O  43      22.364   2.463 -11.464  1.00122.76           C  
ATOM   4923  CA  ASN O  44      20.977  -0.929 -12.232  1.00 51.75           C  
ATOM   4924  CA  ARG O  45      17.391  -2.012 -12.205  1.00163.25           C  
ATOM   4925  CA  ASN O  46      16.696  -5.124 -10.271  1.00 72.05           C  
ATOM   4926  CA  THR O  47      14.238  -7.711 -11.479  1.00 86.56           C  
ATOM   4927  CA  ASP O  48      12.215  -7.016  -8.378  1.00 62.86           C  
ATOM   4928  CA  GLY O  49      11.810  -3.446  -9.516  1.00 27.94           C  
ATOM   4929  CA  SER O  50      14.195  -2.079  -6.963  1.00 96.65           C  
ATOM   4930  CA  THR O  51      17.207  -0.317  -8.303  1.00 41.51           C  
ATOM   4931  CA  ASP O  52      20.786  -0.316  -7.115  1.00 39.97           C  
ATOM   4932  CA  TYR O  53      22.326   3.083  -7.117  1.00 67.89           C  
ATOM   4933  CA  GLY O  54      25.761   4.559  -6.957  1.00 33.10           C  
ATOM   4934  CA  ILE O  55      29.243   3.262  -6.537  1.00133.65           C  
ATOM   4935  CA  LEU O  56      27.981   1.042  -3.734  1.00 98.57           C  
ATOM   4936  CA  GLN O  57      24.971  -0.040  -5.769  1.00 66.61           C  
ATOM   4937  CA  ILE O  58      22.819   0.559  -2.746  1.00 66.81           C  
ATOM   4938  CA  ASN O  59      19.424  -1.011  -3.283  1.00 60.63           C  
ATOM   4939  CA  SER O  60      16.267   1.075  -3.194  1.00 40.89           C  
ATOM   4940  CA  ARG O  61      14.513  -1.913  -1.786  1.00159.59           C  
ATOM   4941  CA  TRP O  62      15.952  -1.335   1.647  1.00118.61           C  
ATOM   4942  CA  TRP O  63      18.236   1.661   1.680  1.00122.71           C  
ATOM   4943  CA  CYS O  64      17.077   4.656  -0.298  1.00 51.06           C  
ATOM   4944  CA  ASN O  65      13.921   5.913  -1.791  1.00 82.53           C  
ATOM   4945  CA  ASP O  66      13.580   6.071  -5.539  1.00 94.70           C  
ATOM   4946  CA  GLY O  67       9.792   6.349  -5.223  1.00 47.71           C  
ATOM   4947  CA  ARG O  68       9.775   3.481  -7.722  1.00138.03           C  
ATOM   4948  CA  THR O  69      10.071   0.520  -5.417  1.00 86.64           C  
ATOM   4949  CA  PRO O  70       6.851  -0.348  -3.794  1.00116.52           C  
ATOM   4950  CA  GLY O  71       7.323  -2.082  -0.414  1.00 70.09           C  
ATOM   4951  CA  SER O  72      10.819  -0.709  -0.159  1.00119.07           C  
ATOM   4952  CA  ARG O  73      12.244   0.928   2.885  1.00130.25           C  
ATOM   4953  CA  ASN O  74      14.458   3.960   2.921  1.00 68.28           C  
ATOM   4954  CA  LEU O  75      16.691   3.024   5.821  1.00 46.80           C  
ATOM   4955  CA  CYS O  76      19.364   5.431   4.702  1.00 59.83           C  
ATOM   4956  CA  ASN O  77      16.625   8.031   4.615  1.00 55.22           C  
ATOM   4957  CA  ILE O  78      17.976   9.460   1.437  1.00 51.46           C  
ATOM   4958  CA  PRO O  79      16.713   9.739  -2.047  1.00 69.25           C  
ATOM   4959  CA  CYS O  80      18.453   7.103  -4.107  1.00 36.79           C  
ATOM   4960  CA  SER O  81      19.499   9.945  -6.344  1.00 36.89           C  
ATOM   4961  CA  ALA O  82      21.733  11.077  -3.524  1.00 36.30           C  
ATOM   4962  CA  LEU O  83      23.611   7.828  -4.046  1.00 67.66           C  
ATOM   4963  CA  LEU O  84      24.502   8.950  -7.581  1.00109.67           C  
ATOM   4964  CA  SER O  85      26.339  12.097  -6.506  1.00101.52           C  
ATOM   4965  CA  SER O  86      29.988  12.548  -7.329  1.00 73.93           C  
ATOM   4966  CA  ASP O  87      30.382  13.165  -3.654  1.00 49.40           C  
ATOM   4967  CA  ILE O  88      30.553   9.729  -2.057  1.00 85.06           C  
ATOM   4968  CA  THR O  89      29.345  10.902   1.360  1.00 59.42           C  
ATOM   4969  CA  ALA O  90      25.749   9.818   0.920  1.00 31.55           C  
ATOM   4970  CA  SER O  91      26.804   6.447  -0.400  1.00 81.62           C  
ATOM   4971  CA  VAL O  92      29.333   6.055   2.358  1.00 34.32           C  
ATOM   4972  CA  ASN O  93      26.952   6.973   5.105  1.00 30.87           C  
ATOM   4973  CA  CYS O  94      24.364   4.688   3.626  1.00 30.82           C  
ATOM   4974  CA  ALA O  95      27.001   2.008   3.215  1.00 27.99           C  
ATOM   4975  CA  LYS O  96      27.930   2.412   6.827  1.00 69.20           C  
ATOM   4976  CA  LYS O  97      24.364   1.703   7.791  1.00 70.49           C  
ATOM   4977  CA  ILE O  98      24.212  -1.190   5.381  1.00 38.34           C  
ATOM   4978  CA  VAL O  99      27.394  -2.763   6.651  1.00 96.27           C  
ATOM   4979  CA  SER O 100      26.099  -2.203  10.157  1.00 95.67           C  
ATOM   4980  CA  ASP O 101      23.107  -4.304   9.135  1.00 52.50           C  
ATOM   4981  CA  GLY O 102      24.765  -7.365  10.609  1.00 28.94           C  
ATOM   4982  CA  ASN O 103      25.104  -8.951   7.211  1.00 44.43           C  
ATOM   4983  CA  GLY O 104      28.313  -7.031   6.930  1.00 21.97           C  
ATOM   4984  CA  MET O 105      29.741  -6.531   3.468  1.00 72.10           C  
ATOM   4985  CA  ASN O 106      27.857  -9.636   2.432  1.00 53.11           C  
ATOM   4986  CA  ALA O 107      25.043  -7.193   1.806  1.00 40.01           C  
ATOM   4987  CA  TRP O 108      26.881  -6.379  -1.373  1.00 57.42           C  
ATOM   4988  CA  VAL O 109      26.508  -9.476  -3.475  1.00 28.46           C  
ATOM   4989  CA  ALA O 110      29.379  -8.502  -5.691  1.00 26.98           C  
ATOM   4990  CA  TRP O 111      31.559  -8.048  -2.670  1.00 54.96           C  
ATOM   4991  CA  ARG O 112      30.652 -11.394  -1.263  1.00 79.07           C  
ATOM   4992  CA  ASN O 113      31.058 -13.023  -4.598  1.00158.57           C  
ATOM   4993  CA  ARG O 114      34.125 -11.271  -5.934  1.00120.34           C  
ATOM   4994  CA  CYS O 115      35.635  -9.426  -2.972  1.00 89.59           C  
ATOM   4995  CA  LYS O 116      35.266 -11.546   0.076  1.00 71.74           C  
ATOM   4996  CA  GLY O 117      38.115 -14.062  -0.094  1.00 42.99           C  
ATOM   4997  CA  THR O 118      40.396 -12.130  -2.414  1.00 56.38           C  
ATOM   4998  CA  ASP O 119      43.361  -9.913  -1.812  1.00 49.17           C  
ATOM   4999  CA  VAL O 120      41.345  -6.776  -1.291  1.00 47.15           C  
ATOM   5000  CA  GLN O 121      44.595  -5.069  -0.384  1.00 59.59           C  
ATOM   5001  CA  ALA O 122      45.479  -4.987  -4.030  1.00 36.23           C  
ATOM   5002  CA  TRP O 123      42.739  -2.482  -4.564  1.00 81.72           C  
ATOM   5003  CA  ILE O 124      44.433  -0.077  -2.143  1.00 67.73           C  
ATOM   5004  CA  ARG O 125      47.997  -0.994  -3.149  1.00 75.76           C  
ATOM   5005  CA  GLY O 126      50.133   1.857  -4.374  1.00 22.13           C  
ATOM   5006  CA  CYS O 127      47.531   4.309  -3.307  1.00 43.21           C  
ATOM   5007  CA  ARG O 128      48.656   7.200  -1.226  1.00120.24           C  
ATOM   5008  CA  LEU O 129      46.004   7.164   1.407  1.00 78.58           C  
TER    5009      LEU O 129                                                      
ATOM   5010  CA  LYS P   1      -8.002  12.123 -31.470  1.00 55.05           C  
ATOM   5011  CA  VAL P   2      -8.684   9.279 -33.754  1.00111.94           C  
ATOM   5012  CA  PHE P   3      -5.889   8.853 -36.195  1.00 72.56           C  
ATOM   5013  CA  GLY P   4      -6.369   7.597 -39.665  1.00 22.79           C  
ATOM   5014  CA  ARG P   5      -4.421   4.496 -40.520  1.00144.74           C  
ATOM   5015  CA  CYS P   6      -1.988   6.417 -42.680  1.00 45.36           C  
ATOM   5016  CA  GLU P   7      -1.945   9.405 -40.408  1.00 86.51           C  
ATOM   5017  CA  LEU P   8      -0.965   7.285 -37.498  1.00 42.33           C  
ATOM   5018  CA  ALA P   9       1.685   5.524 -39.483  1.00 25.52           C  
ATOM   5019  CA  ALA P  10       3.124   8.833 -40.519  1.00 23.55           C  
ATOM   5020  CA  ALA P  11       3.016  10.105 -36.977  1.00 24.75           C  
ATOM   5021  CA  MET P  12       4.616   6.983 -35.642  1.00 26.14           C  
ATOM   5022  CA  LYS P  13       7.260   7.131 -38.296  1.00 49.38           C  
ATOM   5023  CA  ARG P  14       7.925  10.734 -37.497  1.00 72.16           C  
ATOM   5024  CA  HIS P  15       8.269   9.732 -33.876  1.00 79.50           C  
ATOM   5025  CA  GLY P  16      10.761   7.111 -34.904  1.00 32.42           C  
ATOM   5026  CA  LEU P  17       8.618   4.091 -34.184  1.00 56.29           C  
ATOM   5027  CA  ASP P  18       9.208   2.776 -37.684  1.00 62.95           C  
ATOM   5028  CA  ASN P  19      11.463  -0.232 -37.347  1.00 55.26           C  
ATOM   5029  CA  TYR P  20      11.913   0.632 -33.720  1.00 48.62           C  
ATOM   5030  CA  ARG P  21      13.351  -2.368 -31.977  1.00130.56           C  
ATOM   5031  CA  GLY P  22      12.992  -4.006 -35.343  1.00 21.30           C  
ATOM   5032  CA  TYR P  23       9.272  -3.588 -35.414  1.00 54.91           C  
ATOM   5033  CA  SER P  24       7.987  -2.371 -38.724  1.00 82.12           C  
ATOM   5034  CA  LEU P  25       5.605   0.535 -38.797  1.00 52.71           C  
ATOM   5035  CA  GLY P  26       2.855  -1.830 -39.771  1.00 27.62           C  
ATOM   5036  CA  ASN P  27       3.318  -3.601 -36.472  1.00 46.10           C  
ATOM   5037  CA  TRP P  28       2.930  -0.407 -34.536  1.00 60.85           C  
ATOM   5038  CA  VAL P  29      -0.039   0.675 -36.586  1.00 31.80           C  
ATOM   5039  CA  CYS P  30      -1.638  -2.702 -36.215  1.00116.82           C  
ATOM   5040  CA  ALA P  31      -1.000  -2.680 -32.507  1.00 22.50           C  
ATOM   5041  CA  ALA P  32      -2.523   0.750 -32.322  1.00 23.98           C  
ATOM   5042  CA  LYS P  33      -5.496  -0.365 -34.324  1.00103.79           C  
ATOM   5043  CA  PHE P  34      -6.284  -3.270 -32.077  1.00 71.80           C  
ATOM   5044  CA  GLU P  35      -5.232  -1.484 -28.927  1.00 88.05           C  
ATOM   5045  CA  SER P  36      -7.241   1.662 -29.292  1.00 98.52           C  
ATOM   5046  CA  ASN P  37      -8.668   1.726 -32.775  1.00 56.19           C  
ATOM   5047  CA  PHE P  38      -6.300   4.619 -33.342  1.00 71.73           C  
ATOM   5048  CA  ASN P  39      -8.020   6.605 -30.675  1.00 44.78           C  
ATOM   5049  CA  THR P  40      -5.529   8.469 -28.560  1.00 36.58           C  
ATOM   5050  CA  GLN P  41      -8.175   9.006 -25.897  1.00 65.10           C  
ATOM   5051  CA  ALA P  42      -8.917   5.309 -25.487  1.00 49.62           C  
ATOM   5052  CA  THR P  43      -8.621   4.110 -21.940  1.00 39.12           C  
ATOM   5053  CA  ASN P  44      -9.493   0.669 -20.723  1.00 50.98           C  
ATOM   5054  CA  ARG P  45      -9.629  -0.487 -17.176  1.00189.31           C  
ATOM   5055  CA  ASN P  46      -7.897  -3.730 -16.456  1.00 56.75           C  
ATOM   5056  CA  THR P  47      -9.294  -6.250 -14.043  1.00 88.35           C  
ATOM   5057  CA  ASP P  48      -6.268  -5.619 -11.891  1.00 70.71           C  
ATOM   5058  CA  GLY P  49      -7.316  -2.024 -11.537  1.00 26.34           C  
ATOM   5059  CA  SER P  50      -4.581  -0.745 -13.734  1.00 36.04           C  
ATOM   5060  CA  THR P  51      -5.686   1.076 -16.814  1.00 35.43           C  
ATOM   5061  CA  ASP P  52      -4.397   1.002 -20.340  1.00 37.19           C  
ATOM   5062  CA  TYR P  53      -4.149   4.403 -21.845  1.00 66.64           C  
ATOM   5063  CA  GLY P  54      -3.807   5.864 -25.268  1.00 32.58           C  
ATOM   5064  CA  ILE P  55      -3.404   4.579 -28.753  1.00 55.76           C  
ATOM   5065  CA  LEU P  56      -0.856   2.080 -27.467  1.00 89.33           C  
ATOM   5066  CA  GLN P  57      -2.981   1.219 -24.452  1.00 63.46           C  
ATOM   5067  CA  ILE P  58       0.041   1.635 -22.228  1.00132.05           C  
ATOM   5068  CA  ASN P  59      -0.652   0.019 -18.865  1.00 57.35           C  
ATOM   5069  CA  SER P  60      -0.568   2.113 -15.718  1.00 53.02           C  
ATOM   5070  CA  ARG P  61       0.602  -0.890 -13.863  1.00167.22           C  
ATOM   5071  CA  TRP P  62       4.126  -0.615 -15.117  1.00122.39           C  
ATOM   5072  CA  TRP P  63       4.381   2.298 -17.529  1.00119.21           C  
ATOM   5073  CA  CYS P  64       2.583   5.453 -16.462  1.00 50.04           C  
ATOM   5074  CA  ASN P  65       1.197   6.918 -13.336  1.00 78.50           C  
ATOM   5075  CA  ASP P  66      -2.561   7.278 -13.120  1.00 94.86           C  
ATOM   5076  CA  GLY P  67      -2.419   7.571  -9.336  1.00 46.69           C  
ATOM   5077  CA  ARG P  68      -5.175   4.937  -9.305  1.00245.39           C  
ATOM   5078  CA  THR P  69      -3.048   1.878  -9.656  1.00181.26           C  
ATOM   5079  CA  PRO P  70      -1.669   0.752  -6.388  1.00 80.35           C  
ATOM   5080  CA  GLY P  71       1.784  -0.771  -6.364  1.00 36.57           C  
ATOM   5081  CA  SER P  72       2.191   0.249  -9.927  1.00102.81           C  
ATOM   5082  CA  ARG P  73       5.302   1.791 -11.281  1.00152.72           C  
ATOM   5083  CA  ASN P  74       5.629   4.488 -13.838  1.00 91.40           C  
ATOM   5084  CA  LEU P  75       8.602   3.370 -15.865  1.00 53.02           C  
ATOM   5085  CA  CYS P  76       7.754   5.828 -18.591  1.00 60.92           C  
ATOM   5086  CA  ASN P  77       7.797   8.497 -15.911  1.00 57.16           C  
ATOM   5087  CA  ILE P  78       4.762  10.168 -17.306  1.00103.18           C  
ATOM   5088  CA  PRO P  79       1.285  10.606 -16.163  1.00125.35           C  
ATOM   5089  CA  CYS P  80      -0.994   8.186 -17.919  1.00 37.85           C  
ATOM   5090  CA  SER P  81      -2.972  11.175 -19.074  1.00 35.04           C  
ATOM   5091  CA  ALA P  82       0.032  12.091 -21.182  1.00 37.99           C  
ATOM   5092  CA  LEU P  83      -0.701   8.891 -23.057  1.00 71.14           C  
ATOM   5093  CA  LEU P  84      -4.109  10.340 -23.997  1.00106.31           C  
ATOM   5094  CA  SER P  85      -2.628  13.283 -25.901  1.00 51.14           C  
ATOM   5095  CA  SER P  86      -3.496  13.853 -29.509  1.00 28.29           C  
ATOM   5096  CA  ASP P  87       0.220  14.175 -29.823  1.00 46.07           C  
ATOM   5097  CA  ILE P  88       1.604  10.647 -29.975  1.00 80.33           C  
ATOM   5098  CA  THR P  89       5.052  11.579 -28.648  1.00 57.83           C  
ATOM   5099  CA  ALA P  90       4.466  10.490 -25.076  1.00 30.31           C  
ATOM   5100  CA  SER P  91       2.912   7.231 -26.157  1.00 29.89           C  
ATOM   5101  CA  VAL P  92       5.679   6.621 -28.636  1.00 32.57           C  
ATOM   5102  CA  ASN P  93       8.438   7.331 -26.181  1.00 28.73           C  
ATOM   5103  CA  CYS P  94       6.732   5.163 -23.635  1.00 30.33           C  
ATOM   5104  CA  ALA P  95       6.176   2.534 -26.289  1.00 29.34           C  
ATOM   5105  CA  LYS P  96       9.829   2.572 -27.121  1.00128.89           C  
ATOM   5106  CA  LYS P  97      10.596   1.876 -23.516  1.00117.30           C  
ATOM   5107  CA  ILE P  98       8.012  -0.862 -23.368  1.00 35.51           C  
ATOM   5108  CA  VAL P  99       9.189  -2.518 -26.542  1.00 92.31           C  
ATOM   5109  CA  SER P 100      12.728  -2.356 -25.202  1.00 45.01           C  
ATOM   5110  CA  ASP P 101      11.498  -4.195 -22.119  1.00 45.94           C  
ATOM   5111  CA  GLY P 102      12.752  -7.396 -23.698  1.00 27.32           C  
ATOM   5112  CA  ASN P 103       9.316  -8.833 -24.282  1.00 59.54           C  
ATOM   5113  CA  GLY P 104       9.140  -6.764 -27.434  1.00 25.73           C  
ATOM   5114  CA  MET P 105       5.779  -6.036 -28.989  1.00 70.66           C  
ATOM   5115  CA  ASN P 106       4.427  -9.022 -27.114  1.00 53.58           C  
ATOM   5116  CA  ALA P 107       3.922  -6.519 -24.323  1.00 38.20           C  
ATOM   5117  CA  TRP P 108       0.892  -5.491 -26.265  1.00 54.25           C  
ATOM   5118  CA  VAL P 109      -1.424  -8.448 -25.993  1.00 28.12           C  
ATOM   5119  CA  ALA P 110      -3.507  -7.228 -28.863  1.00 19.94           C  
ATOM   5120  CA  TRP P 111      -0.409  -7.050 -30.965  1.00 55.77           C  
ATOM   5121  CA  ARG P 112       0.702 -10.513 -30.134  1.00 88.23           C  
ATOM   5122  CA  ASN P 113      -2.689 -12.015 -30.612  1.00 51.74           C  
ATOM   5123  CA  ARG P 114      -3.902  -9.901 -33.497  1.00174.58           C  
ATOM   5124  CA  CYS P 115      -0.877  -8.443 -35.148  1.00 85.39           C  
ATOM   5125  CA  LYS P 116       2.006 -10.807 -34.747  1.00 92.45           C  
ATOM   5126  CA  GLY P 117       2.624 -12.975 -37.773  1.00 26.22           C  
ATOM   5127  CA  THR P 118       0.007 -11.074 -39.685  1.00121.21           C  
ATOM   5128  CA  ASP P 119       0.288  -9.014 -42.802  1.00 54.53           C  
ATOM   5129  CA  VAL P 120       1.317  -5.997 -40.776  1.00 48.55           C  
ATOM   5130  CA  GLN P 121       2.355  -4.238 -43.945  1.00 92.17           C  
ATOM   5131  CA  ALA P 122      -1.302  -3.947 -44.843  1.00 44.69           C  
ATOM   5132  CA  TRP P 123      -1.602  -1.398 -42.115  1.00 86.26           C  
ATOM   5133  CA  ILE P 124       1.040   0.666 -43.888  1.00157.42           C  
ATOM   5134  CA  ARG P 125      -0.630  -0.007 -47.268  1.00312.35           C  
ATOM   5135  CA  GLY P 126      -1.131   2.939 -49.603  1.00113.16           C  
ATOM   5136  CA  CYS P 127       0.025   5.388 -46.934  1.00 95.76           C  
ATOM   5137  CA  ARG P 128       2.766   7.662 -48.110  1.00 94.83           C  
ATOM   5138  CA  LEU P 129       5.166   7.659 -45.267  1.00 60.71           C  
TER    5139      LEU P 129                                                      
ATOM   5140  CA  LYS Q   1      -8.655 -26.333   8.068  1.00 32.60           C  
ATOM   5141  CA  VAL Q   2      -5.787 -28.472   9.111  1.00 95.52           C  
ATOM   5142  CA  PHE Q   3      -5.280 -31.259   6.661  1.00 64.00           C  
ATOM   5143  CA  GLY Q   4      -3.953 -34.608   7.625  1.00 22.77           C  
ATOM   5144  CA  ARG Q   5      -0.829 -35.643   5.807  1.00 81.66           C  
ATOM   5145  CA  CYS Q   6      -2.596 -38.221   3.695  1.00 31.68           C  
ATOM   5146  CA  GLU Q   7      -5.690 -36.124   3.394  1.00 27.92           C  
ATOM   5147  CA  LEU Q   8      -3.701 -33.272   1.993  1.00 46.60           C  
ATOM   5148  CA  ALA Q   9      -1.837 -35.568  -0.326  1.00 23.59           C  
ATOM   5149  CA  ALA Q  10      -5.101 -36.920  -1.609  1.00 22.66           C  
ATOM   5150  CA  ALA Q  11      -6.485 -33.443  -2.041  1.00 25.49           C  
ATOM   5151  CA  MET Q  12      -3.322 -32.358  -3.753  1.00 47.12           C  
ATOM   5152  CA  LYS Q  13      -3.468 -35.318  -6.091  1.00 56.73           C  
ATOM   5153  CA  ARG Q  14      -7.122 -34.689  -6.716  1.00157.99           C  
ATOM   5154  CA  HIS Q  15      -6.145 -31.157  -7.606  1.00 93.16           C  
ATOM   5155  CA  GLY Q  16      -3.560 -32.530  -9.974  1.00 32.85           C  
ATOM   5156  CA  LEU Q  17      -0.546 -31.387  -8.017  1.00 65.79           C  
ATOM   5157  CA  ASP Q  18       0.902 -34.877  -8.026  1.00 50.78           C  
ATOM   5158  CA  ASN Q  19       3.947 -34.772 -10.249  1.00 52.74           C  
ATOM   5159  CA  TYR Q  20       2.920 -31.333 -11.319  1.00 48.63           C  
ATOM   5160  CA  ARG Q  21       5.877 -29.799 -13.042  1.00139.75           C  
ATOM   5161  CA  GLY Q  22       7.661 -32.978 -12.119  1.00 24.44           C  
ATOM   5162  CA  TYR Q  23       7.197 -32.479  -8.443  1.00 52.12           C  
ATOM   5163  CA  SER Q  24       6.079 -35.579  -6.657  1.00 94.15           C  
ATOM   5164  CA  LEU Q  25       3.166 -35.340  -4.326  1.00 50.02           C  
ATOM   5165  CA  GLY Q  26       5.563 -35.840  -1.467  1.00 25.66           C  
ATOM   5166  CA  ASN Q  27       7.234 -32.601  -2.412  1.00 42.75           C  
ATOM   5167  CA  TRP Q  28       3.974 -30.735  -2.321  1.00 54.38           C  
ATOM   5168  CA  VAL Q  29       2.988 -32.355   0.923  1.00 27.70           C  
ATOM   5169  CA  CYS Q  30       6.308 -31.636   2.497  1.00 44.17           C  
ATOM   5170  CA  ALA Q  31       6.185 -28.083   1.263  1.00 22.06           C  
ATOM   5171  CA  ALA Q  32       2.748 -27.778   2.744  1.00 26.81           C  
ATOM   5172  CA  LYS Q  33       3.887 -29.212   6.008  1.00 83.76           C  
ATOM   5173  CA  PHE Q  34       6.769 -26.838   6.355  1.00 70.41           C  
ATOM   5174  CA  GLU Q  35       4.864 -23.947   4.886  1.00 89.78           C  
ATOM   5175  CA  SER Q  36       1.751 -24.122   6.971  1.00104.18           C  
ATOM   5176  CA  ASN Q  37       1.741 -27.368   8.888  1.00134.28           C  
ATOM   5177  CA  PHE Q  38      -1.107 -28.310   6.600  1.00 75.73           C  
ATOM   5178  CA  ASN Q  39      -3.096 -25.444   7.999  1.00 49.25           C  
ATOM   5179  CA  THR Q  40      -5.078 -23.799   5.228  1.00 36.76           C  
ATOM   5180  CA  GLN Q  41      -5.616 -20.780   7.458  1.00 53.49           C  
ATOM   5181  CA  ALA Q  42      -1.926 -20.163   8.032  1.00 50.15           C  
ATOM   5182  CA  THR Q  43      -0.793 -16.690   7.172  1.00 39.56           C  
ATOM   5183  CA  ASN Q  44       2.597 -15.249   7.878  1.00 49.52           C  
ATOM   5184  CA  ARG Q  45       3.812 -11.851   7.024  1.00131.88           C  
ATOM   5185  CA  ASN Q  46       7.130 -11.418   5.349  1.00 63.99           C  
ATOM   5186  CA  THR Q  47       9.654  -8.781   6.236  1.00 98.86           C  
ATOM   5187  CA  ASP Q  48       9.021  -7.238   2.847  1.00 73.76           C  
ATOM   5188  CA  GLY Q  49       5.477  -6.638   3.940  1.00 36.56           C  
ATOM   5189  CA  SER Q  50       3.999  -9.224   1.692  1.00 47.81           C  
ATOM   5190  CA  THR Q  51       2.299 -12.069   3.431  1.00 41.28           C  
ATOM   5191  CA  ASP Q  52       2.226 -15.751   2.693  1.00 40.28           C  
ATOM   5192  CA  TYR Q  53      -1.155 -17.315   2.807  1.00 63.92           C  
ATOM   5193  CA  GLY Q  54      -2.559 -20.777   2.995  1.00 33.97           C  
ATOM   5194  CA  ILE Q  55      -1.199 -24.277   3.027  1.00162.77           C  
ATOM   5195  CA  LEU Q  56       1.257 -23.310   0.325  1.00 90.65           C  
ATOM   5196  CA  GLN Q  57       2.043 -20.009   1.973  1.00 68.09           C  
ATOM   5197  CA  ILE Q  58       1.638 -18.330  -1.367  1.00 64.12           C  
ATOM   5198  CA  ASN Q  59       3.155 -14.883  -1.237  1.00 61.11           C  
ATOM   5199  CA  SER Q  60       1.007 -11.851  -1.848  1.00 47.89           C  
ATOM   5200  CA  ARG Q  61       3.934 -10.124  -3.351  1.00173.35           C  
ATOM   5201  CA  TRP Q  62       3.661 -12.015  -6.591  1.00121.77           C  
ATOM   5202  CA  TRP Q  63       0.749 -14.408  -6.435  1.00124.60           C  
ATOM   5203  CA  CYS Q  64      -2.331 -13.122  -4.646  1.00 59.86           C  
ATOM   5204  CA  ASN Q  65      -3.928  -9.822  -3.876  1.00 69.51           C  
ATOM   5205  CA  ASP Q  66      -4.067  -9.076  -0.172  1.00 91.84           C  
ATOM   5206  CA  GLY Q  67      -4.408  -5.353  -0.823  1.00 59.43           C  
ATOM   5207  CA  ARG Q  68      -1.730  -4.878   1.845  1.00156.60           C  
ATOM   5208  CA  THR Q  69       1.324  -5.444  -0.283  1.00150.34           C  
ATOM   5209  CA  PRO Q  70       2.371  -2.521  -2.329  1.00 73.71           C  
ATOM   5210  CA  GLY Q  71       3.767  -2.991  -5.787  1.00 31.84           C  
ATOM   5211  CA  SER Q  72       2.758  -6.556  -5.531  1.00 53.21           C  
ATOM   5212  CA  ARG Q  73       1.181  -8.435  -8.316  1.00186.42           C  
ATOM   5213  CA  ASN Q  74      -1.624 -10.916  -8.204  1.00 77.93           C  
ATOM   5214  CA  LEU Q  75      -0.462 -13.417 -10.775  1.00 56.33           C  
ATOM   5215  CA  CYS Q  76      -2.855 -16.029  -9.460  1.00 74.74           C  
ATOM   5216  CA  ASN Q  77      -5.568 -13.420  -9.914  1.00 61.52           C  
ATOM   5217  CA  ILE Q  78      -6.966 -14.474  -6.621  1.00179.67           C  
ATOM   5218  CA  PRO Q  79      -7.649 -12.715  -3.420  1.00165.02           C  
ATOM   5219  CA  CYS Q  80      -5.081 -14.039  -1.073  1.00 68.79           C  
ATOM   5220  CA  SER Q  81      -7.949 -14.860   1.234  1.00 35.16           C  
ATOM   5221  CA  ALA Q  82      -8.944 -17.452  -1.320  1.00 37.24           C  
ATOM   5222  CA  LEU Q  83      -5.683 -19.157  -0.430  1.00 67.13           C  
ATOM   5223  CA  LEU Q  84      -6.974 -19.594   3.128  1.00105.53           C  
ATOM   5224  CA  SER Q  85     -10.006 -21.638   2.121  1.00102.33           C  
ATOM   5225  CA  SER Q  86     -10.490 -25.163   3.344  1.00 26.85           C  
ATOM   5226  CA  ASP Q  87     -10.770 -26.102  -0.267  1.00 51.74           C  
ATOM   5227  CA  ILE Q  88      -7.231 -26.341  -1.570  1.00102.12           C  
ATOM   5228  CA  THR Q  89      -8.198 -25.638  -5.190  1.00155.13           C  
ATOM   5229  CA  ALA Q  90      -7.246 -21.989  -5.164  1.00 38.47           C  
ATOM   5230  CA  SER Q  91      -3.941 -22.716  -3.503  1.00 36.70           C  
ATOM   5231  CA  VAL Q  92      -3.266 -25.579  -5.840  1.00120.86           C  
ATOM   5232  CA  ASN Q  93      -4.049 -23.670  -8.962  1.00107.95           C  
ATOM   5233  CA  CYS Q  94      -1.968 -20.805  -7.698  1.00 37.17           C  
ATOM   5234  CA  ALA Q  95       0.787 -23.217  -6.758  1.00 29.98           C  
ATOM   5235  CA  LYS Q  96       0.717 -24.647 -10.218  1.00 60.61           C  
ATOM   5236  CA  LYS Q  97       1.275 -21.199 -11.587  1.00111.24           C  
ATOM   5237  CA  ILE Q  98       4.037 -20.570  -9.093  1.00 41.99           C  
ATOM   5238  CA  VAL Q  99       5.820 -23.821  -9.703  1.00 94.31           C  
ATOM   5239  CA  SER Q 100       5.692 -23.199 -13.427  1.00 55.01           C  
ATOM   5240  CA  ASP Q 101       7.054 -19.694 -12.848  1.00 96.95           C  
ATOM   5241  CA  GLY Q 102      10.701 -20.389 -13.311  1.00210.22           C  
ATOM   5242  CA  ASN Q 103      12.303 -21.741 -10.229  1.00140.68           C  
ATOM   5243  CA  GLY Q 104      10.020 -24.698  -9.684  1.00 40.52           C  
ATOM   5244  CA  MET Q 105       9.479 -25.577  -6.027  1.00 61.21           C  
ATOM   5245  CA  ASN Q 106      12.403 -23.406  -5.027  1.00 59.43           C  
ATOM   5246  CA  ALA Q 107       9.814 -20.667  -4.953  1.00 41.65           C  
ATOM   5247  CA  TRP Q 108       8.800 -22.187  -1.659  1.00 64.62           C  
ATOM   5248  CA  VAL Q 109      11.741 -21.428   0.578  1.00 29.93           C  
ATOM   5249  CA  ALA Q 110      10.658 -23.947   3.152  1.00 23.08           C  
ATOM   5250  CA  TRP Q 111      10.491 -26.507   0.414  1.00 50.20           C  
ATOM   5251  CA  ARG Q 112      13.917 -25.649  -0.818  1.00124.01           C  
ATOM   5252  CA  ASN Q 113      15.443 -25.667   2.581  1.00 50.24           C  
ATOM   5253  CA  ARG Q 114      13.514 -28.465   4.223  1.00137.42           C  
ATOM   5254  CA  CYS Q 115      11.966 -30.463   1.370  1.00128.87           C  
ATOM   5255  CA  LYS Q 116      14.483 -30.432  -1.374  1.00 53.47           C  
ATOM   5256  CA  GLY Q 117      16.646 -33.504  -1.530  1.00 21.08           C  
ATOM   5257  CA  THR Q 118      14.804 -35.041   1.357  1.00 96.77           C  
ATOM   5258  CA  ASP Q 119      12.849 -38.228   1.446  1.00 46.74           C  
ATOM   5259  CA  VAL Q 120       9.746 -36.457   0.247  1.00 46.67           C  
ATOM   5260  CA  GLN Q 121       8.155 -39.838  -0.281  1.00 87.60           C  
ATOM   5261  CA  ALA Q 122       7.792 -40.138   3.451  1.00 39.30           C  
ATOM   5262  CA  TRP Q 123       5.131 -37.495   3.295  1.00 78.04           C  
ATOM   5263  CA  ILE Q 124       3.072 -39.689   0.954  1.00 68.85           C  
ATOM   5264  CA  ARG Q 125       3.964 -42.927   2.759  1.00169.57           C  
ATOM   5265  CA  GLY Q 126       1.049 -45.080   3.771  1.00 25.60           C  
ATOM   5266  CA  CYS Q 127      -1.360 -42.784   2.073  1.00 45.84           C  
ATOM   5267  CA  ARG Q 128      -3.920 -44.284  -0.198  1.00107.55           C  
ATOM   5268  CA  LEU Q 129      -3.720 -41.837  -2.990  1.00 56.59           C  
TER    5269      LEU Q 129                                                      
ATOM   5270  CA  LYS R   1      11.450  30.217   8.586  1.00 79.24           C  
ATOM   5271  CA  VAL R   2       8.325  32.238   8.765  1.00 92.77           C  
ATOM   5272  CA  PHE R   3       7.995  34.566   5.852  1.00 64.42           C  
ATOM   5273  CA  GLY R   4       6.361  37.910   6.112  1.00 25.70           C  
ATOM   5274  CA  ARG R   5       3.412  38.397   3.839  1.00133.11           C  
ATOM   5275  CA  CYS R   6       5.322  40.706   1.534  1.00 43.04           C  
ATOM   5276  CA  GLU R   7       8.496  38.750   1.854  1.00 31.19           C  
ATOM   5277  CA  LEU R   8       6.752  35.619   0.764  1.00 40.95           C  
ATOM   5278  CA  ALA R   9       5.024  37.395  -2.057  1.00 24.30           C  
ATOM   5279  CA  ALA R  10       8.326  38.722  -3.261  1.00 20.60           C  
ATOM   5280  CA  ALA R  11       9.901  35.320  -2.959  1.00 23.38           C  
ATOM   5281  CA  MET R  12       7.056  33.677  -4.775  1.00 26.67           C  
ATOM   5282  CA  LYS R  13       7.181  36.304  -7.462  1.00 57.82           C  
ATOM   5283  CA  ARG R  14      10.903  35.805  -7.756  1.00103.64           C  
ATOM   5284  CA  HIS R  15      10.235  32.114  -8.143  1.00 80.36           C  
ATOM   5285  CA  GLY R  16       7.767  32.895 -10.883  1.00 31.35           C  
ATOM   5286  CA  LEU R  17       4.671  31.894  -8.972  1.00 58.31           C  
ATOM   5287  CA  ASP R  18       3.021  35.209  -9.716  1.00 47.94           C  
ATOM   5288  CA  ASN R  19       0.243  34.536 -12.176  1.00 50.36           C  
ATOM   5289  CA  TYR R  20       1.570  31.051 -12.503  1.00 60.69           C  
ATOM   5290  CA  ARG R  21      -1.130  29.058 -14.185  1.00135.12           C  
ATOM   5291  CA  GLY R  22      -3.172  32.215 -13.984  1.00 20.65           C  
ATOM   5292  CA  TYR R  23      -3.059  32.335 -10.240  1.00 51.26           C  
ATOM   5293  CA  SER R  24      -2.248  35.740  -8.932  1.00 36.22           C  
ATOM   5294  CA  LEU R  25       0.437  36.155  -6.337  1.00 49.32           C  
ATOM   5295  CA  GLY R  26      -2.225  36.960  -3.812  1.00 24.27           C  
ATOM   5296  CA  ASN R  27      -3.658  33.536  -4.350  1.00 34.05           C  
ATOM   5297  CA  TRP R  28      -0.334  31.897  -3.650  1.00 57.14           C  
ATOM   5298  CA  VAL R  29       0.301  34.106  -0.676  1.00 24.41           C  
ATOM   5299  CA  CYS R  30      -3.149  33.414   0.613  1.00 33.97           C  
ATOM   5300  CA  ALA R  31      -2.693  29.714   0.134  1.00 22.96           C  
ATOM   5301  CA  ALA R  32       0.591  29.898   1.919  1.00 26.83           C  
ATOM   5302  CA  LYS R  33      -0.881  31.794   4.768  1.00 87.67           C  
ATOM   5303  CA  PHE R  34      -3.659  29.352   5.432  1.00 86.67           C  
ATOM   5304  CA  GLU R  35      -1.526  26.409   4.456  1.00143.13           C  
ATOM   5305  CA  SER R  36       1.389  27.048   6.749  1.00 98.27           C  
ATOM   5306  CA  ASN R  37       0.968  30.534   8.109  1.00 61.32           C  
ATOM   5307  CA  PHE R  38       3.996  31.326   5.974  1.00 71.97           C  
ATOM   5308  CA  ASN R  39       6.067  28.873   7.943  1.00 41.86           C  
ATOM   5309  CA  THR R  40       8.334  26.929   5.632  1.00 42.53           C  
ATOM   5310  CA  GLN R  41       8.858  24.465   8.465  1.00 98.02           C  
ATOM   5311  CA  ALA R  42       5.173  23.662   8.797  1.00 58.89           C  
ATOM   5312  CA  THR R  43       4.455  20.009   8.518  1.00122.02           C  
ATOM   5313  CA  ASN R  44       1.135  18.441   9.241  1.00 54.61           C  
ATOM   5314  CA  ARG R  45       0.375  14.798   9.250  1.00 99.12           C  
ATOM   5315  CA  ASN R  46      -2.740  13.755   7.475  1.00 57.70           C  
ATOM   5316  CA  THR R  47      -5.026  11.107   8.850  1.00 45.18           C  
ATOM   5317  CA  ASP R  48      -4.045   8.965   5.902  1.00 72.89           C  
ATOM   5318  CA  GLY R  49      -0.467   8.933   7.096  1.00 37.84           C  
ATOM   5319  CA  SER R  50       0.678  11.270   4.416  1.00 51.35           C  
ATOM   5320  CA  THR R  51       2.074  14.498   5.576  1.00191.29           C  
ATOM   5321  CA  ASP R  52       1.875  17.999   4.205  1.00 52.42           C  
ATOM   5322  CA  TYR R  53       5.087  19.887   4.126  1.00107.85           C  
ATOM   5323  CA  GLY R  54       6.220  23.408   3.784  1.00 34.94           C  
ATOM   5324  CA  ILE R  55       4.650  26.742   3.202  1.00 56.06           C  
ATOM   5325  CA  LEU R  56       2.491  25.173   0.503  1.00 90.14           C  
ATOM   5326  CA  GLN R  57       1.788  22.115   2.634  1.00 76.45           C  
ATOM   5327  CA  ILE R  58       2.469  19.891  -0.307  1.00 64.82           C  
ATOM   5328  CA  ASN R  59       1.246  16.398   0.430  1.00 59.35           C  
ATOM   5329  CA  SER R  60       3.658  13.494   0.494  1.00100.31           C  
ATOM   5330  CA  ARG R  61       0.863  11.363  -0.772  1.00179.05           C  
ATOM   5331  CA  TRP R  62       1.252  12.716  -4.274  1.00115.12           C  
ATOM   5332  CA  TRP R  63       4.041  15.247  -4.542  1.00131.35           C  
ATOM   5333  CA  CYS R  64       7.088  14.552  -2.413  1.00 64.09           C  
ATOM   5334  CA  ASN R  65       8.750  11.597  -0.878  1.00 77.91           C  
ATOM   5335  CA  ASP R  66       8.924  11.511   2.886  1.00101.19           C  
ATOM   5336  CA  GLY R  67       9.675   7.811   2.616  1.00 58.63           C  
ATOM   5337  CA  ARG R  68       6.806   7.907   5.094  1.00160.02           C  
ATOM   5338  CA  THR R  69       3.756   7.433   3.004  1.00170.71           C  
ATOM   5339  CA  PRO R  70       3.041   4.092   1.622  1.00184.36           C  
ATOM   5340  CA  GLY R  71       1.662   3.912  -1.873  1.00 47.37           C  
ATOM   5341  CA  SER R  72       2.411   7.537  -2.253  1.00 69.50           C  
ATOM   5342  CA  ARG R  73       3.928   9.184  -5.268  1.00152.32           C  
ATOM   5343  CA  ASN R  74       6.608  11.769  -5.456  1.00157.39           C  
ATOM   5344  CA  LEU R  75       5.509  13.662  -8.522  1.00117.39           C  
ATOM   5345  CA  CYS R  76       7.679  16.598  -7.582  1.00 70.59           C  
ATOM   5346  CA  ASN R  77      10.559  14.166  -7.385  1.00 78.35           C  
ATOM   5347  CA  ILE R  78      11.867  15.811  -4.287  1.00 55.66           C  
ATOM   5348  CA  PRO R  79      12.280  14.737  -0.740  1.00 82.01           C  
ATOM   5349  CA  CYS R  80       9.486  16.274   1.184  1.00 96.72           C  
ATOM   5350  CA  SER R  81      12.155  17.682   3.458  1.00 84.53           C  
ATOM   5351  CA  ALA R  82      13.107  19.884   0.557  1.00 40.38           C  
ATOM   5352  CA  LEU R  83       9.690  21.461   0.997  1.00 69.94           C  
ATOM   5353  CA  LEU R  84      10.737  22.542   4.508  1.00 71.53           C  
ATOM   5354  CA  SER R  85      13.622  24.693   3.287  1.00 46.78           C  
ATOM   5355  CA  SER R  86      13.722  28.383   4.024  1.00 75.55           C  
ATOM   5356  CA  ASP R  87      14.411  28.613   0.337  1.00 42.76           C  
ATOM   5357  CA  ILE R  88      10.990  28.448  -1.297  1.00 81.57           C  
ATOM   5358  CA  THR R  89      12.279  27.175  -4.647  1.00 59.01           C  
ATOM   5359  CA  ALA R  90      11.498  23.521  -4.068  1.00 32.69           C  
ATOM   5360  CA  SER R  91       8.048  24.326  -2.797  1.00 32.88           C  
ATOM   5361  CA  VAL R  92       7.464  26.670  -5.684  1.00 37.14           C  
ATOM   5362  CA  ASN R  93       8.550  24.244  -8.343  1.00111.36           C  
ATOM   5363  CA  CYS R  94       6.520  21.561  -6.719  1.00 40.47           C  
ATOM   5364  CA  ALA R  95       3.600  23.934  -6.419  1.00 30.61           C  
ATOM   5365  CA  LYS R  96       3.864  24.775 -10.029  1.00109.79           C  
ATOM   5366  CA  LYS R  97       3.636  21.099 -10.819  1.00134.49           C  
ATOM   5367  CA  ILE R  98       0.698  20.677  -8.482  1.00 47.06           C  
ATOM   5368  CA  VAL R  99      -1.148  23.688  -9.826  1.00 91.94           C  
ATOM   5369  CA  SER R 100      -0.538  22.362 -13.315  1.00 47.45           C  
ATOM   5370  CA  ASP R 101      -2.273  19.198 -12.190  1.00 54.73           C  
ATOM   5371  CA  GLY R 102      -5.454  20.540 -13.730  1.00 30.97           C  
ATOM   5372  CA  ASN R 103      -7.281  20.907 -10.461  1.00 60.71           C  
ATOM   5373  CA  GLY R 104      -5.461  24.190 -10.160  1.00 25.14           C  
ATOM   5374  CA  MET R 105      -5.152  25.851  -6.786  1.00 75.60           C  
ATOM   5375  CA  ASN R 106      -8.071  23.729  -5.664  1.00 58.66           C  
ATOM   5376  CA  ALA R 107      -5.382  21.188  -4.915  1.00 43.13           C  
ATOM   5377  CA  TRP R 108      -4.755  23.232  -1.825  1.00 66.85           C  
ATOM   5378  CA  VAL R 109      -7.843  22.699   0.252  1.00 95.76           C  
ATOM   5379  CA  ALA R 110      -7.086  25.719   2.359  1.00 25.13           C  
ATOM   5380  CA  TRP R 111      -6.864  27.775  -0.763  1.00 51.01           C  
ATOM   5381  CA  ARG R 112     -10.154  26.667  -2.116  1.00182.34           C  
ATOM   5382  CA  ASN R 113     -11.860  27.042   1.199  1.00 76.96           C  
ATOM   5383  CA  ARG R 114     -10.204  30.207   2.405  1.00147.58           C  
ATOM   5384  CA  CYS R 115      -8.580  31.818  -0.613  1.00 80.10           C  
ATOM   5385  CA  LYS R 116     -10.715  31.080  -3.615  1.00 79.06           C  
ATOM   5386  CA  GLY R 117     -13.508  33.666  -3.420  1.00 46.00           C  
ATOM   5387  CA  THR R 118     -11.680  36.170  -1.261  1.00128.19           C  
ATOM   5388  CA  ASP R 119      -9.881  39.317  -2.240  1.00 54.30           C  
ATOM   5389  CA  VAL R 120      -6.546  37.623  -2.673  1.00 46.88           C  
ATOM   5390  CA  GLN R 121      -4.909  40.840  -3.780  1.00 63.67           C  
ATOM   5391  CA  ALA R 122      -5.125  41.967  -0.204  1.00 42.76           C  
ATOM   5392  CA  TRP R 123      -2.386  39.474   0.471  1.00 75.00           C  
ATOM   5393  CA  ILE R 124      -0.269  41.359  -2.034  1.00 71.04           C  
ATOM   5394  CA  ARG R 125      -1.337  44.614  -0.389  1.00326.40           C  
ATOM   5395  CA  GLY R 126       1.251  47.303   0.311  1.00113.12           C  
ATOM   5396  CA  CYS R 127       3.986  44.808  -0.492  1.00 86.92           C  
ATOM   5397  CA  ARG R 128       6.288  46.094  -3.136  1.00 93.46           C  
ATOM   5398  CA  LEU R 129       7.094  43.296  -5.477  1.00 90.52           C  
TER    5399      LEU R 129                                                      
MASTER     1377    0    0    0    0    0    0    6 5381   18    0  468          
END                                                                             
