HEADER    HYDROLASE/HYDROLASE                     20-NOV-11   4A8A              
TITLE     ASYMMETRIC CRYO-EM RECONSTRUCTION OF E. COLI DEGQ 12-MER IN COMPLEX   
TITLE    2 WITH LYSOZYME                                                        
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;                                                            
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            
AUTHOR    H.MALET,F.CANELLAS,J.SAWA,J.YAN,K.THALASSINOS,M.EHRMANN,T.CLAUSEN,    
AUTHOR   2 H.R.SAIBIL                                                           
REVDAT   4   23-AUG-17 4A8A    1       REMARK                                   
REVDAT   3   15-FEB-12 4A8A    1       JRNL                                     
REVDAT   2   11-JAN-12 4A8A    1       JRNL                                     
REVDAT   1   28-DEC-11 4A8A    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.   14.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : FLEX-EM, UCSF CHIMERA, 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)  : 14.20                          
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  -1981. (DEPOSITION ID: 10364).                                      
REMARK   4                                                                      
REMARK   4 4A8A 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_1290050378.                                   
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 GALLUS      
REMARK 245                                    GALLUS LYSOZYME                   
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                 : QUALITY OF THE MICROGRAPH         
REMARK 245  CHECKED WITH THE CTF                                                
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: TRIDECAMERIC                      
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M                               
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     ALA A    35                                                      
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     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     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     ALA B    35                                                      
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     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     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     ALA C    35                                                      
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     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     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     ALA D    35                                                      
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     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     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     ALA E    35                                                      
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     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     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     ALA F    35                                                      
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     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     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     ALA G    35                                                      
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     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     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     ALA H    35                                                      
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     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     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     ALA I    35                                                      
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     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     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     ALA J    35                                                      
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     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     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     ALA K    35                                                      
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     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     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     ALA L    35                                                      
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     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     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: 1LJ3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4 .6            
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: 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: 2D91   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HYPER-VIL-LYSOZYME                                      
REMARK 900 RELATED ID: 2XTH   RELATED DB: PDB                                   
REMARK 900 K2PTBR6 BINDING TO 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: 1JA2   RELATED DB: PDB                                   
REMARK 900 BINDING OF N-ACETYLGLUCOSAMINE TO CHICKEN EGG LYSOZYME : APOWDER     
REMARK 900 DIFFRACTION STUDY                                                    
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: 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: 2BLY   RELATED DB: PDB                                   
REMARK 900 HEWL AFTER A HIGH DOSE X-RAY "BURN"                                  
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: 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: 1XGP   RELATED DB: PDB                                   
REMARK 900 STRUCTURE FOR ANTIBODY HYHEL-63 Y33A MUTANT COMPLEXED WITHHEN EGG    
REMARK 900 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: 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: 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: 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: 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: 1HF4   RELATED DB: PDB                                   
REMARK 900 STRUCTURAL EFFECTS OF MONOVALENT ANIONS ON POLYMORPHIC LYSOZYME      
REMARK 900 CRYSTALS                                                             
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: 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: 1IC4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF HYHEL-10 FV MUTANT(HD32A)-HEN LYSOZYMECOMPLEX   
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: 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: 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: 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: 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: 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: 4LZT   RELATED DB: PDB                                   
REMARK 900 ATOMIC RESOLUTION REFINEMENT OF TRICLINIC HEW LYSOZYME AT 295K       
REMARK 900 RELATED ID: 1GXV   RELATED DB: PDB                                   
REMARK 900 SOLUTION STRUCTURE OF LYSOZYME AT LOW AND HIGH PRESSURE              
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: 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: 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: 1LJ4   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MONOCLINIC LYSOZYME GROWN AT PH 4 .6            
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: 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: 2HFM   RELATED DB: PDB                                   
REMARK 900 IGG1 FV FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX ( THEORETICAL       
REMARK 900 MODEL)                                                               
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: 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: 1LZB   RELATED DB: PDB                                   
REMARK 900 LYSOZYME CO-CRYSTALLIZED WITH TRI-N-ACETYL-CHITOTRIOSE (PH 4.7)      
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: 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: 132L   RELATED DB: PDB                                   
REMARK 900 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: 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: 2C8O   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (1SEC) AND UV LASR EXCITED FLUORESCENCE                     
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: 1IOT   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
REMARK 900 RELATED ID: 1DPX   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF HEN EGG-WHITE LYSOZYME                                  
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: 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: 2YBH   RELATED DB: PDB                                   
REMARK 900 NITRATE X-RAY INDUCED REDUCTION ON HEWL CRYSTALS (2. 31 MGY).        
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: 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: 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: 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: 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 RELATED ID: 3HFM   RELATED DB: PDB                                   
REMARK 900 IGG1 FAB FRAGMENT (HYHEL-10) AND LYSOZYME COMPLEX                    
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: 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: 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: 2D4I   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG-WHITE LYSOZYME CRYSTALLIZED AT PH4. 5FORM HEAVY   
REMARK 900 WATER SOLUTION                                                       
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: 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: 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: 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: 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: 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: 1LZD   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH TRP 62 REPLACED BY TYR (W62Y)                   
REMARK 900 RELATED ID: 1LCN   RELATED DB: PDB                                   
REMARK 900 MONOCLINIC HEN EGG WHITE LYSOZYME, THIOCYANATE COMPLEX               
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: 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: 1IOS   RELATED DB: PDB                                   
REMARK 900 STABILIZATION OF HEN EGG WHITE LYSOZYME BY A CAVITY- FILLINGMUTATION 
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: 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: 1BVX   RELATED DB: PDB                                   
REMARK 900 THE 1.8 A STRUCTURE OF GEL GROWN TETRAGONAL HEN EGG WHITE LYSOZYME   
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: 4A7D   RELATED DB: PDB                                   
REMARK 900 X-RAY CRYSTAL STRUCTURE OF HEWL FLASH-COOLED AT HIGH PRESSURE        
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: 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 RELATED ID: 1LSA   RELATED DB: PDB                                   
REMARK 900 LYSOZYME (120 K)                                                     
REMARK 900 RELATED ID: 1HEM   RELATED DB: PDB                                   
REMARK 900 LYSOZYME MUTANT WITH SER 91 REPLACED BY THR (S91T)                   
REMARK 900 RELATED ID: 1F3J   RELATED DB: PDB                                   
REMARK 900 HISTOCOMPATIBILITY ANTIGEN I-AG7                                     
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-1981   RELATED DB: EMDB                              
REMARK 900 ASYMMETRIC CRYO-EM RECONSTRUCTION OF E. COLI DEGQ 12-MER IN COMPLEX  
REMARK 900 WITH LYSOZYME                                                        
DBREF  4A8A A    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A B    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A C    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A D    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A E    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A F    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A G    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A H    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A I    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A J    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A K    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A L    1   428  UNP    P39099   DEGQ_ECOLI      28    455             
DBREF  4A8A M    1   129  UNP    P00698   LYSC_CHICK      19    147             
SEQADV 4A8A ALA A  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU A  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU A  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS A  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA B  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU B  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU B  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS B  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA C  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU C  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU C  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS C  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA D  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU D  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU D  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS D  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA E  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU E  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU E  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS E  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA F  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU F  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU F  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS F  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA G  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU G  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU G  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS G  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA H  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU H  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU H  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS H  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA I  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU I  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU I  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS I  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA J  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU J  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU J  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS J  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA K  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU K  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU K  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS K  436  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A ALA L  187  UNP  P39099    SER   214 ENGINEERED MUTATION            
SEQADV 4A8A LEU L  429  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A GLU L  430  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS L  431  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS L  432  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS L  433  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS L  434  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A HIS L  435  UNP  P39099              EXPRESSION TAG                 
SEQADV 4A8A 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              
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     -39.981  47.357  47.496  1.00 37.64           C  
ATOM      2  CA  LEU A  12     -39.622  44.441  45.146  1.00 95.89           C  
ATOM      3  CA  PRO A  13     -38.133  41.451  46.788  1.00137.81           C  
ATOM      4  CA  SER A  14     -34.461  41.108  46.725  1.00 62.57           C  
ATOM      5  CA  LEU A  15     -32.941  37.847  45.772  1.00146.10           C  
ATOM      6  CA  ALA A  16     -29.977  38.388  48.029  1.00 40.98           C  
ATOM      7  CA  PRO A  17     -31.831  38.564  51.261  1.00128.23           C  
ATOM      8  CA  MET A  18     -33.547  35.261  50.638  1.00 39.53           C  
ATOM      9  CA  LEU A  19     -30.401  33.722  49.232  1.00 45.09           C  
ATOM     10  CA  GLU A  20     -28.215  34.619  52.150  1.00 84.35           C  
ATOM     11  CA  LYS A  21     -30.076  32.402  54.540  1.00155.67           C  
ATOM     12  CA  VAL A  22     -30.719  29.541  52.113  1.00 51.83           C  
ATOM     13  CA  LEU A  23     -27.377  29.235  50.370  1.00 62.70           C  
ATOM     14  CA  PRO A  24     -25.546  27.365  53.052  1.00 65.45           C  
ATOM     15  CA  ALA A  25     -28.067  24.571  52.644  1.00 31.51           C  
ATOM     16  CA  VAL A  26     -26.851  23.783  49.159  1.00102.82           C  
ATOM     17  CA  VAL A  27     -23.594  21.929  48.976  1.00 38.90           C  
ATOM     18  CA  SER A  28     -21.148  20.667  46.413  1.00 82.38           C  
ATOM     19  CA  VAL A  29     -20.592  16.957  46.152  1.00 35.84           C  
ATOM     20  CA  ARG A  30     -17.222  15.571  45.226  1.00 83.26           C  
ATOM     21  CA  VAL A  31     -16.824  12.006  44.143  1.00 39.57           C  
ATOM     22  CA  GLU A  32     -13.996   9.690  43.296  1.00 92.36           C  
ATOM     23  CA  GLY A  33     -14.080   6.126  42.150  1.00 20.46           C  
ATOM     24  CA  THR A  34     -13.279   3.637  39.469  1.00 42.83           C  
ATOM     25  CA  ALA A  58     -10.997   1.014  37.026  1.00 16.67           C  
ATOM     26  CA  GLN A  59      -9.191   4.230  36.246  1.00155.16           C  
ATOM     27  CA  PRO A  60      -9.615   6.813  38.862  1.00 68.59           C  
ATOM     28  CA  PHE A  61     -11.890   9.676  37.996  1.00 54.20           C  
ATOM     29  CA  GLU A  62     -13.265  12.615  39.875  1.00 23.28           C  
ATOM     30  CA  GLY A  63     -16.684  14.080  39.423  1.00 15.73           C  
ATOM     31  CA  LEU A  64     -18.390  17.146  40.775  1.00 76.48           C  
ATOM     32  CA  GLY A  65     -22.044  17.666  41.504  1.00 18.67           C  
ATOM     33  CA  SER A  66     -24.266  19.358  44.024  1.00 25.49           C  
ATOM     34  CA  GLY A  67     -26.618  18.328  46.773  1.00 13.78           C  
ATOM     35  CA  VAL A  68     -29.025  19.853  49.223  1.00 38.78           C  
ATOM     36  CA  ILE A  69     -29.089  19.377  52.948  1.00 50.42           C  
ATOM     37  CA  ILE A  70     -32.491  18.011  53.837  1.00 99.10           C  
ATOM     38  CA  ASN A  71     -31.882  17.609  57.517  1.00 63.39           C  
ATOM     39  CA  ALA A  72     -29.177  19.384  59.401  1.00 32.39           C  
ATOM     40  CA  SER A  73     -29.253  17.189  62.431  1.00 34.08           C  
ATOM     41  CA  LYS A  74     -28.934  13.922  60.611  1.00 81.05           C  
ATOM     42  CA  GLY A  75     -26.828  15.428  57.895  1.00 25.54           C  
ATOM     43  CA  TYR A  76     -28.879  13.977  55.083  1.00 69.82           C  
ATOM     44  CA  VAL A  77     -28.077  15.392  51.690  1.00 33.90           C  
ATOM     45  CA  LEU A  78     -30.216  14.796  48.644  1.00110.96           C  
ATOM     46  CA  THR A  79     -28.503  14.400  45.307  1.00120.34           C  
ATOM     47  CA  ASN A  80     -28.872  12.775  41.927  1.00 59.99           C  
ATOM     48  CA  ASN A  81     -28.145   9.094  41.683  1.00 35.77           C  
ATOM     49  CA  HIS A  82     -26.006   9.601  38.635  1.00 51.67           C  
ATOM     50  CA  VAL A  83     -23.695  11.923  40.470  1.00 36.80           C  
ATOM     51  CA  ILE A  84     -23.223   9.271  43.175  1.00 72.70           C  
ATOM     52  CA  ASN A  85     -23.393   6.089  41.126  1.00 69.20           C  
ATOM     53  CA  GLN A  86     -19.718   5.448  40.416  1.00139.23           C  
ATOM     54  CA  ALA A  87     -18.398   7.052  43.597  1.00 66.05           C  
ATOM     55  CA  GLN A  88     -16.164   4.941  45.771  1.00 45.05           C  
ATOM     56  CA  LYS A  89     -15.782   7.851  48.152  1.00 29.67           C  
ATOM     57  CA  ILE A  90     -17.878  10.944  48.511  1.00 41.90           C  
ATOM     58  CA  SER A  91     -17.139  14.246  50.140  1.00 79.01           C  
ATOM     59  CA  ILE A  92     -19.319  17.261  50.594  1.00 64.37           C  
ATOM     60  CA  GLN A  93     -18.208  20.844  50.721  1.00 55.88           C  
ATOM     61  CA  LEU A  94     -20.031  23.703  52.373  1.00 97.86           C  
ATOM     62  CA  ASN A  95     -20.015  27.159  50.869  1.00 37.26           C  
ATOM     63  CA  ASP A  96     -18.030  28.207  53.908  1.00 56.18           C  
ATOM     64  CA  GLY A  97     -15.258  25.875  52.877  1.00 28.76           C  
ATOM     65  CA  ARG A  98     -15.822  23.211  55.475  1.00113.75           C  
ATOM     66  CA  GLU A  99     -15.693  19.725  54.070  1.00 43.30           C  
ATOM     67  CA  PHE A 100     -17.124  16.472  55.321  1.00 56.79           C  
ATOM     68  CA  ASP A 101     -17.230  12.828  54.316  1.00130.13           C  
ATOM     69  CA  ALA A 102     -20.453  11.277  53.234  1.00 38.04           C  
ATOM     70  CA  LYS A 103     -21.859   7.797  52.892  1.00 37.30           C  
ATOM     71  CA  LEU A 104     -24.538   6.708  50.502  1.00 72.22           C  
ATOM     72  CA  ILE A 105     -27.679   5.948  52.415  1.00 90.52           C  
ATOM     73  CA  GLY A 106     -29.554   4.690  49.404  1.00 30.32           C  
ATOM     74  CA  SER A 107     -30.702   5.667  45.976  1.00101.13           C  
ATOM     75  CA  ASP A 108     -32.660   4.515  43.027  1.00114.60           C  
ATOM     76  CA  ASP A 109     -32.107   4.491  39.297  1.00 63.05           C  
ATOM     77  CA  GLN A 110     -35.532   5.121  37.904  1.00161.56           C  
ATOM     78  CA  SER A 111     -36.232   8.485  39.534  1.00 86.26           C  
ATOM     79  CA  ASP A 112     -32.508   9.226  39.834  1.00 75.01           C  
ATOM     80  CA  ILE A 113     -32.664  10.259  43.486  1.00119.88           C  
ATOM     81  CA  ALA A 114     -29.989   9.378  46.001  1.00 32.72           C  
ATOM     82  CA  LEU A 115     -29.608  10.104  49.684  1.00 96.65           C  
ATOM     83  CA  LEU A 116     -26.291  10.786  51.350  1.00 48.07           C  
ATOM     84  CA  GLN A 117     -25.387  11.191  54.974  1.00 47.58           C  
ATOM     85  CA  ILE A 118     -22.703  13.492  56.227  1.00 61.95           C  
ATOM     86  CA  GLN A 119     -20.255  12.099  58.689  1.00 81.12           C  
ATOM     87  CA  ASN A 120     -19.912  14.134  61.838  1.00133.00           C  
ATOM     88  CA  PRO A 121     -22.295  16.746  60.592  1.00 71.93           C  
ATOM     89  CA  SER A 122     -22.069  19.906  62.640  1.00 38.52           C  
ATOM     90  CA  LYS A 123     -23.656  23.339  62.458  1.00 43.52           C  
ATOM     91  CA  LEU A 124     -25.437  22.631  59.220  1.00 83.85           C  
ATOM     92  CA  THR A 125     -28.294  24.520  57.689  1.00 93.73           C  
ATOM     93  CA  GLN A 126     -31.340  22.813  56.272  1.00 40.51           C  
ATOM     94  CA  ILE A 127     -33.406  23.822  53.332  1.00 97.25           C  
ATOM     95  CA  ALA A 128     -37.169  23.988  53.684  1.00 30.40           C  
ATOM     96  CA  ILE A 129     -39.259  21.978  51.274  1.00100.64           C  
ATOM     97  CA  ALA A 130     -42.077  23.556  49.305  1.00 31.87           C  
ATOM     98  CA  ASP A 131     -45.062  21.778  47.846  1.00 38.08           C  
ATOM     99  CA  SER A 132     -44.179  21.099  44.233  1.00 38.79           C  
ATOM    100  CA  ASP A 133     -47.737  20.430  43.262  1.00 56.79           C  
ATOM    101  CA  LYS A 134     -48.528  24.079  43.898  1.00 77.52           C  
ATOM    102  CA  LEU A 135     -46.139  25.299  41.238  1.00 96.84           C  
ATOM    103  CA  ARG A 136     -47.554  26.866  38.128  1.00124.88           C  
ATOM    104  CA  VAL A 137     -45.882  28.032  34.960  1.00105.63           C  
ATOM    105  CA  GLY A 138     -44.493  31.495  35.371  1.00 27.95           C  
ATOM    106  CA  ASP A 139     -43.379  31.028  38.939  1.00 30.60           C  
ATOM    107  CA  PHE A 140     -39.905  32.314  39.605  1.00 64.00           C  
ATOM    108  CA  ALA A 141     -37.141  29.889  40.355  1.00 30.88           C  
ATOM    109  CA  VAL A 142     -33.515  30.056  41.353  1.00 33.41           C  
ATOM    110  CA  ALA A 143     -31.047  27.289  40.734  1.00 29.18           C  
ATOM    111  CA  VAL A 144     -28.053  26.721  42.933  1.00 29.40           C  
ATOM    112  CA  GLY A 145     -25.249  24.292  42.301  1.00 21.28           C  
ATOM    113  CA  ASN A 146     -21.723  24.167  41.061  1.00 62.44           C  
ATOM    114  CA  PRO A 147     -21.516  24.450  37.377  1.00 70.58           C  
ATOM    115  CA  PHE A 148     -18.158  23.456  35.963  1.00 66.97           C  
ATOM    116  CA  GLY A 149     -16.997  23.115  39.532  1.00 22.39           C  
ATOM    117  CA  LEU A 150     -16.626  26.861  39.767  1.00 85.56           C  
ATOM    118  CA  GLY A 151     -18.176  26.981  43.204  1.00 28.03           C  
ATOM    119  CA  GLN A 152     -21.601  27.758  44.524  1.00 45.63           C  
ATOM    120  CA  THR A 153     -23.432  29.561  41.768  1.00 36.90           C  
ATOM    121  CA  ALA A 154     -26.964  30.858  41.671  1.00 34.23           C  
ATOM    122  CA  THR A 155     -28.975  31.384  38.528  1.00116.46           C  
ATOM    123  CA  SER A 156     -32.454  32.757  38.051  1.00 91.78           C  
ATOM    124  CA  GLY A 157     -35.377  31.943  35.817  1.00 29.30           C  
ATOM    125  CA  ILE A 158     -39.050  31.019  35.840  1.00 46.61           C  
ATOM    126  CA  VAL A 159     -40.737  27.669  35.760  1.00105.38           C  
ATOM    127  CA  SER A 160     -41.135  26.957  32.074  1.00 44.95           C  
ATOM    128  CA  ALA A 161     -43.268  23.871  32.382  1.00 39.61           C  
ATOM    129  CA  LEU A 162     -44.215  21.087  34.725  1.00 91.39           C  
ATOM    130  CA  GLY A 163     -45.158  17.487  34.437  1.00 32.53           C  
ATOM    131  CA  ARG A 164     -42.782  16.870  31.614  1.00124.80           C  
ATOM    132  CA  SER A 165     -41.788  13.467  30.420  1.00 92.25           C  
ATOM    133  CA  GLY A 166     -41.031  11.311  27.499  1.00 45.26           C  
ATOM    134  CA  LEU A 167     -37.579  12.818  27.719  1.00 50.77           C  
ATOM    135  CA  ASN A 168     -36.379   9.269  28.214  1.00 69.23           C  
ATOM    136  CA  LEU A 169     -33.781  10.689  30.527  1.00 48.90           C  
ATOM    137  CA  GLU A 170     -34.987   8.484  33.368  1.00151.10           C  
ATOM    138  CA  GLY A 171     -37.339   5.594  33.976  1.00 37.03           C  
ATOM    139  CA  LEU A 172     -39.652   7.756  35.974  1.00 79.66           C  
ATOM    140  CA  GLU A 173     -39.895  11.328  35.019  1.00 77.47           C  
ATOM    141  CA  ASN A 174     -41.879  14.400  35.910  1.00104.41           C  
ATOM    142  CA  PHE A 175     -39.483  17.134  35.429  1.00 81.04           C  
ATOM    143  CA  ILE A 176     -40.124  20.695  36.275  1.00 58.73           C  
ATOM    144  CA  GLN A 177     -38.695  22.627  33.386  1.00 46.47           C  
ATOM    145  CA  THR A 178     -36.813  25.808  34.048  1.00 43.16           C  
ATOM    146  CA  ASP A 179     -35.033  28.431  31.984  1.00 79.58           C  
ATOM    147  CA  ALA A 180     -32.617  29.070  34.845  1.00 45.87           C  
ATOM    148  CA  SER A 181     -29.162  28.361  33.584  1.00 93.15           C  
ATOM    149  CA  ILE A 182     -28.159  24.886  34.519  1.00 62.09           C  
ATOM    150  CA  ASN A 183     -24.959  23.339  33.325  1.00 40.89           C  
ATOM    151  CA  ARG A 184     -22.820  20.370  34.088  1.00111.38           C  
ATOM    152  CA  GLY A 185     -22.141  20.205  37.791  1.00 23.52           C  
ATOM    153  CA  ASN A 186     -25.638  21.447  38.567  1.00144.54           C  
ATOM    154  CA  ALA A 187     -26.913  17.963  39.111  1.00109.90           C  
ATOM    155  CA  GLY A 188     -28.164  17.287  42.576  1.00 26.79           C  
ATOM    156  CA  GLY A 189     -28.381  21.021  43.080  1.00 21.65           C  
ATOM    157  CA  ALA A 190     -31.410  22.856  44.307  1.00 43.25           C  
ATOM    158  CA  LEU A 191     -34.129  24.712  42.481  1.00 53.46           C  
ATOM    159  CA  LEU A 192     -35.659  27.207  44.839  1.00 51.55           C  
ATOM    160  CA  ASN A 193     -38.687  29.428  44.909  1.00 50.24           C  
ATOM    161  CA  LEU A 194     -38.583  33.023  46.040  1.00 90.53           C  
ATOM    162  CA  ASN A 195     -39.130  31.777  49.563  1.00 54.60           C  
ATOM    163  CA  GLY A 196     -35.904  29.873  49.287  1.00 24.94           C  
ATOM    164  CA  GLU A 197     -37.856  26.673  49.657  1.00 37.96           C  
ATOM    165  CA  LEU A 198     -36.866  23.654  47.619  1.00 63.24           C  
ATOM    166  CA  ILE A 199     -38.944  23.280  44.467  1.00 64.31           C  
ATOM    167  CA  GLY A 200     -36.948  20.406  43.046  1.00 29.37           C  
ATOM    168  CA  ILE A 201     -33.538  18.892  42.386  1.00141.92           C  
ATOM    169  CA  ASN A 202     -31.909  19.833  39.103  1.00 87.54           C  
ATOM    170  CA  THR A 203     -31.426  16.555  37.263  1.00 81.92           C  
ATOM    171  CA  ALA A 204     -30.625  17.320  33.652  1.00 51.14           C  
ATOM    172  CA  ILE A 205     -30.674  19.608  30.658  1.00 58.47           C  
ATOM    173  CA  LEU A 206     -31.194  19.368  26.947  1.00 88.58           C  
ATOM    174  CA  ALA A 207     -28.508  21.169  25.058  1.00 39.52           C  
ATOM    175  CA  PRO A 208     -27.032  20.465  21.729  1.00 66.52           C  
ATOM    176  CA  GLY A 209     -23.868  22.322  22.689  1.00 30.80           C  
ATOM    177  CA  GLY A 210     -23.558  20.679  26.040  1.00 23.00           C  
ATOM    178  CA  GLY A 211     -24.073  24.131  27.472  1.00 25.76           C  
ATOM    179  CA  SER A 212     -27.272  25.484  28.927  1.00105.61           C  
ATOM    180  CA  VAL A 213     -29.829  26.189  26.225  1.00 61.93           C  
ATOM    181  CA  GLY A 214     -32.275  27.442  28.790  1.00 42.11           C  
ATOM    182  CA  ILE A 215     -34.092  24.150  28.948  1.00 91.34           C  
ATOM    183  CA  GLY A 216     -33.387  22.426  32.225  1.00 21.03           C  
ATOM    184  CA  PHE A 217     -35.272  19.807  34.157  1.00 43.33           C  
ATOM    185  CA  ALA A 218     -35.567  19.113  37.837  1.00 32.62           C  
ATOM    186  CA  ILE A 219     -37.163  16.447  39.972  1.00 80.69           C  
ATOM    187  CA  PRO A 220     -39.956  17.970  41.888  1.00 80.00           C  
ATOM    188  CA  SER A 221     -39.484  18.615  45.570  1.00 38.20           C  
ATOM    189  CA  ASN A 222     -42.417  16.488  46.429  1.00 56.87           C  
ATOM    190  CA  MET A 223     -40.533  14.027  44.423  1.00100.44           C  
ATOM    191  CA  ALA A 224     -37.282  14.102  46.261  1.00 50.91           C  
ATOM    192  CA  ARG A 225     -38.804  14.592  49.651  1.00124.84           C  
ATOM    193  CA  THR A 226     -40.865  11.508  50.044  1.00 60.84           C  
ATOM    194  CA  LEU A 227     -38.413   9.457  48.000  1.00 72.99           C  
ATOM    195  CA  ALA A 228     -35.658  10.633  50.258  1.00 45.95           C  
ATOM    196  CA  GLN A 229     -37.800   9.935  53.249  1.00 74.03           C  
ATOM    197  CA  GLN A 230     -37.966   6.193  52.968  1.00 92.47           C  
ATOM    198  CA  LEU A 231     -34.333   6.027  52.063  1.00113.64           C  
ATOM    199  CA  ILE A 232     -34.016   7.212  55.591  1.00 77.15           C  
ATOM    200  CA  ASP A 233     -37.183   5.411  56.641  1.00180.68           C  
ATOM    201  CA  PHE A 234     -39.107   3.225  55.738  1.00184.61           C  
ATOM    202  CA  GLY A 235     -37.195   2.160  52.728  1.00 75.53           C  
ATOM    203  CA  GLU A 236     -39.355  -0.829  52.681  1.00 96.05           C  
ATOM    204  CA  ILE A 237     -36.954  -3.005  50.889  1.00234.80           C  
ATOM    205  CA  LYS A 238     -39.578  -3.647  48.421  1.00337.87           C  
ATOM    206  CA  ARG A 239     -40.343  -2.497  45.962  1.00317.99           C  
ATOM    207  CA  GLY A 240     -37.783   0.177  46.723  1.00 64.08           C  
ATOM    208  CA  LEU A 241     -38.218   1.489  43.158  1.00192.89           C  
ATOM    209  CA  LEU A 242     -39.890   0.078  40.013  1.00120.34           C  
ATOM    210  CA  GLY A 243     -36.766  -0.386  37.947  1.00 55.18           C  
ATOM    211  CA  ILE A 244     -38.278   0.427  34.622  1.00213.98           C  
ATOM    212  CA  LYS A 245     -37.382   2.402  31.543  1.00139.19           C  
ATOM    213  CA  GLY A 246     -39.916   4.281  29.571  1.00 48.63           C  
ATOM    214  CA  THR A 247     -40.725   7.305  27.573  1.00125.15           C  
ATOM    215  CA  GLU A 248     -43.570   9.307  26.257  1.00151.80           C  
ATOM    216  CA  MET A 249     -46.460   8.000  24.319  1.00305.05           C  
ATOM    217  CA  SER A 250     -45.243   9.093  20.885  1.00171.60           C  
ATOM    218  CA  ALA A 251     -47.839  10.688  18.655  1.00 81.00           C  
ATOM    219  CA  ASP A 252     -48.176   8.533  15.577  1.00 47.24           C  
ATOM    220  CA  ILE A 253     -49.610   5.587  17.390  1.00110.67           C  
ATOM    221  CA  ALA A 254     -51.547   7.949  19.561  1.00 39.71           C  
ATOM    222  CA  LYS A 255     -53.305   9.286  16.533  1.00154.49           C  
ATOM    223  CA  ALA A 256     -54.434   5.917  15.285  1.00 43.68           C  
ATOM    224  CA  PHE A 257     -55.046   4.203  18.586  1.00171.68           C  
ATOM    225  CA  ASN A 258     -57.369   6.514  20.392  1.00 71.56           C  
ATOM    226  CA  LEU A 259     -56.176   4.600  23.422  1.00162.11           C  
ATOM    227  CA  ASP A 260     -57.512   5.804  26.720  1.00 85.12           C  
ATOM    228  CA  VAL A 261     -54.666   8.031  27.719  1.00 95.66           C  
ATOM    229  CA  GLN A 262     -53.560  10.916  25.572  1.00139.82           C  
ATOM    230  CA  ARG A 263     -50.142   9.944  26.695  1.00159.78           C  
ATOM    231  CA  GLY A 264     -49.228   7.394  29.149  1.00 71.42           C  
ATOM    232  CA  ALA A 265     -46.075   6.120  30.580  1.00 61.26           C  
ATOM    233  CA  PHE A 266     -44.935   3.614  28.126  1.00161.75           C  
ATOM    234  CA  VAL A 267     -42.359   1.195  29.161  1.00115.11           C  
ATOM    235  CA  SER A 268     -39.878  -0.102  26.699  1.00139.60           C  
ATOM    236  CA  GLU A 269     -37.950  -2.324  28.975  1.00156.21           C  
ATOM    237  CA  VAL A 270     -37.974  -4.648  31.946  1.00117.13           C  
ATOM    238  CA  LEU A 271     -35.183  -4.464  34.487  1.00 95.85           C  
ATOM    239  CA  PRO A 272     -33.881  -7.666  35.885  1.00 68.85           C  
ATOM    240  CA  GLY A 273     -34.451  -8.534  39.512  1.00 31.40           C  
ATOM    241  CA  SER A 274     -36.200  -5.256  39.429  1.00 59.79           C  
ATOM    242  CA  GLY A 275     -39.384  -4.090  41.010  1.00 51.54           C  
ATOM    243  CA  SER A 276     -41.132  -4.131  37.702  1.00 61.40           C  
ATOM    244  CA  ALA A 277     -40.260  -7.736  37.010  1.00 62.93           C  
ATOM    245  CA  LYS A 278     -41.608  -9.568  40.022  1.00108.19           C  
ATOM    246  CA  ALA A 279     -44.541  -7.305  39.928  1.00 64.12           C  
ATOM    247  CA  GLY A 280     -45.197  -8.448  36.622  1.00 82.07           C  
ATOM    248  CA  VAL A 281     -44.871  -5.542  34.373  1.00105.33           C  
ATOM    249  CA  LYS A 282     -42.562  -5.845  31.480  1.00295.67           C  
ATOM    250  CA  ALA A 283     -42.418  -3.298  28.778  1.00153.10           C  
ATOM    251  CA  GLY A 284     -44.669  -1.985  26.133  1.00 84.12           C  
ATOM    252  CA  ASP A 285     -47.176  -1.643  28.738  1.00165.77           C  
ATOM    253  CA  ILE A 286     -48.666   1.533  29.015  1.00136.64           C  
ATOM    254  CA  ILE A 287     -48.836   2.645  32.601  1.00103.72           C  
ATOM    255  CA  THR A 288     -52.198   4.337  32.662  1.00 84.64           C  
ATOM    256  CA  SER A 289     -52.459   5.117  36.273  1.00 56.83           C  
ATOM    257  CA  LEU A 290     -50.781   4.964  39.599  1.00 74.77           C  
ATOM    258  CA  ASN A 291     -52.985   4.326  42.552  1.00186.31           C  
ATOM    259  CA  GLY A 292     -56.710   4.996  42.737  1.00 54.17           C  
ATOM    260  CA  LYS A 293     -56.447   8.302  40.932  1.00 68.82           C  
ATOM    261  CA  PRO A 294     -55.716   8.497  37.292  1.00 80.02           C  
ATOM    262  CA  LEU A 295     -52.169   9.016  36.092  1.00138.11           C  
ATOM    263  CA  ASN A 296     -51.270  11.433  33.350  1.00 74.47           C  
ATOM    264  CA  SER A 297     -48.370  11.287  30.964  1.00 63.51           C  
ATOM    265  CA  PHE A 298     -45.076   9.659  31.675  1.00 88.08           C  
ATOM    266  CA  ALA A 299     -44.387  13.044  33.069  1.00 52.62           C  
ATOM    267  CA  GLU A 300     -46.982  12.800  35.757  1.00 97.16           C  
ATOM    268  CA  LEU A 301     -45.683   9.361  36.453  1.00 67.62           C  
ATOM    269  CA  ARG A 302     -42.424  10.288  37.956  1.00177.31           C  
ATOM    270  CA  SER A 303     -44.025  13.293  39.451  1.00 49.06           C  
ATOM    271  CA  ARG A 304     -46.004  11.131  41.731  1.00107.64           C  
ATOM    272  CA  ILE A 305     -43.510   8.292  42.085  1.00124.81           C  
ATOM    273  CA  ALA A 306     -40.526  10.467  42.319  1.00 72.08           C  
ATOM    274  CA  THR A 307     -42.683  12.164  44.872  1.00 64.95           C  
ATOM    275  CA  THR A 308     -43.536   9.049  46.772  1.00131.13           C  
ATOM    276  CA  GLU A 309     -41.376   7.008  49.076  1.00 84.30           C  
ATOM    277  CA  PRO A 310     -39.162   4.665  47.328  1.00198.33           C  
ATOM    278  CA  GLY A 311     -40.248   2.406  48.897  1.00125.94           C  
ATOM    279  CA  THR A 312     -43.958   2.700  49.291  1.00 56.05           C  
ATOM    280  CA  LYS A 313     -45.989  -0.230  48.176  1.00128.37           C  
ATOM    281  CA  VAL A 314     -48.071   0.989  45.318  1.00 82.38           C  
ATOM    282  CA  LYS A 315     -50.401  -0.462  42.733  1.00101.70           C  
ATOM    283  CA  LEU A 316     -50.091   0.333  39.088  1.00126.98           C  
ATOM    284  CA  GLY A 317     -52.554  -0.068  36.305  1.00 74.75           C  
ATOM    285  CA  LEU A 318     -50.747  -0.361  33.132  1.00210.91           C  
ATOM    286  CA  LEU A 319     -52.716  -1.055  29.899  1.00200.66           C  
ATOM    287  CA  ARG A 320     -51.588  -3.764  28.047  1.00395.68           C  
ATOM    288  CA  ASN A 321     -53.143  -5.262  25.146  1.00180.85           C  
ATOM    289  CA  GLY A 322     -56.269  -3.515  25.280  1.00 63.56           C  
ATOM    290  CA  LYS A 323     -57.053  -5.047  28.497  1.00160.20           C  
ATOM    291  CA  PRO A 324     -56.948  -4.122  32.121  1.00147.33           C  
ATOM    292  CA  LEU A 325     -54.202  -4.308  34.893  1.00191.63           C  
ATOM    293  CA  GLU A 326     -53.931  -4.098  38.476  1.00142.86           C  
ATOM    294  CA  VAL A 327     -50.597  -5.168  39.874  1.00111.06           C  
ATOM    295  CA  GLU A 328     -48.697  -4.357  43.049  1.00 88.09           C  
ATOM    296  CA  VAL A 329     -45.179  -3.195  42.499  1.00 53.28           C  
ATOM    297  CA  SER A 340     -23.751 -29.124  46.452  1.00104.44           C  
ATOM    298  CA  ALA A 341     -20.031 -28.728  45.822  1.00 77.07           C  
ATOM    299  CA  GLU A 342     -20.612 -26.743  42.660  1.00 52.11           C  
ATOM    300  CA  MET A 343     -21.214 -23.357  44.121  1.00 41.40           C  
ATOM    301  CA  ILE A 344     -18.232 -23.508  46.376  1.00 96.91           C  
ATOM    302  CA  THR A 345     -16.090 -25.146  43.791  1.00 65.01           C  
ATOM    303  CA  PRO A 346     -16.300 -24.342  40.163  1.00243.77           C  
ATOM    304  CA  ALA A 347     -18.048 -26.658  37.746  1.00 71.76           C  
ATOM    305  CA  LEU A 348     -17.164 -29.552  40.039  1.00 84.85           C  
ATOM    306  CA  GLU A 349     -20.471 -31.269  40.405  1.00 75.51           C  
ATOM    307  CA  GLY A 350     -20.570 -33.555  43.342  1.00 27.86           C  
ATOM    308  CA  ALA A 351     -21.780 -34.135  46.837  1.00 39.18           C  
ATOM    309  CA  THR A 352     -23.830 -31.434  48.436  1.00 51.03           C  
ATOM    310  CA  LEU A 353     -22.269 -29.343  51.125  1.00 60.97           C  
ATOM    311  CA  SER A 354     -23.679 -27.932  54.316  1.00 35.43           C  
ATOM    312  CA  ASP A 355     -22.174 -25.449  56.712  1.00 33.92           C  
ATOM    313  CA  GLY A 356     -21.825 -25.793  60.402  1.00 43.78           C  
ATOM    314  CA  GLN A 357     -20.599 -28.855  62.191  1.00160.18           C  
ATOM    315  CA  LEU A 358     -24.245 -29.017  62.203  1.00196.11           C  
ATOM    316  CA  LYS A 359     -24.280 -31.805  64.768  1.00115.28           C  
ATOM    317  CA  ASP A 360     -21.437 -30.428  66.901  1.00 46.07           C  
ATOM    318  CA  GLY A 361     -19.381 -27.267  67.050  1.00 29.88           C  
ATOM    319  CA  GLY A 362     -18.397 -26.270  63.552  1.00 40.31           C  
ATOM    320  CA  LYS A 363     -15.545 -28.543  62.630  1.00103.45           C  
ATOM    321  CA  GLY A 364     -16.147 -27.333  59.146  1.00 28.87           C  
ATOM    322  CA  ILE A 365     -18.346 -27.776  56.116  1.00 62.54           C  
ATOM    323  CA  LYS A 366     -19.965 -31.141  55.747  1.00 74.10           C  
ATOM    324  CA  ILE A 367     -20.599 -32.927  52.525  1.00 58.54           C  
ATOM    325  CA  ASP A 368     -24.103 -34.283  52.631  1.00 58.84           C  
ATOM    326  CA  GLU A 369     -24.023 -36.963  50.010  1.00 85.17           C  
ATOM    327  CA  VAL A 370     -21.912 -38.081  47.117  1.00128.01           C  
ATOM    328  CA  VAL A 371     -23.363 -37.977  43.606  1.00196.35           C  
ATOM    329  CA  LYS A 372     -20.358 -40.241  42.898  1.00155.33           C  
ATOM    330  CA  GLY A 373     -20.724 -40.279  39.143  1.00 37.94           C  
ATOM    331  CA  SER A 374     -19.897 -36.568  39.536  1.00 51.10           C  
ATOM    332  CA  PRO A 375     -16.419 -35.217  39.493  1.00 66.49           C  
ATOM    333  CA  ALA A 376     -16.534 -34.088  43.089  1.00 42.19           C  
ATOM    334  CA  ALA A 377     -16.642 -37.813  43.598  1.00 49.21           C  
ATOM    335  CA  GLN A 378     -13.736 -38.504  41.273  1.00 58.46           C  
ATOM    336  CA  ALA A 379     -11.062 -36.720  43.306  1.00 56.10           C  
ATOM    337  CA  GLY A 380     -11.792 -38.364  46.620  1.00 63.25           C  
ATOM    338  CA  LEU A 381     -14.715 -36.609  48.189  1.00 60.88           C  
ATOM    339  CA  GLN A 382     -16.952 -39.113  49.909  1.00 56.94           C  
ATOM    340  CA  LYS A 383     -19.963 -38.255  51.989  1.00138.29           C  
ATOM    341  CA  ASP A 384     -19.785 -37.718  55.720  1.00154.97           C  
ATOM    342  CA  ASP A 385     -16.513 -35.918  55.344  1.00 58.66           C  
ATOM    343  CA  VAL A 386     -15.973 -32.716  57.263  1.00131.90           C  
ATOM    344  CA  ILE A 387     -13.731 -30.165  55.730  1.00 64.32           C  
ATOM    345  CA  ILE A 388     -11.899 -28.726  58.678  1.00 85.60           C  
ATOM    346  CA  GLY A 389      -9.998 -26.204  56.603  1.00 49.57           C  
ATOM    347  CA  VAL A 390      -8.249 -25.430  53.353  1.00144.41           C  
ATOM    348  CA  ASN A 391      -4.700 -24.434  52.569  1.00 88.83           C  
ATOM    349  CA  ARG A 392      -3.582 -24.276  56.188  1.00194.65           C  
ATOM    350  CA  ASP A 393      -6.654 -22.220  56.855  1.00 62.32           C  
ATOM    351  CA  ARG A 394      -9.344 -23.397  59.186  1.00 39.75           C  
ATOM    352  CA  VAL A 395     -12.770 -23.534  57.658  1.00 43.61           C  
ATOM    353  CA  ASN A 396     -15.504 -22.985  60.196  1.00 42.64           C  
ATOM    354  CA  SER A 397     -18.191 -22.816  57.556  1.00 39.78           C  
ATOM    355  CA  ILE A 398     -18.732 -22.324  53.850  1.00170.03           C  
ATOM    356  CA  ALA A 399     -18.121 -18.619  53.939  1.00 28.59           C  
ATOM    357  CA  GLU A 400     -14.640 -19.092  55.299  1.00 27.30           C  
ATOM    358  CA  MET A 401     -13.928 -21.851  52.844  1.00 34.47           C  
ATOM    359  CA  ARG A 402     -15.023 -19.510  50.127  1.00 80.48           C  
ATOM    360  CA  LYS A 403     -12.436 -17.057  51.345  1.00 81.21           C  
ATOM    361  CA  VAL A 404      -9.548 -19.410  50.798  1.00 35.67           C  
ATOM    362  CA  LEU A 405     -11.009 -20.108  47.386  1.00 97.59           C  
ATOM    363  CA  ALA A 406     -11.122 -16.393  46.790  1.00 34.28           C  
ATOM    364  CA  ALA A 407      -7.348 -16.452  46.856  1.00 32.46           C  
ATOM    365  CA  LYS A 408      -7.679 -18.944  44.036  1.00132.86           C  
ATOM    366  CA  PRO A 409      -4.477 -20.748  44.833  1.00 69.91           C  
ATOM    367  CA  ALA A 410      -3.448 -23.073  42.037  1.00 32.90           C  
ATOM    368  CA  ILE A 411      -3.164 -25.709  44.703  1.00127.07           C  
ATOM    369  CA  ILE A 412      -6.087 -26.221  46.976  1.00 55.02           C  
ATOM    370  CA  ALA A 413      -5.714 -28.599  49.808  1.00 58.43           C  
ATOM    371  CA  LEU A 414      -8.720 -29.758  51.713  1.00120.64           C  
ATOM    372  CA  GLN A 415      -8.318 -31.734  54.809  1.00123.92           C  
ATOM    373  CA  ILE A 416     -11.383 -33.321  56.047  1.00122.26           C  
ATOM    374  CA  VAL A 417     -11.917 -35.726  58.832  1.00 48.12           C  
ATOM    375  CA  ARG A 418     -13.445 -38.990  57.878  1.00114.11           C  
ATOM    376  CA  GLY A 419     -14.369 -41.456  60.516  1.00 24.15           C  
ATOM    377  CA  ASN A 420     -11.906 -41.033  63.262  1.00 86.75           C  
ATOM    378  CA  GLU A 421      -9.007 -40.008  61.100  1.00 94.60           C  
ATOM    379  CA  SER A 422      -7.531 -37.115  59.226  1.00 45.62           C  
ATOM    380  CA  ILE A 423      -8.037 -36.930  55.513  1.00 80.04           C  
ATOM    381  CA  TYR A 424      -6.577 -34.756  52.865  1.00173.28           C  
ATOM    382  CA  LEU A 425      -8.231 -33.874  49.659  1.00102.27           C  
ATOM    383  CA  LEU A 426      -7.180 -31.699  46.878  1.00235.11           C  
ATOM    384  CA  MET A 427      -7.850 -30.051  43.577  1.00104.05           C  
ATOM    385  CA  ARG A 428      -6.035 -29.378  40.349  1.00202.51           C  
TER     386      ARG A 428                                                      
ATOM    387  CA  PRO B  11     -39.176  40.778  40.055  1.00135.28           C  
ATOM    388  CA  LEU B  12     -37.093  43.296  38.313  1.00110.99           C  
ATOM    389  CA  PRO B  13     -38.630  46.541  37.474  1.00 80.82           C  
ATOM    390  CA  SER B  14     -38.956  47.485  33.846  1.00 65.63           C  
ATOM    391  CA  LEU B  15     -35.344  47.713  32.793  1.00107.79           C  
ATOM    392  CA  ALA B  16     -36.003  49.893  29.806  1.00 39.97           C  
ATOM    393  CA  PRO B  17     -36.496  53.030  31.759  1.00 65.93           C  
ATOM    394  CA  MET B  18     -33.190  52.626  33.554  1.00 37.46           C  
ATOM    395  CA  LEU B  19     -31.469  51.492  30.392  1.00 50.08           C  
ATOM    396  CA  GLU B  20     -32.577  54.425  28.330  1.00 66.79           C  
ATOM    397  CA  LYS B  21     -30.539  56.850  30.329  1.00125.77           C  
ATOM    398  CA  VAL B  22     -27.490  54.663  30.947  1.00151.96           C  
ATOM    399  CA  LEU B  23     -26.981  52.987  27.604  1.00 79.51           C  
ATOM    400  CA  PRO B  24     -25.307  55.829  25.818  1.00 66.13           C  
ATOM    401  CA  ALA B  25     -22.591  55.631  28.452  1.00 36.98           C  
ATOM    402  CA  VAL B  26     -21.530  52.213  27.235  1.00 40.63           C  
ATOM    403  CA  VAL B  27     -19.513  52.252  24.088  1.00117.92           C  
ATOM    404  CA  SER B  28     -17.959  49.872  21.598  1.00 36.21           C  
ATOM    405  CA  VAL B  29     -14.234  49.912  21.197  1.00 34.83           C  
ATOM    406  CA  ARG B  30     -12.673  49.114  17.887  1.00102.36           C  
ATOM    407  CA  VAL B  31      -9.057  48.193  17.576  1.00 40.31           C  
ATOM    408  CA  GLU B  32      -6.633  47.669  14.753  1.00 35.24           C  
ATOM    409  CA  GLY B  33      -3.039  46.643  14.946  1.00 30.95           C  
ATOM    410  CA  THR B  34      -0.303  44.145  14.243  1.00140.10           C  
ATOM    411  CA  ALA B  58       2.308  42.138  11.030  1.00 28.07           C  
ATOM    412  CA  GLN B  59      -0.941  41.073   9.486  1.00155.34           C  
ATOM    413  CA  PRO B  60      -3.519  43.525  10.503  1.00159.32           C  
ATOM    414  CA  PHE B  61      -6.351  42.332  12.620  1.00 70.26           C  
ATOM    415  CA  GLU B  62      -9.399  44.100  13.869  1.00 30.08           C  
ATOM    416  CA  GLY B  63     -10.714  43.495  17.323  1.00 22.36           C  
ATOM    417  CA  LEU B  64     -13.954  44.491  18.925  1.00 46.68           C  
ATOM    418  CA  GLY B  65     -14.572  45.210  22.562  1.00 26.63           C  
ATOM    419  CA  SER B  66     -16.550  47.540  24.734  1.00 32.31           C  
ATOM    420  CA  GLY B  67     -15.832  50.323  27.158  1.00 16.08           C  
ATOM    421  CA  VAL B  68     -17.603  52.621  29.552  1.00 32.24           C  
ATOM    422  CA  ILE B  69     -17.423  56.375  29.653  1.00 97.52           C  
ATOM    423  CA  ILE B  70     -16.371  57.316  33.147  1.00111.05           C  
ATOM    424  CA  ASN B  71     -15.941  61.012  32.520  1.00 42.90           C  
ATOM    425  CA  ALA B  72     -18.044  62.712  29.902  1.00 31.75           C  
ATOM    426  CA  SER B  73     -16.215  65.996  29.905  1.00 31.03           C  
ATOM    427  CA  LYS B  74     -12.790  64.446  29.774  1.00 88.43           C  
ATOM    428  CA  GLY B  75     -13.911  61.639  27.543  1.00 24.90           C  
ATOM    429  CA  TYR B  76     -12.289  58.949  29.620  1.00 66.14           C  
ATOM    430  CA  VAL B  77     -13.348  55.455  28.743  1.00 39.93           C  
ATOM    431  CA  LEU B  78     -12.590  52.415  30.858  1.00 45.44           C  
ATOM    432  CA  THR B  79     -11.820  49.165  29.107  1.00 41.97           C  
ATOM    433  CA  ASN B  80      -9.946  45.944  29.550  1.00 54.07           C  
ATOM    434  CA  ASN B  81      -6.257  46.020  28.890  1.00 59.55           C  
ATOM    435  CA  HIS B  82      -6.512  42.934  26.748  1.00 49.53           C  
ATOM    436  CA  VAL B  83      -8.842  44.586  24.326  1.00 48.23           C  
ATOM    437  CA  ILE B  84      -6.434  47.533  24.008  1.00120.03           C  
ATOM    438  CA  ASN B  85      -3.074  45.767  24.186  1.00147.88           C  
ATOM    439  CA  GLN B  86      -2.336  45.054  20.543  1.00 77.56           C  
ATOM    440  CA  ALA B  87      -4.074  48.171  19.257  1.00 71.77           C  
ATOM    441  CA  GLN B  88      -2.138  50.453  16.994  1.00113.02           C  
ATOM    442  CA  LYS B  89      -5.206  52.625  16.670  1.00 32.78           C  
ATOM    443  CA  ILE B  90      -8.361  52.804  18.706  1.00 93.26           C  
ATOM    444  CA  SER B  91     -11.773  54.080  17.788  1.00 31.34           C  
ATOM    445  CA  ILE B  92     -14.831  54.473  19.954  1.00103.40           C  
ATOM    446  CA  GLN B  93     -18.365  54.201  18.675  1.00 40.43           C  
ATOM    447  CA  LEU B  94     -21.427  55.466  20.464  1.00 49.44           C  
ATOM    448  CA  ASN B  95     -24.803  53.809  20.327  1.00 39.23           C  
ATOM    449  CA  ASP B  96     -25.972  56.771  18.301  1.00 45.72           C  
ATOM    450  CA  GLY B  97     -23.466  55.922  15.623  1.00 30.38           C  
ATOM    451  CA  ARG B  98     -21.055  58.740  16.265  1.00 62.42           C  
ATOM    452  CA  GLU B  99     -17.457  57.633  16.247  1.00 35.06           C  
ATOM    453  CA  PHE B 100     -14.412  59.136  17.871  1.00 45.50           C  
ATOM    454  CA  ASP B 101     -10.702  58.489  18.018  1.00 33.40           C  
ATOM    455  CA  ALA B 102      -9.163  57.395  21.253  1.00 28.58           C  
ATOM    456  CA  LYS B 103      -5.715  57.307  22.734  1.00 98.96           C  
ATOM    457  CA  LEU B 104      -4.447  55.073  25.484  1.00 50.14           C  
ATOM    458  CA  ILE B 105      -3.985  57.017  28.675  1.00 92.44           C  
ATOM    459  CA  GLY B 106      -2.550  54.050  30.503  1.00 24.93           C  
ATOM    460  CA  SER B 107      -3.280  50.527  31.571  1.00 96.27           C  
ATOM    461  CA  ASP B 108      -1.972  47.654  33.583  1.00105.20           C  
ATOM    462  CA  ASP B 109      -1.674  43.960  32.842  1.00 68.61           C  
ATOM    463  CA  GLN B 110      -2.082  42.511  36.290  1.00 97.08           C  
ATOM    464  CA  SER B 111      -5.619  43.802  36.942  1.00 63.76           C  
ATOM    465  CA  ASP B 112      -6.334  44.080  33.213  1.00 71.63           C  
ATOM    466  CA  ILE B 113      -7.693  47.620  33.359  1.00 43.10           C  
ATOM    467  CA  ALA B 114      -6.944  50.287  30.782  1.00 31.36           C  
ATOM    468  CA  LEU B 115      -7.993  53.894  30.418  1.00 94.96           C  
ATOM    469  CA  LEU B 116      -8.703  55.538  27.080  1.00 84.98           C  
ATOM    470  CA  GLN B 117      -9.441  59.121  26.256  1.00 55.59           C  
ATOM    471  CA  ILE B 118     -11.681  60.216  23.447  1.00 41.90           C  
ATOM    472  CA  GLN B 119     -10.349  62.913  21.227  1.00 92.63           C  
ATOM    473  CA  ASN B 120     -12.625  65.918  20.950  1.00 49.14           C  
ATOM    474  CA  PRO B 121     -15.311  64.279  22.981  1.00 62.24           C  
ATOM    475  CA  SER B 122     -18.629  66.049  22.647  1.00 36.14           C  
ATOM    476  CA  LYS B 123     -22.069  65.576  24.169  1.00 42.60           C  
ATOM    477  CA  LEU B 124     -21.094  62.404  25.954  1.00 93.58           C  
ATOM    478  CA  THR B 125     -22.973  60.554  28.628  1.00100.72           C  
ATOM    479  CA  GLN B 126     -21.251  59.411  31.779  1.00 55.35           C  
ATOM    480  CA  ILE B 127     -22.023  56.361  33.842  1.00120.68           C  
ATOM    481  CA  ALA B 128     -22.320  56.623  37.599  1.00 30.67           C  
ATOM    482  CA  ILE B 129     -20.273  54.211  39.608  1.00 41.81           C  
ATOM    483  CA  ALA B 130     -21.666  52.211  42.492  1.00 34.92           C  
ATOM    484  CA  ASP B 131     -19.847  50.811  45.483  1.00 36.50           C  
ATOM    485  CA  SER B 132     -18.808  47.315  44.516  1.00 36.29           C  
ATOM    486  CA  ASP B 133     -18.173  46.449  48.128  1.00 33.56           C  
ATOM    487  CA  LYS B 134     -21.891  46.706  48.838  1.00139.25           C  
ATOM    488  CA  LEU B 135     -22.816  44.035  46.341  1.00107.52           C  
ATOM    489  CA  ARG B 136     -24.133  40.775  47.638  1.00205.02           C  
ATOM    490  CA  VAL B 137     -25.058  37.573  45.891  1.00 85.70           C  
ATOM    491  CA  GLY B 138     -28.527  37.677  44.459  1.00 25.73           C  
ATOM    492  CA  ASP B 139     -28.341  41.292  43.418  1.00 37.23           C  
ATOM    493  CA  PHE B 140     -29.572  41.899  39.909  1.00 75.30           C  
ATOM    494  CA  ALA B 141     -27.110  42.806  37.215  1.00 35.40           C  
ATOM    495  CA  VAL B 142     -27.255  43.850  33.596  1.00 38.60           C  
ATOM    496  CA  ALA B 143     -24.367  43.519  31.227  1.00 28.58           C  
ATOM    497  CA  VAL B 144     -23.908  45.796  28.278  1.00 33.49           C  
ATOM    498  CA  GLY B 145     -21.334  45.342  25.577  1.00 25.19           C  
ATOM    499  CA  ASN B 146     -20.917  44.200  22.041  1.00 76.44           C  
ATOM    500  CA  PRO B 147     -20.984  40.496  21.751  1.00166.27           C  
ATOM    501  CA  PHE B 148     -19.757  39.213  18.426  1.00 75.20           C  
ATOM    502  CA  GLY B 149     -19.587  42.816  17.364  1.00 31.88           C  
ATOM    503  CA  LEU B 150     -23.311  42.696  16.902  1.00 58.98           C  
ATOM    504  CA  GLY B 151     -23.804  46.124  18.385  1.00 38.98           C  
ATOM    505  CA  GLN B 152     -24.734  47.308  21.817  1.00114.78           C  
ATOM    506  CA  THR B 153     -26.500  44.475  23.539  1.00 50.99           C  
ATOM    507  CA  ALA B 154     -27.879  44.187  27.020  1.00 34.64           C  
ATOM    508  CA  THR B 155     -28.234  40.970  28.962  1.00 32.03           C  
ATOM    509  CA  SER B 156     -29.625  40.396  32.406  1.00 85.63           C  
ATOM    510  CA  GLY B 157     -28.684  38.161  35.298  1.00 24.13           C  
ATOM    511  CA  ILE B 158     -27.808  38.221  38.983  1.00 95.64           C  
ATOM    512  CA  VAL B 159     -24.544  38.422  40.842  1.00 48.41           C  
ATOM    513  CA  SER B 160     -23.575  34.800  41.233  1.00 42.38           C  
ATOM    514  CA  ALA B 161     -20.616  35.364  43.489  1.00 38.29           C  
ATOM    515  CA  LEU B 162     -17.993  37.854  44.491  1.00 94.61           C  
ATOM    516  CA  GLY B 163     -14.419  37.897  45.578  1.00 33.28           C  
ATOM    517  CA  ARG B 164     -13.367  35.077  43.429  1.00111.35           C  
ATOM    518  CA  SER B 165      -9.895  34.399  42.207  1.00 75.06           C  
ATOM    519  CA  GLY B 166      -7.644  31.517  41.461  1.00 34.37           C  
ATOM    520  CA  LEU B 167      -9.023  31.583  37.966  1.00 48.95           C  
ATOM    521  CA  ASN B 168      -5.485  32.397  36.937  1.00 59.63           C  
ATOM    522  CA  LEU B 169      -7.001  34.635  34.330  1.00 50.38           C  
ATOM    523  CA  GLU B 170      -5.251  37.688  35.707  1.00 98.77           C  
ATOM    524  CA  GLY B 171      -2.384  38.537  38.034  1.00 41.48           C  
ATOM    525  CA  LEU B 172      -4.771  40.179  40.432  1.00139.49           C  
ATOM    526  CA  GLU B 173      -8.243  38.837  40.487  1.00 78.53           C  
ATOM    527  CA  ASN B 174     -11.383  39.600  42.410  1.00 98.81           C  
ATOM    528  CA  PHE B 175     -14.008  38.930  39.924  1.00 76.86           C  
ATOM    529  CA  ILE B 176     -17.639  39.500  40.464  1.00 60.35           C  
ATOM    530  CA  GLN B 177     -19.289  36.490  38.929  1.00 57.65           C  
ATOM    531  CA  THR B 178     -22.480  36.916  36.960  1.00134.72           C  
ATOM    532  CA  ASP B 179     -24.961  34.756  35.094  1.00 66.76           C  
ATOM    533  CA  ALA B 180     -25.673  37.534  32.639  1.00 46.16           C  
ATOM    534  CA  SER B 181     -24.751  36.343  29.212  1.00 44.53           C  
ATOM    535  CA  ILE B 182     -21.315  37.572  28.360  1.00111.46           C  
ATOM    536  CA  ASN B 183     -19.601  36.595  25.177  1.00103.70           C  
ATOM    537  CA  ARG B 184     -16.564  37.530  23.152  1.00348.79           C  
ATOM    538  CA  GLY B 185     -17.199  41.238  22.423  1.00178.51           C  
ATOM    539  CA  ASN B 186     -18.266  41.890  26.015  1.00 88.37           C  
ATOM    540  CA  ALA B 187     -14.840  42.687  27.437  1.00 96.84           C  
ATOM    541  CA  GLY B 188     -14.477  46.221  28.690  1.00 30.10           C  
ATOM    542  CA  GLY B 189     -18.242  46.416  28.807  1.00 24.13           C  
ATOM    543  CA  ALA B 190     -20.241  47.462  31.789  1.00 45.69           C  
ATOM    544  CA  LEU B 191     -22.029  45.422  34.372  1.00115.35           C  
ATOM    545  CA  LEU B 192     -24.746  47.540  35.895  1.00120.60           C  
ATOM    546  CA  ASN B 193     -27.077  47.285  38.835  1.00 68.64           C  
ATOM    547  CA  LEU B 194     -30.790  48.012  38.725  1.00 57.62           C  
ATOM    548  CA  ASN B 195     -29.803  51.588  39.058  1.00 65.95           C  
ATOM    549  CA  GLY B 196     -27.838  52.638  36.018  1.00 63.30           C  
ATOM    550  CA  GLU B 197     -24.739  52.453  38.251  1.00 69.99           C  
ATOM    551  CA  LEU B 198     -21.636  50.544  37.230  1.00100.95           C  
ATOM    552  CA  ILE B 199     -20.842  47.549  39.410  1.00 82.20           C  
ATOM    553  CA  GLY B 200     -17.905  46.269  37.379  1.00 33.02           C  
ATOM    554  CA  ILE B 201     -16.241  45.836  34.008  1.00 99.88           C  
ATOM    555  CA  ASN B 202     -16.818  42.482  32.351  1.00 82.13           C  
ATOM    556  CA  THR B 203     -13.376  40.954  31.929  1.00 83.70           C  
ATOM    557  CA  ALA B 204     -13.775  37.288  31.123  1.00 58.74           C  
ATOM    558  CA  ILE B 205     -15.839  34.149  30.845  1.00 95.35           C  
ATOM    559  CA  LEU B 206     -15.434  30.490  31.615  1.00 64.60           C  
ATOM    560  CA  ALA B 207     -16.858  28.438  28.823  1.00 42.77           C  
ATOM    561  CA  PRO B 208     -15.813  25.223  27.292  1.00 68.59           C  
ATOM    562  CA  GLY B 209     -17.635  26.055  24.075  1.00 28.36           C  
ATOM    563  CA  GLY B 210     -16.242  29.524  23.859  1.00 23.57           C  
ATOM    564  CA  GLY B 211     -19.816  30.661  24.232  1.00 23.73           C  
ATOM    565  CA  SER B 212     -21.487  31.975  27.350  1.00 59.02           C  
ATOM    566  CA  VAL B 213     -22.010  29.188  29.878  1.00 61.65           C  
ATOM    567  CA  GLY B 214     -23.536  31.605  32.319  1.00 39.06           C  
ATOM    568  CA  ILE B 215     -20.340  32.010  34.252  1.00 65.67           C  
ATOM    569  CA  GLY B 216     -18.873  35.430  33.630  1.00 24.18           C  
ATOM    570  CA  PHE B 217     -16.423  37.506  35.593  1.00 54.12           C  
ATOM    571  CA  ALA B 218     -16.080  41.233  35.999  1.00 33.04           C  
ATOM    572  CA  ILE B 219     -13.655  43.578  37.703  1.00 69.97           C  
ATOM    573  CA  PRO B 220     -15.410  45.327  40.477  1.00 82.21           C  
ATOM    574  CA  SER B 221     -16.357  48.954  40.030  1.00 39.57           C  
ATOM    575  CA  ASN B 222     -14.325  49.981  42.964  1.00 60.96           C  
ATOM    576  CA  MET B 223     -11.704  48.141  41.126  1.00104.86           C  
ATOM    577  CA  ALA B 224     -11.835  50.022  37.899  1.00 52.35           C  
ATOM    578  CA  ARG B 225     -12.682  53.277  39.575  1.00 99.87           C  
ATOM    579  CA  THR B 226      -9.637  53.941  41.625  1.00 62.42           C  
ATOM    580  CA  LEU B 227      -7.361  52.096  39.191  1.00112.19           C  
ATOM    581  CA  ALA B 228      -8.697  54.310  36.470  1.00 46.13           C  
ATOM    582  CA  GLN B 229      -8.318  57.301  38.672  1.00 81.08           C  
ATOM    583  CA  GLN B 230      -4.599  57.410  38.990  1.00106.41           C  
ATOM    584  CA  LEU B 231      -4.397  56.487  35.359  1.00 57.06           C  
ATOM    585  CA  ILE B 232      -5.561  60.022  34.983  1.00127.04           C  
ATOM    586  CA  ASP B 233      -4.281  61.113  38.456  1.00183.63           C  
ATOM    587  CA  PHE B 234      -2.601  60.883  41.002  1.00173.25           C  
ATOM    588  CA  GLY B 235      -0.811  58.527  38.706  1.00 57.62           C  
ATOM    589  CA  GLU B 236       2.306  57.487  40.487  1.00 71.62           C  
ATOM    590  CA  ILE B 237       4.286  55.462  38.084  1.00144.63           C  
ATOM    591  CA  LYS B 238       5.599  53.220  40.770  1.00275.27           C  
ATOM    592  CA  ARG B 239       4.355  50.759  41.418  1.00220.35           C  
ATOM    593  CA  GLY B 240       1.685  51.475  38.881  1.00 57.95           C  
ATOM    594  CA  LEU B 241       0.813  47.905  39.489  1.00135.54           C  
ATOM    595  CA  LEU B 242       2.646  44.817  40.766  1.00 94.22           C  
ATOM    596  CA  GLY B 243       3.188  42.948  37.553  1.00 53.24           C  
ATOM    597  CA  ILE B 244       2.803  39.415  38.859  1.00 75.06           C  
ATOM    598  CA  LYS B 245       0.882  36.302  37.991  1.00131.95           C  
ATOM    599  CA  GLY B 246      -0.735  34.104  40.548  1.00 37.21           C  
ATOM    600  CA  THR B 247      -3.638  31.852  41.336  1.00 79.21           C  
ATOM    601  CA  GLU B 248      -5.277  30.565  44.469  1.00 91.40           C  
ATOM    602  CA  MET B 249      -2.798  29.219  46.953  1.00128.24           C  
ATOM    603  CA  SER B 250      -1.863  25.654  46.463  1.00104.29           C  
ATOM    604  CA  ALA B 251      -4.514  23.469  47.968  1.00 45.90           C  
ATOM    605  CA  ASP B 252      -2.415  20.625  49.276  1.00 41.00           C  
ATOM    606  CA  ILE B 253      -0.316  22.659  51.631  1.00101.70           C  
ATOM    607  CA  ALA B 254      -3.290  24.816  52.383  1.00 37.60           C  
ATOM    608  CA  LYS B 255      -5.131  21.851  53.766  1.00120.26           C  
ATOM    609  CA  ALA B 256      -2.312  20.766  56.013  1.00 36.36           C  
ATOM    610  CA  PHE B 257      -1.075  24.173  57.076  1.00 68.26           C  
ATOM    611  CA  ASN B 258      -4.201  25.933  58.186  1.00 61.21           C  
ATOM    612  CA  LEU B 259      -2.115  29.075  57.820  1.00 64.73           C  
ATOM    613  CA  ASP B 260      -3.340  32.377  59.133  1.00111.04           C  
ATOM    614  CA  VAL B 261      -4.801  33.353  55.842  1.00 61.56           C  
ATOM    615  CA  GLN B 262      -7.270  30.762  54.761  1.00 69.60           C  
ATOM    616  CA  ARG B 263      -6.571  31.493  51.223  1.00273.33           C  
ATOM    617  CA  GLY B 264      -3.897  33.725  49.854  1.00 84.38           C  
ATOM    618  CA  ALA B 265      -2.703  34.810  46.547  1.00 52.65           C  
ATOM    619  CA  PHE B 266       0.144  32.715  45.535  1.00135.71           C  
ATOM    620  CA  VAL B 267       2.475  33.960  42.921  1.00 75.00           C  
ATOM    621  CA  SER B 268       3.995  31.535  40.468  1.00 64.35           C  
ATOM    622  CA  GLU B 269       5.905  34.153  38.571  1.00 83.03           C  
ATOM    623  CA  VAL B 270       8.017  37.265  38.674  1.00109.27           C  
ATOM    624  CA  LEU B 271       7.761  39.801  35.922  1.00 97.73           C  
ATOM    625  CA  PRO B 272      10.781  41.542  34.653  1.00 69.82           C  
ATOM    626  CA  GLY B 273      11.157  45.228  35.296  1.00 26.55           C  
ATOM    627  CA  SER B 274       7.861  44.721  36.957  1.00 95.04           C  
ATOM    628  CA  GLY B 275       6.611  46.114  40.164  1.00 42.18           C  
ATOM    629  CA  SER B 276       7.012  42.910  42.015  1.00 56.52           C  
ATOM    630  CA  ALA B 277      10.556  42.451  40.851  1.00 49.65           C  
ATOM    631  CA  LYS B 278      12.142  45.527  42.434  1.00139.47           C  
ATOM    632  CA  ALA B 279       9.856  45.150  45.358  1.00 44.72           C  
ATOM    633  CA  GLY B 280      11.729  41.964  45.539  1.00 42.90           C  
ATOM    634  CA  VAL B 281       8.724  39.723  45.510  1.00 84.10           C  
ATOM    635  CA  LYS B 282       9.458  36.746  43.480  1.00226.49           C  
ATOM    636  CA  ALA B 283       7.664  33.570  43.052  1.00104.96           C  
ATOM    637  CA  GLY B 284       6.585  30.908  45.338  1.00 49.18           C  
ATOM    638  CA  ASP B 285       5.338  33.330  47.873  1.00129.58           C  
ATOM    639  CA  ILE B 286       2.060  33.670  49.287  1.00102.93           C  
ATOM    640  CA  ILE B 287       0.645  37.093  49.559  1.00163.55           C  
ATOM    641  CA  THR B 288      -1.064  37.013  52.911  1.00 78.73           C  
ATOM    642  CA  SER B 289      -2.335  40.514  53.065  1.00 54.82           C  
ATOM    643  CA  LEU B 290      -2.447  43.928  51.496  1.00 81.22           C  
ATOM    644  CA  ASN B 291      -2.195  46.758  53.937  1.00263.12           C  
ATOM    645  CA  GLY B 292      -3.121  47.367  56.797  1.00137.03           C  
ATOM    646  CA  LYS B 293      -5.801  44.759  57.251  1.00161.66           C  
ATOM    647  CA  PRO B 294      -5.743  41.143  56.396  1.00 64.66           C  
ATOM    648  CA  LEU B 295      -6.444  40.141  52.844  1.00127.12           C  
ATOM    649  CA  ASN B 296      -8.201  36.956  51.958  1.00107.27           C  
ATOM    650  CA  SER B 297      -7.937  34.820  48.897  1.00100.26           C  
ATOM    651  CA  PHE B 298      -6.255  35.885  45.746  1.00 97.05           C  
ATOM    652  CA  ALA B 299      -9.765  36.909  44.901  1.00 47.80           C  
ATOM    653  CA  GLU B 300      -9.793  39.585  47.500  1.00 78.49           C  
ATOM    654  CA  LEU B 301      -6.410  40.534  46.247  1.00 61.86           C  
ATOM    655  CA  ARG B 302      -7.517  41.907  42.981  1.00161.18           C  
ATOM    656  CA  SER B 303     -10.604  43.178  44.621  1.00 53.24           C  
ATOM    657  CA  ARG B 304      -8.691  45.626  46.625  1.00128.12           C  
ATOM    658  CA  ILE B 305      -5.813  46.173  44.229  1.00121.80           C  
ATOM    659  CA  ALA B 306      -7.971  46.330  41.205  1.00 65.92           C  
ATOM    660  CA  THR B 307      -9.938  48.710  43.317  1.00129.76           C  
ATOM    661  CA  THR B 308      -6.986  50.816  44.272  1.00126.09           C  
ATOM    662  CA  GLU B 309      -5.120  53.360  42.230  1.00 85.38           C  
ATOM    663  CA  PRO B 310      -2.618  51.823  40.002  1.00188.36           C  
ATOM    664  CA  GLY B 311      -0.481  53.543  41.096  1.00124.00           C  
ATOM    665  CA  THR B 312      -0.876  53.904  44.810  1.00 73.85           C  
ATOM    666  CA  LYS B 313       2.109  52.926  46.830  1.00 71.81           C  
ATOM    667  CA  VAL B 314       1.097  49.989  48.940  1.00 46.17           C  
ATOM    668  CA  LYS B 315       2.673  47.429  51.227  1.00 92.35           C  
ATOM    669  CA  LEU B 316       2.299  43.720  50.712  1.00 51.82           C  
ATOM    670  CA  GLY B 317       2.660  40.960  53.228  1.00 43.29           C  
ATOM    671  CA  LEU B 318       3.844  37.724  51.852  1.00165.32           C  
ATOM    672  CA  LEU B 319       4.806  34.455  53.385  1.00110.07           C  
ATOM    673  CA  ARG B 320       7.980  33.178  52.153  1.00187.46           C  
ATOM    674  CA  ASN B 321       9.742  30.259  53.644  1.00132.58           C  
ATOM    675  CA  GLY B 322       7.626  30.137  56.592  1.00 46.55           C  
ATOM    676  CA  LYS B 323       8.832  33.404  57.586  1.00125.17           C  
ATOM    677  CA  PRO B 324       7.309  36.778  57.495  1.00120.16           C  
ATOM    678  CA  LEU B 325       7.877  40.005  55.554  1.00180.14           C  
ATOM    679  CA  GLU B 326       6.269  43.090  54.307  1.00107.95           C  
ATOM    680  CA  VAL B 327       7.616  44.995  51.337  1.00 59.62           C  
ATOM    681  CA  GLU B 328       6.602  48.181  49.642  1.00 43.88           C  
ATOM    682  CA  VAL B 329       5.472  47.654  46.124  1.00 52.77           C  
ATOM    683  CA  SER B 340      30.444  50.774  21.680  1.00 42.38           C  
ATOM    684  CA  ALA B 341      30.239  50.390  17.958  1.00 50.18           C  
ATOM    685  CA  GLU B 342      28.144  47.290  18.307  1.00 64.00           C  
ATOM    686  CA  MET B 343      24.882  48.939  19.249  1.00 78.66           C  
ATOM    687  CA  ILE B 344      24.863  51.398  16.408  1.00 49.14           C  
ATOM    688  CA  THR B 345      26.508  48.864  14.191  1.00129.25           C  
ATOM    689  CA  PRO B 346      25.386  45.316  14.104  1.00151.19           C  
ATOM    690  CA  ALA B 347      27.532  42.626  15.688  1.00 82.09           C  
ATOM    691  CA  LEU B 348      30.633  44.680  14.996  1.00109.54           C  
ATOM    692  CA  GLU B 349      32.299  44.851  18.342  1.00128.51           C  
ATOM    693  CA  GLY B 350      34.718  47.651  18.537  1.00 27.60           C  
ATOM    694  CA  ALA B 351      35.518  51.007  19.952  1.00 36.96           C  
ATOM    695  CA  THR B 352      32.815  52.694  21.929  1.00 49.76           C  
ATOM    696  CA  LEU B 353      31.135  55.708  20.441  1.00 96.57           C  
ATOM    697  CA  SER B 354      29.926  58.921  21.994  1.00 37.64           C  
ATOM    698  CA  ASP B 355      27.829  61.870  20.821  1.00 63.53           C  
ATOM    699  CA  GLY B 356      28.635  65.566  20.507  1.00 48.27           C  
ATOM    700  CA  GLN B 357      31.912  66.856  19.267  1.00140.47           C  
ATOM    701  CA  LEU B 358      32.719  66.213  22.685  1.00173.85           C  
ATOM    702  CA  LYS B 359      31.648  69.590  23.984  1.00142.68           C  
ATOM    703  CA  ASP B 360      32.034  71.541  20.771  1.00 51.36           C  
ATOM    704  CA  GLY B 361      29.762  71.853  17.819  1.00 23.13           C  
ATOM    705  CA  GLY B 362      29.097  68.298  16.908  1.00 36.72           C  
ATOM    706  CA  LYS B 363      31.343  67.307  14.087  1.00 97.91           C  
ATOM    707  CA  GLY B 364      29.799  63.950  14.661  1.00 29.26           C  
ATOM    708  CA  ILE B 365      30.010  60.818  16.746  1.00193.76           C  
ATOM    709  CA  LYS B 366      33.277  60.178  18.454  1.00 60.41           C  
ATOM    710  CA  ILE B 367      34.972  56.833  18.835  1.00113.69           C  
ATOM    711  CA  ASP B 368      36.078  56.668  22.434  1.00 65.02           C  
ATOM    712  CA  GLU B 369      38.516  53.796  22.444  1.00136.96           C  
ATOM    713  CA  VAL B 370      39.540  51.010  20.171  1.00125.93           C  
ATOM    714  CA  VAL B 371      39.082  47.469  21.444  1.00124.66           C  
ATOM    715  CA  LYS B 372      41.388  46.715  18.474  1.00216.81           C  
ATOM    716  CA  GLY B 373      41.193  42.955  18.684  1.00 39.50           C  
ATOM    717  CA  SER B 374      37.541  43.691  17.780  1.00105.37           C  
ATOM    718  CA  PRO B 375      36.230  43.837  14.312  1.00 74.64           C  
ATOM    719  CA  ALA B 376      35.344  47.493  14.527  1.00 52.44           C  
ATOM    720  CA  ALA B 377      39.089  47.707  14.752  1.00 50.51           C  
ATOM    721  CA  GLN B 378      39.713  45.491  11.760  1.00106.26           C  
ATOM    722  CA  ALA B 379      38.236  47.756   9.097  1.00 64.93           C  
ATOM    723  CA  GLY B 380      39.914  50.969  10.009  1.00 69.16           C  
ATOM    724  CA  LEU B 381      38.184  52.463  12.982  1.00 65.90           C  
ATOM    725  CA  GLN B 382      40.794  53.924  15.261  1.00107.03           C  
ATOM    726  CA  LYS B 383      40.219  55.863  18.417  1.00 96.81           C  
ATOM    727  CA  ASP B 384      39.771  59.630  18.359  1.00 80.36           C  
ATOM    728  CA  ASP B 385      38.119  59.503  14.976  1.00 54.35           C  
ATOM    729  CA  VAL B 386      35.130  61.725  14.401  1.00 57.65           C  
ATOM    730  CA  ILE B 387      32.400  60.453  12.173  1.00131.17           C  
ATOM    731  CA  ILE B 388      31.200  63.557  10.430  1.00 85.02           C  
ATOM    732  CA  GLY B 389      28.654  61.773   8.247  1.00 39.63           C  
ATOM    733  CA  VAL B 390      27.698  58.577   6.526  1.00 48.78           C  
ATOM    734  CA  ASN B 391      26.514  57.943   2.998  1.00 75.07           C  
ATOM    735  CA  ARG B 392      26.604  61.591   1.923  1.00151.67           C  
ATOM    736  CA  ASP B 393      24.663  62.371   5.044  1.00 43.48           C  
ATOM    737  CA  ARG B 394      26.013  64.422   7.877  1.00 66.45           C  
ATOM    738  CA  VAL B 395      25.918  62.838  11.292  1.00130.45           C  
ATOM    739  CA  ASN B 396      25.591  65.340  14.059  1.00 48.06           C  
ATOM    740  CA  SER B 397      25.070  62.638  16.630  1.00101.10           C  
ATOM    741  CA  ILE B 398      24.409  58.971  17.108  1.00100.56           C  
ATOM    742  CA  ALA B 399      20.724  59.350  16.471  1.00 25.20           C  
ATOM    743  CA  GLU B 400      21.322  60.814  13.050  1.00 28.24           C  
ATOM    744  CA  MET B 401      23.887  58.175  12.291  1.00 36.06           C  
ATOM    745  CA  ARG B 402      21.361  55.580  13.254  1.00155.50           C  
ATOM    746  CA  LYS B 403      19.028  57.099  10.712  1.00 53.37           C  
ATOM    747  CA  VAL B 404      21.363  56.445   7.830  1.00 30.22           C  
ATOM    748  CA  LEU B 405      21.726  52.894   9.051  1.00 92.18           C  
ATOM    749  CA  ALA B 406      17.974  52.674   9.147  1.00 33.95           C  
ATOM    750  CA  ALA B 407      18.159  52.840   5.372  1.00 34.10           C  
ATOM    751  CA  LYS B 408      20.399  49.803   5.712  1.00170.34           C  
ATOM    752  CA  PRO B 409      22.376  50.546   2.598  1.00 65.30           C  
ATOM    753  CA  ALA B 410      24.474  47.614   1.463  1.00 23.69           C  
ATOM    754  CA  ILE B 411      27.525  49.806   1.595  1.00 82.99           C  
ATOM    755  CA  ILE B 412      27.830  52.273   4.399  1.00 47.40           C  
ATOM    756  CA  ALA B 413      30.237  55.141   4.183  1.00 73.98           C  
ATOM    757  CA  LEU B 414      31.159  56.284   7.598  1.00179.51           C  
ATOM    758  CA  GLN B 415      32.898  59.746   7.758  1.00207.84           C  
ATOM    759  CA  ILE B 416      35.874  60.355   9.740  1.00227.12           C  
ATOM    760  CA  VAL B 417      38.247  63.048  10.478  1.00128.52           C  
ATOM    761  CA  ARG B 418      41.471  61.721  11.823  1.00103.54           C  
ATOM    762  CA  GLY B 419      44.056  64.162  12.985  1.00 30.02           C  
ATOM    763  CA  ASN B 420      43.919  67.101  10.720  1.00 93.82           C  
ATOM    764  CA  GLU B 421      43.224  64.685   7.970  1.00 63.27           C  
ATOM    765  CA  SER B 422      40.091  63.517   6.478  1.00 86.50           C  
ATOM    766  CA  ILE B 423      39.731  59.832   6.850  1.00185.51           C  
ATOM    767  CA  TYR B 424      37.602  57.808   4.607  1.00247.37           C  
ATOM    768  CA  LEU B 425      36.188  54.485   6.322  1.00217.75           C  
ATOM    769  CA  LEU B 426      33.400  52.038   5.453  1.00262.24           C  
ATOM    770  CA  MET B 427      31.689  48.686   5.688  1.00 75.83           C  
ATOM    771  CA  ARG B 428      30.843  45.651   3.658  1.00109.30           C  
TER     772      ARG B 428                                                      
ATOM    773  CA  PRO C  11     -44.451  40.339  42.695  1.00 85.77           C  
ATOM    774  CA  LEU C  12     -45.751  40.166  39.166  1.00111.04           C  
ATOM    775  CA  PRO C  13     -49.029  38.649  38.532  1.00 92.64           C  
ATOM    776  CA  SER C  14     -48.856  34.960  38.051  1.00104.33           C  
ATOM    777  CA  LEU C  15     -48.514  33.908  34.451  1.00172.76           C  
ATOM    778  CA  ALA C  16     -50.487  30.766  35.006  1.00 45.64           C  
ATOM    779  CA  PRO C  17     -53.786  32.466  35.350  1.00 70.33           C  
ATOM    780  CA  MET C  18     -53.347  34.364  32.104  1.00 59.62           C  
ATOM    781  CA  LEU C  19     -51.898  31.357  30.358  1.00117.94           C  
ATOM    782  CA  GLU C  20     -54.720  29.017  31.206  1.00 34.97           C  
ATOM    783  CA  LYS C  21     -57.217  30.971  29.179  1.00 62.35           C  
ATOM    784  CA  VAL C  22     -54.893  31.780  26.266  1.00 52.23           C  
ATOM    785  CA  LEU C  23     -53.035  28.529  25.718  1.00114.97           C  
ATOM    786  CA  PRO C  24     -55.712  26.672  23.861  1.00 65.40           C  
ATOM    787  CA  ALA C  25     -55.533  29.342  21.178  1.00 29.75           C  
ATOM    788  CA  VAL C  26     -52.009  28.334  20.239  1.00 31.39           C  
ATOM    789  CA  VAL C  27     -51.722  25.159  18.252  1.00 35.69           C  
ATOM    790  CA  SER C  28     -49.073  22.918  16.802  1.00 88.05           C  
ATOM    791  CA  VAL C  29     -48.952  22.480  13.090  1.00123.49           C  
ATOM    792  CA  ARG C  30     -47.887  19.242  11.542  1.00 71.15           C  
ATOM    793  CA  VAL C  31     -46.737  19.061   7.985  1.00 41.93           C  
ATOM    794  CA  GLU C  32     -46.015  16.290   5.563  1.00 90.21           C  
ATOM    795  CA  GLY C  33     -44.994  16.446   1.966  1.00 24.10           C  
ATOM    796  CA  THR C  34     -42.347  15.790  -0.602  1.00118.34           C  
ATOM    797  CA  ALA C  58     -40.141  13.238  -3.428  1.00 25.71           C  
ATOM    798  CA  GLN C  59     -39.118  11.568  -0.213  1.00 60.73           C  
ATOM    799  CA  PRO C  60     -41.562  12.110   2.533  1.00 60.42           C  
ATOM    800  CA  PHE C  61     -40.634  14.414   5.344  1.00 52.56           C  
ATOM    801  CA  GLU C  62     -42.458  15.594   8.393  1.00 24.44           C  
ATOM    802  CA  GLY C  63     -42.140  19.059   9.783  1.00 16.45           C  
ATOM    803  CA  LEU C  64     -43.297  20.566  13.008  1.00101.31           C  
ATOM    804  CA  GLY C  65     -44.310  24.131  13.696  1.00 20.94           C  
ATOM    805  CA  SER C  66     -46.890  26.149  15.548  1.00 27.78           C  
ATOM    806  CA  GLY C  67     -49.767  28.429  14.705  1.00 16.64           C  
ATOM    807  CA  VAL C  68     -52.292  30.632  16.405  1.00 91.67           C  
ATOM    808  CA  ILE C  69     -55.998  30.526  15.983  1.00 72.77           C  
ATOM    809  CA  ILE C  70     -57.176  33.926  14.860  1.00 60.41           C  
ATOM    810  CA  ASN C  71     -60.833  33.170  14.199  1.00 45.33           C  
ATOM    811  CA  ALA C  72     -62.651  30.503  16.113  1.00 37.88           C  
ATOM    812  CA  SER C  73     -65.706  30.228  13.998  1.00 31.42           C  
ATOM    813  CA  LYS C  74     -63.857  30.152  10.753  1.00 83.81           C  
ATOM    814  CA  GLY C  75     -60.979  28.183  12.141  1.00 24.75           C  
ATOM    815  CA  TYR C  76     -58.344  30.466  10.696  1.00 66.43           C  
ATOM    816  CA  VAL C  77     -54.867  29.765  11.965  1.00 41.97           C  
ATOM    817  CA  LEU C  78     -51.902  32.024  11.356  1.00 48.71           C  
ATOM    818  CA  THR C  79     -48.507  30.487  10.753  1.00146.74           C  
ATOM    819  CA  ASN C  80     -45.214  31.137   9.101  1.00 67.05           C  
ATOM    820  CA  ASN C  81     -45.071  30.518   5.405  1.00 46.66           C  
ATOM    821  CA  HIS C  82     -41.898  28.534   5.749  1.00 51.41           C  
ATOM    822  CA  VAL C  83     -43.506  25.964   7.948  1.00 61.09           C  
ATOM    823  CA  ILE C  84     -46.343  25.502   5.425  1.00119.00           C  
ATOM    824  CA  ASN C  85     -44.455  25.854   2.137  1.00150.57           C  
ATOM    825  CA  GLN C  86     -43.523  22.240   1.401  1.00 83.02           C  
ATOM    826  CA  ALA C  87     -46.625  20.787   3.030  1.00 68.28           C  
ATOM    827  CA  GLN C  88     -48.659  18.454   0.912  1.00104.40           C  
ATOM    828  CA  LYS C  89     -50.973  17.918   3.861  1.00 34.10           C  
ATOM    829  CA  ILE C  90     -51.344  19.892   7.040  1.00 42.69           C  
ATOM    830  CA  SER C  91     -52.803  18.969  10.368  1.00 68.23           C  
ATOM    831  CA  ILE C  92     -53.304  21.037  13.481  1.00 85.04           C  
ATOM    832  CA  GLN C  93     -53.252  19.730  17.008  1.00 42.75           C  
ATOM    833  CA  LEU C  94     -54.799  21.420  19.987  1.00 84.88           C  
ATOM    834  CA  ASN C  95     -53.392  21.381  23.490  1.00 45.33           C  
ATOM    835  CA  ASP C  96     -56.325  19.207  24.434  1.00 54.79           C  
ATOM    836  CA  GLY C  97     -55.142  16.588  22.011  1.00 32.81           C  
ATOM    837  CA  ARG C  98     -57.820  17.134  19.425  1.00 87.88           C  
ATOM    838  CA  GLU C  99     -56.527  17.135  15.888  1.00 39.23           C  
ATOM    839  CA  PHE C 100     -57.921  18.619  12.716  1.00 40.12           C  
ATOM    840  CA  ASP C 101     -57.016  18.883   9.075  1.00 28.06           C  
ATOM    841  CA  ALA C 102     -56.141  22.210   7.585  1.00 35.11           C  
ATOM    842  CA  LYS C 103     -55.940  23.742   4.165  1.00 78.90           C  
ATOM    843  CA  LEU C 104     -53.776  26.607   3.035  1.00 52.26           C  
ATOM    844  CA  ILE C 105     -55.852  29.700   2.532  1.00104.03           C  
ATOM    845  CA  GLY C 106     -52.936  31.693   1.223  1.00 26.66           C  
ATOM    846  CA  SER C 107     -49.532  32.961   2.166  1.00 95.46           C  
ATOM    847  CA  ASP C 108     -46.749  35.212   1.085  1.00101.00           C  
ATOM    848  CA  ASP C 109     -43.012  34.738   0.902  1.00 65.85           C  
ATOM    849  CA  GLN C 110     -41.681  38.171   1.579  1.00148.56           C  
ATOM    850  CA  SER C 111     -43.314  38.694   4.989  1.00 65.24           C  
ATOM    851  CA  ASP C 112     -43.390  34.940   5.622  1.00 68.72           C  
ATOM    852  CA  ILE C 113     -47.021  34.910   6.759  1.00 99.19           C  
ATOM    853  CA  ALA C 114     -49.435  32.118   5.894  1.00 35.38           C  
ATOM    854  CA  LEU C 115     -53.088  31.545   6.668  1.00 64.88           C  
ATOM    855  CA  LEU C 116     -54.590  28.142   7.260  1.00 76.48           C  
ATOM    856  CA  GLN C 117     -58.141  27.062   7.809  1.00 35.13           C  
ATOM    857  CA  ILE C 118     -59.163  24.155   9.964  1.00 42.79           C  
ATOM    858  CA  GLN C 119     -61.632  21.751   8.490  1.00 91.54           C  
ATOM    859  CA  ASN C 120     -64.767  21.353  10.567  1.00 59.10           C  
ATOM    860  CA  PRO C 121     -63.400  23.479  13.315  1.00 65.35           C  
ATOM    861  CA  SER C 122     -65.321  23.001  16.498  1.00 82.49           C  
ATOM    862  CA  LYS C 123     -65.160  24.489  19.984  1.00 43.99           C  
ATOM    863  CA  LEU C 124     -62.056  26.506  19.288  1.00 84.57           C  
ATOM    864  CA  THR C 125     -60.570  29.262  21.371  1.00 94.79           C  
ATOM    865  CA  GLN C 126     -59.268  32.395  19.768  1.00 61.15           C  
ATOM    866  CA  ILE C 127     -56.456  34.659  20.684  1.00 99.08           C  
ATOM    867  CA  ALA C 128     -57.006  38.384  20.958  1.00 26.70           C  
ATOM    868  CA  ILE C 129     -54.719  40.622  18.985  1.00 90.96           C  
ATOM    869  CA  ALA C 130     -52.867  43.484  20.610  1.00 31.94           C  
ATOM    870  CA  ASP C 131     -51.602  46.563  18.857  1.00 44.01           C  
ATOM    871  CA  SER C 132     -47.969  45.879  18.093  1.00 33.15           C  
ATOM    872  CA  ASP C 133     -47.337  49.547  17.486  1.00 31.79           C  
ATOM    873  CA  LYS C 134     -47.836  50.171  21.189  1.00 90.64           C  
ATOM    874  CA  LEU C 135     -45.071  47.803  22.238  1.00 58.92           C  
ATOM    875  CA  ARG C 136     -42.040  49.312  23.892  1.00 70.60           C  
ATOM    876  CA  VAL C 137     -38.790  47.729  24.879  1.00 82.17           C  
ATOM    877  CA  GLY C 138     -38.919  46.220  28.317  1.00 23.75           C  
ATOM    878  CA  ASP C 139     -42.430  44.937  27.916  1.00 28.94           C  
ATOM    879  CA  PHE C 140     -42.954  41.398  29.112  1.00 48.90           C  
ATOM    880  CA  ALA C 141     -43.537  38.722  26.528  1.00 33.98           C  
ATOM    881  CA  VAL C 142     -44.331  35.056  26.588  1.00101.47           C  
ATOM    882  CA  ALA C 143     -43.690  32.743  23.696  1.00 33.31           C  
ATOM    883  CA  VAL C 144     -45.770  29.686  23.048  1.00 28.99           C  
ATOM    884  CA  GLY C 145     -45.082  27.029  20.478  1.00 23.28           C  
ATOM    885  CA  ASN C 146     -43.640  23.609  20.289  1.00 73.64           C  
ATOM    886  CA  PRO C 147     -39.954  23.487  20.378  1.00 68.65           C  
ATOM    887  CA  PHE C 148     -38.394  20.276  19.178  1.00 67.02           C  
ATOM    888  CA  GLY C 149     -41.931  19.012  18.863  1.00 27.71           C  
ATOM    889  CA  LEU C 150     -42.074  18.454  22.610  1.00 95.33           C  
ATOM    890  CA  GLY C 151     -45.580  19.816  22.911  1.00 36.10           C  
ATOM    891  CA  GLN C 152     -46.925  23.186  23.803  1.00 56.49           C  
ATOM    892  CA  THR C 153     -44.231  25.025  25.669  1.00 33.56           C  
ATOM    893  CA  ALA C 154     -44.289  28.471  27.151  1.00 34.22           C  
ATOM    894  CA  THR C 155     -41.218  30.582  27.669  1.00 98.63           C  
ATOM    895  CA  SER C 156     -40.904  34.033  29.130  1.00 36.87           C  
ATOM    896  CA  GLY C 157     -38.852  37.100  28.370  1.00 26.19           C  
ATOM    897  CA  ILE C 158     -39.111  40.783  27.530  1.00 63.41           C  
ATOM    898  CA  VAL C 159     -39.258  42.669  24.271  1.00 47.16           C  
ATOM    899  CA  SER C 160     -35.618  43.270  23.477  1.00 45.52           C  
ATOM    900  CA  ALA C 161     -36.111  45.501  20.481  1.00 36.93           C  
ATOM    901  CA  LEU C 162     -38.546  46.445  17.771  1.00 93.28           C  
ATOM    902  CA  GLY C 163     -38.405  47.546  14.197  1.00 31.97           C  
ATOM    903  CA  ARG C 164     -35.446  45.427  13.401  1.00105.76           C  
ATOM    904  CA  SER C 165     -34.399  44.485   9.923  1.00149.68           C  
ATOM    905  CA  GLY C 166     -31.431  43.983   7.715  1.00 44.26           C  
ATOM    906  CA  LEU C 167     -31.375  40.465   9.053  1.00 50.45           C  
ATOM    907  CA  ASN C 168     -31.937  39.424   5.471  1.00 63.79           C  
ATOM    908  CA  LEU C 169     -34.058  36.641   6.848  1.00 48.95           C  
ATOM    909  CA  GLU C 170     -37.101  37.846   4.963  1.00102.70           C  
ATOM    910  CA  GLY C 171     -37.847  40.132   2.044  1.00 34.76           C  
ATOM    911  CA  LEU C 172     -39.878  42.338   4.317  1.00 70.61           C  
ATOM    912  CA  GLU C 173     -38.767  42.486   7.875  1.00 98.69           C  
ATOM    913  CA  ASN C 174     -39.769  44.291  11.033  1.00109.72           C  
ATOM    914  CA  PHE C 175     -39.082  41.830  13.672  1.00 91.89           C  
ATOM    915  CA  ILE C 176     -39.843  42.351  17.265  1.00153.21           C  
ATOM    916  CA  GLN C 177     -36.923  40.861  19.076  1.00146.73           C  
ATOM    917  CA  THR C 178     -37.395  38.910  22.248  1.00 46.23           C  
ATOM    918  CA  ASP C 179     -35.182  37.120  24.753  1.00 65.69           C  
ATOM    919  CA  ALA C 180     -37.854  34.492  25.344  1.00 36.21           C  
ATOM    920  CA  SER C 181     -36.426  31.147  24.448  1.00 42.14           C  
ATOM    921  CA  ILE C 182     -37.395  30.312  20.928  1.00 41.42           C  
ATOM    922  CA  ASN C 183     -36.144  27.181  19.285  1.00 43.83           C  
ATOM    923  CA  ARG C 184     -36.887  25.201  16.209  1.00118.57           C  
ATOM    924  CA  GLY C 185     -40.544  24.308  16.129  1.00 22.92           C  
ATOM    925  CA  ASN C 186     -41.412  27.698  17.561  1.00 51.31           C  
ATOM    926  CA  ALA C 187     -42.134  29.158  14.169  1.00104.72           C  
ATOM    927  CA  GLY C 188     -45.692  30.194  13.596  1.00 25.49           C  
ATOM    928  CA  GLY C 189     -46.092  30.246  17.349  1.00 21.78           C  
ATOM    929  CA  ALA C 190     -47.413  33.133  19.328  1.00 44.24           C  
ATOM    930  CA  LEU C 191     -45.675  35.826  21.276  1.00 61.57           C  
ATOM    931  CA  LEU C 192     -48.028  37.132  23.908  1.00 95.63           C  
ATOM    932  CA  ASN C 193     -48.155  40.022  26.305  1.00 58.82           C  
ATOM    933  CA  LEU C 194     -49.143  39.778  29.946  1.00 55.64           C  
ATOM    934  CA  ASN C 195     -52.717  40.196  28.812  1.00 48.72           C  
ATOM    935  CA  GLY C 196     -52.386  37.069  26.747  1.00 24.13           C  
ATOM    936  CA  GLU C 197     -52.918  39.168  23.657  1.00 42.88           C  
ATOM    937  CA  LEU C 198     -50.937  38.377  20.536  1.00145.81           C  
ATOM    938  CA  ILE C 199     -48.001  40.729  20.033  1.00 97.55           C  
ATOM    939  CA  GLY C 200     -46.453  38.824  17.135  1.00 31.59           C  
ATOM    940  CA  ILE C 201     -45.742  35.517  15.432  1.00 92.52           C  
ATOM    941  CA  ASN C 202     -42.343  34.028  16.190  1.00 65.84           C  
ATOM    942  CA  THR C 203     -40.575  33.660  12.856  1.00 82.37           C  
ATOM    943  CA  ALA C 204     -36.896  33.068  13.483  1.00 54.37           C  
ATOM    944  CA  ILE C 205     -33.850  33.286  15.675  1.00 50.28           C  
ATOM    945  CA  LEU C 206     -30.176  33.984  15.390  1.00 48.12           C  
ATOM    946  CA  ALA C 207     -28.114  31.283  16.964  1.00 41.76           C  
ATOM    947  CA  PRO C 208     -24.725  30.019  16.103  1.00 66.50           C  
ATOM    948  CA  GLY C 209     -25.456  26.752  17.866  1.00 29.29           C  
ATOM    949  CA  GLY C 210     -28.823  26.344  16.285  1.00 22.89           C  
ATOM    950  CA  GLY C 211     -30.180  26.618  19.790  1.00 23.04           C  
ATOM    951  CA  SER C 212     -31.767  29.640  21.395  1.00 52.09           C  
ATOM    952  CA  VAL C 213     -29.191  32.319  22.127  1.00 60.66           C  
ATOM    953  CA  GLY C 214     -31.859  34.561  23.535  1.00 34.60           C  
ATOM    954  CA  ILE C 215     -32.188  36.462  20.301  1.00 95.68           C  
ATOM    955  CA  GLY C 216     -35.507  35.714  18.676  1.00 21.18           C  
ATOM    956  CA  PHE C 217     -37.559  37.579  16.123  1.00 51.19           C  
ATOM    957  CA  ALA C 218     -41.273  37.734  15.521  1.00 34.92           C  
ATOM    958  CA  ILE C 219     -43.556  39.424  13.030  1.00116.17           C  
ATOM    959  CA  PRO C 220     -45.585  41.977  14.777  1.00 86.85           C  
ATOM    960  CA  SER C 221     -49.236  41.254  15.355  1.00 95.49           C  
ATOM    961  CA  ASN C 222     -50.276  44.262  13.423  1.00 64.41           C  
ATOM    962  CA  MET C 223     -48.244  42.575  10.855  1.00108.27           C  
ATOM    963  CA  ALA C 224     -49.917  39.235  10.861  1.00 49.81           C  
ATOM    964  CA  ARG C 225     -53.367  40.537  11.449  1.00150.72           C  
ATOM    965  CA  THR C 226     -53.928  42.705   8.461  1.00 63.50           C  
ATOM    966  CA  LEU C 227     -51.795  40.399   6.312  1.00 97.27           C  
ATOM    967  CA  ALA C 228     -53.955  37.545   7.440  1.00 49.74           C  
ATOM    968  CA  GLN C 229     -57.044  39.574   6.853  1.00 85.83           C  
ATOM    969  CA  GLN C 230     -56.773  39.951   3.117  1.00178.95           C  
ATOM    970  CA  LEU C 231     -55.753  36.361   2.924  1.00 58.98           C  
ATOM    971  CA  ILE C 232     -59.268  35.731   3.999  1.00160.89           C  
ATOM    972  CA  ASP C 233     -60.520  38.988   2.425  1.00173.38           C  
ATOM    973  CA  PHE C 234     -60.296  41.195   0.491  1.00154.01           C  
ATOM    974  CA  GLY C 235     -57.082  39.680  -0.739  1.00 77.64           C  
ATOM    975  CA  GLU C 236     -56.806  40.424  -4.330  1.00110.53           C  
ATOM    976  CA  ILE C 237     -54.559  37.485  -4.828  1.00132.52           C  
ATOM    977  CA  LYS C 238     -51.944  39.232  -6.808  1.00230.88           C  
ATOM    978  CA  ARG C 239     -49.595  40.508  -6.216  1.00249.52           C  
ATOM    979  CA  GLY C 240     -50.355  39.796  -2.582  1.00 52.42           C  
ATOM    980  CA  LEU C 241     -46.918  41.111  -1.913  1.00207.01           C  
ATOM    981  CA  LEU C 242     -43.707  42.585  -3.221  1.00179.02           C  
ATOM    982  CA  GLY C 243     -41.902  39.433  -3.755  1.00 59.36           C  
ATOM    983  CA  ILE C 244     -38.511  40.952  -3.092  1.00 79.91           C  
ATOM    984  CA  LYS C 245     -35.422  40.242  -1.062  1.00121.85           C  
ATOM    985  CA  GLY C 246     -33.570  42.937   0.721  1.00 42.83           C  
ATOM    986  CA  THR C 247     -31.541  43.798   3.699  1.00140.46           C  
ATOM    987  CA  GLU C 248     -29.932  46.807   5.225  1.00101.38           C  
ATOM    988  CA  MET C 249     -28.375  49.286   3.054  1.00104.03           C  
ATOM    989  CA  SER C 250     -24.769  48.254   3.514  1.00 59.97           C  
ATOM    990  CA  ALA C 251     -22.841  49.333   6.589  1.00 50.66           C  
ATOM    991  CA  ASP C 252     -19.886  51.108   5.041  1.00 41.53           C  
ATOM    992  CA  ILE C 253     -21.878  53.849   3.404  1.00 91.00           C  
ATOM    993  CA  ALA C 254     -24.207  53.855   6.346  1.00 33.39           C  
ATOM    994  CA  LYS C 255     -21.402  54.762   8.657  1.00105.35           C  
ATOM    995  CA  ALA C 256     -20.325  57.676   6.531  1.00 40.93           C  
ATOM    996  CA  PHE C 257     -23.720  58.923   5.420  1.00 74.39           C  
ATOM    997  CA  ASN C 258     -25.745  59.077   8.595  1.00 88.00           C  
ATOM    998  CA  LEU C 259     -28.662  59.384   6.229  1.00 99.93           C  
ATOM    999  CA  ASP C 260     -31.757  61.285   7.142  1.00 47.29           C  
ATOM   1000  CA  VAL C 261     -33.549  58.101   7.701  1.00127.78           C  
ATOM   1001  CA  GLN C 262     -32.211  55.461  10.026  1.00186.21           C  
ATOM   1002  CA  ARG C 263     -31.877  53.398   6.963  1.00163.84           C  
ATOM   1003  CA  GLY C 264     -33.950  52.389   4.008  1.00 57.44           C  
ATOM   1004  CA  ALA C 265     -34.719  48.939   2.714  1.00 44.72           C  
ATOM   1005  CA  PHE C 266     -32.365  48.032  -0.007  1.00128.56           C  
ATOM   1006  CA  VAL C 267     -33.387  45.485  -2.510  1.00 63.22           C  
ATOM   1007  CA  SER C 268     -30.724  43.142  -3.752  1.00 68.88           C  
ATOM   1008  CA  GLU C 269     -32.992  41.085  -5.937  1.00111.13           C  
ATOM   1009  CA  VAL C 270     -36.036  40.994  -8.180  1.00128.99           C  
ATOM   1010  CA  LEU C 271     -38.441  38.107  -8.037  1.00113.77           C  
ATOM   1011  CA  PRO C 272     -39.772  36.728 -11.236  1.00 73.77           C  
ATOM   1012  CA  GLY C 273     -43.414  37.322 -12.045  1.00 27.70           C  
ATOM   1013  CA  SER C 274     -43.325  38.825  -8.650  1.00102.27           C  
ATOM   1014  CA  GLY C 275     -44.993  41.803  -7.261  1.00 60.45           C  
ATOM   1015  CA  SER C 276     -41.737  43.556  -7.573  1.00 84.33           C  
ATOM   1016  CA  ALA C 277     -41.289  42.666 -11.212  1.00 67.39           C  
ATOM   1017  CA  LYS C 278     -44.151  44.217 -13.208  1.00162.28           C  
ATOM   1018  CA  ALA C 279     -44.304  47.488 -11.340  1.00 56.22           C  
ATOM   1019  CA  GLY C 280     -40.728  47.447 -12.301  1.00 54.18           C  
ATOM   1020  CA  VAL C 281     -38.820  47.638  -9.090  1.00130.29           C  
ATOM   1021  CA  LYS C 282     -35.261  46.568  -9.858  1.00179.62           C  
ATOM   1022  CA  ALA C 283     -32.718  44.999  -7.696  1.00 92.85           C  
ATOM   1023  CA  GLY C 284     -30.487  47.819  -6.426  1.00 65.27           C  
ATOM   1024  CA  ASP C 285     -33.239  50.054  -5.215  1.00110.10           C  
ATOM   1025  CA  ILE C 286     -33.512  51.591  -1.986  1.00180.20           C  
ATOM   1026  CA  ILE C 287     -37.035  51.813  -0.731  1.00 80.19           C  
ATOM   1027  CA  THR C 288     -37.192  54.983   1.275  1.00 82.47           C  
ATOM   1028  CA  SER C 289     -40.823  55.084   2.004  1.00 50.33           C  
ATOM   1029  CA  LEU C 290     -44.042  53.235   1.738  1.00 74.46           C  
ATOM   1030  CA  ASN C 291     -47.143  55.317   1.444  1.00179.81           C  
ATOM   1031  CA  GLY C 292     -47.458  59.037   2.047  1.00 54.57           C  
ATOM   1032  CA  LYS C 293     -45.558  58.945   5.298  1.00149.04           C  
ATOM   1033  CA  PRO C 294     -41.926  58.202   5.486  1.00137.00           C  
ATOM   1034  CA  LEU C 295     -40.626  54.686   5.872  1.00135.18           C  
ATOM   1035  CA  ASN C 296     -37.811  53.837   8.222  1.00 86.46           C  
ATOM   1036  CA  SER C 297     -35.250  51.117   7.906  1.00 56.88           C  
ATOM   1037  CA  PHE C 298     -35.910  47.863   6.223  1.00100.38           C  
ATOM   1038  CA  ALA C 299     -37.131  47.006   9.668  1.00 49.15           C  
ATOM   1039  CA  GLU C 300     -39.924  49.463   9.512  1.00127.04           C  
ATOM   1040  CA  LEU C 301     -40.585  48.152   6.072  1.00 75.63           C  
ATOM   1041  CA  ARG C 302     -41.925  44.823   7.048  1.00267.25           C  
ATOM   1042  CA  SER C 303     -43.418  46.356  10.096  1.00 53.99           C  
ATOM   1043  CA  ARG C 304     -45.892  48.242   8.100  1.00 76.35           C  
ATOM   1044  CA  ILE C 305     -46.151  45.851   5.177  1.00116.98           C  
ATOM   1045  CA  ALA C 306     -46.218  42.767   7.251  1.00 66.54           C  
ATOM   1046  CA  THR C 307     -48.803  44.769   9.075  1.00 61.67           C  
ATOM   1047  CA  THR C 308     -50.828  45.598   6.060  1.00 54.80           C  
ATOM   1048  CA  GLU C 309     -53.152  43.598   3.953  1.00101.17           C  
ATOM   1049  CA  PRO C 310     -51.322  41.412   1.597  1.00223.14           C  
ATOM   1050  CA  GLY C 311     -52.997  42.374  -0.624  1.00122.69           C  
ATOM   1051  CA  THR C 312     -53.636  46.047  -0.223  1.00114.04           C  
ATOM   1052  CA  LYS C 313     -52.513  48.200  -3.075  1.00124.89           C  
ATOM   1053  CA  VAL C 314     -49.743  50.463  -1.953  1.00 46.01           C  
ATOM   1054  CA  LYS C 315     -47.300  52.891  -3.458  1.00 96.31           C  
ATOM   1055  CA  LEU C 316     -43.593  52.591  -2.897  1.00 98.49           C  
ATOM   1056  CA  GLY C 317     -41.019  55.310  -3.045  1.00 49.15           C  
ATOM   1057  CA  LEU C 318     -37.773  53.829  -4.003  1.00129.72           C  
ATOM   1058  CA  LEU C 319     -34.467  55.830  -4.133  1.00210.00           C  
ATOM   1059  CA  ARG C 320     -32.154  54.636  -6.593  1.00302.54           C  
ATOM   1060  CA  ASN C 321     -30.828  56.331  -9.497  1.00201.89           C  
ATOM   1061  CA  GLY C 322     -30.251  59.337  -7.350  1.00 58.83           C  
ATOM   1062  CA  LYS C 323     -33.440  60.292  -9.047  1.00158.66           C  
ATOM   1063  CA  PRO C 324     -36.713  60.029  -7.245  1.00152.63           C  
ATOM   1064  CA  LEU C 325     -39.163  57.251  -8.260  1.00154.61           C  
ATOM   1065  CA  GLU C 326     -42.717  56.397  -7.207  1.00108.69           C  
ATOM   1066  CA  VAL C 327     -44.312  53.098  -8.141  1.00114.69           C  
ATOM   1067  CA  GLU C 328     -47.429  51.324  -7.066  1.00102.03           C  
ATOM   1068  CA  VAL C 329     -48.030  47.617  -6.631  1.00120.86           C  
ATOM   1069  CA  SER C 340     -45.409  24.202 -33.064  1.00 42.86           C  
ATOM   1070  CA  ALA C 341     -45.034  20.482 -32.774  1.00 53.72           C  
ATOM   1071  CA  GLU C 342     -41.923  20.962 -30.705  1.00 73.96           C  
ATOM   1072  CA  MET C 343     -43.603  21.928 -27.474  1.00139.87           C  
ATOM   1073  CA  ILE C 344     -46.036  19.061 -27.292  1.00177.18           C  
ATOM   1074  CA  THR C 345     -43.679  16.706 -28.999  1.00 77.68           C  
ATOM   1075  CA  PRO C 346     -40.064  16.651 -28.039  1.00170.81           C  
ATOM   1076  CA  ALA C 347     -37.347  18.170 -30.195  1.00 85.88           C  
ATOM   1077  CA  LEU C 348     -39.599  17.396 -33.136  1.00213.52           C  
ATOM   1078  CA  GLU C 349     -39.524  20.670 -34.999  1.00143.01           C  
ATOM   1079  CA  GLY C 350     -42.360  20.970 -37.394  1.00 28.19           C  
ATOM   1080  CA  ALA C 351     -45.738  22.426 -38.095  1.00 38.19           C  
ATOM   1081  CA  THR C 352     -47.236  24.484 -35.359  1.00 93.89           C  
ATOM   1082  CA  LEU C 353     -50.335  23.231 -33.664  1.00 59.45           C  
ATOM   1083  CA  SER C 354     -53.489  24.900 -32.484  1.00 84.16           C  
ATOM   1084  CA  ASP C 355     -56.131  23.724 -30.058  1.00 47.22           C  
ATOM   1085  CA  GLY C 356     -59.806  23.467 -30.608  1.00 49.37           C  
ATOM   1086  CA  GLN C 357     -61.447  22.249 -33.749  1.00164.97           C  
ATOM   1087  CA  LEU C 358     -61.326  25.871 -33.946  1.00207.98           C  
ATOM   1088  CA  LYS C 359     -63.785  25.956 -36.813  1.00107.40           C  
ATOM   1089  CA  ASP C 360     -66.063  23.182 -35.519  1.00 44.88           C  
ATOM   1090  CA  GLY C 361     -66.438  21.325 -32.263  1.00 28.65           C  
ATOM   1091  CA  GLY C 362     -63.041  20.124 -31.162  1.00 38.55           C  
ATOM   1092  CA  LYS C 363     -62.191  17.200 -33.361  1.00 83.08           C  
ATOM   1093  CA  GLY C 364     -58.750  17.669 -31.960  1.00 28.91           C  
ATOM   1094  CA  ILE C 365     -55.545  19.634 -32.298  1.00 63.91           C  
ATOM   1095  CA  LYS C 366     -54.954  21.337 -35.608  1.00 77.16           C  
ATOM   1096  CA  ILE C 367     -51.636  21.562 -37.352  1.00137.93           C  
ATOM   1097  CA  ASP C 368     -51.314  25.117 -38.532  1.00 63.20           C  
ATOM   1098  CA  GLU C 369     -48.506  24.990 -41.025  1.00102.37           C  
ATOM   1099  CA  VAL C 370     -45.834  22.562 -42.061  1.00154.99           C  
ATOM   1100  CA  VAL C 371     -42.227  23.647 -41.673  1.00148.28           C  
ATOM   1101  CA  LYS C 372     -41.690  20.751 -44.160  1.00175.63           C  
ATOM   1102  CA  GLY C 373     -37.905  20.740 -44.014  1.00 42.04           C  
ATOM   1103  CA  SER C 374     -38.464  20.005 -40.296  1.00 49.95           C  
ATOM   1104  CA  PRO C 375     -38.746  16.559 -38.870  1.00 83.74           C  
ATOM   1105  CA  ALA C 376     -42.383  16.927 -37.938  1.00 53.26           C  
ATOM   1106  CA  ALA C 377     -42.689  17.010 -41.683  1.00 60.48           C  
ATOM   1107  CA  GLN C 378     -40.336  14.035 -41.995  1.00 73.50           C  
ATOM   1108  CA  ALA C 379     -42.669  11.584 -40.348  1.00 89.98           C  
ATOM   1109  CA  GLY C 380     -45.717  12.751 -42.231  1.00100.53           C  
ATOM   1110  CA  LEU C 381     -47.418  15.516 -40.443  1.00109.52           C  
ATOM   1111  CA  GLN C 382     -49.050  17.635 -43.113  1.00 68.62           C  
ATOM   1112  CA  LYS C 383     -50.804  20.945 -42.714  1.00118.99           C  
ATOM   1113  CA  ASP C 384     -54.535  21.056 -42.078  1.00145.75           C  
ATOM   1114  CA  ASP C 385     -54.494  17.725 -40.387  1.00166.17           C  
ATOM   1115  CA  VAL C 386     -56.659  17.274 -37.294  1.00 63.32           C  
ATOM   1116  CA  ILE C 387     -55.383  14.990 -34.617  1.00 76.79           C  
ATOM   1117  CA  ILE C 388     -58.511  13.388 -33.231  1.00 85.34           C  
ATOM   1118  CA  GLY C 389     -56.875  11.495 -30.434  1.00 75.15           C  
ATOM   1119  CA  VAL C 390     -53.642   9.913 -29.119  1.00167.88           C  
ATOM   1120  CA  ASN C 391     -53.019   6.139 -28.755  1.00100.30           C  
ATOM   1121  CA  ARG C 392     -56.649   4.992 -28.577  1.00159.44           C  
ATOM   1122  CA  ASP C 393     -57.398   8.094 -26.598  1.00 49.75           C  
ATOM   1123  CA  ARG C 394     -59.376  10.948 -27.998  1.00 76.49           C  
ATOM   1124  CA  VAL C 395     -57.652  14.292 -28.021  1.00 51.74           C  
ATOM   1125  CA  ASN C 396     -60.047  17.197 -27.717  1.00 46.09           C  
ATOM   1126  CA  SER C 397     -57.303  19.746 -27.339  1.00 41.29           C  
ATOM   1127  CA  ILE C 398     -53.599  20.148 -26.689  1.00101.08           C  
ATOM   1128  CA  ALA C 399     -53.894  19.514 -22.988  1.00 26.75           C  
ATOM   1129  CA  GLU C 400     -55.446  16.125 -23.522  1.00 28.23           C  
ATOM   1130  CA  MET C 401     -52.879  15.226 -26.124  1.00 33.88           C  
ATOM   1131  CA  ARG C 402     -50.207  16.100 -23.651  1.00124.09           C  
ATOM   1132  CA  LYS C 403     -51.741  13.727 -21.173  1.00 60.14           C  
ATOM   1133  CA  VAL C 404     -51.246  10.683 -23.355  1.00 50.05           C  
ATOM   1134  CA  LEU C 405     -47.748  11.882 -24.112  1.00 50.05           C  
ATOM   1135  CA  ALA C 406     -47.314  11.992 -20.372  1.00 29.69           C  
ATOM   1136  CA  ALA C 407     -47.549   8.223 -20.409  1.00 28.73           C  
ATOM   1137  CA  LYS C 408     -44.747   8.503 -22.932  1.00 99.12           C  
ATOM   1138  CA  PRO C 409     -45.438   5.243 -24.658  1.00 69.02           C  
ATOM   1139  CA  ALA C 410     -42.596   4.115 -26.874  1.00 32.57           C  
ATOM   1140  CA  ILE C 411     -45.082   3.989 -29.684  1.00 88.17           C  
ATOM   1141  CA  ILE C 412     -47.338   7.059 -29.912  1.00 68.38           C  
ATOM   1142  CA  ALA C 413     -50.007   6.829 -32.502  1.00 87.32           C  
ATOM   1143  CA  LEU C 414     -51.366  10.031 -34.116  1.00152.00           C  
ATOM   1144  CA  GLN C 415     -54.848  10.113 -35.563  1.00171.49           C  
ATOM   1145  CA  ILE C 416     -55.374  12.775 -37.898  1.00182.19           C  
ATOM   1146  CA  VAL C 417     -58.296  13.322 -40.109  1.00 83.77           C  
ATOM   1147  CA  ARG C 418     -57.172  14.626 -43.422  1.00154.54           C  
ATOM   1148  CA  GLY C 419     -59.745  15.548 -45.954  1.00 27.43           C  
ATOM   1149  CA  ASN C 420     -62.747  13.385 -45.486  1.00 61.99           C  
ATOM   1150  CA  GLU C 421     -60.475  10.550 -44.638  1.00 51.52           C  
ATOM   1151  CA  SER C 422     -58.658   9.180 -41.708  1.00110.09           C  
ATOM   1152  CA  ILE C 423     -54.934   9.875 -40.948  1.00175.36           C  
ATOM   1153  CA  TYR C 424     -52.475   7.552 -39.233  1.00247.06           C  
ATOM   1154  CA  LEU C 425     -49.452   9.182 -37.815  1.00133.17           C  
ATOM   1155  CA  LEU C 426     -46.749   7.342 -36.045  1.00236.56           C  
ATOM   1156  CA  MET C 427     -44.008   9.152 -33.782  1.00164.59           C  
ATOM   1157  CA  ARG C 428     -40.640   7.311 -33.109  1.00133.67           C  
TER    1158      ARG C 428                                                      
ATOM   1159  CA  PRO D  11      40.404 -40.261  39.695  1.00132.62           C  
ATOM   1160  CA  LEU D  12      40.618 -42.064  42.976  1.00 98.32           C  
ATOM   1161  CA  PRO D  13      38.243 -41.986  45.828  1.00178.05           C  
ATOM   1162  CA  SER D  14      37.126 -40.252  47.624  1.00126.73           C  
ATOM   1163  CA  LEU D  15      36.169 -36.595  47.522  1.00107.90           C  
ATOM   1164  CA  ALA D  16      33.100 -37.064  49.647  1.00 40.74           C  
ATOM   1165  CA  PRO D  17      34.924 -37.359  52.888  1.00 72.64           C  
ATOM   1166  CA  MET D  18      36.886 -34.192  52.271  1.00 35.91           C  
ATOM   1167  CA  LEU D  19      33.812 -32.433  50.974  1.00 46.28           C  
ATOM   1168  CA  GLU D  20      31.596 -33.283  53.886  1.00 83.75           C  
ATOM   1169  CA  LYS D  21      33.628 -31.202  56.278  1.00 80.90           C  
ATOM   1170  CA  VAL D  22      34.410 -28.329  53.893  1.00109.58           C  
ATOM   1171  CA  LEU D  23      31.091 -27.718  52.192  1.00115.36           C  
ATOM   1172  CA  PRO D  24      29.403 -25.858  54.978  1.00 65.73           C  
ATOM   1173  CA  ALA D  25      32.074 -23.198  54.577  1.00 37.15           C  
ATOM   1174  CA  VAL D  26      30.890 -22.290  51.110  1.00 96.13           C  
ATOM   1175  CA  VAL D  27      27.774 -20.233  51.003  1.00121.18           C  
ATOM   1176  CA  SER D  28      25.350 -18.805  48.485  1.00 41.39           C  
ATOM   1177  CA  VAL D  29      24.940 -15.091  48.333  1.00105.53           C  
ATOM   1178  CA  ARG D  30      21.655 -13.468  47.471  1.00100.49           C  
ATOM   1179  CA  VAL D  31      21.454  -9.862  46.459  1.00 44.12           C  
ATOM   1180  CA  GLU D  32      18.744  -7.358  45.766  1.00 89.80           C  
ATOM   1181  CA  GLY D  33      19.033  -3.791  44.676  1.00 25.89           C  
ATOM   1182  CA  THR D  34      18.266  -0.974  42.286  1.00 47.00           C  
ATOM   1183  CA  ALA D  58      15.219   1.480  40.493  1.00 56.51           C  
ATOM   1184  CA  GLN D  59      13.038  -1.583  40.026  1.00194.34           C  
ATOM   1185  CA  PRO D  60      14.193  -4.387  42.131  1.00149.62           C  
ATOM   1186  CA  PHE D  61      16.267  -7.216  40.759  1.00 53.64           C  
ATOM   1187  CA  GLU D  62      17.780 -10.233  42.392  1.00 32.92           C  
ATOM   1188  CA  GLY D  63      21.137 -11.774  41.706  1.00 28.05           C  
ATOM   1189  CA  LEU D  64      22.667 -14.952  42.973  1.00114.54           C  
ATOM   1190  CA  GLY D  65      26.284 -15.777  43.619  1.00 24.20           C  
ATOM   1191  CA  SER D  66      28.441 -17.613  46.099  1.00 28.32           C  
ATOM   1192  CA  GLY D  67      30.899 -16.768  48.822  1.00 15.37           C  
ATOM   1193  CA  VAL D  68      33.216 -18.493  51.220  1.00 88.78           C  
ATOM   1194  CA  ILE D  69      33.381 -17.904  54.898  1.00138.15           C  
ATOM   1195  CA  ILE D  70      36.891 -16.982  55.882  1.00123.95           C  
ATOM   1196  CA  ASN D  71      36.272 -16.215  59.546  1.00 58.35           C  
ATOM   1197  CA  ALA D  72      33.704 -18.129  61.518  1.00 41.22           C  
ATOM   1198  CA  SER D  73      33.583 -15.996  64.580  1.00 33.96           C  
ATOM   1199  CA  LYS D  74      33.566 -12.751  62.718  1.00 92.05           C  
ATOM   1200  CA  GLY D  75      31.368 -14.099  59.990  1.00 26.64           C  
ATOM   1201  CA  TYR D  76      33.516 -12.716  57.209  1.00 78.85           C  
ATOM   1202  CA  VAL D  77      32.575 -13.997  53.799  1.00 42.52           C  
ATOM   1203  CA  LEU D  78      34.663 -13.442  50.703  1.00 46.79           C  
ATOM   1204  CA  THR D  79      32.929 -12.893  47.406  1.00 41.05           C  
ATOM   1205  CA  ASN D  80      33.370 -11.240  44.065  1.00 50.44           C  
ATOM   1206  CA  ASN D  81      32.794  -7.533  43.919  1.00 36.69           C  
ATOM   1207  CA  HIS D  82      30.642  -7.906  40.856  1.00 44.06           C  
ATOM   1208  CA  VAL D  83      28.192 -10.086  42.676  1.00 42.56           C  
ATOM   1209  CA  ILE D  84      27.934  -7.509  45.469  1.00119.11           C  
ATOM   1210  CA  ASN D  85      28.248  -4.234  43.592  1.00 72.12           C  
ATOM   1211  CA  GLN D  86      24.625  -3.318  42.893  1.00 71.36           C  
ATOM   1212  CA  ALA D  87      23.213  -4.956  46.006  1.00 65.68           C  
ATOM   1213  CA  GLN D  88      21.187  -2.801  48.338  1.00 53.38           C  
ATOM   1214  CA  LYS D  89      20.671  -5.773  50.610  1.00 30.30           C  
ATOM   1215  CA  ILE D  90      22.688  -8.928  50.946  1.00 86.69           C  
ATOM   1216  CA  SER D  91      21.652 -12.270  52.335  1.00 28.92           C  
ATOM   1217  CA  ILE D  92      23.726 -15.361  52.830  1.00 70.93           C  
ATOM   1218  CA  GLN D  93      22.385 -18.869  52.939  1.00 41.91           C  
ATOM   1219  CA  LEU D  94      24.174 -21.876  54.294  1.00 92.17           C  
ATOM   1220  CA  ASN D  95      23.901 -25.341  52.847  1.00 42.80           C  
ATOM   1221  CA  ASP D  96      21.957 -26.260  55.959  1.00 50.82           C  
ATOM   1222  CA  GLY D  97      19.260 -23.837  54.938  1.00 31.34           C  
ATOM   1223  CA  ARG D  98      19.969 -21.233  57.565  1.00 69.91           C  
ATOM   1224  CA  GLU D  99      19.889 -17.703  56.252  1.00 45.26           C  
ATOM   1225  CA  PHE D 100      21.583 -14.562  57.475  1.00 62.57           C  
ATOM   1226  CA  ASP D 101      21.831 -10.947  56.457  1.00 35.86           C  
ATOM   1227  CA  ALA D 102      25.183  -9.484  55.578  1.00 32.07           C  
ATOM   1228  CA  LYS D 103      26.773  -6.076  55.227  1.00 85.89           C  
ATOM   1229  CA  LEU D 104      29.557  -5.141  52.882  1.00 67.39           C  
ATOM   1230  CA  ILE D 105      32.762  -4.488  54.739  1.00 85.61           C  
ATOM   1231  CA  GLY D 106      34.596  -3.313  51.662  1.00 28.74           C  
ATOM   1232  CA  SER D 107      35.611  -4.307  48.187  1.00 64.46           C  
ATOM   1233  CA  ASP D 108      37.517  -3.166  45.218  1.00136.07           C  
ATOM   1234  CA  ASP D 109      36.933  -3.141  41.491  1.00 66.08           C  
ATOM   1235  CA  GLN D 110      40.370  -3.852  40.103  1.00 89.81           C  
ATOM   1236  CA  SER D 111      40.853  -7.294  41.610  1.00 64.13           C  
ATOM   1237  CA  ASP D 112      37.109  -7.839  41.955  1.00 72.34           C  
ATOM   1238  CA  ILE D 113      37.256  -8.966  45.572  1.00 50.28           C  
ATOM   1239  CA  ALA D 114      34.680  -8.028  48.183  1.00 35.25           C  
ATOM   1240  CA  LEU D 115      34.366  -8.757  51.877  1.00 96.59           C  
ATOM   1241  CA  LEU D 116      31.033  -9.335  53.561  1.00 47.79           C  
ATOM   1242  CA  GLN D 117      30.082  -9.674  57.183  1.00131.39           C  
ATOM   1243  CA  ILE D 118      27.343 -11.939  58.460  1.00120.42           C  
ATOM   1244  CA  GLN D 119      25.145 -10.400  61.071  1.00 61.03           C  
ATOM   1245  CA  ASN D 120      24.719 -12.623  64.108  1.00167.22           C  
ATOM   1246  CA  PRO D 121      26.868 -15.284  62.557  1.00271.78           C  
ATOM   1247  CA  SER D 122      26.423 -18.297  64.901  1.00130.48           C  
ATOM   1248  CA  LYS D 123      27.730 -21.836  64.423  1.00 61.68           C  
ATOM   1249  CA  LEU D 124      29.674 -21.235  61.262  1.00 93.90           C  
ATOM   1250  CA  THR D 125      32.320 -23.402  59.686  1.00 99.50           C  
ATOM   1251  CA  GLN D 126      35.340 -21.841  58.099  1.00 72.66           C  
ATOM   1252  CA  ILE D 127      37.473 -22.715  55.166  1.00 95.92           C  
ATOM   1253  CA  ALA D 128      41.196 -23.084  55.543  1.00 31.55           C  
ATOM   1254  CA  ILE D 129      43.264 -21.200  53.038  1.00 40.00           C  
ATOM   1255  CA  ALA D 130      46.080 -22.780  51.074  1.00 38.38           C  
ATOM   1256  CA  ASP D 131      49.116 -21.118  49.569  1.00 35.97           C  
ATOM   1257  CA  SER D 132      48.201 -20.330  45.989  1.00 79.65           C  
ATOM   1258  CA  ASP D 133      51.817 -19.843  45.062  1.00 34.74           C  
ATOM   1259  CA  LYS D 134      52.405 -23.529  45.693  1.00 69.89           C  
ATOM   1260  CA  LEU D 135      49.862 -24.532  43.051  1.00 57.12           C  
ATOM   1261  CA  ARG D 136      51.175 -26.340  40.009  1.00115.86           C  
ATOM   1262  CA  VAL D 137      49.395 -27.224  36.825  1.00102.10           C  
ATOM   1263  CA  GLY D 138      47.892 -30.644  37.107  1.00 32.59           C  
ATOM   1264  CA  ASP D 139      46.801 -30.217  40.693  1.00 42.38           C  
ATOM   1265  CA  PHE D 140      43.245 -31.316  41.262  1.00152.86           C  
ATOM   1266  CA  ALA D 141      40.659 -28.731  42.096  1.00 31.45           C  
ATOM   1267  CA  VAL D 142      37.037 -28.756  43.113  1.00 35.01           C  
ATOM   1268  CA  ALA D 143      34.741 -25.842  42.569  1.00 27.32           C  
ATOM   1269  CA  VAL D 144      31.812 -25.168  44.815  1.00 29.69           C  
ATOM   1270  CA  GLY D 145      29.144 -22.568  44.261  1.00 21.23           C  
ATOM   1271  CA  ASN D 146      25.618 -22.225  43.068  1.00 65.25           C  
ATOM   1272  CA  PRO D 147      25.318 -22.461  39.381  1.00149.53           C  
ATOM   1273  CA  PHE D 148      22.028 -21.218  38.020  1.00 68.24           C  
ATOM   1274  CA  GLY D 149      20.949 -20.835  41.613  1.00 24.57           C  
ATOM   1275  CA  LEU D 150      20.361 -24.551  41.790  1.00 88.26           C  
ATOM   1276  CA  GLY D 151      21.958 -24.857  45.194  1.00 31.64           C  
ATOM   1277  CA  GLN D 152      25.340 -25.884  46.472  1.00 45.19           C  
ATOM   1278  CA  THR D 153      27.033 -27.726  43.656  1.00 32.65           C  
ATOM   1279  CA  ALA D 154      30.473 -29.236  43.449  1.00 28.51           C  
ATOM   1280  CA  THR D 155      32.420 -29.809  40.263  1.00101.10           C  
ATOM   1281  CA  SER D 156      35.850 -31.297  39.770  1.00 89.35           C  
ATOM   1282  CA  GLY D 157      38.777 -30.613  37.517  1.00 32.97           C  
ATOM   1283  CA  ILE D 158      42.464 -29.773  37.543  1.00131.16           C  
ATOM   1284  CA  VAL D 159      44.430 -26.573  37.581  1.00 50.62           C  
ATOM   1285  CA  SER D 160      44.831 -25.901  33.903  1.00 94.84           C  
ATOM   1286  CA  ALA D 161      47.109 -22.894  34.212  1.00 42.15           C  
ATOM   1287  CA  LEU D 162      48.177 -20.143  36.545  1.00 54.82           C  
ATOM   1288  CA  GLY D 163      49.340 -16.594  36.360  1.00 31.99           C  
ATOM   1289  CA  ARG D 164      47.215 -15.767  33.446  1.00122.21           C  
ATOM   1290  CA  SER D 165      46.059 -12.397  32.326  1.00 81.72           C  
ATOM   1291  CA  GLY D 166      45.340 -10.130  29.485  1.00 36.91           C  
ATOM   1292  CA  LEU D 167      41.835 -11.520  29.704  1.00 52.97           C  
ATOM   1293  CA  ASN D 168      40.724  -7.946  30.253  1.00 95.37           C  
ATOM   1294  CA  LEU D 169      38.121  -9.265  32.592  1.00 51.96           C  
ATOM   1295  CA  GLU D 170      39.474  -7.197  35.460  1.00 84.94           C  
ATOM   1296  CA  GLY D 171      41.939  -4.399  36.030  1.00 36.05           C  
ATOM   1297  CA  LEU D 172      44.261  -6.659  37.895  1.00115.78           C  
ATOM   1298  CA  GLU D 173      44.283 -10.243  37.011  1.00 75.37           C  
ATOM   1299  CA  ASN D 174      46.196 -13.369  37.811  1.00 98.40           C  
ATOM   1300  CA  PHE D 175      43.696 -16.005  37.348  1.00 76.95           C  
ATOM   1301  CA  ILE D 176      44.239 -19.584  38.098  1.00 68.48           C  
ATOM   1302  CA  GLN D 177      42.554 -21.403  35.284  1.00 53.35           C  
ATOM   1303  CA  THR D 178      40.554 -24.518  35.907  1.00 44.92           C  
ATOM   1304  CA  ASP D 179      38.707 -27.118  33.884  1.00145.19           C  
ATOM   1305  CA  ALA D 180      36.160 -27.577  36.644  1.00 41.78           C  
ATOM   1306  CA  SER D 181      32.732 -26.672  35.428  1.00 82.87           C  
ATOM   1307  CA  ILE D 182      32.032 -23.098  36.367  1.00 95.62           C  
ATOM   1308  CA  ASN D 183      28.805 -21.481  35.346  1.00 36.03           C  
ATOM   1309  CA  ARG D 184      26.895 -18.375  36.162  1.00 88.84           C  
ATOM   1310  CA  GLY D 185      26.205 -18.224  39.863  1.00 23.93           C  
ATOM   1311  CA  ASN D 186      29.626 -19.696  40.550  1.00 54.18           C  
ATOM   1312  CA  ALA D 187      31.115 -16.269  41.134  1.00 87.35           C  
ATOM   1313  CA  GLY D 188      32.431 -15.731  44.616  1.00 23.80           C  
ATOM   1314  CA  GLY D 189      32.463 -19.475  45.063  1.00 21.19           C  
ATOM   1315  CA  ALA D 190      35.419 -21.463  46.208  1.00 43.46           C  
ATOM   1316  CA  LEU D 191      37.983 -23.480  44.341  1.00 94.03           C  
ATOM   1317  CA  LEU D 192      39.324 -26.142  46.622  1.00 98.39           C  
ATOM   1318  CA  ASN D 193      42.324 -28.416  46.887  1.00 85.74           C  
ATOM   1319  CA  LEU D 194      41.735 -32.046  47.628  1.00145.17           C  
ATOM   1320  CA  ASN D 195      42.757 -30.976  51.051  1.00107.90           C  
ATOM   1321  CA  GLY D 196      39.599 -28.911  51.040  1.00 25.18           C  
ATOM   1322  CA  GLU D 197      41.742 -25.820  51.360  1.00 42.98           C  
ATOM   1323  CA  LEU D 198      40.838 -22.666  49.479  1.00 61.07           C  
ATOM   1324  CA  ILE D 199      42.970 -22.266  46.365  1.00 77.85           C  
ATOM   1325  CA  GLY D 200      41.053 -19.336  44.922  1.00 30.90           C  
ATOM   1326  CA  ILE D 201      37.722 -17.628  44.362  1.00 90.27           C  
ATOM   1327  CA  ASN D 202      35.981 -18.404  41.081  1.00 63.39           C  
ATOM   1328  CA  THR D 203      35.703 -15.071  39.313  1.00 81.19           C  
ATOM   1329  CA  ALA D 204      34.790 -15.743  35.708  1.00 55.78           C  
ATOM   1330  CA  ILE D 205      34.727 -17.977  32.683  1.00133.08           C  
ATOM   1331  CA  LEU D 206      35.380 -17.712  28.991  1.00 59.20           C  
ATOM   1332  CA  ALA D 207      32.660 -19.277  27.034  1.00 53.12           C  
ATOM   1333  CA  PRO D 208      30.987 -18.613  23.859  1.00 77.92           C  
ATOM   1334  CA  GLY D 209      27.516 -19.844  24.583  1.00 26.24           C  
ATOM   1335  CA  GLY D 210      27.493 -18.526  28.107  1.00 14.65           C  
ATOM   1336  CA  GLY D 211      27.941 -22.045  29.400  1.00 22.73           C  
ATOM   1337  CA  SER D 212      31.018 -23.657  30.856  1.00 55.21           C  
ATOM   1338  CA  VAL D 213      33.514 -24.387  28.103  1.00119.39           C  
ATOM   1339  CA  GLY D 214      35.938 -25.833  30.598  1.00 36.91           C  
ATOM   1340  CA  ILE D 215      37.906 -22.646  30.873  1.00 45.62           C  
ATOM   1341  CA  GLY D 216      37.288 -20.940  34.179  1.00 21.41           C  
ATOM   1342  CA  PHE D 217      39.311 -18.421  36.099  1.00 47.33           C  
ATOM   1343  CA  ALA D 218      39.696 -17.821  39.787  1.00 31.46           C  
ATOM   1344  CA  ILE D 219      41.469 -15.282  41.937  1.00 65.81           C  
ATOM   1345  CA  PRO D 220      44.172 -17.006  43.807  1.00 85.01           C  
ATOM   1346  CA  SER D 221      43.717 -17.671  47.499  1.00 40.30           C  
ATOM   1347  CA  ASN D 222      46.729 -15.671  48.349  1.00 62.40           C  
ATOM   1348  CA  MET D 223      44.964 -13.116  46.361  1.00109.62           C  
ATOM   1349  CA  ALA D 224      41.749 -13.075  48.267  1.00 53.35           C  
ATOM   1350  CA  ARG D 225      43.365 -13.653  51.602  1.00129.97           C  
ATOM   1351  CA  THR D 226      45.509 -10.623  51.986  1.00 62.72           C  
ATOM   1352  CA  LEU D 227      43.079  -8.465  50.005  1.00115.97           C  
ATOM   1353  CA  ALA D 228      40.371  -9.588  52.347  1.00 51.27           C  
ATOM   1354  CA  GLN D 229      42.678  -9.044  55.252  1.00 89.45           C  
ATOM   1355  CA  GLN D 230      43.085  -5.305  54.969  1.00182.33           C  
ATOM   1356  CA  LEU D 231      39.425  -4.953  54.179  1.00 56.79           C  
ATOM   1357  CA  ILE D 232      39.118  -6.255  57.675  1.00 69.10           C  
ATOM   1358  CA  ASP D 233      42.359  -4.565  58.719  1.00176.28           C  
ATOM   1359  CA  PHE D 234      44.580  -2.710  58.326  1.00149.18           C  
ATOM   1360  CA  GLY D 235      42.177  -1.161  55.941  1.00 35.79           C  
ATOM   1361  CA  GLU D 236      44.625   1.435  54.756  1.00 62.86           C  
ATOM   1362  CA  ILE D 237      42.594   3.350  52.257  1.00 87.34           C  
ATOM   1363  CA  LYS D 238      45.129   3.396  49.482  1.00197.08           C  
ATOM   1364  CA  ARG D 239      45.425   1.954  47.113  1.00235.45           C  
ATOM   1365  CA  GLY D 240      42.295   0.212  48.288  1.00 90.57           C  
ATOM   1366  CA  LEU D 241      42.615  -0.828  44.790  1.00232.55           C  
ATOM   1367  CA  LEU D 242      44.571   1.059  42.370  1.00 97.69           C  
ATOM   1368  CA  GLY D 243      41.690   1.600  40.028  1.00 56.62           C  
ATOM   1369  CA  ILE D 244      43.000   0.847  36.566  1.00 82.00           C  
ATOM   1370  CA  LYS D 245      42.007  -1.235  33.592  1.00126.52           C  
ATOM   1371  CA  GLY D 246      44.524  -3.115  31.575  1.00 44.91           C  
ATOM   1372  CA  THR D 247      45.250  -6.064  29.413  1.00129.01           C  
ATOM   1373  CA  GLU D 248      48.108  -8.150  28.142  1.00 97.07           C  
ATOM   1374  CA  MET D 249      51.170  -6.571  26.710  1.00135.42           C  
ATOM   1375  CA  SER D 250      50.175  -5.370  23.300  1.00 50.02           C  
ATOM   1376  CA  ALA D 251      50.271  -7.802  20.449  1.00 52.36           C  
ATOM   1377  CA  ASP D 252      52.244  -5.674  18.095  1.00 95.32           C  
ATOM   1378  CA  ILE D 253      54.989  -4.691  20.483  1.00 60.19           C  
ATOM   1379  CA  ALA D 254      55.359  -7.946  22.309  1.00 37.27           C  
ATOM   1380  CA  LYS D 255      55.901  -9.895  19.142  1.00 83.27           C  
ATOM   1381  CA  ALA D 256      58.415  -7.578  17.598  1.00 41.15           C  
ATOM   1382  CA  PHE D 257      61.087  -8.053  20.216  1.00143.35           C  
ATOM   1383  CA  ASN D 258      59.849 -11.486  21.183  1.00 70.41           C  
ATOM   1384  CA  LEU D 259      61.796 -11.345  24.426  1.00 68.53           C  
ATOM   1385  CA  ASP D 260      61.808 -13.922  27.148  1.00 77.99           C  
ATOM   1386  CA  VAL D 261      59.072 -12.158  29.057  1.00111.34           C  
ATOM   1387  CA  GLN D 262      55.589 -13.097  28.114  1.00 62.41           C  
ATOM   1388  CA  ARG D 263      54.077  -9.746  28.720  1.00106.02           C  
ATOM   1389  CA  GLY D 264      53.649  -6.799  30.993  1.00 31.13           C  
ATOM   1390  CA  ALA D 265      50.605  -5.091  32.315  1.00 43.16           C  
ATOM   1391  CA  PHE D 266      49.406  -2.469  29.905  1.00 96.22           C  
ATOM   1392  CA  VAL D 267      46.725  -0.213  30.913  1.00126.19           C  
ATOM   1393  CA  SER D 268      44.401   1.521  28.651  1.00142.92           C  
ATOM   1394  CA  GLU D 269      42.500   3.381  31.268  1.00120.07           C  
ATOM   1395  CA  VAL D 270      42.813   5.901  34.057  1.00115.92           C  
ATOM   1396  CA  LEU D 271      40.098   5.779  36.687  1.00104.88           C  
ATOM   1397  CA  PRO D 272      38.803   8.963  38.132  1.00 69.81           C  
ATOM   1398  CA  GLY D 273      39.528   9.782  41.759  1.00 28.83           C  
ATOM   1399  CA  SER D 274      41.239   6.492  41.459  1.00 49.73           C  
ATOM   1400  CA  GLY D 275      44.382   5.388  43.079  1.00 46.13           C  
ATOM   1401  CA  SER D 276      45.819   5.178  39.668  1.00 64.74           C  
ATOM   1402  CA  ALA D 277      44.932   8.766  39.133  1.00 62.43           C  
ATOM   1403  CA  LYS D 278      46.487  10.498  42.065  1.00 62.03           C  
ATOM   1404  CA  ALA D 279      49.523   8.298  42.052  1.00 55.41           C  
ATOM   1405  CA  GLY D 280      50.304   9.450  38.745  1.00 76.82           C  
ATOM   1406  CA  VAL D 281      49.604   6.633  36.465  1.00108.77           C  
ATOM   1407  CA  LYS D 282      47.499   7.200  33.403  1.00256.56           C  
ATOM   1408  CA  ALA D 283      47.064   4.541  30.745  1.00128.63           C  
ATOM   1409  CA  GLY D 284      49.281   3.194  28.219  1.00 90.27           C  
ATOM   1410  CA  ASP D 285      51.709   2.461  30.732  1.00191.28           C  
ATOM   1411  CA  ILE D 286      53.523  -0.544  30.809  1.00142.30           C  
ATOM   1412  CA  ILE D 287      53.500  -1.738  34.375  1.00103.16           C  
ATOM   1413  CA  THR D 288      56.856  -3.422  34.429  1.00 66.71           C  
ATOM   1414  CA  SER D 289      57.062  -4.321  38.039  1.00 98.24           C  
ATOM   1415  CA  LEU D 290      55.508  -4.286  41.440  1.00 82.71           C  
ATOM   1416  CA  ASN D 291      57.973  -3.942  44.233  1.00270.67           C  
ATOM   1417  CA  GLY D 292      60.768  -4.932  44.955  1.00139.09           C  
ATOM   1418  CA  LYS D 293      61.015  -7.863  42.612  1.00165.26           C  
ATOM   1419  CA  PRO D 294      60.314  -8.138  38.969  1.00 61.13           C  
ATOM   1420  CA  LEU D 295      56.718  -8.253  37.803  1.00118.04           C  
ATOM   1421  CA  ASN D 296      55.675 -10.595  35.071  1.00 82.00           C  
ATOM   1422  CA  SER D 297      52.769 -10.246  32.740  1.00101.68           C  
ATOM   1423  CA  PHE D 298      49.493  -8.632  33.563  1.00 76.62           C  
ATOM   1424  CA  ALA D 299      48.699 -12.017  34.934  1.00 47.80           C  
ATOM   1425  CA  GLU D 300      51.357 -11.914  37.567  1.00 94.03           C  
ATOM   1426  CA  LEU D 301      50.207  -8.437  38.308  1.00 67.97           C  
ATOM   1427  CA  ARG D 302      46.958  -9.317  39.861  1.00177.79           C  
ATOM   1428  CA  SER D 303      48.509 -12.383  41.279  1.00104.98           C  
ATOM   1429  CA  ARG D 304      50.502 -10.321  43.605  1.00163.34           C  
ATOM   1430  CA  ILE D 305      48.119  -7.412  43.959  1.00114.24           C  
ATOM   1431  CA  ALA D 306      45.085  -9.530  44.239  1.00 68.74           C  
ATOM   1432  CA  THR D 307      47.202 -11.352  46.732  1.00132.51           C  
ATOM   1433  CA  THR D 308      48.181  -8.342  48.733  1.00 53.50           C  
ATOM   1434  CA  GLU D 309      46.100  -6.232  51.029  1.00 84.84           C  
ATOM   1435  CA  PRO D 310      44.001  -3.909  49.051  1.00172.96           C  
ATOM   1436  CA  GLY D 311      45.280  -1.144  51.021  1.00194.71           C  
ATOM   1437  CA  THR D 312      48.880  -2.096  51.366  1.00141.52           C  
ATOM   1438  CA  LYS D 313      50.927   0.763  50.026  1.00 76.79           C  
ATOM   1439  CA  VAL D 314      53.140  -0.417  47.258  1.00106.83           C  
ATOM   1440  CA  LYS D 315      55.404   0.981  44.579  1.00121.34           C  
ATOM   1441  CA  LEU D 316      54.870   0.414  40.931  1.00 95.91           C  
ATOM   1442  CA  GLY D 317      57.479   0.541  38.213  1.00 59.36           C  
ATOM   1443  CA  LEU D 318      56.337   1.459  34.918  1.00182.04           C  
ATOM   1444  CA  LEU D 319      57.826   2.102  31.597  1.00128.31           C  
ATOM   1445  CA  ARG D 320      56.469   4.748  29.781  1.00282.75           C  
ATOM   1446  CA  ASN D 321      57.488   6.440  26.805  1.00333.56           C  
ATOM   1447  CA  GLY D 322      61.024   5.449  26.493  1.00232.41           C  
ATOM   1448  CA  LYS D 323      61.698   5.502  30.107  1.00244.45           C  
ATOM   1449  CA  PRO D 324      60.875   4.114  33.398  1.00185.99           C  
ATOM   1450  CA  LEU D 325      59.152   5.382  36.567  1.00253.59           C  
ATOM   1451  CA  GLU D 326      58.626   4.231  39.988  1.00198.54           C  
ATOM   1452  CA  VAL D 327      55.731   5.930  41.765  1.00149.61           C  
ATOM   1453  CA  GLU D 328      54.060   4.735  44.872  1.00 90.18           C  
ATOM   1454  CA  VAL D 329      50.356   4.449  45.495  1.00123.73           C  
ATOM   1455  CA  SER D 340      27.360  32.136  45.178  1.00 39.72           C  
ATOM   1456  CA  ALA D 341      23.656  31.734  44.743  1.00 53.28           C  
ATOM   1457  CA  GLU D 342      24.182  29.768  41.583  1.00 58.79           C  
ATOM   1458  CA  MET D 343      25.272  26.532  43.199  1.00 49.43           C  
ATOM   1459  CA  ILE D 344      22.377  26.261  45.603  1.00 89.59           C  
ATOM   1460  CA  THR D 345      20.003  27.821  43.153  1.00 67.41           C  
ATOM   1461  CA  PRO D 346      20.118  26.881  39.542  1.00152.51           C  
ATOM   1462  CA  ALA D 347      21.540  29.206  36.920  1.00 73.71           C  
ATOM   1463  CA  LEU D 348      20.658  32.155  39.125  1.00 87.79           C  
ATOM   1464  CA  GLU D 349      23.893  34.028  39.298  1.00131.14           C  
ATOM   1465  CA  GLY D 350      23.961  36.375  42.178  1.00 28.14           C  
ATOM   1466  CA  ALA D 351      25.274  37.090  45.604  1.00 33.77           C  
ATOM   1467  CA  THR D 352      27.433  34.462  47.180  1.00 35.48           C  
ATOM   1468  CA  LEU D 353      26.061  32.497  50.085  1.00 90.04           C  
ATOM   1469  CA  SER D 354      27.749  31.425  53.282  1.00 39.21           C  
ATOM   1470  CA  ASP D 355      26.616  28.912  55.852  1.00 51.51           C  
ATOM   1471  CA  GLY D 356      26.175  29.384  59.526  1.00 46.23           C  
ATOM   1472  CA  GLN D 357      24.885  32.502  61.152  1.00155.84           C  
ATOM   1473  CA  LEU D 358      28.516  32.703  61.156  1.00150.70           C  
ATOM   1474  CA  LYS D 359      28.596  35.665  63.474  1.00143.20           C  
ATOM   1475  CA  ASP D 360      25.664  34.541  65.643  1.00 43.09           C  
ATOM   1476  CA  GLY D 361      23.864  31.259  66.154  1.00 31.20           C  
ATOM   1477  CA  GLY D 362      22.834  29.872  62.799  1.00 40.14           C  
ATOM   1478  CA  LYS D 363      19.897  31.977  61.795  1.00 70.13           C  
ATOM   1479  CA  GLY D 364      20.443  30.565  58.371  1.00 26.95           C  
ATOM   1480  CA  ILE D 365      22.539  31.046  55.289  1.00127.36           C  
ATOM   1481  CA  LYS D 366      23.927  34.476  54.675  1.00 62.53           C  
ATOM   1482  CA  ILE D 367      24.345  36.114  51.343  1.00 81.06           C  
ATOM   1483  CA  ASP D 368      27.806  37.614  51.285  1.00145.88           C  
ATOM   1484  CA  GLU D 369      27.694  40.082  48.469  1.00141.09           C  
ATOM   1485  CA  VAL D 370      25.283  41.096  45.805  1.00141.97           C  
ATOM   1486  CA  VAL D 371      26.531  40.833  42.225  1.00176.62           C  
ATOM   1487  CA  LYS D 372      23.476  43.076  41.557  1.00199.03           C  
ATOM   1488  CA  GLY D 373      23.703  43.030  37.790  1.00 38.69           C  
ATOM   1489  CA  SER D 374      23.039  39.289  38.221  1.00 37.95           C  
ATOM   1490  CA  PRO D 375      19.631  37.787  38.452  1.00 72.69           C  
ATOM   1491  CA  ALA D 376      19.923  36.765  42.062  1.00 46.65           C  
ATOM   1492  CA  ALA D 377      19.875  40.514  42.403  1.00 51.02           C  
ATOM   1493  CA  GLN D 378      16.871  41.038  40.149  1.00 56.59           C  
ATOM   1494  CA  ALA D 379      14.448  39.103  42.362  1.00 65.46           C  
ATOM   1495  CA  GLY D 380      15.095  40.944  45.605  1.00 62.86           C  
ATOM   1496  CA  LEU D 381      18.190  39.295  46.980  1.00164.08           C  
ATOM   1497  CA  GLN D 382      20.258  41.943  48.693  1.00119.83           C  
ATOM   1498  CA  LYS D 383      23.454  41.612  50.651  1.00155.78           C  
ATOM   1499  CA  ASP D 384      23.471  40.817  54.364  1.00148.67           C  
ATOM   1500  CA  ASP D 385      20.163  39.026  54.275  1.00161.08           C  
ATOM   1501  CA  VAL D 386      19.941  35.877  56.288  1.00 57.06           C  
ATOM   1502  CA  ILE D 387      17.702  33.173  54.980  1.00 57.81           C  
ATOM   1503  CA  ILE D 388      16.052  31.803  58.088  1.00100.16           C  
ATOM   1504  CA  GLY D 389      13.934  29.188  56.433  1.00 39.95           C  
ATOM   1505  CA  VAL D 390      12.555  27.719  53.207  1.00137.29           C  
ATOM   1506  CA  ASN D 391       8.984  26.600  52.437  1.00 95.44           C  
ATOM   1507  CA  ARG D 392       7.900  26.662  56.030  1.00110.66           C  
ATOM   1508  CA  ASP D 393      11.108  24.860  56.790  1.00 50.20           C  
ATOM   1509  CA  ARG D 394      13.861  26.353  58.814  1.00 91.37           C  
ATOM   1510  CA  VAL D 395      17.224  26.594  57.159  1.00 44.42           C  
ATOM   1511  CA  ASN D 396      20.049  26.256  59.631  1.00 44.55           C  
ATOM   1512  CA  SER D 397      22.662  26.064  56.933  1.00 89.54           C  
ATOM   1513  CA  ILE D 398      23.153  25.531  53.208  1.00 97.24           C  
ATOM   1514  CA  ALA D 399      22.683  21.810  53.433  1.00 26.13           C  
ATOM   1515  CA  GLU D 400      19.229  22.186  54.877  1.00 30.37           C  
ATOM   1516  CA  MET D 401      18.331  24.851  52.371  1.00 29.24           C  
ATOM   1517  CA  ARG D 402      19.350  22.617  49.542  1.00 93.28           C  
ATOM   1518  CA  LYS D 403      17.179  19.915  51.027  1.00108.88           C  
ATOM   1519  CA  VAL D 404      14.021  21.917  50.560  1.00 37.86           C  
ATOM   1520  CA  LEU D 405      15.215  22.693  47.079  1.00 61.46           C  
ATOM   1521  CA  ALA D 406      15.595  18.990  46.560  1.00 30.93           C  
ATOM   1522  CA  ALA D 407      11.827  18.817  46.786  1.00 26.95           C  
ATOM   1523  CA  LYS D 408      11.937  21.408  44.034  1.00 96.98           C  
ATOM   1524  CA  PRO D 409       8.598  22.933  44.774  1.00 67.03           C  
ATOM   1525  CA  ALA D 410       7.330  25.152  41.981  1.00 30.11           C  
ATOM   1526  CA  ILE D 411       6.939  27.760  44.678  1.00135.60           C  
ATOM   1527  CA  ILE D 412      10.062  28.526  46.601  1.00 63.70           C  
ATOM   1528  CA  ALA D 413       9.941  31.176  49.116  1.00 99.59           C  
ATOM   1529  CA  LEU D 414      12.719  32.750  50.958  1.00138.73           C  
ATOM   1530  CA  GLN D 415      12.371  34.051  54.323  1.00178.87           C  
ATOM   1531  CA  ILE D 416      15.205  36.152  55.185  1.00105.27           C  
ATOM   1532  CA  VAL D 417      15.716  38.723  57.807  1.00 53.71           C  
ATOM   1533  CA  ARG D 418      16.856  42.081  56.648  1.00162.24           C  
ATOM   1534  CA  GLY D 419      17.745  44.675  59.182  1.00 19.76           C  
ATOM   1535  CA  ASN D 420      15.515  44.097  62.116  1.00 52.05           C  
ATOM   1536  CA  GLU D 421      12.575  42.875  60.112  1.00 45.07           C  
ATOM   1537  CA  SER D 422      11.307  39.742  58.458  1.00 51.36           C  
ATOM   1538  CA  ILE D 423      11.853  39.561  54.701  1.00134.74           C  
ATOM   1539  CA  TYR D 424      10.155  37.851  51.803  1.00211.26           C  
ATOM   1540  CA  LEU D 425      11.920  36.355  49.008  1.00120.38           C  
ATOM   1541  CA  LEU D 426      10.618  34.261  46.281  1.00180.35           C  
ATOM   1542  CA  MET D 427      11.467  32.431  43.115  1.00 76.94           C  
ATOM   1543  CA  ARG D 428       9.481  31.461  40.093  1.00 50.00           C  
TER    1544      ARG D 428                                                      
ATOM   1545  CA  PRO E  11      47.698 -46.357  37.686  1.00 52.21           C  
ATOM   1546  CA  LEU E  12      45.032 -47.413  35.298  1.00 92.12           C  
ATOM   1547  CA  PRO E  13      42.105 -48.962  36.969  1.00254.47           C  
ATOM   1548  CA  SER E  14      41.537 -49.419  34.189  1.00197.67           C  
ATOM   1549  CA  LEU E  15      37.933 -48.833  33.205  1.00114.77           C  
ATOM   1550  CA  ALA E  16      38.200 -51.238  30.297  1.00 44.52           C  
ATOM   1551  CA  PRO E  17      38.572 -54.393  32.278  1.00 73.31           C  
ATOM   1552  CA  MET E  18      35.396 -53.589  34.140  1.00125.81           C  
ATOM   1553  CA  LEU E  19      33.625 -52.584  30.968  1.00 57.81           C  
ATOM   1554  CA  GLU E  20      34.455 -55.674  29.027  1.00 72.86           C  
ATOM   1555  CA  LYS E  21      32.416 -57.891  31.262  1.00 95.75           C  
ATOM   1556  CA  VAL E  22      29.556 -55.448  31.828  1.00 81.41           C  
ATOM   1557  CA  LEU E  23      28.992 -53.990  28.392  1.00 80.95           C  
ATOM   1558  CA  PRO E  24      27.126 -56.856  26.847  1.00 66.39           C  
ATOM   1559  CA  ALA E  25      24.477 -56.311  29.497  1.00 33.81           C  
ATOM   1560  CA  VAL E  26      23.561 -52.918  28.122  1.00 43.48           C  
ATOM   1561  CA  VAL E  27      21.455 -53.005  25.032  1.00 96.61           C  
ATOM   1562  CA  SER E  28      20.029 -50.662  22.447  1.00 35.37           C  
ATOM   1563  CA  VAL E  29      16.290 -50.515  22.073  1.00 33.66           C  
ATOM   1564  CA  ARG E  30      14.693 -49.900  18.722  1.00 86.05           C  
ATOM   1565  CA  VAL E  31      11.091 -48.891  18.434  1.00 43.69           C  
ATOM   1566  CA  GLU E  32       8.585 -48.382  15.660  1.00 73.90           C  
ATOM   1567  CA  GLY E  33       5.047 -47.180  15.900  1.00 30.29           C  
ATOM   1568  CA  THR E  34       2.584 -44.423  15.262  1.00 75.70           C  
ATOM   1569  CA  ALA E  58       0.191 -41.586  12.759  1.00 24.06           C  
ATOM   1570  CA  GLN E  59       3.115 -41.613  10.417  1.00103.08           C  
ATOM   1571  CA  PRO E  60       5.595 -44.294  11.089  1.00 64.70           C  
ATOM   1572  CA  PHE E  61       8.500 -43.240  13.216  1.00 54.21           C  
ATOM   1573  CA  GLU E  62      11.547 -44.979  14.503  1.00 26.61           C  
ATOM   1574  CA  GLY E  63      13.051 -44.182  17.842  1.00 17.66           C  
ATOM   1575  CA  LEU E  64      16.234 -45.313  19.462  1.00 40.99           C  
ATOM   1576  CA  GLY E  65      16.955 -45.782  23.125  1.00 21.08           C  
ATOM   1577  CA  SER E  66      18.827 -48.109  25.414  1.00 77.59           C  
ATOM   1578  CA  GLY E  67      18.024 -50.681  28.027  1.00 18.99           C  
ATOM   1579  CA  VAL E  68      19.713 -52.929  30.522  1.00109.48           C  
ATOM   1580  CA  ILE E  69      19.359 -56.664  30.840  1.00 50.01           C  
ATOM   1581  CA  ILE E  70      18.277 -57.374  34.383  1.00 90.84           C  
ATOM   1582  CA  ASN E  71      17.692 -61.060  33.992  1.00147.58           C  
ATOM   1583  CA  ALA E  72      19.610 -63.019  31.401  1.00 38.54           C  
ATOM   1584  CA  SER E  73      17.589 -66.175  31.653  1.00 37.96           C  
ATOM   1585  CA  LYS E  74      14.227 -64.508  31.441  1.00 91.05           C  
ATOM   1586  CA  GLY E  75      15.445 -61.832  29.105  1.00 27.50           C  
ATOM   1587  CA  TYR E  76      14.071 -58.951  31.122  1.00 79.97           C  
ATOM   1588  CA  VAL E  77      15.308 -55.559  30.033  1.00 40.16           C  
ATOM   1589  CA  LEU E  78      14.721 -52.324  31.898  1.00 57.74           C  
ATOM   1590  CA  THR E  79      14.097 -49.173  29.949  1.00 45.28           C  
ATOM   1591  CA  ASN E  80      12.453 -45.818  30.252  1.00 56.90           C  
ATOM   1592  CA  ASN E  81       8.750 -45.743  29.659  1.00 46.42           C  
ATOM   1593  CA  HIS E  82       9.064 -42.813  27.330  1.00 51.57           C  
ATOM   1594  CA  VAL E  83      11.291 -44.758  25.027  1.00 41.53           C  
ATOM   1595  CA  ILE E  84       8.720 -47.566  24.825  1.00179.81           C  
ATOM   1596  CA  ASN E  85       5.514 -45.570  25.046  1.00 74.81           C  
ATOM   1597  CA  GLN E  86       4.593 -45.159  21.368  1.00128.09           C  
ATOM   1598  CA  ALA E  87       6.224 -48.364  20.204  1.00 69.39           C  
ATOM   1599  CA  GLN E  88       4.001 -50.714  18.298  1.00 59.04           C  
ATOM   1600  CA  LYS E  89       6.933 -53.055  17.995  1.00 39.66           C  
ATOM   1601  CA  ILE E  90      10.228 -53.167  19.792  1.00177.66           C  
ATOM   1602  CA  SER E  91      13.510 -54.763  19.000  1.00 36.79           C  
ATOM   1603  CA  ILE E  92      16.580 -55.209  21.131  1.00100.76           C  
ATOM   1604  CA  GLN E  93      20.090 -55.221  19.748  1.00 65.15           C  
ATOM   1605  CA  LEU E  94      23.116 -56.582  21.529  1.00 51.38           C  
ATOM   1606  CA  ASN E  95      26.549 -55.069  21.215  1.00 41.00           C  
ATOM   1607  CA  ASP E  96      27.538 -58.225  19.384  1.00 66.24           C  
ATOM   1608  CA  GLY E  97      25.055 -57.336  16.691  1.00 35.52           C  
ATOM   1609  CA  ARG E  98      22.488 -59.980  17.461  1.00100.61           C  
ATOM   1610  CA  GLU E  99      18.985 -58.662  17.612  1.00109.31           C  
ATOM   1611  CA  PHE E 100      15.771 -59.886  19.136  1.00 48.32           C  
ATOM   1612  CA  ASP E 101      12.161 -58.879  19.432  1.00 29.25           C  
ATOM   1613  CA  ALA E 102      10.744 -57.761  22.727  1.00 28.60           C  
ATOM   1614  CA  LYS E 103       7.349 -57.343  24.296  1.00 56.82           C  
ATOM   1615  CA  LEU E 104       6.382 -54.816  26.902  1.00 49.76           C  
ATOM   1616  CA  ILE E 105       5.942 -56.563  30.204  1.00137.12           C  
ATOM   1617  CA  GLY E 106       4.658 -53.477  31.935  1.00 23.09           C  
ATOM   1618  CA  SER E 107       5.601 -49.926  32.696  1.00 51.08           C  
ATOM   1619  CA  ASP E 108       4.525 -46.880  34.588  1.00 96.95           C  
ATOM   1620  CA  ASP E 109       4.363 -43.221  33.663  1.00 64.49           C  
ATOM   1621  CA  GLN E 110       5.027 -41.485  36.917  1.00 86.21           C  
ATOM   1622  CA  SER E 111       8.453 -43.017  37.607  1.00 62.97           C  
ATOM   1623  CA  ASP E 112       9.063 -43.565  33.890  1.00 76.29           C  
ATOM   1624  CA  ILE E 113      10.173 -47.187  34.317  1.00 96.88           C  
ATOM   1625  CA  ALA E 114       9.276 -49.907  31.859  1.00 31.08           C  
ATOM   1626  CA  LEU E 115      10.104 -53.583  31.680  1.00105.06           C  
ATOM   1627  CA  LEU E 116      10.562 -55.471  28.443  1.00 51.64           C  
ATOM   1628  CA  GLN E 117      11.101 -59.126  27.785  1.00 42.10           C  
ATOM   1629  CA  ILE E 118      13.155 -60.483  24.946  1.00 85.79           C  
ATOM   1630  CA  GLN E 119      11.683 -63.363  23.083  1.00 92.84           C  
ATOM   1631  CA  ASN E 120      14.017 -66.325  22.754  1.00 57.06           C  
ATOM   1632  CA  PRO E 121      16.693 -64.547  24.713  1.00105.36           C  
ATOM   1633  CA  SER E 122      19.593 -67.044  24.335  1.00195.55           C  
ATOM   1634  CA  LYS E 123      23.090 -66.416  25.709  1.00 76.84           C  
ATOM   1635  CA  LEU E 124      22.534 -63.116  27.412  1.00 90.05           C  
ATOM   1636  CA  THR E 125      24.597 -61.281  29.974  1.00 51.58           C  
ATOM   1637  CA  GLN E 126      23.014 -59.761  33.041  1.00119.61           C  
ATOM   1638  CA  ILE E 127      24.069 -56.684  34.928  1.00109.25           C  
ATOM   1639  CA  ALA E 128      24.361 -56.718  38.700  1.00 30.82           C  
ATOM   1640  CA  ILE E 129      22.507 -54.078  40.640  1.00100.12           C  
ATOM   1641  CA  ALA E 130      24.116 -51.978  43.331  1.00 39.89           C  
ATOM   1642  CA  ASP E 131      22.466 -50.289  46.274  1.00 32.68           C  
ATOM   1643  CA  SER E 132      21.672 -46.777  45.141  1.00 81.99           C  
ATOM   1644  CA  ASP E 133      21.136 -45.673  48.702  1.00 30.27           C  
ATOM   1645  CA  LYS E 134      24.831 -46.166  49.312  1.00 38.00           C  
ATOM   1646  CA  LEU E 135      25.868 -43.679  46.654  1.00 55.30           C  
ATOM   1647  CA  ARG E 136      27.419 -40.428  47.771  1.00 98.98           C  
ATOM   1648  CA  VAL E 137      28.377 -37.391  45.779  1.00 77.70           C  
ATOM   1649  CA  GLY E 138      31.796 -37.774  44.280  1.00 22.43           C  
ATOM   1650  CA  ASP E 139      31.394 -41.419  43.438  1.00 30.16           C  
ATOM   1651  CA  PHE E 140      32.532 -42.396  39.978  1.00 59.86           C  
ATOM   1652  CA  ALA E 141      29.946 -43.295  37.392  1.00 30.95           C  
ATOM   1653  CA  VAL E 142      29.952 -44.572  33.841  1.00 33.67           C  
ATOM   1654  CA  ALA E 143      27.052 -44.177  31.488  1.00 29.59           C  
ATOM   1655  CA  VAL E 144      26.368 -46.586  28.697  1.00106.97           C  
ATOM   1656  CA  GLY E 145      23.757 -46.199  26.010  1.00 23.35           C  
ATOM   1657  CA  ASN E 146      23.388 -45.193  22.425  1.00 65.47           C  
ATOM   1658  CA  PRO E 147      23.584 -41.535  21.918  1.00147.99           C  
ATOM   1659  CA  PHE E 148      22.416 -40.363  18.533  1.00 69.24           C  
ATOM   1660  CA  GLY E 149      22.047 -44.018  17.709  1.00 22.29           C  
ATOM   1661  CA  LEU E 150      25.760 -44.225  17.091  1.00 84.15           C  
ATOM   1662  CA  GLY E 151      26.054 -47.543  18.855  1.00 34.27           C  
ATOM   1663  CA  GLN E 152      27.032 -48.573  22.322  1.00 47.45           C  
ATOM   1664  CA  THR E 153      28.956 -45.736  23.874  1.00130.56           C  
ATOM   1665  CA  ALA E 154      30.402 -45.324  27.292  1.00 41.01           C  
ATOM   1666  CA  THR E 155      30.960 -42.024  29.030  1.00119.94           C  
ATOM   1667  CA  SER E 156      32.507 -41.304  32.373  1.00 37.31           C  
ATOM   1668  CA  GLY E 157      31.754 -38.871  35.154  1.00 26.15           C  
ATOM   1669  CA  ILE E 158      30.964 -38.637  38.844  1.00 56.25           C  
ATOM   1670  CA  VAL E 159      27.746 -38.475  40.784  1.00123.47           C  
ATOM   1671  CA  SER E 160      27.017 -34.802  40.953  1.00 49.57           C  
ATOM   1672  CA  ALA E 161      24.025 -35.021  43.228  1.00 45.98           C  
ATOM   1673  CA  LEU E 162      21.377 -37.343  44.526  1.00 95.69           C  
ATOM   1674  CA  GLY E 163      17.814 -37.091  45.637  1.00 31.05           C  
ATOM   1675  CA  ARG E 164      17.016 -34.364  43.250  1.00 73.22           C  
ATOM   1676  CA  SER E 165      13.574 -33.321  42.216  1.00 91.30           C  
ATOM   1677  CA  GLY E 166      11.220 -30.602  41.350  1.00 46.13           C  
ATOM   1678  CA  LEU E 167      12.555 -30.912  37.834  1.00121.92           C  
ATOM   1679  CA  ASN E 168       8.947 -31.755  36.966  1.00141.52           C  
ATOM   1680  CA  LEU E 169      10.296 -34.103  34.373  1.00 51.71           C  
ATOM   1681  CA  GLU E 170       8.389 -36.960  35.981  1.00118.28           C  
ATOM   1682  CA  GLY E 171       5.587 -37.496  38.458  1.00 37.35           C  
ATOM   1683  CA  LEU E 172       7.899 -39.204  40.869  1.00122.79           C  
ATOM   1684  CA  GLU E 173      11.423 -38.111  40.753  1.00 82.74           C  
ATOM   1685  CA  ASN E 174      14.595 -38.808  42.641  1.00103.11           C  
ATOM   1686  CA  PHE E 175      17.193 -38.449  40.077  1.00 91.31           C  
ATOM   1687  CA  ILE E 176      20.804 -39.234  40.554  1.00133.20           C  
ATOM   1688  CA  GLN E 177      22.572 -36.375  38.864  1.00 54.13           C  
ATOM   1689  CA  THR E 178      25.640 -37.149  36.832  1.00113.79           C  
ATOM   1690  CA  ASP E 179      28.302 -35.293  34.869  1.00 98.99           C  
ATOM   1691  CA  ALA E 180      28.748 -38.192  32.491  1.00 42.35           C  
ATOM   1692  CA  SER E 181      27.812 -37.170  29.013  1.00 45.18           C  
ATOM   1693  CA  ILE E 182      24.260 -38.181  28.386  1.00 93.29           C  
ATOM   1694  CA  ASN E 183      22.538 -37.330  25.169  1.00 46.30           C  
ATOM   1695  CA  ARG E 184      19.431 -38.301  23.335  1.00 89.63           C  
ATOM   1696  CA  GLY E 185      19.385 -42.027  22.826  1.00 21.84           C  
ATOM   1697  CA  ASN E 186      20.873 -42.492  26.275  1.00 53.21           C  
ATOM   1698  CA  ALA E 187      17.466 -43.025  27.819  1.00 96.82           C  
ATOM   1699  CA  GLY E 188      16.938 -46.415  29.327  1.00 26.10           C  
ATOM   1700  CA  GLY E 189      20.687 -46.822  29.383  1.00 24.95           C  
ATOM   1701  CA  ALA E 190      22.690 -47.764  32.396  1.00 57.06           C  
ATOM   1702  CA  LEU E 191      24.733 -45.777  34.838  1.00 81.45           C  
ATOM   1703  CA  LEU E 192      27.359 -47.975  36.375  1.00117.21           C  
ATOM   1704  CA  ASN E 193      29.748 -47.751  39.261  1.00 59.85           C  
ATOM   1705  CA  LEU E 194      33.375 -48.800  39.061  1.00 88.86           C  
ATOM   1706  CA  ASN E 195      32.252 -52.299  39.911  1.00 47.97           C  
ATOM   1707  CA  GLY E 196      30.126 -52.312  36.822  1.00 26.27           C  
ATOM   1708  CA  GLU E 197      27.010 -52.641  38.871  1.00111.52           C  
ATOM   1709  CA  LEU E 198      23.909 -50.675  37.967  1.00144.53           C  
ATOM   1710  CA  ILE E 199      23.534 -47.437  39.934  1.00114.22           C  
ATOM   1711  CA  GLY E 200      20.571 -46.163  37.941  1.00 28.90           C  
ATOM   1712  CA  ILE E 201      18.894 -45.805  34.569  1.00 52.69           C  
ATOM   1713  CA  ASN E 202      19.579 -42.612  32.645  1.00 84.18           C  
ATOM   1714  CA  THR E 203      16.230 -40.889  32.264  1.00 86.24           C  
ATOM   1715  CA  ALA E 204      16.841 -37.326  31.145  1.00 53.65           C  
ATOM   1716  CA  ILE E 205      19.075 -34.305  30.776  1.00109.65           C  
ATOM   1717  CA  LEU E 206      18.841 -30.577  31.239  1.00 52.39           C  
ATOM   1718  CA  ALA E 207      20.345 -28.904  28.236  1.00 41.58           C  
ATOM   1719  CA  PRO E 208      19.426 -25.730  26.540  1.00 66.61           C  
ATOM   1720  CA  GLY E 209      21.194 -26.837  23.380  1.00 28.48           C  
ATOM   1721  CA  GLY E 210      19.601 -30.220  23.366  1.00 22.21           C  
ATOM   1722  CA  GLY E 211      23.110 -31.525  23.798  1.00 22.77           C  
ATOM   1723  CA  SER E 212      24.778 -32.732  26.960  1.00 56.08           C  
ATOM   1724  CA  VAL E 213      25.476 -29.837  29.303  1.00 60.47           C  
ATOM   1725  CA  GLY E 214      26.936 -32.174  31.862  1.00 35.47           C  
ATOM   1726  CA  ILE E 215      23.730 -32.254  33.837  1.00 87.13           C  
ATOM   1727  CA  GLY E 216      22.095 -35.630  33.503  1.00 21.08           C  
ATOM   1728  CA  PHE E 217      19.581 -37.429  35.647  1.00 54.72           C  
ATOM   1729  CA  ALA E 218      18.998 -41.097  36.240  1.00 37.40           C  
ATOM   1730  CA  ILE E 219      16.520 -43.142  38.186  1.00162.81           C  
ATOM   1731  CA  PRO E 220      18.296 -44.887  40.931  1.00103.52           C  
ATOM   1732  CA  SER E 221      18.946 -48.601  40.749  1.00 40.23           C  
ATOM   1733  CA  ASN E 222      16.992 -49.243  43.850  1.00 57.49           C  
ATOM   1734  CA  MET E 223      14.371 -47.465  41.946  1.00114.80           C  
ATOM   1735  CA  ALA E 224      14.375 -49.530  38.847  1.00 51.91           C  
ATOM   1736  CA  ARG E 225      15.038 -52.769  40.619  1.00160.00           C  
ATOM   1737  CA  THR E 226      12.053 -53.087  42.816  1.00 64.50           C  
ATOM   1738  CA  LEU E 227       9.849 -51.236  40.340  1.00113.47           C  
ATOM   1739  CA  ALA E 228      10.948 -53.709  37.741  1.00 46.58           C  
ATOM   1740  CA  GLN E 229      10.480 -56.612  40.049  1.00 81.01           C  
ATOM   1741  CA  GLN E 230       6.770 -56.345  40.516  1.00 92.65           C  
ATOM   1742  CA  LEU E 231       6.432 -55.751  36.829  1.00129.60           C  
ATOM   1743  CA  ILE E 232       7.488 -59.327  36.643  1.00123.44           C  
ATOM   1744  CA  ASP E 233       6.241 -60.212  40.165  1.00161.08           C  
ATOM   1745  CA  PHE E 234       4.244 -59.697  42.280  1.00148.38           C  
ATOM   1746  CA  GLY E 235       2.489 -58.604  39.176  1.00 40.80           C  
ATOM   1747  CA  GLU E 236      -0.148 -56.473  40.768  1.00 96.70           C  
ATOM   1748  CA  ILE E 237      -0.905 -54.021  38.010  1.00 83.87           C  
ATOM   1749  CA  LYS E 238      -2.551 -51.581  40.343  1.00222.68           C  
ATOM   1750  CA  ARG E 239      -1.739 -48.984  40.726  1.00229.79           C  
ATOM   1751  CA  GLY E 240       1.593 -49.661  39.092  1.00 46.07           C  
ATOM   1752  CA  LEU E 241       2.573 -46.195  40.248  1.00103.29           C  
ATOM   1753  CA  LEU E 242       0.636 -43.328  41.697  1.00 81.37           C  
ATOM   1754  CA  GLY E 243      -0.289 -41.595  38.469  1.00 49.40           C  
ATOM   1755  CA  ILE E 244       0.356 -37.983  39.404  1.00 68.55           C  
ATOM   1756  CA  LYS E 245       2.460 -35.052  38.322  1.00108.75           C  
ATOM   1757  CA  GLY E 246       4.267 -32.826  40.717  1.00 35.82           C  
ATOM   1758  CA  THR E 247       7.303 -30.717  41.265  1.00130.97           C  
ATOM   1759  CA  GLU E 248       8.895 -28.944  44.142  1.00 97.99           C  
ATOM   1760  CA  MET E 249       6.439 -27.821  46.773  1.00 91.51           C  
ATOM   1761  CA  SER E 250       3.964 -26.064  44.690  1.00236.46           C  
ATOM   1762  CA  ALA E 251       4.835 -23.421  42.777  1.00156.22           C  
ATOM   1763  CA  ASP E 252       5.705 -20.405  44.754  1.00 87.38           C  
ATOM   1764  CA  ILE E 253       6.864 -21.450  48.128  1.00 85.46           C  
ATOM   1765  CA  ALA E 254       9.351 -24.283  47.952  1.00 73.32           C  
ATOM   1766  CA  LYS E 255      10.493 -24.366  44.412  1.00183.62           C  
ATOM   1767  CA  ALA E 256      12.481 -21.328  43.669  1.00 90.88           C  
ATOM   1768  CA  PHE E 257      15.361 -20.725  45.955  1.00219.15           C  
ATOM   1769  CA  ASN E 258      15.105 -24.086  47.163  1.00304.93           C  
ATOM   1770  CA  LEU E 259      13.703 -23.405  50.570  1.00154.41           C  
ATOM   1771  CA  ASP E 260      15.519 -24.291  53.747  1.00117.45           C  
ATOM   1772  CA  VAL E 261      13.205 -27.093  54.570  1.00 68.04           C  
ATOM   1773  CA  GLN E 262      14.181 -28.906  51.454  1.00 80.14           C  
ATOM   1774  CA  ARG E 263      10.835 -29.454  49.836  1.00128.45           C  
ATOM   1775  CA  GLY E 264       7.741 -31.511  49.779  1.00 46.27           C  
ATOM   1776  CA  ALA E 265       6.346 -33.288  46.822  1.00 46.49           C  
ATOM   1777  CA  PHE E 266       3.641 -31.061  45.620  1.00142.75           C  
ATOM   1778  CA  VAL E 267       1.137 -32.274  43.159  1.00 72.37           C  
ATOM   1779  CA  SER E 268      -0.285 -29.953  40.563  1.00 61.77           C  
ATOM   1780  CA  GLU E 269      -2.411 -32.571  38.931  1.00116.47           C  
ATOM   1781  CA  VAL E 270      -4.713 -35.522  39.346  1.00106.54           C  
ATOM   1782  CA  LEU E 271      -4.566 -38.284  36.789  1.00 52.97           C  
ATOM   1783  CA  PRO E 272      -7.736 -39.820  35.597  1.00 67.74           C  
ATOM   1784  CA  GLY E 273      -8.464 -43.411  36.536  1.00 24.54           C  
ATOM   1785  CA  SER E 274      -5.157 -42.974  38.210  1.00 41.86           C  
ATOM   1786  CA  GLY E 275      -3.999 -44.435  41.409  1.00 33.15           C  
ATOM   1787  CA  SER E 276      -3.897 -41.055  42.937  1.00 42.88           C  
ATOM   1788  CA  ALA E 277      -7.369 -40.430  41.684  1.00 53.54           C  
ATOM   1789  CA  LYS E 278      -9.133 -43.276  43.399  1.00121.78           C  
ATOM   1790  CA  ALA E 279      -6.904 -42.992  46.415  1.00 40.80           C  
ATOM   1791  CA  GLY E 280      -8.438 -39.628  46.597  1.00 40.08           C  
ATOM   1792  CA  VAL E 281      -5.241 -37.688  46.412  1.00 74.87           C  
ATOM   1793  CA  LYS E 282      -5.870 -34.627  44.490  1.00133.92           C  
ATOM   1794  CA  ALA E 283      -4.129 -31.506  43.407  1.00114.95           C  
ATOM   1795  CA  GLY E 284      -2.614 -28.855  45.511  1.00 50.39           C  
ATOM   1796  CA  ASP E 285      -1.547 -31.853  47.481  1.00108.98           C  
ATOM   1797  CA  ILE E 286       1.548 -31.748  49.431  1.00119.39           C  
ATOM   1798  CA  ILE E 287       3.027 -35.163  49.938  1.00 71.43           C  
ATOM   1799  CA  THR E 288       4.845 -34.894  53.234  1.00 54.55           C  
ATOM   1800  CA  SER E 289       5.858 -38.450  53.690  1.00 94.92           C  
ATOM   1801  CA  LEU E 290       5.723 -41.912  52.316  1.00 74.99           C  
ATOM   1802  CA  ASN E 291       5.357 -44.830  54.666  1.00177.23           C  
ATOM   1803  CA  GLY E 292       6.257 -44.599  58.350  1.00 53.33           C  
ATOM   1804  CA  LYS E 293       9.536 -42.804  57.822  1.00 69.63           C  
ATOM   1805  CA  PRO E 294       9.473 -39.236  56.816  1.00 63.56           C  
ATOM   1806  CA  LEU E 295       9.684 -38.165  53.207  1.00 95.48           C  
ATOM   1807  CA  ASN E 296      12.007 -35.521  51.929  1.00 71.51           C  
ATOM   1808  CA  SER E 297      11.582 -33.388  48.880  1.00 56.36           C  
ATOM   1809  CA  PHE E 298       9.882 -34.375  45.690  1.00 75.45           C  
ATOM   1810  CA  ALA E 299      13.268 -35.801  45.000  1.00 50.06           C  
ATOM   1811  CA  GLU E 300      13.214 -38.274  47.810  1.00 98.50           C  
ATOM   1812  CA  LEU E 301       9.733 -39.117  46.683  1.00 73.26           C  
ATOM   1813  CA  ARG E 302      10.591 -40.896  43.533  1.00195.95           C  
ATOM   1814  CA  SER E 303      13.658 -42.155  45.193  1.00 59.07           C  
ATOM   1815  CA  ARG E 304      11.803 -44.445  47.397  1.00170.49           C  
ATOM   1816  CA  ILE E 305       8.798 -44.970  45.152  1.00 85.13           C  
ATOM   1817  CA  ALA E 306      10.773 -45.424  42.047  1.00 69.35           C  
ATOM   1818  CA  THR E 307      12.669 -47.734  44.278  1.00 55.04           C  
ATOM   1819  CA  THR E 308       9.679 -49.630  45.461  1.00 75.77           C  
ATOM   1820  CA  GLU E 309       7.579 -52.190  43.659  1.00 85.12           C  
ATOM   1821  CA  PRO E 310       5.132 -50.643  41.374  1.00193.85           C  
ATOM   1822  CA  GLY E 311       2.952 -52.185  42.651  1.00123.53           C  
ATOM   1823  CA  THR E 312       3.398 -52.382  46.361  1.00119.86           C  
ATOM   1824  CA  LYS E 313       0.604 -51.058  48.462  1.00 70.98           C  
ATOM   1825  CA  VAL E 314       1.915 -48.092  50.345  1.00 46.63           C  
ATOM   1826  CA  LYS E 315       0.490 -45.276  52.385  1.00 31.69           C  
ATOM   1827  CA  LEU E 316       1.145 -41.670  51.641  1.00106.70           C  
ATOM   1828  CA  GLY E 317       1.091 -38.715  53.927  1.00 51.84           C  
ATOM   1829  CA  LEU E 318       0.053 -35.416  52.540  1.00189.81           C  
ATOM   1830  CA  LEU E 319      -1.054 -32.162  53.784  1.00109.95           C  
ATOM   1831  CA  ARG E 320      -4.184 -30.827  52.538  1.00215.01           C  
ATOM   1832  CA  ASN E 321      -5.710 -27.718  54.021  1.00201.68           C  
ATOM   1833  CA  GLY E 322      -3.131 -27.686  56.629  1.00 45.60           C  
ATOM   1834  CA  LYS E 323      -4.487 -30.907  57.818  1.00119.22           C  
ATOM   1835  CA  PRO E 324      -3.318 -34.365  57.820  1.00153.66           C  
ATOM   1836  CA  LEU E 325      -4.446 -37.664  56.315  1.00197.09           C  
ATOM   1837  CA  GLU E 326      -3.138 -41.012  55.615  1.00115.54           C  
ATOM   1838  CA  VAL E 327      -4.307 -42.674  52.483  1.00114.02           C  
ATOM   1839  CA  GLU E 328      -3.454 -45.941  50.825  1.00 49.27           C  
ATOM   1840  CA  VAL E 329      -2.368 -45.396  47.294  1.00 50.06           C  
ATOM   1841  CA  SER E 340     -25.871 -45.025  20.640  1.00 39.81           C  
ATOM   1842  CA  ALA E 341     -25.841 -44.923  16.896  1.00 52.76           C  
ATOM   1843  CA  GLU E 342     -23.720 -41.837  16.778  1.00 61.86           C  
ATOM   1844  CA  MET E 343     -20.475 -43.442  17.855  1.00 50.93           C  
ATOM   1845  CA  ILE E 344     -20.535 -46.092  15.186  1.00 75.84           C  
ATOM   1846  CA  THR E 345     -22.214 -43.642  12.889  1.00166.63           C  
ATOM   1847  CA  PRO E 346     -21.028 -40.149  12.589  1.00160.94           C  
ATOM   1848  CA  ALA E 347     -23.180 -37.345  13.928  1.00 81.87           C  
ATOM   1849  CA  LEU E 348     -26.312 -39.458  13.612  1.00 87.78           C  
ATOM   1850  CA  GLU E 349     -27.829 -39.282  17.035  1.00 76.84           C  
ATOM   1851  CA  GLY E 350     -30.285 -42.027  17.554  1.00 25.44           C  
ATOM   1852  CA  ALA E 351     -31.032 -45.293  19.222  1.00 31.23           C  
ATOM   1853  CA  THR E 352     -28.192 -46.821  21.132  1.00 26.04           C  
ATOM   1854  CA  LEU E 353     -26.612 -49.974  19.852  1.00 62.69           C  
ATOM   1855  CA  SER E 354     -25.536 -53.144  21.579  1.00 38.35           C  
ATOM   1856  CA  ASP E 355     -23.316 -55.998  20.456  1.00 59.30           C  
ATOM   1857  CA  GLY E 356     -24.016 -59.758  20.336  1.00 58.58           C  
ATOM   1858  CA  GLN E 357     -27.399 -61.014  19.381  1.00197.45           C  
ATOM   1859  CA  LEU E 358     -27.783 -60.500  22.892  1.00227.93           C  
ATOM   1860  CA  LYS E 359     -28.956 -63.835  23.798  1.00157.19           C  
ATOM   1861  CA  ASP E 360     -28.813 -65.694  20.573  1.00 51.54           C  
ATOM   1862  CA  GLY E 361     -25.968 -66.290  18.249  1.00 30.21           C  
ATOM   1863  CA  GLY E 362     -24.924 -62.904  17.073  1.00 37.33           C  
ATOM   1864  CA  LYS E 363     -27.246 -62.013  14.271  1.00 96.54           C  
ATOM   1865  CA  GLY E 364     -25.615 -58.663  14.568  1.00 27.98           C  
ATOM   1866  CA  ILE E 365     -25.776 -55.440  16.491  1.00162.50           C  
ATOM   1867  CA  LYS E 366     -28.966 -54.588  18.219  1.00 81.17           C  
ATOM   1868  CA  ILE E 367     -30.354 -51.135  18.555  1.00 69.28           C  
ATOM   1869  CA  ASP E 368     -31.491 -50.763  22.121  1.00 57.13           C  
ATOM   1870  CA  GLU E 369     -33.913 -47.916  21.981  1.00 87.25           C  
ATOM   1871  CA  VAL E 370     -35.003 -45.210  19.621  1.00128.03           C  
ATOM   1872  CA  VAL E 371     -34.425 -41.596  20.630  1.00176.07           C  
ATOM   1873  CA  LYS E 372     -37.007 -40.992  17.853  1.00149.45           C  
ATOM   1874  CA  GLY E 373     -36.672 -37.238  17.742  1.00 37.99           C  
ATOM   1875  CA  SER E 374     -33.066 -37.983  16.711  1.00 41.47           C  
ATOM   1876  CA  PRO E 375     -31.898 -38.469  13.207  1.00 65.95           C  
ATOM   1877  CA  ALA E 376     -31.151 -42.141  13.593  1.00 42.41           C  
ATOM   1878  CA  ALA E 377     -34.896 -42.261  14.005  1.00 51.21           C  
ATOM   1879  CA  GLN E 378     -35.732 -40.170  10.957  1.00 95.50           C  
ATOM   1880  CA  ALA E 379     -34.267 -42.593   8.443  1.00 79.18           C  
ATOM   1881  CA  GLY E 380     -35.893 -45.784   9.521  1.00 67.33           C  
ATOM   1882  CA  LEU E 381     -34.054 -47.076  12.528  1.00 59.14           C  
ATOM   1883  CA  GLN E 382     -36.588 -48.502  14.931  1.00 57.89           C  
ATOM   1884  CA  LYS E 383     -35.807 -50.166  18.218  1.00105.77           C  
ATOM   1885  CA  ASP E 384     -35.388 -53.912  18.414  1.00 71.14           C  
ATOM   1886  CA  ASP E 385     -33.883 -54.091  14.976  1.00 59.54           C  
ATOM   1887  CA  VAL E 386     -30.954 -56.386  14.437  1.00 60.74           C  
ATOM   1888  CA  ILE E 387     -28.338 -55.350  11.980  1.00 63.54           C  
ATOM   1889  CA  ILE E 388     -27.281 -58.535  10.304  1.00116.74           C  
ATOM   1890  CA  GLY E 389     -24.801 -56.967   7.927  1.00 35.38           C  
ATOM   1891  CA  VAL E 390     -23.930 -53.847   6.014  1.00103.05           C  
ATOM   1892  CA  ASN E 391     -22.916 -53.397   2.416  1.00 66.22           C  
ATOM   1893  CA  ARG E 392     -22.974 -57.076   1.535  1.00137.22           C  
ATOM   1894  CA  ASP E 393     -20.931 -57.760   4.612  1.00 39.34           C  
ATOM   1895  CA  ARG E 394     -22.097 -59.690   7.624  1.00 96.09           C  
ATOM   1896  CA  VAL E 395     -21.977 -57.814  10.876  1.00 47.60           C  
ATOM   1897  CA  ASN E 396     -21.530 -60.202  13.747  1.00 58.06           C  
ATOM   1898  CA  SER E 397     -20.729 -57.444  16.160  1.00 48.21           C  
ATOM   1899  CA  ILE E 398     -20.084 -53.764  16.541  1.00142.70           C  
ATOM   1900  CA  ALA E 399     -16.455 -54.114  15.594  1.00 25.97           C  
ATOM   1901  CA  GLU E 400     -17.215 -55.695  12.266  1.00 52.85           C  
ATOM   1902  CA  MET E 401     -19.826 -53.119  11.484  1.00 33.24           C  
ATOM   1903  CA  ARG E 402     -17.198 -50.536  12.220  1.00157.36           C  
ATOM   1904  CA  LYS E 403     -15.024 -52.241   9.653  1.00134.11           C  
ATOM   1905  CA  VAL E 404     -17.531 -51.740   6.882  1.00 24.38           C  
ATOM   1906  CA  LEU E 405     -17.775 -48.131   7.917  1.00 45.02           C  
ATOM   1907  CA  ALA E 406     -14.022 -47.978   7.710  1.00 26.52           C  
ATOM   1908  CA  ALA E 407     -14.438 -48.320   3.971  1.00 27.16           C  
ATOM   1909  CA  LYS E 408     -16.637 -45.261   4.279  1.00109.43           C  
ATOM   1910  CA  PRO E 409     -18.722 -46.126   1.287  1.00 65.15           C  
ATOM   1911  CA  ALA E 410     -20.828 -43.217   0.136  1.00 23.10           C  
ATOM   1912  CA  ILE E 411     -23.861 -45.408   0.431  1.00 90.75           C  
ATOM   1913  CA  ILE E 412     -24.259 -47.742   3.362  1.00 48.01           C  
ATOM   1914  CA  ALA E 413     -26.908 -50.445   3.552  1.00 56.49           C  
ATOM   1915  CA  LEU E 414     -27.468 -51.498   7.102  1.00159.65           C  
ATOM   1916  CA  GLN E 415     -29.052 -54.922   7.473  1.00156.36           C  
ATOM   1917  CA  ILE E 416     -31.839 -55.179   9.813  1.00 93.14           C  
ATOM   1918  CA  VAL E 417     -34.271 -57.826  10.743  1.00 69.69           C  
ATOM   1919  CA  ARG E 418     -37.442 -56.382  12.094  1.00 86.35           C  
ATOM   1920  CA  GLY E 419     -40.015 -58.671  13.558  1.00 24.38           C  
ATOM   1921  CA  ASN E 420     -40.202 -61.695  11.399  1.00 72.55           C  
ATOM   1922  CA  GLU E 421     -39.316 -59.634   8.435  1.00111.31           C  
ATOM   1923  CA  SER E 422     -36.260 -58.301   6.956  1.00 98.62           C  
ATOM   1924  CA  ILE E 423     -36.001 -54.654   6.823  1.00178.16           C  
ATOM   1925  CA  TYR E 424     -33.779 -53.099   4.417  1.00260.10           C  
ATOM   1926  CA  LEU E 425     -31.933 -50.006   6.003  1.00131.02           C  
ATOM   1927  CA  LEU E 426     -30.336 -47.055   4.487  1.00193.72           C  
ATOM   1928  CA  MET E 427     -27.706 -44.350   4.764  1.00 83.11           C  
ATOM   1929  CA  ARG E 428     -26.946 -41.139   2.920  1.00114.35           C  
TER    1930      ARG E 428                                                      
ATOM   1931  CA  PRO F  11      43.301 -37.604  41.994  1.00185.60           C  
ATOM   1932  CA  LEU F  12      45.990 -39.787  40.596  1.00121.56           C  
ATOM   1933  CA  PRO F  13      49.538 -39.373  41.609  1.00121.76           C  
ATOM   1934  CA  SER F  14      50.672 -35.846  41.196  1.00113.20           C  
ATOM   1935  CA  LEU F  15      50.065 -34.717  37.682  1.00122.87           C  
ATOM   1936  CA  ALA F  16      52.189 -31.629  38.161  1.00 41.48           C  
ATOM   1937  CA  PRO F  17      55.470 -33.364  38.491  1.00139.93           C  
ATOM   1938  CA  MET F  18      54.896 -35.253  35.268  1.00132.77           C  
ATOM   1939  CA  LEU F  19      53.587 -32.144  33.549  1.00 63.64           C  
ATOM   1940  CA  GLU F  20      56.516 -30.025  34.537  1.00144.12           C  
ATOM   1941  CA  LYS F  21      58.932 -31.918  32.359  1.00118.80           C  
ATOM   1942  CA  VAL F  22      56.555 -32.577  29.455  1.00 61.92           C  
ATOM   1943  CA  LEU F  23      54.889 -29.203  29.019  1.00 83.30           C  
ATOM   1944  CA  PRO F  24      57.615 -27.453  27.148  1.00 64.70           C  
ATOM   1945  CA  ALA F  25      57.293 -30.045  24.409  1.00 30.57           C  
ATOM   1946  CA  VAL F  26      53.828 -28.859  23.483  1.00 33.09           C  
ATOM   1947  CA  VAL F  27      53.675 -25.643  21.557  1.00 33.94           C  
ATOM   1948  CA  SER F  28      51.146 -23.211  20.185  1.00 88.47           C  
ATOM   1949  CA  VAL F  29      50.972 -22.763  16.476  1.00 92.84           C  
ATOM   1950  CA  ARG F  30      50.026 -19.451  14.966  1.00 51.10           C  
ATOM   1951  CA  VAL F  31      48.995 -19.099  11.382  1.00 37.91           C  
ATOM   1952  CA  GLU F  32      48.277 -16.282   9.001  1.00 30.11           C  
ATOM   1953  CA  GLY F  33      47.040 -16.530   5.470  1.00 21.61           C  
ATOM   1954  CA  THR F  34      44.571 -15.566   2.777  1.00 37.92           C  
ATOM   1955  CA  ALA F  58      42.163 -13.024   0.317  1.00 16.61           C  
ATOM   1956  CA  GLN F  59      41.508 -11.120   3.491  1.00151.46           C  
ATOM   1957  CA  PRO F  60      44.017 -11.865   6.120  1.00154.23           C  
ATOM   1958  CA  PHE F  61      42.921 -14.303   8.781  1.00 47.93           C  
ATOM   1959  CA  GLU F  62      44.666 -15.539  11.864  1.00 24.95           C  
ATOM   1960  CA  GLY F  63      44.253 -18.960  13.330  1.00 15.78           C  
ATOM   1961  CA  LEU F  64      45.552 -20.595  16.439  1.00 75.28           C  
ATOM   1962  CA  GLY F  65      46.299 -24.226  17.085  1.00 18.66           C  
ATOM   1963  CA  SER F  66      48.802 -26.392  18.875  1.00 26.66           C  
ATOM   1964  CA  GLY F  67      51.592 -28.751  17.964  1.00 18.60           C  
ATOM   1965  CA  VAL F  68      54.018 -31.096  19.602  1.00 98.34           C  
ATOM   1966  CA  ILE F  69      57.763 -31.139  19.229  1.00 47.91           C  
ATOM   1967  CA  ILE F  70      58.776 -34.568  18.031  1.00 98.37           C  
ATOM   1968  CA  ASN F  71      62.431 -33.855  17.469  1.00 44.63           C  
ATOM   1969  CA  ALA F  72      64.136 -31.169  19.454  1.00 30.98           C  
ATOM   1970  CA  SER F  73      67.299 -31.131  17.441  1.00 31.92           C  
ATOM   1971  CA  LYS F  74      65.635 -30.948  14.081  1.00109.21           C  
ATOM   1972  CA  GLY F  75      62.790 -28.865  15.383  1.00 25.39           C  
ATOM   1973  CA  TYR F  76      60.071 -31.031  13.910  1.00 54.88           C  
ATOM   1974  CA  VAL F  77      56.624 -30.278  15.213  1.00 42.50           C  
ATOM   1975  CA  LEU F  78      53.555 -32.300  14.439  1.00102.20           C  
ATOM   1976  CA  THR F  79      50.210 -30.649  14.050  1.00 48.59           C  
ATOM   1977  CA  ASN F  80      46.926 -31.108  12.309  1.00 50.58           C  
ATOM   1978  CA  ASN F  81      46.810 -30.390   8.633  1.00 41.91           C  
ATOM   1979  CA  HIS F  82      43.681 -28.341   9.043  1.00 44.39           C  
ATOM   1980  CA  VAL F  83      45.409 -25.942  11.340  1.00119.56           C  
ATOM   1981  CA  ILE F  84      48.207 -25.506   8.759  1.00138.34           C  
ATOM   1982  CA  ASN F  85      46.219 -25.723   5.527  1.00 66.84           C  
ATOM   1983  CA  GLN F  86      45.500 -22.071   4.767  1.00 64.95           C  
ATOM   1984  CA  ALA F  87      48.600 -20.703   6.463  1.00 68.36           C  
ATOM   1985  CA  GLN F  88      50.817 -18.538   4.348  1.00 96.48           C  
ATOM   1986  CA  LYS F  89      53.130 -18.099   7.303  1.00 30.52           C  
ATOM   1987  CA  ILE F  90      53.395 -20.059  10.490  1.00 47.14           C  
ATOM   1988  CA  SER F  91      54.996 -19.332  13.804  1.00 26.67           C  
ATOM   1989  CA  ILE F  92      55.371 -21.489  16.859  1.00 85.17           C  
ATOM   1990  CA  GLN F  93      55.544 -20.240  20.370  1.00103.13           C  
ATOM   1991  CA  LEU F  94      56.897 -22.075  23.341  1.00 88.95           C  
ATOM   1992  CA  ASN F  95      55.475 -22.024  26.826  1.00 37.70           C  
ATOM   1993  CA  ASP F  96      58.496 -19.973  27.797  1.00 53.19           C  
ATOM   1994  CA  GLY F  97      57.417 -17.248  25.427  1.00 29.70           C  
ATOM   1995  CA  ARG F  98      60.072 -17.774  22.814  1.00109.91           C  
ATOM   1996  CA  GLU F  99      58.748 -17.729  19.293  1.00 43.25           C  
ATOM   1997  CA  PHE F 100      60.075 -19.207  16.105  1.00 58.91           C  
ATOM   1998  CA  ASP F 101      59.255 -19.342  12.428  1.00122.47           C  
ATOM   1999  CA  ALA F 102      58.199 -22.631  10.935  1.00 38.50           C  
ATOM   2000  CA  LYS F 103      57.966 -24.080   7.479  1.00102.36           C  
ATOM   2001  CA  LEU F 104      55.605 -26.786   6.377  1.00105.95           C  
ATOM   2002  CA  ILE F 105      57.630 -29.897   5.743  1.00 39.76           C  
ATOM   2003  CA  GLY F 106      54.683 -31.872   4.489  1.00 22.44           C  
ATOM   2004  CA  SER F 107      51.163 -32.861   5.337  1.00 51.20           C  
ATOM   2005  CA  ASP F 108      48.314 -35.045   4.259  1.00101.08           C  
ATOM   2006  CA  ASP F 109      44.605 -34.317   4.092  1.00 62.64           C  
ATOM   2007  CA  GLN F 110      43.048 -37.683   4.660  1.00 98.45           C  
ATOM   2008  CA  SER F 111      44.704 -38.460   7.996  1.00 65.66           C  
ATOM   2009  CA  ASP F 112      44.947 -34.736   8.773  1.00 71.71           C  
ATOM   2010  CA  ILE F 113      48.578 -34.888   9.895  1.00107.72           C  
ATOM   2011  CA  ALA F 114      51.101 -32.184   9.082  1.00 32.22           C  
ATOM   2012  CA  LEU F 115      54.743 -31.812   9.940  1.00106.90           C  
ATOM   2013  CA  LEU F 116      56.424 -28.491  10.482  1.00105.00           C  
ATOM   2014  CA  GLN F 117      60.012 -27.590  11.061  1.00 32.53           C  
ATOM   2015  CA  ILE F 118      61.136 -24.772  13.252  1.00 56.76           C  
ATOM   2016  CA  GLN F 119      63.710 -22.503  11.778  1.00106.41           C  
ATOM   2017  CA  ASN F 120      66.823 -22.156  13.893  1.00 62.42           C  
ATOM   2018  CA  PRO F 121      65.383 -24.239  16.655  1.00 62.33           C  
ATOM   2019  CA  SER F 122      67.327 -23.957  19.872  1.00 36.76           C  
ATOM   2020  CA  LYS F 123      67.119 -25.427  23.358  1.00 42.33           C  
ATOM   2021  CA  LEU F 124      63.932 -27.259  22.614  1.00 46.32           C  
ATOM   2022  CA  THR F 125      62.335 -30.118  24.474  1.00 27.64           C  
ATOM   2023  CA  GLN F 126      60.944 -33.161  22.782  1.00 94.32           C  
ATOM   2024  CA  ILE F 127      58.074 -35.399  23.706  1.00 47.93           C  
ATOM   2025  CA  ALA F 128      58.448 -39.125  24.026  1.00 25.70           C  
ATOM   2026  CA  ILE F 129      56.068 -41.202  21.977  1.00 40.49           C  
ATOM   2027  CA  ALA F 130      54.114 -44.064  23.474  1.00 34.35           C  
ATOM   2028  CA  ASP F 131      52.723 -47.050  21.652  1.00 38.99           C  
ATOM   2029  CA  SER F 132      49.120 -46.204  20.877  1.00 38.69           C  
ATOM   2030  CA  ASP F 133      48.108 -49.767  20.214  1.00 51.41           C  
ATOM   2031  CA  LYS F 134      48.719 -50.585  23.871  1.00 98.50           C  
ATOM   2032  CA  LEU F 135      46.118 -48.090  25.030  1.00 57.51           C  
ATOM   2033  CA  ARG F 136      43.000 -49.479  26.593  1.00187.28           C  
ATOM   2034  CA  VAL F 137      39.802 -47.810  27.648  1.00 37.04           C  
ATOM   2035  CA  GLY F 138      40.030 -46.404  31.124  1.00 21.71           C  
ATOM   2036  CA  ASP F 139      43.602 -45.292  30.709  1.00 41.42           C  
ATOM   2037  CA  PHE F 140      44.239 -41.801  32.005  1.00 51.65           C  
ATOM   2038  CA  ALA F 141      44.977 -39.068  29.530  1.00 30.03           C  
ATOM   2039  CA  VAL F 142      45.910 -35.434  29.672  1.00 86.55           C  
ATOM   2040  CA  ALA F 143      45.369 -33.036  26.840  1.00 27.14           C  
ATOM   2041  CA  VAL F 144      47.553 -30.035  26.283  1.00 30.73           C  
ATOM   2042  CA  GLY F 145      46.923 -27.306  23.777  1.00 21.98           C  
ATOM   2043  CA  ASN F 146      45.683 -23.784  23.459  1.00 65.96           C  
ATOM   2044  CA  PRO F 147      41.989 -23.587  23.811  1.00 70.13           C  
ATOM   2045  CA  PHE F 148      40.538 -20.287  22.676  1.00 61.78           C  
ATOM   2046  CA  GLY F 149      44.120 -19.171  22.292  1.00 24.76           C  
ATOM   2047  CA  LEU F 150      44.334 -18.694  26.030  1.00 89.89           C  
ATOM   2048  CA  GLY F 151      47.790 -20.198  26.275  1.00 31.14           C  
ATOM   2049  CA  GLN F 152      49.012 -23.616  27.207  1.00 65.39           C  
ATOM   2050  CA  THR F 153      46.242 -25.381  29.005  1.00 32.77           C  
ATOM   2051  CA  ALA F 154      46.120 -28.876  30.364  1.00 28.49           C  
ATOM   2052  CA  THR F 155      42.953 -30.858  30.866  1.00 37.04           C  
ATOM   2053  CA  SER F 156      42.535 -34.322  32.191  1.00 80.70           C  
ATOM   2054  CA  GLY F 157      40.319 -37.273  31.414  1.00 27.89           C  
ATOM   2055  CA  ILE F 158      40.405 -40.931  30.482  1.00 57.78           C  
ATOM   2056  CA  VAL F 159      40.508 -42.785  27.205  1.00 40.46           C  
ATOM   2057  CA  SER F 160      36.846 -43.206  26.397  1.00 45.49           C  
ATOM   2058  CA  ALA F 161      37.225 -45.385  23.340  1.00 46.00           C  
ATOM   2059  CA  LEU F 162      39.606 -46.337  20.589  1.00 77.10           C  
ATOM   2060  CA  GLY F 163      39.433 -47.359  16.977  1.00 28.62           C  
ATOM   2061  CA  ARG F 164      36.607 -45.036  16.271  1.00114.66           C  
ATOM   2062  CA  SER F 165      35.653 -43.986  12.824  1.00 69.79           C  
ATOM   2063  CA  GLY F 166      32.702 -43.287  10.620  1.00 32.88           C  
ATOM   2064  CA  LEU F 167      32.716 -39.805  12.097  1.00 47.88           C  
ATOM   2065  CA  ASN F 168      33.317 -38.602   8.557  1.00 73.46           C  
ATOM   2066  CA  LEU F 169      35.553 -35.971  10.024  1.00 50.44           C  
ATOM   2067  CA  GLU F 170      38.518 -37.277   8.063  1.00 96.79           C  
ATOM   2068  CA  GLY F 171      39.179 -39.531   5.091  1.00 38.27           C  
ATOM   2069  CA  LEU F 172      41.086 -41.875   7.317  1.00153.98           C  
ATOM   2070  CA  GLU F 173      40.032 -42.059  10.854  1.00 83.92           C  
ATOM   2071  CA  ASN F 174      40.921 -44.089  13.894  1.00 91.85           C  
ATOM   2072  CA  PHE F 175      40.402 -41.666  16.619  1.00 82.33           C  
ATOM   2073  CA  ILE F 176      41.136 -42.270  20.209  1.00 81.69           C  
ATOM   2074  CA  GLN F 177      38.221 -40.789  22.047  1.00125.48           C  
ATOM   2075  CA  THR F 178      38.785 -38.887  25.252  1.00 41.77           C  
ATOM   2076  CA  ASP F 179      36.715 -37.122  27.900  1.00 61.45           C  
ATOM   2077  CA  ALA F 180      39.462 -34.586  28.476  1.00 38.06           C  
ATOM   2078  CA  SER F 181      38.186 -31.169  27.651  1.00 41.90           C  
ATOM   2079  CA  ILE F 182      39.162 -30.278  24.128  1.00 88.89           C  
ATOM   2080  CA  ASN F 183      38.005 -27.056  22.597  1.00 42.15           C  
ATOM   2081  CA  ARG F 184      38.846 -25.106  19.526  1.00117.36           C  
ATOM   2082  CA  GLY F 185      42.524 -24.300  19.508  1.00 21.66           C  
ATOM   2083  CA  ASN F 186      43.283 -27.755  20.863  1.00 50.80           C  
ATOM   2084  CA  ALA F 187      43.918 -29.114  17.396  1.00 39.36           C  
ATOM   2085  CA  GLY F 188      47.436 -30.330  16.839  1.00 22.67           C  
ATOM   2086  CA  GLY F 189      47.857 -30.493  20.584  1.00 22.36           C  
ATOM   2087  CA  ALA F 190      49.030 -33.509  22.464  1.00 44.28           C  
ATOM   2088  CA  LEU F 191      47.205 -36.175  24.392  1.00 94.96           C  
ATOM   2089  CA  LEU F 192      49.526 -37.614  26.956  1.00 51.25           C  
ATOM   2090  CA  ASN F 193      49.556 -40.579  29.266  1.00 59.34           C  
ATOM   2091  CA  LEU F 194      50.554 -40.347  32.895  1.00 98.50           C  
ATOM   2092  CA  ASN F 195      54.096 -40.977  31.763  1.00 52.32           C  
ATOM   2093  CA  GLY F 196      53.885 -37.805  29.762  1.00 26.59           C  
ATOM   2094  CA  GLU F 197      54.344 -39.795  26.584  1.00107.79           C  
ATOM   2095  CA  LEU F 198      52.415 -38.880  23.459  1.00123.77           C  
ATOM   2096  CA  ILE F 199      49.320 -41.049  23.008  1.00 64.58           C  
ATOM   2097  CA  GLY F 200      47.880 -39.055  20.124  1.00 28.15           C  
ATOM   2098  CA  ILE F 201      47.258 -35.678  18.512  1.00 98.32           C  
ATOM   2099  CA  ASN F 202      43.943 -34.022  19.348  1.00 65.68           C  
ATOM   2100  CA  THR F 203      42.184 -33.657  16.010  1.00 84.88           C  
ATOM   2101  CA  ALA F 204      38.561 -32.802  16.674  1.00 50.50           C  
ATOM   2102  CA  ILE F 205      35.508 -32.900  18.873  1.00 42.91           C  
ATOM   2103  CA  LEU F 206      31.831 -33.576  18.598  1.00 55.73           C  
ATOM   2104  CA  ALA F 207      29.834 -30.839  20.205  1.00 42.00           C  
ATOM   2105  CA  PRO F 208      26.497 -29.452  19.355  1.00127.90           C  
ATOM   2106  CA  GLY F 209      27.360 -26.235  21.167  1.00 34.31           C  
ATOM   2107  CA  GLY F 210      30.734 -25.877  19.582  1.00 23.40           C  
ATOM   2108  CA  GLY F 211      32.086 -26.315  23.074  1.00 25.72           C  
ATOM   2109  CA  SER F 212      33.566 -29.420  24.620  1.00 57.28           C  
ATOM   2110  CA  VAL F 213      30.851 -31.956  25.370  1.00140.24           C  
ATOM   2111  CA  GLY F 214      33.413 -34.371  26.672  1.00 40.88           C  
ATOM   2112  CA  ILE F 215      33.710 -36.231  23.413  1.00 86.37           C  
ATOM   2113  CA  GLY F 216      37.036 -35.525  21.789  1.00 19.10           C  
ATOM   2114  CA  PHE F 217      39.000 -37.425  19.204  1.00 42.63           C  
ATOM   2115  CA  ALA F 218      42.714 -37.712  18.634  1.00 32.77           C  
ATOM   2116  CA  ILE F 219      44.854 -39.403  16.049  1.00155.72           C  
ATOM   2117  CA  PRO F 220      46.806 -42.109  17.651  1.00 92.19           C  
ATOM   2118  CA  SER F 221      50.466 -41.655  18.395  1.00 41.31           C  
ATOM   2119  CA  ASN F 222      51.439 -44.562  16.277  1.00 59.94           C  
ATOM   2120  CA  MET F 223      49.472 -42.721  13.769  1.00141.82           C  
ATOM   2121  CA  ALA F 224      51.281 -39.441  13.877  1.00 53.68           C  
ATOM   2122  CA  ARG F 225      54.631 -41.055  14.460  1.00 81.81           C  
ATOM   2123  CA  THR F 226      55.116 -43.018  11.333  1.00 59.98           C  
ATOM   2124  CA  LEU F 227      53.097 -40.560   9.250  1.00137.79           C  
ATOM   2125  CA  ALA F 228      55.357 -37.854  10.518  1.00 49.36           C  
ATOM   2126  CA  GLN F 229      58.384 -39.962   9.927  1.00 82.19           C  
ATOM   2127  CA  GLN F 230      58.232 -40.290   6.236  1.00141.98           C  
ATOM   2128  CA  LEU F 231      57.296 -36.662   6.080  1.00 62.41           C  
ATOM   2129  CA  ILE F 232      60.890 -36.213   7.056  1.00 71.71           C  
ATOM   2130  CA  ASP F 233      61.965 -39.666   5.689  1.00175.21           C  
ATOM   2131  CA  PHE F 234      61.392 -42.166   3.865  1.00212.68           C  
ATOM   2132  CA  GLY F 235      60.937 -38.788   2.512  1.00 59.54           C  
ATOM   2133  CA  GLU F 236      58.010 -38.746   0.248  1.00 58.68           C  
ATOM   2134  CA  ILE F 237      56.719 -35.565   1.776  1.00 49.05           C  
ATOM   2135  CA  LYS F 238      53.458 -35.707  -0.049  1.00290.71           C  
ATOM   2136  CA  ARG F 239      51.008 -36.693  -0.400  1.00260.33           C  
ATOM   2137  CA  GLY F 240      51.752 -40.269   0.451  1.00 49.34           C  
ATOM   2138  CA  LEU F 241      48.232 -40.751   1.641  1.00141.22           C  
ATOM   2139  CA  LEU F 242      45.308 -41.928  -0.324  1.00136.03           C  
ATOM   2140  CA  GLY F 243      43.259 -38.829  -0.649  1.00 52.92           C  
ATOM   2141  CA  ILE F 244      39.844 -40.311  -0.030  1.00 80.10           C  
ATOM   2142  CA  LYS F 245      36.748 -39.549   1.949  1.00 86.63           C  
ATOM   2143  CA  GLY F 246      34.751 -42.222   3.608  1.00 37.49           C  
ATOM   2144  CA  THR F 247      32.668 -43.164   6.541  1.00 77.85           C  
ATOM   2145  CA  GLU F 248      31.375 -46.159   8.403  1.00 91.53           C  
ATOM   2146  CA  MET F 249      28.826 -48.567   7.236  1.00 68.38           C  
ATOM   2147  CA  SER F 250      25.247 -47.483   7.612  1.00 38.49           C  
ATOM   2148  CA  ALA F 251      23.475 -47.943  10.915  1.00 50.50           C  
ATOM   2149  CA  ASP F 252      20.725 -50.301   9.884  1.00 79.19           C  
ATOM   2150  CA  ILE F 253      22.987 -52.688   8.119  1.00113.55           C  
ATOM   2151  CA  ALA F 254      25.530 -52.457  10.875  1.00 43.02           C  
ATOM   2152  CA  LYS F 255      22.888 -53.308  13.457  1.00141.58           C  
ATOM   2153  CA  ALA F 256      21.550 -56.506  11.906  1.00 60.42           C  
ATOM   2154  CA  PHE F 257      24.620 -58.568  11.015  1.00103.30           C  
ATOM   2155  CA  ASN F 258      26.442 -59.372  14.254  1.00161.45           C  
ATOM   2156  CA  LEU F 259      29.438 -60.017  12.134  1.00167.24           C  
ATOM   2157  CA  ASP F 260      32.697 -59.855  13.998  1.00109.22           C  
ATOM   2158  CA  VAL F 261      34.080 -56.855  12.124  1.00118.13           C  
ATOM   2159  CA  GLN F 262      32.345 -53.700  13.234  1.00 63.02           C  
ATOM   2160  CA  ARG F 263      32.388 -51.973   9.907  1.00202.25           C  
ATOM   2161  CA  GLY F 264      34.330 -51.505   6.728  1.00 35.77           C  
ATOM   2162  CA  ALA F 265      35.757 -48.344   5.349  1.00 52.68           C  
ATOM   2163  CA  PHE F 266      33.410 -47.187   2.703  1.00124.26           C  
ATOM   2164  CA  VAL F 267      34.486 -44.537   0.319  1.00 76.20           C  
ATOM   2165  CA  SER F 268      31.897 -42.077  -0.887  1.00106.86           C  
ATOM   2166  CA  GLU F 269      34.317 -39.992  -2.900  1.00113.01           C  
ATOM   2167  CA  VAL F 270      37.348 -39.918  -5.168  1.00 83.99           C  
ATOM   2168  CA  LEU F 271      39.817 -37.117  -4.837  1.00 88.67           C  
ATOM   2169  CA  PRO F 272      41.249 -35.634  -7.935  1.00 74.21           C  
ATOM   2170  CA  GLY F 273      44.944 -36.010  -8.615  1.00 30.79           C  
ATOM   2171  CA  SER F 274      44.706 -37.798  -5.348  1.00106.32           C  
ATOM   2172  CA  GLY F 275      46.371 -41.028  -4.476  1.00 49.33           C  
ATOM   2173  CA  SER F 276      43.196 -42.956  -4.625  1.00106.02           C  
ATOM   2174  CA  ALA F 277      42.432 -41.920  -8.179  1.00 52.46           C  
ATOM   2175  CA  LYS F 278      45.595 -43.086  -9.957  1.00125.95           C  
ATOM   2176  CA  ALA F 279      45.454 -46.147  -7.836  1.00 46.59           C  
ATOM   2177  CA  GLY F 280      42.098 -46.210  -9.414  1.00 43.90           C  
ATOM   2178  CA  VAL F 281      39.981 -46.646  -6.357  1.00 71.29           C  
ATOM   2179  CA  LYS F 282      36.449 -45.713  -7.205  1.00147.13           C  
ATOM   2180  CA  ALA F 283      34.014 -43.983  -5.016  1.00121.47           C  
ATOM   2181  CA  GLY F 284      31.444 -46.462  -3.477  1.00114.57           C  
ATOM   2182  CA  ASP F 285      33.623 -49.418  -2.725  1.00231.84           C  
ATOM   2183  CA  ILE F 286      34.446 -50.727   0.601  1.00148.79           C  
ATOM   2184  CA  ILE F 287      37.963 -51.056   1.845  1.00148.23           C  
ATOM   2185  CA  THR F 288      38.012 -54.415   3.533  1.00 75.63           C  
ATOM   2186  CA  SER F 289      41.647 -54.587   4.297  1.00108.45           C  
ATOM   2187  CA  LEU F 290      44.996 -52.897   4.321  1.00 88.01           C  
ATOM   2188  CA  ASN F 291      47.881 -55.268   3.992  1.00275.37           C  
ATOM   2189  CA  GLY F 292      48.583 -58.143   4.747  1.00140.80           C  
ATOM   2190  CA  LYS F 293      46.136 -58.491   7.600  1.00190.34           C  
ATOM   2191  CA  PRO F 294      42.411 -58.152   7.790  1.00216.51           C  
ATOM   2192  CA  LEU F 295      41.544 -54.468   8.521  1.00225.96           C  
ATOM   2193  CA  ASN F 296      38.518 -53.699  10.629  1.00 89.33           C  
ATOM   2194  CA  SER F 297      36.177 -50.767  10.468  1.00115.24           C  
ATOM   2195  CA  PHE F 298      36.855 -47.463   8.910  1.00 99.95           C  
ATOM   2196  CA  ALA F 299      38.134 -46.786  12.377  1.00 50.66           C  
ATOM   2197  CA  GLU F 300      40.878 -49.328  12.154  1.00157.06           C  
ATOM   2198  CA  LEU F 301      41.612 -47.936   8.754  1.00 80.73           C  
ATOM   2199  CA  ARG F 302      43.006 -44.694   9.855  1.00169.90           C  
ATOM   2200  CA  SER F 303      44.446 -46.388  12.834  1.00 53.66           C  
ATOM   2201  CA  ARG F 304      46.919 -48.248  10.819  1.00 85.95           C  
ATOM   2202  CA  ILE F 305      47.294 -45.779   7.981  1.00 87.05           C  
ATOM   2203  CA  ALA F 306      47.372 -42.778  10.156  1.00 72.72           C  
ATOM   2204  CA  THR F 307      49.920 -44.900  11.916  1.00 60.22           C  
ATOM   2205  CA  THR F 308      51.901 -45.706   8.819  1.00121.52           C  
ATOM   2206  CA  GLU F 309      54.267 -43.542   6.868  1.00 90.70           C  
ATOM   2207  CA  PRO F 310      52.544 -41.260   4.563  1.00192.97           C  
ATOM   2208  CA  GLY F 311      54.201 -42.285   2.320  1.00131.13           C  
ATOM   2209  CA  THR F 312      54.623 -46.026   2.511  1.00175.16           C  
ATOM   2210  CA  LYS F 313      53.608 -47.892  -0.601  1.00157.41           C  
ATOM   2211  CA  VAL F 314      50.904 -50.216   0.829  1.00208.63           C  
ATOM   2212  CA  LYS F 315      48.282 -52.243  -0.922  1.00 61.80           C  
ATOM   2213  CA  LEU F 316      44.638 -51.980  -0.121  1.00111.98           C  
ATOM   2214  CA  GLY F 317      41.910 -54.516  -0.551  1.00 53.62           C  
ATOM   2215  CA  LEU F 318      38.856 -52.682  -1.623  1.00159.99           C  
ATOM   2216  CA  LEU F 319      35.303 -54.068  -2.333  1.00194.98           C  
ATOM   2217  CA  ARG F 320      33.025 -53.300  -5.304  1.00409.27           C  
ATOM   2218  CA  ASN F 321      31.354 -55.676  -7.232  1.00346.76           C  
ATOM   2219  CA  GLY F 322      31.329 -58.470  -5.126  1.00 98.09           C  
ATOM   2220  CA  LYS F 323      34.557 -59.209  -6.984  1.00269.92           C  
ATOM   2221  CA  PRO F 324      37.718 -58.461  -5.045  1.00183.82           C  
ATOM   2222  CA  LEU F 325      40.154 -55.640  -5.715  1.00184.57           C  
ATOM   2223  CA  GLU F 326      43.793 -55.516  -4.701  1.00113.18           C  
ATOM   2224  CA  VAL F 327      45.606 -52.366  -5.617  1.00122.95           C  
ATOM   2225  CA  GLU F 328      48.839 -50.593  -4.926  1.00 94.26           C  
ATOM   2226  CA  VAL F 329      48.062 -47.142  -3.760  1.00 61.82           C  
ATOM   2227  CA  SER F 340      48.121 -23.262 -29.124  1.00 39.31           C  
ATOM   2228  CA  ALA F 341      47.722 -19.537 -29.118  1.00 51.88           C  
ATOM   2229  CA  GLU F 342      44.561 -19.798 -27.100  1.00 67.74           C  
ATOM   2230  CA  MET F 343      46.136 -20.531 -23.763  1.00173.92           C  
ATOM   2231  CA  ILE F 344      48.542 -17.637 -23.782  1.00104.79           C  
ATOM   2232  CA  THR F 345      46.108 -15.532 -25.714  1.00133.19           C  
ATOM   2233  CA  PRO F 346      42.523 -15.499 -24.653  1.00151.14           C  
ATOM   2234  CA  ALA F 347      39.896 -17.075 -26.865  1.00 69.60           C  
ATOM   2235  CA  LEU F 348      42.084 -16.679 -29.929  1.00121.29           C  
ATOM   2236  CA  GLU F 349      42.219 -20.107 -31.429  1.00 71.10           C  
ATOM   2237  CA  GLY F 350      45.149 -20.415 -33.698  1.00 25.58           C  
ATOM   2238  CA  ALA F 351      48.552 -21.859 -34.274  1.00 30.42           C  
ATOM   2239  CA  THR F 352      50.072 -23.647 -31.353  1.00 26.68           C  
ATOM   2240  CA  LEU F 353      53.069 -22.117 -29.700  1.00 50.40           C  
ATOM   2241  CA  SER F 354      56.179 -23.582 -28.178  1.00 75.96           C  
ATOM   2242  CA  ASP F 355      58.873 -22.165 -25.935  1.00131.41           C  
ATOM   2243  CA  GLY F 356      62.545 -21.886 -26.514  1.00 36.28           C  
ATOM   2244  CA  GLN F 357      64.160 -20.784 -29.713  1.00148.40           C  
ATOM   2245  CA  LEU F 358      63.920 -24.483 -29.835  1.00153.17           C  
ATOM   2246  CA  LYS F 359      66.835 -24.626 -32.177  1.00119.53           C  
ATOM   2247  CA  ASP F 360      69.027 -21.936 -30.736  1.00 51.92           C  
ATOM   2248  CA  GLY F 361      69.068 -19.643 -27.784  1.00 25.24           C  
ATOM   2249  CA  GLY F 362      65.548 -18.496 -27.199  1.00 37.91           C  
ATOM   2250  CA  LYS F 363      64.731 -15.776 -29.658  1.00105.84           C  
ATOM   2251  CA  GLY F 364      61.293 -16.225 -28.275  1.00 30.12           C  
ATOM   2252  CA  ILE F 365      58.115 -18.241 -28.554  1.00 69.06           C  
ATOM   2253  CA  LYS F 366      57.674 -20.310 -31.666  1.00106.48           C  
ATOM   2254  CA  ILE F 367      54.402 -20.682 -33.495  1.00 55.56           C  
ATOM   2255  CA  ASP F 368      54.201 -24.340 -34.365  1.00 58.79           C  
ATOM   2256  CA  GLU F 369      51.541 -24.400 -37.015  1.00 91.18           C  
ATOM   2257  CA  VAL F 370      48.745 -22.227 -38.255  1.00125.16           C  
ATOM   2258  CA  VAL F 371      45.186 -23.492 -37.873  1.00180.41           C  
ATOM   2259  CA  LYS F 372      44.553 -20.717 -40.446  1.00161.41           C  
ATOM   2260  CA  GLY F 373      40.789 -20.917 -40.391  1.00 37.25           C  
ATOM   2261  CA  SER F 374      41.226 -19.859 -36.745  1.00 40.27           C  
ATOM   2262  CA  PRO F 375      41.449 -16.311 -35.605  1.00 69.93           C  
ATOM   2263  CA  ALA F 376      45.087 -16.461 -34.625  1.00 47.40           C  
ATOM   2264  CA  ALA F 377      45.419 -16.816 -38.356  1.00 48.02           C  
ATOM   2265  CA  GLN F 378      42.901 -14.032 -38.850  1.00 53.00           C  
ATOM   2266  CA  ALA F 379      45.185 -11.405 -37.381  1.00 90.05           C  
ATOM   2267  CA  GLY F 380      48.283 -12.499 -39.235  1.00 92.80           C  
ATOM   2268  CA  LEU F 381      50.095 -15.012 -37.225  1.00107.05           C  
ATOM   2269  CA  GLN F 382      51.764 -17.327 -39.703  1.00 63.41           C  
ATOM   2270  CA  LYS F 383      53.624 -20.422 -38.750  1.00178.34           C  
ATOM   2271  CA  ASP F 384      57.353 -20.402 -38.222  1.00 65.85           C  
ATOM   2272  CA  ASP F 385      57.173 -16.952 -36.734  1.00 67.25           C  
ATOM   2273  CA  VAL F 386      59.234 -16.275 -33.657  1.00 80.48           C  
ATOM   2274  CA  ILE F 387      57.858 -13.904 -31.135  1.00 92.91           C  
ATOM   2275  CA  ILE F 388      60.962 -12.169 -29.902  1.00102.31           C  
ATOM   2276  CA  GLY F 389      59.429  -9.842 -27.363  1.00 97.45           C  
ATOM   2277  CA  VAL F 390      56.140  -8.291 -26.033  1.00222.67           C  
ATOM   2278  CA  ASN F 391      55.182  -4.580 -26.219  1.00140.72           C  
ATOM   2279  CA  ARG F 392      58.684  -3.182 -26.023  1.00190.53           C  
ATOM   2280  CA  ASP F 393      59.657  -6.180 -23.920  1.00 66.76           C  
ATOM   2281  CA  ARG F 394      61.738  -9.127 -24.938  1.00 96.16           C  
ATOM   2282  CA  VAL F 395      60.120 -12.515 -24.720  1.00 61.10           C  
ATOM   2283  CA  ASN F 396      62.522 -15.329 -24.038  1.00 51.53           C  
ATOM   2284  CA  SER F 397      59.798 -17.895 -23.536  1.00 91.99           C  
ATOM   2285  CA  ILE F 398      56.068 -18.281 -22.958  1.00 62.88           C  
ATOM   2286  CA  ALA F 399      56.333 -17.437 -19.307  1.00 30.30           C  
ATOM   2287  CA  GLU F 400      57.774 -14.020 -20.067  1.00 36.03           C  
ATOM   2288  CA  MET F 401      55.266 -13.547 -22.848  1.00 50.45           C  
ATOM   2289  CA  ARG F 402      52.571 -14.239 -20.344  1.00 98.97           C  
ATOM   2290  CA  LYS F 403      54.000 -11.610 -18.051  1.00 73.71           C  
ATOM   2291  CA  VAL F 404      53.501  -8.802 -20.517  1.00101.80           C  
ATOM   2292  CA  LEU F 405      50.016 -10.155 -21.106  1.00104.70           C  
ATOM   2293  CA  ALA F 406      49.544  -9.973 -17.380  1.00 26.39           C  
ATOM   2294  CA  ALA F 407      49.630  -6.219 -17.747  1.00 29.65           C  
ATOM   2295  CA  LYS F 408      46.855  -6.809 -20.242  1.00 85.33           C  
ATOM   2296  CA  PRO F 409      47.528  -3.724 -22.252  1.00 74.68           C  
ATOM   2297  CA  ALA F 410      44.672  -2.923 -24.583  1.00 27.51           C  
ATOM   2298  CA  ILE F 411      47.153  -3.131 -27.388  1.00122.42           C  
ATOM   2299  CA  ILE F 412      49.650  -5.905 -27.421  1.00165.64           C  
ATOM   2300  CA  ALA F 413      52.240  -5.832 -30.073  1.00102.83           C  
ATOM   2301  CA  LEU F 414      53.634  -9.297 -30.748  1.00232.18           C  
ATOM   2302  CA  GLN F 415      57.273  -9.231 -32.300  1.00200.91           C  
ATOM   2303  CA  ILE F 416      57.791 -11.811 -34.686  1.00128.67           C  
ATOM   2304  CA  VAL F 417      60.651 -12.492 -36.899  1.00123.41           C  
ATOM   2305  CA  ARG F 418      59.727 -13.983 -40.210  1.00151.08           C  
ATOM   2306  CA  GLY F 419      62.532 -15.330 -42.301  1.00 26.28           C  
ATOM   2307  CA  ASN F 420      65.411 -12.994 -41.843  1.00102.31           C  
ATOM   2308  CA  GLU F 421      62.990 -10.141 -41.534  1.00 98.63           C  
ATOM   2309  CA  SER F 422      61.139  -9.069 -38.550  1.00 78.61           C  
ATOM   2310  CA  ILE F 423      57.340  -8.878 -38.639  1.00155.49           C  
ATOM   2311  CA  TYR F 424      55.459  -6.661 -36.354  1.00293.72           C  
ATOM   2312  CA  LEU F 425      51.876  -7.451 -35.869  1.00234.22           C  
ATOM   2313  CA  LEU F 426      49.287  -6.909 -33.355  1.00269.48           C  
ATOM   2314  CA  MET F 427      46.429  -8.359 -31.040  1.00214.94           C  
ATOM   2315  CA  ARG F 428      42.995  -6.466 -30.689  1.00252.00           C  
TER    2316      ARG F 428                                                      
ATOM   2317  CA  PRO G  11      44.048  36.420 -46.377  1.00108.65           C  
ATOM   2318  CA  LEU G  12      41.906  37.167 -49.335  1.00 65.61           C  
ATOM   2319  CA  PRO G  13      40.262  40.441 -48.778  1.00101.38           C  
ATOM   2320  CA  SER G  14      36.876  39.554 -50.055  1.00 83.64           C  
ATOM   2321  CA  LEU G  15      35.605  36.102 -49.321  1.00 49.26           C  
ATOM   2322  CA  ALA G  16      32.575  36.580 -51.501  1.00 35.35           C  
ATOM   2323  CA  PRO G  17      34.405  36.870 -54.739  1.00 72.70           C  
ATOM   2324  CA  MET G  18      36.186  33.606 -54.103  1.00 94.30           C  
ATOM   2325  CA  LEU G  19      33.069  31.960 -52.786  1.00 55.53           C  
ATOM   2326  CA  GLU G  20      30.855  32.768 -55.698  1.00 80.37           C  
ATOM   2327  CA  LYS G  21      32.866  30.648 -58.054  1.00100.52           C  
ATOM   2328  CA  VAL G  22      33.554  27.778 -55.654  1.00113.13           C  
ATOM   2329  CA  LEU G  23      30.256  27.337 -53.867  1.00 79.77           C  
ATOM   2330  CA  PRO G  24      28.382  25.465 -56.517  1.00 65.01           C  
ATOM   2331  CA  ALA G  25      30.991  22.753 -56.234  1.00 44.43           C  
ATOM   2332  CA  VAL G  26      29.942  21.948 -52.685  1.00 36.03           C  
ATOM   2333  CA  VAL G  27      26.795  19.933 -52.461  1.00116.29           C  
ATOM   2334  CA  SER G  28      24.420  18.613 -49.844  1.00 37.07           C  
ATOM   2335  CA  VAL G  29      23.916  14.910 -49.620  1.00 94.10           C  
ATOM   2336  CA  ARG G  30      20.598  13.416 -48.644  1.00130.62           C  
ATOM   2337  CA  VAL G  31      20.342   9.905 -47.338  1.00 45.86           C  
ATOM   2338  CA  GLU G  32      17.509   7.518 -46.673  1.00 69.83           C  
ATOM   2339  CA  GLY G  33      17.798   4.025 -45.345  1.00 29.05           C  
ATOM   2340  CA  THR G  34      17.068   1.302 -42.849  1.00 34.56           C  
ATOM   2341  CA  ALA G  58      14.904  -0.811 -39.737  1.00 16.95           C  
ATOM   2342  CA  GLN G  59      12.544   2.092 -39.629  1.00 98.33           C  
ATOM   2343  CA  PRO G  60      13.121   4.611 -42.337  1.00 95.17           C  
ATOM   2344  CA  PHE G  61      15.420   7.445 -41.387  1.00 69.21           C  
ATOM   2345  CA  GLU G  62      16.737  10.472 -43.164  1.00 32.64           C  
ATOM   2346  CA  GLY G  63      20.184  11.905 -42.774  1.00 22.38           C  
ATOM   2347  CA  LEU G  64      21.819  14.995 -44.147  1.00 41.25           C  
ATOM   2348  CA  GLY G  65      25.443  15.606 -44.979  1.00 20.24           C  
ATOM   2349  CA  SER G  66      27.573  17.366 -47.534  1.00 27.16           C  
ATOM   2350  CA  GLY G  67      29.884  16.411 -50.348  1.00 20.06           C  
ATOM   2351  CA  VAL G  68      32.270  17.969 -52.797  1.00 99.26           C  
ATOM   2352  CA  ILE G  69      32.218  17.635 -56.553  1.00108.64           C  
ATOM   2353  CA  ILE G  70      35.624  16.341 -57.524  1.00123.66           C  
ATOM   2354  CA  ASN G  71      34.912  15.696 -61.169  1.00 46.84           C  
ATOM   2355  CA  ALA G  72      32.210  17.620 -62.928  1.00 29.77           C  
ATOM   2356  CA  SER G  73      32.182  15.491 -66.023  1.00 32.14           C  
ATOM   2357  CA  LYS G  74      32.000  12.204 -64.199  1.00158.21           C  
ATOM   2358  CA  GLY G  75      29.920  13.607 -61.424  1.00 27.78           C  
ATOM   2359  CA  TYR G  76      32.113  12.151 -58.723  1.00 70.27           C  
ATOM   2360  CA  VAL G  77      31.381  13.529 -55.290  1.00134.51           C  
ATOM   2361  CA  LEU G  78      33.534  12.971 -52.268  1.00 63.90           C  
ATOM   2362  CA  THR G  79      31.882  12.486 -48.931  1.00123.14           C  
ATOM   2363  CA  ASN G  80      32.401  10.866 -45.579  1.00 55.27           C  
ATOM   2364  CA  ASN G  81      31.697   7.188 -45.362  1.00 48.72           C  
ATOM   2365  CA  HIS G  82      29.688   7.672 -42.217  1.00 48.17           C  
ATOM   2366  CA  VAL G  83      27.274   9.907 -44.021  1.00 64.78           C  
ATOM   2367  CA  ILE G  84      26.753   7.297 -46.737  1.00113.59           C  
ATOM   2368  CA  ASN G  85      27.067   4.039 -44.848  1.00122.79           C  
ATOM   2369  CA  GLN G  86      23.440   3.411 -43.853  1.00 70.00           C  
ATOM   2370  CA  ALA G  87      21.999   4.908 -47.040  1.00 69.24           C  
ATOM   2371  CA  GLN G  88      19.633   2.820 -49.098  1.00 56.34           C  
ATOM   2372  CA  LYS G  89      19.211   5.734 -51.467  1.00 30.20           C  
ATOM   2373  CA  ILE G  90      21.324   8.804 -51.978  1.00 86.12           C  
ATOM   2374  CA  SER G  91      20.418  12.124 -53.473  1.00 73.68           C  
ATOM   2375  CA  ILE G  92      22.546  15.161 -54.091  1.00 60.79           C  
ATOM   2376  CA  GLN G  93      21.305  18.700 -54.203  1.00 47.34           C  
ATOM   2377  CA  LEU G  94      23.084  21.658 -55.692  1.00 46.05           C  
ATOM   2378  CA  ASN G  95      22.966  25.129 -54.256  1.00 99.77           C  
ATOM   2379  CA  ASP G  96      20.942  26.113 -57.298  1.00 45.91           C  
ATOM   2380  CA  GLY G  97      18.231  23.751 -56.156  1.00 28.36           C  
ATOM   2381  CA  ARG G  98      18.768  21.092 -58.771  1.00 60.60           C  
ATOM   2382  CA  GLU G  99      18.760  17.585 -57.394  1.00 39.80           C  
ATOM   2383  CA  PHE G 100      20.301  14.403 -58.685  1.00 50.47           C  
ATOM   2384  CA  ASP G 101      20.456  10.781 -57.666  1.00102.25           C  
ATOM   2385  CA  ALA G 102      23.739   9.224 -56.704  1.00 30.08           C  
ATOM   2386  CA  LYS G 103      25.233   5.781 -56.356  1.00 75.73           C  
ATOM   2387  CA  LEU G 104      28.030   4.736 -54.076  1.00 44.62           C  
ATOM   2388  CA  ILE G 105      31.128   4.054 -56.099  1.00 40.04           C  
ATOM   2389  CA  GLY G 106      33.148   2.867 -53.142  1.00 23.40           C  
ATOM   2390  CA  SER G 107      34.273   3.823 -49.686  1.00103.00           C  
ATOM   2391  CA  ASP G 108      36.397   2.731 -46.845  1.00109.47           C  
ATOM   2392  CA  ASP G 109      35.815   2.689 -43.116  1.00 63.74           C  
ATOM   2393  CA  GLN G 110      39.241   3.303 -41.736  1.00 91.78           C  
ATOM   2394  CA  SER G 111      39.885   6.682 -43.379  1.00 67.37           C  
ATOM   2395  CA  ASP G 112      36.153   7.400 -43.566  1.00 73.42           C  
ATOM   2396  CA  ILE G 113      36.184   8.474 -47.202  1.00 50.20           C  
ATOM   2397  CA  ALA G 114      33.483   7.557 -49.690  1.00 38.60           C  
ATOM   2398  CA  LEU G 115      33.047   8.289 -53.363  1.00 99.11           C  
ATOM   2399  CA  LEU G 116      29.651   8.872 -54.936  1.00 55.43           C  
ATOM   2400  CA  GLN G 117      28.677   9.308 -58.539  1.00 38.25           C  
ATOM   2401  CA  ILE G 118      25.869  11.538 -59.694  1.00 40.67           C  
ATOM   2402  CA  GLN G 119      23.520  10.008 -62.165  1.00 52.55           C  
ATOM   2403  CA  ASN G 120      23.350  11.901 -65.429  1.00 57.10           C  
ATOM   2404  CA  PRO G 121      25.282  14.791 -64.043  1.00 63.53           C  
ATOM   2405  CA  SER G 122      24.923  17.958 -66.056  1.00 34.82           C  
ATOM   2406  CA  LYS G 123      26.461  21.418 -65.917  1.00 42.79           C  
ATOM   2407  CA  LEU G 124      28.335  20.789 -62.713  1.00 86.33           C  
ATOM   2408  CA  THR G 125      31.201  22.723 -61.219  1.00115.62           C  
ATOM   2409  CA  GLN G 126      34.316  21.109 -59.868  1.00 65.41           C  
ATOM   2410  CA  ILE G 127      36.500  22.009 -56.935  1.00117.37           C  
ATOM   2411  CA  ALA G 128      40.194  22.383 -57.504  1.00 27.86           C  
ATOM   2412  CA  ILE G 129      42.253  20.455 -55.024  1.00 80.68           C  
ATOM   2413  CA  ALA G 130      45.165  21.992 -53.172  1.00 37.28           C  
ATOM   2414  CA  ASP G 131      48.213  20.270 -51.762  1.00 33.68           C  
ATOM   2415  CA  SER G 132      47.373  19.582 -48.141  1.00 39.39           C  
ATOM   2416  CA  ASP G 133      50.999  18.990 -47.296  1.00 40.42           C  
ATOM   2417  CA  LYS G 134      51.700  22.658 -47.954  1.00123.62           C  
ATOM   2418  CA  LEU G 135      49.218  23.718 -45.309  1.00186.24           C  
ATOM   2419  CA  ARG G 136      50.701  25.516 -42.321  1.00102.73           C  
ATOM   2420  CA  VAL G 137      49.065  26.513 -39.101  1.00 82.91           C  
ATOM   2421  CA  GLY G 138      47.615  29.967 -39.345  1.00 24.29           C  
ATOM   2422  CA  ASP G 139      46.407  29.499 -42.877  1.00 29.89           C  
ATOM   2423  CA  PHE G 140      42.896  30.738 -43.430  1.00 58.73           C  
ATOM   2424  CA  ALA G 141      40.205  28.211 -44.120  1.00 37.70           C  
ATOM   2425  CA  VAL G 142      36.562  28.293 -45.000  1.00 95.90           C  
ATOM   2426  CA  ALA G 143      34.186  25.457 -44.356  1.00 30.30           C  
ATOM   2427  CA  VAL G 144      31.169  24.823 -46.495  1.00 28.37           C  
ATOM   2428  CA  GLY G 145      28.460  22.311 -45.791  1.00 19.91           C  
ATOM   2429  CA  ASN G 146      24.960  22.064 -44.487  1.00 55.77           C  
ATOM   2430  CA  PRO G 147      24.844  22.296 -40.810  1.00105.24           C  
ATOM   2431  CA  PHE G 148      21.518  21.329 -39.317  1.00 61.97           C  
ATOM   2432  CA  GLY G 149      20.321  20.916 -42.868  1.00 22.47           C  
ATOM   2433  CA  LEU G 150      19.817  24.642 -43.123  1.00 80.59           C  
ATOM   2434  CA  GLY G 151      21.272  24.826 -46.597  1.00 28.46           C  
ATOM   2435  CA  GLN G 152      24.682  25.646 -47.900  1.00 69.11           C  
ATOM   2436  CA  THR G 153      26.492  27.514 -45.189  1.00 32.27           C  
ATOM   2437  CA  ALA G 154      29.970  28.947 -45.154  1.00 29.28           C  
ATOM   2438  CA  THR G 155      32.026  29.507 -42.040  1.00 97.43           C  
ATOM   2439  CA  SER G 156      35.483  30.946 -41.686  1.00 33.84           C  
ATOM   2440  CA  GLY G 157      38.462  30.169 -39.520  1.00 21.86           C  
ATOM   2441  CA  ILE G 158      42.127  29.269 -39.580  1.00 95.32           C  
ATOM   2442  CA  VAL G 159      43.975  26.003 -39.669  1.00114.00           C  
ATOM   2443  CA  SER G 160      44.540  25.323 -36.016  1.00 96.83           C  
ATOM   2444  CA  ALA G 161      46.690  22.247 -36.364  1.00 43.12           C  
ATOM   2445  CA  LEU G 162      47.643  19.437 -38.663  1.00 93.21           C  
ATOM   2446  CA  GLY G 163      48.745  15.875 -38.404  1.00 28.05           C  
ATOM   2447  CA  ARG G 164      46.576  15.178 -35.480  1.00 90.70           C  
ATOM   2448  CA  SER G 165      45.471  11.809 -34.277  1.00 83.09           C  
ATOM   2449  CA  GLY G 166      44.770   9.580 -31.409  1.00 36.71           C  
ATOM   2450  CA  LEU G 167      41.297  11.052 -31.529  1.00 48.27           C  
ATOM   2451  CA  ASN G 168      40.167   7.494 -32.107  1.00 75.06           C  
ATOM   2452  CA  LEU G 169      37.519   8.904 -34.361  1.00 49.79           C  
ATOM   2453  CA  GLU G 170      38.687   6.651 -37.162  1.00146.94           C  
ATOM   2454  CA  GLY G 171      41.146   3.863 -37.882  1.00 42.09           C  
ATOM   2455  CA  LEU G 172      43.438   6.057 -39.861  1.00156.65           C  
ATOM   2456  CA  GLU G 173      43.572   9.619 -38.845  1.00 79.43           C  
ATOM   2457  CA  ASN G 174      45.477  12.730 -39.780  1.00102.05           C  
ATOM   2458  CA  PHE G 175      43.051  15.437 -39.297  1.00 89.05           C  
ATOM   2459  CA  ILE G 176      43.596  19.015 -40.112  1.00 70.53           C  
ATOM   2460  CA  GLN G 177      42.140  20.889 -37.201  1.00 55.94           C  
ATOM   2461  CA  THR G 178      40.169  23.996 -37.850  1.00125.53           C  
ATOM   2462  CA  ASP G 179      38.450  26.728 -35.850  1.00 97.22           C  
ATOM   2463  CA  ALA G 180      35.839  27.202 -38.536  1.00 47.31           C  
ATOM   2464  CA  SER G 181      32.416  26.457 -37.200  1.00 82.51           C  
ATOM   2465  CA  ILE G 182      31.588  22.892 -38.008  1.00 56.31           C  
ATOM   2466  CA  ASN G 183      28.381  21.330 -36.829  1.00 46.35           C  
ATOM   2467  CA  ARG G 184      26.334  18.295 -37.593  1.00 56.09           C  
ATOM   2468  CA  GLY G 185      25.551  18.127 -41.267  1.00 25.52           C  
ATOM   2469  CA  ASN G 186      28.970  19.490 -42.122  1.00138.38           C  
ATOM   2470  CA  ALA G 187      30.369  16.019 -42.674  1.00 88.83           C  
ATOM   2471  CA  GLY G 188      31.560  15.378 -46.178  1.00 24.32           C  
ATOM   2472  CA  GLY G 189      31.671  19.117 -46.674  1.00 21.32           C  
ATOM   2473  CA  ALA G 190      34.625  21.022 -47.969  1.00 41.90           C  
ATOM   2474  CA  LEU G 191      37.292  22.955 -46.176  1.00 61.28           C  
ATOM   2475  CA  LEU G 192      38.684  25.534 -48.544  1.00102.98           C  
ATOM   2476  CA  ASN G 193      41.699  27.758 -48.888  1.00156.72           C  
ATOM   2477  CA  LEU G 194      41.408  31.444 -49.720  1.00 59.04           C  
ATOM   2478  CA  ASN G 195      41.966  30.288 -53.259  1.00 65.52           C  
ATOM   2479  CA  GLY G 196      38.834  28.222 -53.002  1.00 28.90           C  
ATOM   2480  CA  GLU G 197      40.894  25.107 -53.400  1.00 52.98           C  
ATOM   2481  CA  LEU G 198      39.989  22.058 -51.354  1.00 71.75           C  
ATOM   2482  CA  ILE G 199      42.245  21.589 -48.341  1.00 84.44           C  
ATOM   2483  CA  GLY G 200      40.267  18.739 -46.803  1.00 29.32           C  
ATOM   2484  CA  ILE G 201      36.908  17.159 -46.116  1.00 62.28           C  
ATOM   2485  CA  ASN G 202      35.326  17.988 -42.790  1.00 78.19           C  
ATOM   2486  CA  THR G 203      34.953  14.693 -40.963  1.00 81.87           C  
ATOM   2487  CA  ALA G 204      34.208  15.414 -37.325  1.00 52.08           C  
ATOM   2488  CA  ILE G 205      34.178  17.703 -34.324  1.00109.27           C  
ATOM   2489  CA  LEU G 206      34.900  17.372 -30.674  1.00118.43           C  
ATOM   2490  CA  ALA G 207      32.250  19.130 -28.740  1.00 61.81           C  
ATOM   2491  CA  PRO G 208      30.862  18.592 -25.354  1.00192.34           C  
ATOM   2492  CA  GLY G 209      27.405  19.878 -26.060  1.00224.20           C  
ATOM   2493  CA  GLY G 210      27.198  18.550 -29.563  1.00 45.28           C  
ATOM   2494  CA  GLY G 211      27.651  22.022 -30.946  1.00 25.72           C  
ATOM   2495  CA  SER G 212      30.702  23.547 -32.535  1.00 61.34           C  
ATOM   2496  CA  VAL G 213      33.325  24.195 -29.888  1.00156.87           C  
ATOM   2497  CA  GLY G 214      35.734  25.536 -32.419  1.00 47.45           C  
ATOM   2498  CA  ILE G 215      37.655  22.345 -32.760  1.00122.76           C  
ATOM   2499  CA  GLY G 216      36.859  20.551 -35.955  1.00 21.19           C  
ATOM   2500  CA  PHE G 217      38.775  17.988 -37.911  1.00 48.00           C  
ATOM   2501  CA  ALA G 218      39.008  17.316 -41.598  1.00 35.36           C  
ATOM   2502  CA  ILE G 219      40.722  14.748 -43.722  1.00175.94           C  
ATOM   2503  CA  PRO G 220      43.366  16.330 -45.746  1.00 90.81           C  
ATOM   2504  CA  SER G 221      42.775  16.891 -49.423  1.00 93.60           C  
ATOM   2505  CA  ASN G 222      45.799  14.903 -50.299  1.00 60.23           C  
ATOM   2506  CA  MET G 223      43.997  12.389 -48.297  1.00104.77           C  
ATOM   2507  CA  ALA G 224      40.710  12.430 -50.079  1.00 53.94           C  
ATOM   2508  CA  ARG G 225      42.196  12.956 -53.481  1.00159.09           C  
ATOM   2509  CA  THR G 226      44.243   9.873 -53.915  1.00 65.85           C  
ATOM   2510  CA  LEU G 227      41.856   7.805 -51.803  1.00109.14           C  
ATOM   2511  CA  ALA G 228      39.073   8.945 -54.049  1.00 43.71           C  
ATOM   2512  CA  GLN G 229      41.129   8.316 -57.108  1.00 77.81           C  
ATOM   2513  CA  GLN G 230      41.616   4.641 -56.569  1.00 91.55           C  
ATOM   2514  CA  LEU G 231      37.919   4.393 -55.864  1.00 67.53           C  
ATOM   2515  CA  ILE G 232      37.354   5.342 -59.436  1.00 60.77           C  
ATOM   2516  CA  ASP G 233      40.724   3.941 -60.535  1.00165.52           C  
ATOM   2517  CA  PHE G 234      42.551   1.855 -60.016  1.00153.65           C  
ATOM   2518  CA  GLY G 235      40.864   0.816 -56.853  1.00 53.92           C  
ATOM   2519  CA  GLU G 236      42.359  -2.519 -56.275  1.00144.23           C  
ATOM   2520  CA  ILE G 237      39.603  -3.803 -54.151  1.00105.84           C  
ATOM   2521  CA  LYS G 238      42.085  -4.803 -51.551  1.00151.08           C  
ATOM   2522  CA  ARG G 239      43.224  -3.674 -49.356  1.00253.10           C  
ATOM   2523  CA  GLY G 240      40.880  -0.759 -49.993  1.00 58.01           C  
ATOM   2524  CA  LEU G 241      41.860   0.295 -46.528  1.00183.76           C  
ATOM   2525  CA  LEU G 242      43.681  -1.561 -43.850  1.00109.51           C  
ATOM   2526  CA  GLY G 243      40.551  -2.086 -41.854  1.00 54.17           C  
ATOM   2527  CA  ILE G 244      41.703  -1.407 -38.325  1.00 78.66           C  
ATOM   2528  CA  LYS G 245      40.928   0.703 -35.305  1.00151.39           C  
ATOM   2529  CA  GLY G 246      43.554   2.578 -33.441  1.00 42.43           C  
ATOM   2530  CA  THR G 247      44.403   5.587 -31.403  1.00146.61           C  
ATOM   2531  CA  GLU G 248      47.277   7.442 -29.878  1.00 77.61           C  
ATOM   2532  CA  MET G 249      49.272   5.824 -27.142  1.00133.33           C  
ATOM   2533  CA  SER G 250      48.059   7.125 -23.841  1.00 94.16           C  
ATOM   2534  CA  ALA G 251      49.875   9.472 -21.534  1.00 39.94           C  
ATOM   2535  CA  ASP G 252      50.313   7.163 -18.587  1.00 49.58           C  
ATOM   2536  CA  ILE G 253      52.402   4.683 -20.464  1.00153.33           C  
ATOM   2537  CA  ALA G 254      54.086   7.485 -22.295  1.00 30.66           C  
ATOM   2538  CA  LYS G 255      55.264   8.966 -19.053  1.00 51.45           C  
ATOM   2539  CA  ALA G 256      56.863   5.781 -17.821  1.00 36.13           C  
ATOM   2540  CA  PHE G 257      58.079   4.437 -21.135  1.00 74.24           C  
ATOM   2541  CA  ASN G 258      59.925   7.353 -22.592  1.00 59.56           C  
ATOM   2542  CA  LEU G 259      59.698   5.259 -25.713  1.00117.31           C  
ATOM   2543  CA  ASP G 260      61.931   6.329 -28.532  1.00 40.48           C  
ATOM   2544  CA  VAL G 261      58.948   7.330 -30.538  1.00 42.64           C  
ATOM   2545  CA  GLN G 262      56.784   9.991 -29.044  1.00 51.95           C  
ATOM   2546  CA  ARG G 263      53.764   8.329 -30.441  1.00125.83           C  
ATOM   2547  CA  GLY G 264      52.813   5.832 -33.056  1.00 26.44           C  
ATOM   2548  CA  ALA G 265      49.663   4.336 -34.390  1.00 44.04           C  
ATOM   2549  CA  PHE G 266      48.391   1.823 -31.883  1.00141.75           C  
ATOM   2550  CA  VAL G 267      45.738  -0.537 -32.805  1.00 85.23           C  
ATOM   2551  CA  SER G 268      43.095  -1.705 -30.434  1.00 90.92           C  
ATOM   2552  CA  GLU G 269      41.401  -3.821 -33.046  1.00139.26           C  
ATOM   2553  CA  VAL G 270      41.498  -6.311 -35.863  1.00 77.18           C  
ATOM   2554  CA  LEU G 271      38.796  -6.138 -38.430  1.00 76.52           C  
ATOM   2555  CA  PRO G 272      37.423  -9.327 -39.768  1.00 71.41           C  
ATOM   2556  CA  GLY G 273      38.076 -10.188 -43.390  1.00 26.52           C  
ATOM   2557  CA  SER G 274      39.940  -6.954 -43.175  1.00 93.68           C  
ATOM   2558  CA  GLY G 275      43.082  -6.049 -44.933  1.00 37.16           C  
ATOM   2559  CA  SER G 276      44.775  -5.828 -41.637  1.00100.66           C  
ATOM   2560  CA  ALA G 277      43.567  -9.263 -40.832  1.00 59.92           C  
ATOM   2561  CA  LYS G 278      44.920 -11.083 -43.816  1.00107.87           C  
ATOM   2562  CA  ALA G 279      48.068  -9.045 -43.926  1.00 52.07           C  
ATOM   2563  CA  GLY G 280      48.829 -10.044 -40.574  1.00 78.37           C  
ATOM   2564  CA  VAL G 281      48.511  -7.202 -38.236  1.00100.71           C  
ATOM   2565  CA  LYS G 282      46.228  -7.705 -35.268  1.00198.67           C  
ATOM   2566  CA  ALA G 283      45.866  -5.082 -32.570  1.00138.95           C  
ATOM   2567  CA  GLY G 284      48.282  -3.878 -30.125  1.00 91.72           C  
ATOM   2568  CA  ASP G 285      51.061  -3.645 -32.241  1.00258.56           C  
ATOM   2569  CA  ILE G 286      52.151  -0.266 -32.815  1.00127.53           C  
ATOM   2570  CA  ILE G 287      52.512   0.852 -36.360  1.00 76.61           C  
ATOM   2571  CA  THR G 288      55.904   2.489 -36.400  1.00 58.33           C  
ATOM   2572  CA  SER G 289      56.122   3.413 -40.006  1.00 47.04           C  
ATOM   2573  CA  LEU G 290      54.433   3.290 -43.340  1.00 78.62           C  
ATOM   2574  CA  ASN G 291      56.593   2.824 -46.359  1.00180.91           C  
ATOM   2575  CA  GLY G 292      60.331   3.385 -46.561  1.00 55.60           C  
ATOM   2576  CA  LYS G 293      60.150   6.676 -44.720  1.00 90.18           C  
ATOM   2577  CA  PRO G 294      59.346   6.874 -41.107  1.00 60.50           C  
ATOM   2578  CA  LEU G 295      55.811   7.298 -39.883  1.00 90.41           C  
ATOM   2579  CA  ASN G 296      54.880   9.690 -37.168  1.00 76.07           C  
ATOM   2580  CA  SER G 297      51.970   9.524 -34.829  1.00 52.91           C  
ATOM   2581  CA  PHE G 298      48.641   7.966 -35.510  1.00 75.56           C  
ATOM   2582  CA  ALA G 299      48.011  11.364 -36.957  1.00 45.64           C  
ATOM   2583  CA  GLU G 300      50.602  11.122 -39.642  1.00 91.57           C  
ATOM   2584  CA  LEU G 301      49.271   7.683 -40.314  1.00 80.08           C  
ATOM   2585  CA  ARG G 302      46.033   8.670 -41.839  1.00191.65           C  
ATOM   2586  CA  SER G 303      47.653  11.672 -43.326  1.00 54.89           C  
ATOM   2587  CA  ARG G 304      49.606   9.516 -45.623  1.00189.67           C  
ATOM   2588  CA  ILE G 305      47.101   6.700 -45.963  1.00126.50           C  
ATOM   2589  CA  ALA G 306      44.097   8.851 -46.186  1.00 69.58           C  
ATOM   2590  CA  THR G 307      46.203  10.579 -48.752  1.00 57.89           C  
ATOM   2591  CA  THR G 308      47.082   7.451 -50.632  1.00127.76           C  
ATOM   2592  CA  GLU G 309      44.946   5.405 -52.941  1.00104.55           C  
ATOM   2593  CA  PRO G 310      42.789   3.079 -51.146  1.00217.91           C  
ATOM   2594  CA  GLY G 311      43.793   0.847 -52.809  1.00123.48           C  
ATOM   2595  CA  THR G 312      47.515   1.090 -53.275  1.00139.91           C  
ATOM   2596  CA  LYS G 313      49.550  -1.754 -51.962  1.00112.05           C  
ATOM   2597  CA  VAL G 314      51.799  -0.519 -49.208  1.00 52.91           C  
ATOM   2598  CA  LYS G 315      54.022  -1.996 -46.533  1.00 74.38           C  
ATOM   2599  CA  LEU G 316      53.808  -1.317 -42.843  1.00115.37           C  
ATOM   2600  CA  GLY G 317      56.270  -1.758 -40.055  1.00 60.46           C  
ATOM   2601  CA  LEU G 318      54.550  -2.157 -36.842  1.00227.44           C  
ATOM   2602  CA  LEU G 319      56.130  -2.966 -33.486  1.00154.87           C  
ATOM   2603  CA  ARG G 320      54.985  -6.009 -32.089  1.00298.45           C  
ATOM   2604  CA  ASN G 321      56.208  -7.321 -28.815  1.00205.72           C  
ATOM   2605  CA  GLY G 322      59.511  -5.620 -28.748  1.00 60.96           C  
ATOM   2606  CA  LYS G 323      60.554  -6.690 -32.130  1.00151.30           C  
ATOM   2607  CA  PRO G 324      60.509  -5.834 -35.726  1.00164.14           C  
ATOM   2608  CA  LEU G 325      57.884  -5.944 -38.594  1.00193.42           C  
ATOM   2609  CA  GLU G 326      57.732  -5.772 -42.200  1.00146.84           C  
ATOM   2610  CA  VAL G 327      54.425  -6.833 -43.731  1.00 61.20           C  
ATOM   2611  CA  GLU G 328      52.564  -5.866 -46.867  1.00 49.71           C  
ATOM   2612  CA  VAL G 329      49.091  -4.638 -46.370  1.00 59.72           C  
ATOM   2613  CA  SER G 340      23.048 -24.388 -45.631  1.00 92.68           C  
ATOM   2614  CA  ALA G 341      19.284 -24.325 -45.198  1.00 76.89           C  
ATOM   2615  CA  GLU G 342      19.520 -22.356 -41.984  1.00 68.23           C  
ATOM   2616  CA  MET G 343      19.754 -18.887 -43.324  1.00129.07           C  
ATOM   2617  CA  ILE G 344      16.962 -19.214 -45.785  1.00 86.81           C  
ATOM   2618  CA  THR G 345      14.860 -21.181 -43.402  1.00 68.15           C  
ATOM   2619  CA  PRO G 346      14.770 -20.446 -39.750  1.00245.03           C  
ATOM   2620  CA  ALA G 347      16.632 -22.601 -37.261  1.00 74.21           C  
ATOM   2621  CA  LEU G 348      16.158 -25.565 -39.589  1.00 88.66           C  
ATOM   2622  CA  GLU G 349      19.560 -27.155 -39.682  1.00 93.53           C  
ATOM   2623  CA  GLY G 350      20.078 -29.117 -42.797  1.00 29.12           C  
ATOM   2624  CA  ALA G 351      21.544 -29.506 -46.217  1.00 35.54           C  
ATOM   2625  CA  THR G 352      23.388 -26.557 -47.598  1.00 28.00           C  
ATOM   2626  CA  LEU G 353      21.811 -24.573 -50.365  1.00 54.85           C  
ATOM   2627  CA  SER G 354      23.286 -23.040 -53.467  1.00 87.36           C  
ATOM   2628  CA  ASP G 355      21.756 -20.820 -56.109  1.00117.64           C  
ATOM   2629  CA  GLY G 356      21.944 -21.060 -59.901  1.00 44.55           C  
ATOM   2630  CA  GLN G 357      20.919 -24.211 -61.639  1.00191.25           C  
ATOM   2631  CA  LEU G 358      24.363 -24.979 -61.047  1.00202.09           C  
ATOM   2632  CA  LYS G 359      25.609 -23.193 -64.146  1.00 93.59           C  
ATOM   2633  CA  ASP G 360      22.550 -23.481 -66.360  1.00156.83           C  
ATOM   2634  CA  GLY G 361      19.448 -21.451 -66.447  1.00 39.96           C  
ATOM   2635  CA  GLY G 362      18.414 -21.523 -62.865  1.00 43.97           C  
ATOM   2636  CA  LYS G 363      15.894 -24.232 -62.241  1.00166.00           C  
ATOM   2637  CA  GLY G 364      16.104 -22.922 -58.747  1.00 27.25           C  
ATOM   2638  CA  ILE G 365      18.127 -23.305 -55.591  1.00 57.76           C  
ATOM   2639  CA  LYS G 366      20.022 -26.518 -55.169  1.00 44.45           C  
ATOM   2640  CA  ILE G 367      20.567 -28.282 -51.919  1.00 58.40           C  
ATOM   2641  CA  ASP G 368      24.163 -29.374 -51.891  1.00 55.99           C  
ATOM   2642  CA  GLU G 369      24.284 -32.040 -49.251  1.00 87.91           C  
ATOM   2643  CA  VAL G 370      22.022 -33.377 -46.592  1.00147.35           C  
ATOM   2644  CA  VAL G 371      23.241 -33.323 -43.018  1.00186.41           C  
ATOM   2645  CA  LYS G 372      20.438 -35.916 -42.556  1.00166.39           C  
ATOM   2646  CA  GLY G 373      20.556 -35.968 -38.779  1.00 37.31           C  
ATOM   2647  CA  SER G 374      19.429 -32.332 -39.158  1.00 48.02           C  
ATOM   2648  CA  PRO G 375      15.858 -31.255 -39.255  1.00 74.30           C  
ATOM   2649  CA  ALA G 376      16.091 -30.059 -42.831  1.00 48.32           C  
ATOM   2650  CA  ALA G 377      16.545 -33.744 -43.391  1.00 58.32           C  
ATOM   2651  CA  GLN G 378      13.550 -34.720 -41.288  1.00140.07           C  
ATOM   2652  CA  ALA G 379      10.953 -33.063 -43.497  1.00 72.43           C  
ATOM   2653  CA  GLY G 380      12.000 -34.661 -46.742  1.00 67.46           C  
ATOM   2654  CA  LEU G 381      14.835 -32.567 -48.062  1.00 97.08           C  
ATOM   2655  CA  GLN G 382      17.231 -34.856 -49.880  1.00114.87           C  
ATOM   2656  CA  LYS G 383      20.422 -33.898 -51.592  1.00109.94           C  
ATOM   2657  CA  ASP G 384      20.428 -32.987 -55.273  1.00 75.64           C  
ATOM   2658  CA  ASP G 385      16.929 -31.636 -55.170  1.00 47.59           C  
ATOM   2659  CA  VAL G 386      16.295 -28.453 -57.085  1.00 59.76           C  
ATOM   2660  CA  ILE G 387      13.734 -26.139 -55.642  1.00103.24           C  
ATOM   2661  CA  ILE G 388      12.042 -24.677 -58.649  1.00 68.32           C  
ATOM   2662  CA  GLY G 389       9.668 -22.581 -56.637  1.00 36.68           C  
ATOM   2663  CA  VAL G 390       7.715 -22.047 -53.470  1.00 51.37           C  
ATOM   2664  CA  ASN G 391       4.056 -21.259 -52.931  1.00 78.70           C  
ATOM   2665  CA  ARG G 392       3.105 -21.086 -56.587  1.00109.78           C  
ATOM   2666  CA  ASP G 393       6.020 -18.778 -57.116  1.00 59.30           C  
ATOM   2667  CA  ARG G 394       9.032 -19.676 -59.160  1.00 97.18           C  
ATOM   2668  CA  VAL G 395      12.345 -19.416 -57.394  1.00 56.70           C  
ATOM   2669  CA  ASN G 396      15.170 -18.694 -59.767  1.00 47.19           C  
ATOM   2670  CA  SER G 397      17.624 -18.238 -56.964  1.00 39.09           C  
ATOM   2671  CA  ILE G 398      18.019 -17.857 -53.243  1.00 50.38           C  
ATOM   2672  CA  ALA G 399      16.973 -14.240 -53.262  1.00 24.02           C  
ATOM   2673  CA  GLU G 400      13.637 -14.960 -54.846  1.00 39.82           C  
ATOM   2674  CA  MET G 401      13.042 -17.851 -52.526  1.00 29.56           C  
ATOM   2675  CA  ARG G 402      13.648 -15.575 -49.608  1.00 70.65           C  
ATOM   2676  CA  LYS G 403      11.065 -13.207 -50.997  1.00101.62           C  
ATOM   2677  CA  VAL G 404       8.396 -15.853 -50.809  1.00 31.04           C  
ATOM   2678  CA  LEU G 405       9.457 -16.453 -47.240  1.00 73.86           C  
ATOM   2679  CA  ALA G 406       9.308 -12.748 -46.611  1.00 33.60           C  
ATOM   2680  CA  ALA G 407       5.568 -13.059 -47.007  1.00 35.08           C  
ATOM   2681  CA  LYS G 408       5.900 -15.678 -44.313  1.00110.86           C  
ATOM   2682  CA  PRO G 409       2.903 -17.717 -45.231  1.00 73.31           C  
ATOM   2683  CA  ALA G 410       2.037 -20.153 -42.497  1.00 31.45           C  
ATOM   2684  CA  ILE G 411       2.194 -22.820 -45.129  1.00114.58           C  
ATOM   2685  CA  ILE G 412       5.289 -22.996 -47.297  1.00 91.02           C  
ATOM   2686  CA  ALA G 413       5.355 -25.296 -50.217  1.00 62.90           C  
ATOM   2687  CA  LEU G 414       8.570 -26.205 -51.922  1.00139.84           C  
ATOM   2688  CA  GLN G 415       9.092 -27.160 -55.503  1.00161.53           C  
ATOM   2689  CA  ILE G 416      11.618 -29.673 -55.836  1.00100.70           C  
ATOM   2690  CA  VAL G 417      12.461 -31.672 -58.824  1.00 51.52           C  
ATOM   2691  CA  ARG G 418      14.134 -34.908 -57.978  1.00 69.72           C  
ATOM   2692  CA  GLY G 419      15.292 -37.006 -60.844  1.00 27.86           C  
ATOM   2693  CA  ASN G 420      13.125 -36.181 -63.766  1.00 99.40           C  
ATOM   2694  CA  GLU G 421      10.041 -35.944 -61.614  1.00136.11           C  
ATOM   2695  CA  SER G 422       8.616 -33.314 -59.405  1.00 51.02           C  
ATOM   2696  CA  ILE G 423       8.442 -33.707 -55.667  1.00110.97           C  
ATOM   2697  CA  TYR G 424       6.620 -31.637 -53.146  1.00217.83           C  
ATOM   2698  CA  LEU G 425       8.221 -30.432 -50.034  1.00 85.50           C  
ATOM   2699  CA  LEU G 426       6.930 -28.498 -47.176  1.00250.77           C  
ATOM   2700  CA  MET G 427       7.201 -26.644 -43.930  1.00 77.31           C  
ATOM   2701  CA  ARG G 428       5.148 -26.313 -40.792  1.00 67.69           C  
TER    2702      ARG G 428                                                      
ATOM   2703  CA  PRO H  11      48.707  46.360 -42.813  1.00138.27           C  
ATOM   2704  CA  LEU H  12      45.069  46.672 -41.950  1.00140.53           C  
ATOM   2705  CA  PRO H  13      44.196  49.908 -40.306  1.00101.03           C  
ATOM   2706  CA  SER H  14      43.174  49.665 -36.688  1.00 86.07           C  
ATOM   2707  CA  LEU H  15      39.557  49.655 -35.615  1.00 52.75           C  
ATOM   2708  CA  ALA H  16      40.075  52.112 -32.814  1.00 38.43           C  
ATOM   2709  CA  PRO H  17      40.452  55.150 -34.957  1.00138.52           C  
ATOM   2710  CA  MET H  18      37.276  54.389 -36.867  1.00128.73           C  
ATOM   2711  CA  LEU H  19      35.591  53.393 -33.647  1.00164.21           C  
ATOM   2712  CA  GLU H  20      36.425  56.597 -31.850  1.00 49.50           C  
ATOM   2713  CA  LYS H  21      34.352  58.775 -34.105  1.00 40.58           C  
ATOM   2714  CA  VAL H  22      31.456  56.358 -34.508  1.00 56.40           C  
ATOM   2715  CA  LEU H  23      30.852  55.078 -31.005  1.00123.92           C  
ATOM   2716  CA  PRO H  24      29.051  58.025 -29.579  1.00 65.88           C  
ATOM   2717  CA  ALA H  25      26.381  57.448 -32.200  1.00 31.23           C  
ATOM   2718  CA  VAL H  26      25.461  54.123 -30.643  1.00 31.82           C  
ATOM   2719  CA  VAL H  27      23.269  54.434 -27.608  1.00 40.87           C  
ATOM   2720  CA  SER H  28      21.910  52.183 -24.911  1.00 36.68           C  
ATOM   2721  CA  VAL H  29      18.179  52.149 -24.486  1.00 34.08           C  
ATOM   2722  CA  ARG H  30      16.565  51.567 -21.144  1.00 79.03           C  
ATOM   2723  CA  VAL H  31      12.957  50.565 -20.827  1.00 39.37           C  
ATOM   2724  CA  GLU H  32      10.475  50.323 -17.999  1.00 35.91           C  
ATOM   2725  CA  GLY H  33       6.898  49.181 -18.124  1.00 22.05           C  
ATOM   2726  CA  THR H  34       4.453  46.497 -17.215  1.00 61.08           C  
ATOM   2727  CA  ALA H  58       1.934  43.821 -14.984  1.00 20.34           C  
ATOM   2728  CA  GLN H  59       4.920  43.530 -12.727  1.00 91.21           C  
ATOM   2729  CA  PRO H  60       7.388  46.305 -13.265  1.00149.20           C  
ATOM   2730  CA  PHE H  61      10.227  45.206 -15.452  1.00 58.22           C  
ATOM   2731  CA  GLU H  62      13.333  46.855 -16.733  1.00 26.49           C  
ATOM   2732  CA  GLY H  63      14.795  45.960 -20.064  1.00 17.27           C  
ATOM   2733  CA  LEU H  64      17.976  46.994 -21.734  1.00 75.54           C  
ATOM   2734  CA  GLY H  65      18.718  47.304 -25.403  1.00 22.01           C  
ATOM   2735  CA  SER H  66      20.609  49.520 -27.763  1.00 72.63           C  
ATOM   2736  CA  GLY H  67      19.826  52.016 -30.474  1.00 18.46           C  
ATOM   2737  CA  VAL H  68      21.524  54.103 -33.099  1.00 38.79           C  
ATOM   2738  CA  ILE H  69      21.315  57.847 -33.525  1.00152.58           C  
ATOM   2739  CA  ILE H  70      20.111  58.428 -37.039  1.00121.93           C  
ATOM   2740  CA  ASN H  71      19.741  62.173 -36.768  1.00 51.71           C  
ATOM   2741  CA  ALA H  72      21.633  64.186 -34.222  1.00 36.97           C  
ATOM   2742  CA  SER H  73      19.679  67.348 -34.682  1.00 32.86           C  
ATOM   2743  CA  LYS H  74      16.298  65.760 -34.380  1.00111.45           C  
ATOM   2744  CA  GLY H  75      17.498  63.159 -31.956  1.00 26.70           C  
ATOM   2745  CA  TYR H  76      16.013  60.232 -33.825  1.00 62.79           C  
ATOM   2746  CA  VAL H  77      17.176  56.865 -32.590  1.00 46.88           C  
ATOM   2747  CA  LEU H  78      16.567  53.630 -34.436  1.00152.68           C  
ATOM   2748  CA  THR H  79      15.890  50.554 -32.350  1.00 62.20           C  
ATOM   2749  CA  ASN H  80      14.134  47.234 -32.536  1.00 69.92           C  
ATOM   2750  CA  ASN H  81      10.432  47.179 -31.911  1.00 41.68           C  
ATOM   2751  CA  HIS H  82      10.718  44.370 -29.435  1.00 53.35           C  
ATOM   2752  CA  VAL H  83      13.013  46.340 -27.217  1.00 38.06           C  
ATOM   2753  CA  ILE H  84      10.489  49.205 -27.178  1.00119.42           C  
ATOM   2754  CA  ASN H  85       7.196  47.328 -27.297  1.00 65.79           C  
ATOM   2755  CA  GLN H  86       6.406  46.980 -23.585  1.00 59.81           C  
ATOM   2756  CA  ALA H  87       8.023  50.270 -22.588  1.00 67.72           C  
ATOM   2757  CA  GLN H  88       5.935  52.668 -20.584  1.00 55.21           C  
ATOM   2758  CA  LYS H  89       8.925  54.960 -20.421  1.00 31.18           C  
ATOM   2759  CA  ILE H  90      12.139  54.962 -22.362  1.00 48.94           C  
ATOM   2760  CA  SER H  91      15.456  56.566 -21.670  1.00 32.79           C  
ATOM   2761  CA  ILE H  92      18.630  56.548 -23.655  1.00 73.94           C  
ATOM   2762  CA  GLN H  93      22.148  56.772 -22.377  1.00 37.63           C  
ATOM   2763  CA  LEU H  94      25.128  58.030 -24.263  1.00 43.78           C  
ATOM   2764  CA  ASN H  95      28.599  56.554 -24.017  1.00 44.50           C  
ATOM   2765  CA  ASP H  96      29.602  59.685 -22.184  1.00 57.82           C  
ATOM   2766  CA  GLY H  97      27.103  58.990 -19.448  1.00 26.93           C  
ATOM   2767  CA  ARG H  98      24.616  61.639 -20.437  1.00141.00           C  
ATOM   2768  CA  GLU H  99      21.056  60.421 -20.273  1.00 41.55           C  
ATOM   2769  CA  PHE H 100      17.929  61.571 -22.047  1.00 49.85           C  
ATOM   2770  CA  ASP H 101      14.288  60.628 -22.153  1.00 31.77           C  
ATOM   2771  CA  ALA H 102      12.790  59.404 -25.374  1.00 28.91           C  
ATOM   2772  CA  LYS H 103       9.386  59.053 -26.957  1.00106.10           C  
ATOM   2773  CA  LEU H 104       8.341  56.448 -29.456  1.00107.09           C  
ATOM   2774  CA  ILE H 105       7.731  58.088 -32.803  1.00 95.04           C  
ATOM   2775  CA  GLY H 106       6.513  54.925 -34.440  1.00 23.22           C  
ATOM   2776  CA  SER H 107       7.319  51.299 -35.017  1.00 88.10           C  
ATOM   2777  CA  ASP H 108       6.463  48.233 -37.059  1.00 87.57           C  
ATOM   2778  CA  ASP H 109       5.907  44.736 -35.763  1.00 55.90           C  
ATOM   2779  CA  GLN H 110       6.577  42.735 -38.860  1.00156.40           C  
ATOM   2780  CA  SER H 111       9.980  44.213 -39.715  1.00130.40           C  
ATOM   2781  CA  ASP H 112      10.679  44.856 -36.027  1.00 73.70           C  
ATOM   2782  CA  ILE H 113      11.926  48.407 -36.475  1.00 48.20           C  
ATOM   2783  CA  ALA H 114      11.010  51.297 -34.212  1.00 31.28           C  
ATOM   2784  CA  LEU H 115      11.946  54.949 -34.202  1.00 96.86           C  
ATOM   2785  CA  LEU H 116      12.503  56.920 -31.033  1.00 48.63           C  
ATOM   2786  CA  GLN H 117      13.046  60.601 -30.500  1.00130.88           C  
ATOM   2787  CA  ILE H 118      15.220  61.993 -27.794  1.00135.23           C  
ATOM   2788  CA  GLN H 119      13.754  64.840 -25.861  1.00101.87           C  
ATOM   2789  CA  ASN H 120      15.871  67.949 -25.758  1.00 50.48           C  
ATOM   2790  CA  PRO H 121      18.641  66.327 -27.697  1.00 70.59           C  
ATOM   2791  CA  SER H 122      21.891  68.200 -27.479  1.00 39.33           C  
ATOM   2792  CA  LYS H 123      25.425  67.766 -28.770  1.00 43.23           C  
ATOM   2793  CA  LEU H 124      24.702  64.405 -30.292  1.00 47.41           C  
ATOM   2794  CA  THR H 125      26.596  62.530 -32.963  1.00 37.09           C  
ATOM   2795  CA  GLN H 126      24.968  60.736 -35.866  1.00173.17           C  
ATOM   2796  CA  ILE H 127      25.848  57.563 -37.652  1.00 83.46           C  
ATOM   2797  CA  ALA H 128      26.252  57.523 -41.396  1.00 28.95           C  
ATOM   2798  CA  ILE H 129      24.327  54.866 -43.245  1.00 54.47           C  
ATOM   2799  CA  ALA H 130      25.838  52.611 -45.872  1.00 37.00           C  
ATOM   2800  CA  ASP H 131      24.108  50.861 -48.729  1.00 37.03           C  
ATOM   2801  CA  SER H 132      23.188  47.436 -47.444  1.00 38.02           C  
ATOM   2802  CA  ASP H 133      22.606  46.175 -50.947  1.00 33.04           C  
ATOM   2803  CA  LYS H 134      26.309  46.503 -51.688  1.00137.47           C  
ATOM   2804  CA  LEU H 135      27.353  44.161 -48.929  1.00111.54           C  
ATOM   2805  CA  ARG H 136      28.755  40.814 -49.853  1.00118.37           C  
ATOM   2806  CA  VAL H 137      29.759  37.875 -47.758  1.00 84.12           C  
ATOM   2807  CA  GLY H 138      33.192  38.254 -46.284  1.00 24.69           C  
ATOM   2808  CA  ASP H 139      32.828  41.937 -45.562  1.00127.82           C  
ATOM   2809  CA  PHE H 140      34.057  43.025 -42.170  1.00 54.72           C  
ATOM   2810  CA  ALA H 141      31.509  44.025 -39.605  1.00 32.32           C  
ATOM   2811  CA  VAL H 142      31.599  45.410 -36.110  1.00 88.90           C  
ATOM   2812  CA  ALA H 143      28.704  45.195 -33.738  1.00 31.44           C  
ATOM   2813  CA  VAL H 144      28.095  47.733 -31.041  1.00 29.65           C  
ATOM   2814  CA  GLY H 145      25.508  47.475 -28.330  1.00 25.19           C  
ATOM   2815  CA  ASN H 146      25.140  46.649 -24.707  1.00110.09           C  
ATOM   2816  CA  PRO H 147      25.265  43.011 -24.059  1.00 73.03           C  
ATOM   2817  CA  PHE H 148      24.159  42.027 -20.588  1.00 62.94           C  
ATOM   2818  CA  GLY H 149      23.778  45.721 -19.928  1.00 22.02           C  
ATOM   2819  CA  LEU H 150      27.501  45.861 -19.369  1.00 41.89           C  
ATOM   2820  CA  GLY H 151      27.922  49.097 -21.251  1.00 30.28           C  
ATOM   2821  CA  GLN H 152      28.840  49.911 -24.779  1.00 59.79           C  
ATOM   2822  CA  THR H 153      30.687  46.959 -26.175  1.00 50.02           C  
ATOM   2823  CA  ALA H 154      32.132  46.409 -29.591  1.00 37.07           C  
ATOM   2824  CA  THR H 155      32.624  43.040 -31.196  1.00107.78           C  
ATOM   2825  CA  SER H 156      34.082  42.164 -34.547  1.00 79.72           C  
ATOM   2826  CA  GLY H 157      33.279  39.637 -37.229  1.00 21.84           C  
ATOM   2827  CA  ILE H 158      32.457  39.248 -40.898  1.00 57.29           C  
ATOM   2828  CA  VAL H 159      29.241  39.239 -42.863  1.00 55.74           C  
ATOM   2829  CA  SER H 160      28.371  35.563 -42.820  1.00 53.99           C  
ATOM   2830  CA  ALA H 161      25.385  35.688 -45.115  1.00 46.93           C  
ATOM   2831  CA  LEU H 162      22.724  37.972 -46.422  1.00116.41           C  
ATOM   2832  CA  GLY H 163      19.211  37.773 -47.668  1.00 31.80           C  
ATOM   2833  CA  ARG H 164      18.230  35.185 -45.222  1.00102.62           C  
ATOM   2834  CA  SER H 165      14.954  34.384 -43.699  1.00 89.66           C  
ATOM   2835  CA  GLY H 166      12.420  31.746 -42.979  1.00 40.92           C  
ATOM   2836  CA  LEU H 167      13.830  32.043 -39.485  1.00 51.05           C  
ATOM   2837  CA  ASN H 168      10.282  32.910 -38.505  1.00 65.98           C  
ATOM   2838  CA  LEU H 169      11.715  35.403 -36.092  1.00 46.75           C  
ATOM   2839  CA  GLU H 170       9.582  38.107 -37.648  1.00108.39           C  
ATOM   2840  CA  GLY H 171       6.948  38.678 -40.316  1.00 40.43           C  
ATOM   2841  CA  LEU H 172       9.351  40.267 -42.736  1.00164.25           C  
ATOM   2842  CA  GLU H 173      12.824  38.980 -42.603  1.00 93.02           C  
ATOM   2843  CA  ASN H 174      15.984  39.634 -44.521  1.00114.47           C  
ATOM   2844  CA  PHE H 175      18.647  39.351 -42.026  1.00 99.62           C  
ATOM   2845  CA  ILE H 176      22.251  39.988 -42.635  1.00 77.54           C  
ATOM   2846  CA  GLN H 177      23.993  37.258 -40.735  1.00 44.79           C  
ATOM   2847  CA  THR H 178      27.143  38.010 -38.820  1.00 46.51           C  
ATOM   2848  CA  ASP H 179      29.707  36.127 -36.764  1.00 59.19           C  
ATOM   2849  CA  ALA H 180      30.247  39.138 -34.541  1.00 40.46           C  
ATOM   2850  CA  SER H 181      29.361  38.282 -31.003  1.00 88.51           C  
ATOM   2851  CA  ILE H 182      25.790  39.322 -30.401  1.00114.55           C  
ATOM   2852  CA  ASN H 183      24.219  38.711 -27.045  1.00 58.89           C  
ATOM   2853  CA  ARG H 184      21.105  39.768 -25.278  1.00117.60           C  
ATOM   2854  CA  GLY H 185      21.055  43.518 -24.977  1.00 23.95           C  
ATOM   2855  CA  ASN H 186      22.557  43.886 -28.430  1.00 56.57           C  
ATOM   2856  CA  ALA H 187      19.128  44.387 -29.929  1.00 43.00           C  
ATOM   2857  CA  GLY H 188      18.658  47.713 -31.615  1.00 23.66           C  
ATOM   2858  CA  GLY H 189      22.415  48.057 -31.697  1.00 21.18           C  
ATOM   2859  CA  ALA H 190      24.438  48.900 -34.733  1.00 44.15           C  
ATOM   2860  CA  LEU H 191      26.327  46.686 -37.084  1.00133.03           C  
ATOM   2861  CA  LEU H 192      28.987  48.715 -38.779  1.00 70.95           C  
ATOM   2862  CA  ASN H 193      31.310  48.641 -41.743  1.00153.74           C  
ATOM   2863  CA  LEU H 194      35.030  49.282 -41.444  1.00 45.11           C  
ATOM   2864  CA  ASN H 195      34.017  52.750 -42.519  1.00 57.74           C  
ATOM   2865  CA  GLY H 196      31.892  53.033 -39.424  1.00 27.92           C  
ATOM   2866  CA  GLU H 197      28.813  53.272 -41.570  1.00 55.80           C  
ATOM   2867  CA  LEU H 198      25.637  51.535 -40.452  1.00140.26           C  
ATOM   2868  CA  ILE H 199      25.146  48.266 -42.324  1.00 84.73           C  
ATOM   2869  CA  GLY H 200      22.207  47.084 -40.230  1.00 31.73           C  
ATOM   2870  CA  ILE H 201      20.553  46.903 -36.833  1.00 58.14           C  
ATOM   2871  CA  ASN H 202      21.195  43.765 -34.829  1.00 68.27           C  
ATOM   2872  CA  THR H 203      17.813  42.143 -34.307  1.00 84.15           C  
ATOM   2873  CA  ALA H 204      18.401  38.633 -33.033  1.00 62.37           C  
ATOM   2874  CA  ILE H 205      20.510  35.522 -32.702  1.00199.06           C  
ATOM   2875  CA  LEU H 206      20.072  31.828 -32.905  1.00 81.51           C  
ATOM   2876  CA  ALA H 207      21.670  30.233 -29.926  1.00 57.92           C  
ATOM   2877  CA  PRO H 208      20.744  27.094 -28.162  1.00144.49           C  
ATOM   2878  CA  GLY H 209      22.531  28.226 -25.015  1.00 31.24           C  
ATOM   2879  CA  GLY H 210      21.036  31.656 -25.099  1.00 23.63           C  
ATOM   2880  CA  GLY H 211      24.571  32.870 -25.584  1.00 25.26           C  
ATOM   2881  CA  SER H 212      26.217  33.957 -28.796  1.00 56.35           C  
ATOM   2882  CA  VAL H 213      26.858  30.993 -31.066  1.00139.25           C  
ATOM   2883  CA  GLY H 214      28.352  33.231 -33.679  1.00 37.19           C  
ATOM   2884  CA  ILE H 215      25.101  33.258 -35.577  1.00110.86           C  
ATOM   2885  CA  GLY H 216      23.575  36.706 -35.397  1.00 23.30           C  
ATOM   2886  CA  PHE H 217      21.046  38.462 -37.562  1.00 47.85           C  
ATOM   2887  CA  ALA H 218      20.574  42.119 -38.342  1.00 36.43           C  
ATOM   2888  CA  ILE H 219      18.097  44.160 -40.315  1.00 92.95           C  
ATOM   2889  CA  PRO H 220      19.819  45.693 -43.222  1.00 88.67           C  
ATOM   2890  CA  SER H 221      20.602  49.376 -43.122  1.00 98.19           C  
ATOM   2891  CA  ASN H 222      18.657  50.001 -46.231  1.00 63.87           C  
ATOM   2892  CA  MET H 223      16.048  48.311 -44.264  1.00113.55           C  
ATOM   2893  CA  ALA H 224      16.080  50.491 -41.232  1.00 51.31           C  
ATOM   2894  CA  ARG H 225      16.799  53.650 -43.127  1.00 91.58           C  
ATOM   2895  CA  THR H 226      13.825  53.948 -45.355  1.00 60.63           C  
ATOM   2896  CA  LEU H 227      11.595  52.274 -42.766  1.00110.76           C  
ATOM   2897  CA  ALA H 228      12.763  54.816 -40.249  1.00 45.29           C  
ATOM   2898  CA  GLN H 229      12.308  57.525 -42.786  1.00 83.40           C  
ATOM   2899  CA  GLN H 230       8.581  57.416 -43.122  1.00 90.78           C  
ATOM   2900  CA  LEU H 231       8.257  57.008 -39.398  1.00109.31           C  
ATOM   2901  CA  ILE H 232       9.473  60.530 -39.396  1.00125.14           C  
ATOM   2902  CA  ASP H 233       8.188  61.240 -42.957  1.00164.90           C  
ATOM   2903  CA  PHE H 234       6.276  60.639 -45.216  1.00195.86           C  
ATOM   2904  CA  GLY H 235       4.560  59.298 -42.210  1.00 28.39           C  
ATOM   2905  CA  GLU H 236       1.835  58.225 -44.530  1.00129.40           C  
ATOM   2906  CA  ILE H 237      -0.343  55.944 -42.464  1.00 41.73           C  
ATOM   2907  CA  LYS H 238      -0.854  53.352 -45.095  1.00182.21           C  
ATOM   2908  CA  ARG H 239       0.037  50.734 -45.394  1.00180.40           C  
ATOM   2909  CA  GLY H 240       2.586  51.071 -42.658  1.00 42.02           C  
ATOM   2910  CA  LEU H 241       3.428  47.453 -43.344  1.00261.73           C  
ATOM   2911  CA  LEU H 242       1.861  44.161 -43.954  1.00201.42           C  
ATOM   2912  CA  GLY H 243       1.177  42.979 -40.498  1.00 60.82           C  
ATOM   2913  CA  ILE H 244       1.814  39.331 -41.335  1.00 88.81           C  
ATOM   2914  CA  LYS H 245       3.788  36.406 -40.067  1.00149.73           C  
ATOM   2915  CA  GLY H 246       5.513  34.001 -42.335  1.00 33.06           C  
ATOM   2916  CA  THR H 247       8.497  31.813 -42.778  1.00113.90           C  
ATOM   2917  CA  GLU H 248      10.312  29.988 -45.474  1.00 48.64           C  
ATOM   2918  CA  MET H 249       8.430  27.319 -47.315  1.00101.26           C  
ATOM   2919  CA  SER H 250       9.666  23.903 -46.262  1.00 49.71           C  
ATOM   2920  CA  ALA H 251      11.970  21.543 -48.103  1.00 56.02           C  
ATOM   2921  CA  ASP H 252       9.597  19.039 -49.572  1.00102.33           C  
ATOM   2922  CA  ILE H 253       7.744  21.523 -51.692  1.00100.47           C  
ATOM   2923  CA  ALA H 254      11.075  23.004 -52.612  1.00 31.64           C  
ATOM   2924  CA  LYS H 255      12.171  19.652 -53.887  1.00 73.91           C  
ATOM   2925  CA  ALA H 256       9.123  19.204 -56.079  1.00 39.89           C  
ATOM   2926  CA  PHE H 257       8.713  22.815 -57.171  1.00 75.28           C  
ATOM   2927  CA  ASN H 258      12.113  23.766 -58.435  1.00 61.37           C  
ATOM   2928  CA  LEU H 259      10.556  27.194 -58.337  1.00 70.89           C  
ATOM   2929  CA  ASP H 260      12.402  30.138 -59.755  1.00 32.97           C  
ATOM   2930  CA  VAL H 261      12.598  31.527 -56.290  1.00129.59           C  
ATOM   2931  CA  GLN H 262      14.506  29.245 -53.987  1.00 55.28           C  
ATOM   2932  CA  ARG H 263      11.918  29.883 -51.378  1.00153.97           C  
ATOM   2933  CA  GLY H 264       9.068  32.281 -51.309  1.00 31.93           C  
ATOM   2934  CA  ALA H 265       7.618  34.111 -48.419  1.00 43.05           C  
ATOM   2935  CA  PHE H 266       4.864  31.963 -47.137  1.00120.05           C  
ATOM   2936  CA  VAL H 267       2.307  33.511 -44.902  1.00 64.66           C  
ATOM   2937  CA  SER H 268       0.981  31.345 -42.091  1.00111.55           C  
ATOM   2938  CA  GLU H 269      -1.124  34.031 -40.525  1.00113.39           C  
ATOM   2939  CA  VAL H 270      -3.356  37.016 -40.998  1.00 63.50           C  
ATOM   2940  CA  LEU H 271      -3.195  39.938 -38.646  1.00 93.83           C  
ATOM   2941  CA  PRO H 272      -6.373  41.529 -37.570  1.00 68.95           C  
ATOM   2942  CA  GLY H 273      -7.018  45.075 -38.671  1.00 29.65           C  
ATOM   2943  CA  SER H 274      -3.703  44.537 -40.237  1.00104.41           C  
ATOM   2944  CA  GLY H 275      -2.178  45.805 -43.350  1.00 57.61           C  
ATOM   2945  CA  SER H 276      -2.585  42.455 -44.894  1.00129.10           C  
ATOM   2946  CA  ALA H 277      -6.100  41.933 -43.747  1.00 57.66           C  
ATOM   2947  CA  LYS H 278      -7.960  44.584 -45.715  1.00155.68           C  
ATOM   2948  CA  ALA H 279      -6.150  44.079 -49.010  1.00 50.53           C  
ATOM   2949  CA  GLY H 280      -7.197  40.604 -48.620  1.00 58.08           C  
ATOM   2950  CA  VAL H 281      -4.012  38.688 -47.975  1.00 95.94           C  
ATOM   2951  CA  LYS H 282      -4.862  35.833 -45.712  1.00183.79           C  
ATOM   2952  CA  ALA H 283      -2.813  32.817 -44.936  1.00112.78           C  
ATOM   2953  CA  GLY H 284      -1.593  29.879 -46.786  1.00 60.98           C  
ATOM   2954  CA  ASP H 285      -0.267  31.904 -49.519  1.00143.24           C  
ATOM   2955  CA  ILE H 286       2.958  32.651 -50.936  1.00 90.88           C  
ATOM   2956  CA  ILE H 287       4.172  36.065 -51.705  1.00131.41           C  
ATOM   2957  CA  THR H 288       6.080  35.548 -54.904  1.00122.74           C  
ATOM   2958  CA  SER H 289       7.188  39.062 -55.493  1.00 46.44           C  
ATOM   2959  CA  LEU H 290       7.025  42.581 -54.250  1.00118.86           C  
ATOM   2960  CA  ASN H 291       6.905  45.305 -56.835  1.00184.33           C  
ATOM   2961  CA  GLY H 292       7.500  44.946 -60.543  1.00 58.02           C  
ATOM   2962  CA  LYS H 293      10.688  42.990 -60.061  1.00148.14           C  
ATOM   2963  CA  PRO H 294      10.670  39.521 -58.752  1.00 63.78           C  
ATOM   2964  CA  LEU H 295      10.967  38.698 -55.073  1.00 68.17           C  
ATOM   2965  CA  ASN H 296      13.299  36.141 -53.639  1.00 72.51           C  
ATOM   2966  CA  SER H 297      12.837  34.079 -50.575  1.00 47.48           C  
ATOM   2967  CA  PHE H 298      11.118  35.295 -47.514  1.00 95.81           C  
ATOM   2968  CA  ALA H 299      14.534  36.617 -46.757  1.00 47.53           C  
ATOM   2969  CA  GLU H 300      14.606  38.985 -49.651  1.00 91.49           C  
ATOM   2970  CA  LEU H 301      11.134  39.956 -48.630  1.00 98.75           C  
ATOM   2971  CA  ARG H 302      12.082  41.721 -45.489  1.00232.10           C  
ATOM   2972  CA  SER H 303      15.169  42.866 -47.232  1.00 59.21           C  
ATOM   2973  CA  ARG H 304      13.188  45.041 -49.479  1.00114.01           C  
ATOM   2974  CA  ILE H 305      10.294  45.774 -47.167  1.00132.81           C  
ATOM   2975  CA  ALA H 306      12.394  46.333 -44.179  1.00 73.30           C  
ATOM   2976  CA  THR H 307      14.282  48.534 -46.527  1.00130.63           C  
ATOM   2977  CA  THR H 308      11.267  50.375 -47.774  1.00129.65           C  
ATOM   2978  CA  GLU H 309       9.362  53.099 -46.021  1.00 80.13           C  
ATOM   2979  CA  PRO H 310       6.816  51.744 -43.723  1.00190.54           C  
ATOM   2980  CA  GLY H 311       4.658  53.277 -45.075  1.00118.12           C  
ATOM   2981  CA  THR H 312       5.228  53.169 -48.784  1.00 42.31           C  
ATOM   2982  CA  LYS H 313       2.241  51.906 -50.651  1.00147.66           C  
ATOM   2983  CA  VAL H 314       3.327  48.899 -52.586  1.00100.60           C  
ATOM   2984  CA  LYS H 315       1.853  45.976 -54.445  1.00 85.36           C  
ATOM   2985  CA  LEU H 316       2.508  42.368 -53.657  1.00 99.57           C  
ATOM   2986  CA  GLY H 317       2.347  39.270 -55.752  1.00 51.54           C  
ATOM   2987  CA  LEU H 318       1.194  36.065 -54.201  1.00182.97           C  
ATOM   2988  CA  LEU H 319       0.125  32.709 -55.242  1.00145.51           C  
ATOM   2989  CA  ARG H 320      -3.176  31.627 -53.962  1.00218.52           C  
ATOM   2990  CA  ASN H 321      -5.050  28.438 -55.034  1.00131.85           C  
ATOM   2991  CA  GLY H 322      -2.508  28.007 -57.744  1.00 31.17           C  
ATOM   2992  CA  LYS H 323      -3.328  31.285 -59.144  1.00150.68           C  
ATOM   2993  CA  PRO H 324      -2.005  34.701 -59.355  1.00122.82           C  
ATOM   2994  CA  LEU H 325      -3.149  38.148 -58.293  1.00180.81           C  
ATOM   2995  CA  GLU H 326      -1.796  41.459 -57.413  1.00115.81           C  
ATOM   2996  CA  VAL H 327      -2.978  43.403 -54.432  1.00 57.64           C  
ATOM   2997  CA  GLU H 328      -1.924  46.689 -52.960  1.00 99.40           C  
ATOM   2998  CA  VAL H 329      -0.904  46.331 -49.374  1.00 53.15           C  
ATOM   2999  CA  SER H 340     -27.024  48.015 -25.674  1.00101.39           C  
ATOM   3000  CA  ALA H 341     -26.711  47.717 -21.911  1.00 78.53           C  
ATOM   3001  CA  GLU H 342     -24.444  44.721 -22.060  1.00 59.59           C  
ATOM   3002  CA  MET H 343     -21.163  46.371 -22.742  1.00 37.89           C  
ATOM   3003  CA  ILE H 344     -21.508  48.867 -19.973  1.00106.96           C  
ATOM   3004  CA  THR H 345     -23.154  46.404 -17.686  1.00 72.14           C  
ATOM   3005  CA  PRO H 346     -22.029  42.854 -17.528  1.00155.20           C  
ATOM   3006  CA  ALA H 347     -24.029  40.055 -19.083  1.00 70.96           C  
ATOM   3007  CA  LEU H 348     -27.091  42.213 -18.492  1.00102.92           C  
ATOM   3008  CA  GLU H 349     -28.735  42.026 -21.850  1.00 76.19           C  
ATOM   3009  CA  GLY H 350     -31.224  44.752 -22.304  1.00 27.11           C  
ATOM   3010  CA  ALA H 351     -32.105  48.012 -23.913  1.00 36.55           C  
ATOM   3011  CA  THR H 352     -29.422  49.705 -25.910  1.00 28.37           C  
ATOM   3012  CA  LEU H 353     -27.778  52.763 -24.506  1.00 50.37           C  
ATOM   3013  CA  SER H 354     -26.567  55.943 -26.129  1.00 87.43           C  
ATOM   3014  CA  ASP H 355     -24.375  58.671 -24.747  1.00 34.40           C  
ATOM   3015  CA  GLY H 356     -25.090  62.357 -24.710  1.00 37.67           C  
ATOM   3016  CA  GLN H 357     -28.413  63.861 -23.816  1.00101.62           C  
ATOM   3017  CA  LEU H 358     -28.385  63.341 -27.475  1.00158.77           C  
ATOM   3018  CA  LYS H 359     -30.894  66.055 -28.004  1.00 59.39           C  
ATOM   3019  CA  ASP H 360     -29.988  68.432 -25.223  1.00 44.74           C  
ATOM   3020  CA  GLY H 361     -27.098  68.944 -22.900  1.00 23.79           C  
ATOM   3021  CA  GLY H 362     -26.058  65.597 -21.570  1.00 37.81           C  
ATOM   3022  CA  LYS H 363     -28.367  64.735 -18.742  1.00 84.53           C  
ATOM   3023  CA  GLY H 364     -26.773  61.368 -19.035  1.00 27.03           C  
ATOM   3024  CA  ILE H 365     -26.831  58.140 -20.975  1.00 64.11           C  
ATOM   3025  CA  LYS H 366     -30.027  57.330 -22.771  1.00 73.96           C  
ATOM   3026  CA  ILE H 367     -31.610  53.944 -23.098  1.00 70.28           C  
ATOM   3027  CA  ASP H 368     -32.630  53.542 -26.697  1.00 57.17           C  
ATOM   3028  CA  GLU H 369     -35.101  50.723 -26.547  1.00 91.11           C  
ATOM   3029  CA  VAL H 370     -36.074  47.954 -24.216  1.00125.24           C  
ATOM   3030  CA  VAL H 371     -35.472  44.373 -25.316  1.00126.12           C  
ATOM   3031  CA  LYS H 372     -37.860  43.713 -22.390  1.00191.12           C  
ATOM   3032  CA  GLY H 373     -37.589  39.954 -22.443  1.00 38.76           C  
ATOM   3033  CA  SER H 374     -33.956  40.707 -21.515  1.00 38.44           C  
ATOM   3034  CA  PRO H 375     -32.759  41.129 -17.997  1.00 70.33           C  
ATOM   3035  CA  ALA H 376     -31.999  44.807 -18.322  1.00 45.01           C  
ATOM   3036  CA  ALA H 377     -35.741  44.909 -18.653  1.00 51.28           C  
ATOM   3037  CA  GLN H 378     -36.441  42.747 -15.631  1.00 53.66           C  
ATOM   3038  CA  ALA H 379     -35.109  45.154 -13.038  1.00 64.64           C  
ATOM   3039  CA  GLY H 380     -36.777  48.311 -14.115  1.00 72.28           C  
ATOM   3040  CA  LEU H 381     -34.918  49.714 -17.053  1.00 69.65           C  
ATOM   3041  CA  GLN H 382     -37.508  51.137 -19.398  1.00 60.15           C  
ATOM   3042  CA  LYS H 383     -36.726  52.872 -22.620  1.00169.02           C  
ATOM   3043  CA  ASP H 384     -36.517  56.620 -22.787  1.00 69.49           C  
ATOM   3044  CA  ASP H 385     -35.059  56.846 -19.368  1.00160.38           C  
ATOM   3045  CA  VAL H 386     -32.052  59.041 -18.866  1.00 56.06           C  
ATOM   3046  CA  ILE H 387     -29.371  57.982 -16.525  1.00 71.87           C  
ATOM   3047  CA  ILE H 388     -28.341  61.130 -14.768  1.00129.49           C  
ATOM   3048  CA  GLY H 389     -25.841  59.463 -12.449  1.00 36.90           C  
ATOM   3049  CA  VAL H 390     -24.954  56.384 -10.492  1.00 50.38           C  
ATOM   3050  CA  ASN H 391     -23.894  55.951  -6.902  1.00 63.98           C  
ATOM   3051  CA  ARG H 392     -24.023  59.631  -6.054  1.00113.37           C  
ATOM   3052  CA  ASP H 393     -21.959  60.255  -9.135  1.00 47.03           C  
ATOM   3053  CA  ARG H 394     -23.197  62.249 -12.071  1.00 86.79           C  
ATOM   3054  CA  VAL H 395     -23.033  60.473 -15.379  1.00 47.36           C  
ATOM   3055  CA  ASN H 396     -22.517  62.861 -18.257  1.00 57.08           C  
ATOM   3056  CA  SER H 397     -21.988  60.082 -20.736  1.00 41.21           C  
ATOM   3057  CA  ILE H 398     -21.100  56.434 -21.103  1.00 37.16           C  
ATOM   3058  CA  ALA H 399     -17.492  56.946 -20.129  1.00 26.10           C  
ATOM   3059  CA  GLU H 400     -18.426  58.540 -16.835  1.00111.79           C  
ATOM   3060  CA  MET H 401     -20.874  55.747 -16.177  1.00 80.50           C  
ATOM   3061  CA  ARG H 402     -18.265  53.134 -16.758  1.00 90.04           C  
ATOM   3062  CA  LYS H 403     -16.037  54.879 -14.273  1.00108.38           C  
ATOM   3063  CA  VAL H 404     -18.526  54.353 -11.494  1.00 99.22           C  
ATOM   3064  CA  LEU H 405     -18.749  50.766 -12.587  1.00 66.56           C  
ATOM   3065  CA  ALA H 406     -15.002  50.561 -12.465  1.00 29.82           C  
ATOM   3066  CA  ALA H 407     -15.333  50.866  -8.720  1.00 25.77           C  
ATOM   3067  CA  LYS H 408     -17.654  47.906  -9.073  1.00 89.32           C  
ATOM   3068  CA  PRO H 409     -19.610  48.626  -5.991  1.00 65.61           C  
ATOM   3069  CA  ALA H 410     -21.641  45.662  -4.854  1.00 21.10           C  
ATOM   3070  CA  ILE H 411     -24.723  47.771  -5.174  1.00 87.36           C  
ATOM   3071  CA  ILE H 412     -25.126  50.224  -7.983  1.00 53.02           C  
ATOM   3072  CA  ALA H 413     -27.770  52.880  -8.084  1.00 50.28           C  
ATOM   3073  CA  LEU H 414     -28.235  53.963 -11.625  1.00170.79           C  
ATOM   3074  CA  GLN H 415     -30.064  57.362 -12.039  1.00170.33           C  
ATOM   3075  CA  ILE H 416     -32.828  57.981 -14.286  1.00127.20           C  
ATOM   3076  CA  VAL H 417     -35.356  60.526 -15.113  1.00 80.33           C  
ATOM   3077  CA  ARG H 418     -38.502  59.016 -16.421  1.00171.56           C  
ATOM   3078  CA  GLY H 419     -41.123  61.327 -17.759  1.00 22.98           C  
ATOM   3079  CA  ASN H 420     -41.045  64.419 -15.711  1.00 74.47           C  
ATOM   3080  CA  GLU H 421     -40.291  62.427 -12.654  1.00115.06           C  
ATOM   3081  CA  SER H 422     -37.377  60.856 -11.157  1.00103.05           C  
ATOM   3082  CA  ILE H 423     -36.842  57.265 -11.229  1.00200.67           C  
ATOM   3083  CA  TYR H 424     -34.778  55.485  -8.851  1.00262.41           C  
ATOM   3084  CA  LEU H 425     -32.873  52.404 -10.380  1.00234.15           C  
ATOM   3085  CA  LEU H 426     -31.194  49.458  -9.072  1.00189.84           C  
ATOM   3086  CA  MET H 427     -28.505  46.837  -9.432  1.00200.04           C  
ATOM   3087  CA  ARG H 428     -27.793  43.507  -7.790  1.00125.38           C  
TER    3088      ARG H 428                                                      
ATOM   3089  CA  PRO I  11      50.950  43.261 -46.643  1.00 44.51           C  
ATOM   3090  CA  LEU I  12      49.298  41.950 -43.541  1.00 70.31           C  
ATOM   3091  CA  PRO I  13      51.796  39.422 -42.477  1.00 98.17           C  
ATOM   3092  CA  SER I  14      50.907  35.846 -41.775  1.00 40.54           C  
ATOM   3093  CA  LEU I  15      50.155  34.776 -38.263  1.00 40.81           C  
ATOM   3094  CA  ALA I  16      52.200  31.659 -38.719  1.00 36.04           C  
ATOM   3095  CA  PRO I  17      55.427  33.438 -39.288  1.00 71.44           C  
ATOM   3096  CA  MET I  18      55.300  35.340 -36.044  1.00 60.72           C  
ATOM   3097  CA  LEU I  19      53.636  32.397 -34.391  1.00118.39           C  
ATOM   3098  CA  GLU I  20      56.459  29.996 -35.026  1.00 43.26           C  
ATOM   3099  CA  LYS I  21      59.004  31.985 -33.123  1.00 69.38           C  
ATOM   3100  CA  VAL I  22      56.873  32.898 -30.133  1.00146.71           C  
ATOM   3101  CA  LEU I  23      55.043  29.684 -29.399  1.00129.36           C  
ATOM   3102  CA  PRO I  24      57.766  27.806 -27.651  1.00 64.19           C  
ATOM   3103  CA  ALA I  25      57.646  30.541 -25.050  1.00 40.94           C  
ATOM   3104  CA  VAL I  26      54.146  29.616 -23.967  1.00111.13           C  
ATOM   3105  CA  VAL I  27      53.937  26.518 -21.878  1.00 44.22           C  
ATOM   3106  CA  SER I  28      51.377  24.307 -20.247  1.00 32.06           C  
ATOM   3107  CA  VAL I  29      51.306  24.040 -16.506  1.00 34.10           C  
ATOM   3108  CA  ARG I  30      50.232  20.878 -14.816  1.00141.52           C  
ATOM   3109  CA  VAL I  31      49.304  20.733 -11.192  1.00 51.20           C  
ATOM   3110  CA  GLU I  32      48.660  18.032  -8.645  1.00105.89           C  
ATOM   3111  CA  GLY I  33      47.594  18.472  -5.097  1.00 28.10           C  
ATOM   3112  CA  THR I  34      45.032  18.021  -2.363  1.00 41.62           C  
ATOM   3113  CA  ALA I  58      42.422  15.878   0.254  1.00 16.69           C  
ATOM   3114  CA  GLN I  59      41.840  13.560  -2.653  1.00156.44           C  
ATOM   3115  CA  PRO I  60      44.329  14.070  -5.333  1.00 72.02           C  
ATOM   3116  CA  PHE I  61      43.245  15.962  -8.384  1.00 51.45           C  
ATOM   3117  CA  GLU I  62      45.088  17.303 -11.352  1.00 25.07           C  
ATOM   3118  CA  GLY I  63      44.548  20.636 -12.980  1.00 17.32           C  
ATOM   3119  CA  LEU I  64      45.865  22.074 -16.178  1.00 81.36           C  
ATOM   3120  CA  GLY I  65      46.667  25.634 -17.083  1.00 21.88           C  
ATOM   3121  CA  SER I  66      49.214  27.570 -19.062  1.00 75.35           C  
ATOM   3122  CA  GLY I  67      52.079  29.911 -18.394  1.00 16.65           C  
ATOM   3123  CA  VAL I  68      54.534  32.099 -20.229  1.00 39.99           C  
ATOM   3124  CA  ILE I  69      58.292  32.002 -20.025  1.00 46.50           C  
ATOM   3125  CA  ILE I  70      59.425  35.441 -18.951  1.00 89.70           C  
ATOM   3126  CA  ASN I  71      63.075  34.673 -18.750  1.00132.02           C  
ATOM   3127  CA  ALA I  72      64.672  31.761 -20.448  1.00 37.63           C  
ATOM   3128  CA  SER I  73      67.849  31.788 -18.472  1.00 40.21           C  
ATOM   3129  CA  LYS I  74      66.274  31.900 -15.074  1.00141.67           C  
ATOM   3130  CA  GLY I  75      63.351  29.794 -16.159  1.00 28.29           C  
ATOM   3131  CA  TYR I  76      60.746  32.130 -14.741  1.00 66.29           C  
ATOM   3132  CA  VAL I  77      57.236  31.395 -15.879  1.00 37.38           C  
ATOM   3133  CA  LEU I  78      54.272  33.645 -15.239  1.00 56.66           C  
ATOM   3134  CA  THR I  79      50.910  32.120 -14.527  1.00130.48           C  
ATOM   3135  CA  ASN I  80      47.685  32.804 -12.738  1.00108.67           C  
ATOM   3136  CA  ASN I  81      47.643  32.271  -9.017  1.00 38.58           C  
ATOM   3137  CA  HIS I  82      44.451  30.298  -9.232  1.00 44.69           C  
ATOM   3138  CA  VAL I  83      46.107  27.740 -11.432  1.00 39.80           C  
ATOM   3139  CA  ILE I  84      48.918  27.301  -8.891  1.00122.61           C  
ATOM   3140  CA  ASN I  85      47.069  27.787  -5.613  1.00 74.00           C  
ATOM   3141  CA  GLN I  86      46.221  24.193  -4.654  1.00 94.39           C  
ATOM   3142  CA  ALA I  87      49.291  22.695  -6.326  1.00 66.52           C  
ATOM   3143  CA  GLN I  88      51.389  20.391  -4.213  1.00 49.37           C  
ATOM   3144  CA  LYS I  89      53.609  19.790  -7.203  1.00 29.83           C  
ATOM   3145  CA  ILE I  90      53.914  21.666 -10.446  1.00 72.56           C  
ATOM   3146  CA  SER I  91      55.271  20.591 -13.784  1.00 27.39           C  
ATOM   3147  CA  ILE I  92      55.711  22.555 -16.962  1.00 84.39           C  
ATOM   3148  CA  GLN I  93      55.576  21.128 -20.442  1.00 98.07           C  
ATOM   3149  CA  LEU I  94      57.006  22.670 -23.517  1.00103.99           C  
ATOM   3150  CA  ASN I  95      55.434  22.474 -26.931  1.00 38.79           C  
ATOM   3151  CA  ASP I  96      58.306  20.234 -27.884  1.00 47.57           C  
ATOM   3152  CA  GLY I  97      57.254  17.720 -25.280  1.00 31.52           C  
ATOM   3153  CA  ARG I  98      59.970  18.473 -22.780  1.00 67.76           C  
ATOM   3154  CA  GLU I  99      58.804  18.465 -19.211  1.00 40.43           C  
ATOM   3155  CA  PHE I 100      60.317  20.170 -16.218  1.00 37.41           C  
ATOM   3156  CA  ASP I 101      59.449  20.584 -12.585  1.00 30.03           C  
ATOM   3157  CA  ALA I 102      58.706  23.997 -11.214  1.00 27.23           C  
ATOM   3158  CA  LYS I 103      58.573  25.644  -7.840  1.00 35.71           C  
ATOM   3159  CA  LEU I 104      56.372  28.522  -6.844  1.00105.50           C  
ATOM   3160  CA  ILE I 105      58.523  31.590  -6.445  1.00 39.21           C  
ATOM   3161  CA  GLY I 106      55.677  33.738  -5.226  1.00 24.40           C  
ATOM   3162  CA  SER I 107      52.235  34.938  -6.123  1.00 99.82           C  
ATOM   3163  CA  ASP I 108      49.433  37.124  -4.972  1.00104.09           C  
ATOM   3164  CA  ASP I 109      45.693  36.666  -4.678  1.00 62.37           C  
ATOM   3165  CA  GLN I 110      44.301  40.064  -5.461  1.00 91.49           C  
ATOM   3166  CA  SER I 111      45.860  40.485  -8.910  1.00 62.18           C  
ATOM   3167  CA  ASP I 112      45.940  36.712  -9.395  1.00 69.25           C  
ATOM   3168  CA  ILE I 113      49.539  36.662 -10.630  1.00 92.02           C  
ATOM   3169  CA  ALA I 114      51.993  33.930  -9.707  1.00 32.42           C  
ATOM   3170  CA  LEU I 115      55.599  33.363 -10.645  1.00 99.96           C  
ATOM   3171  CA  LEU I 116      57.068  29.923 -11.173  1.00 50.65           C  
ATOM   3172  CA  GLN I 117      60.646  28.792 -11.556  1.00 59.39           C  
ATOM   3173  CA  ILE I 118      61.595  25.910 -13.770  1.00 44.72           C  
ATOM   3174  CA  GLN I 119      64.168  23.703 -12.216  1.00 51.69           C  
ATOM   3175  CA  ASN I 120      67.203  23.046 -14.345  1.00 47.31           C  
ATOM   3176  CA  PRO I 121      65.766  25.011 -17.201  1.00 61.62           C  
ATOM   3177  CA  SER I 122      67.594  24.403 -20.440  1.00 34.19           C  
ATOM   3178  CA  LYS I 123      67.315  25.737 -23.977  1.00 43.30           C  
ATOM   3179  CA  LEU I 124      64.190  27.734 -23.302  1.00 85.07           C  
ATOM   3180  CA  THR I 125      62.666  30.528 -25.313  1.00 94.33           C  
ATOM   3181  CA  GLN I 126      61.313  33.669 -23.743  1.00 96.50           C  
ATOM   3182  CA  ILE I 127      58.644  36.039 -24.895  1.00165.54           C  
ATOM   3183  CA  ALA I 128      59.120  39.725 -25.222  1.00 41.04           C  
ATOM   3184  CA  ILE I 129      56.785  41.960 -23.303  1.00111.78           C  
ATOM   3185  CA  ALA I 130      54.891  44.806 -24.936  1.00 34.42           C  
ATOM   3186  CA  ASP I 131      53.651  47.961 -23.303  1.00 38.77           C  
ATOM   3187  CA  SER I 132      50.062  47.266 -22.358  1.00 32.26           C  
ATOM   3188  CA  ASP I 133      49.423  50.951 -21.899  1.00 40.55           C  
ATOM   3189  CA  LYS I 134      49.713  51.431 -25.630  1.00124.18           C  
ATOM   3190  CA  LEU I 135      46.942  49.019 -26.546  1.00 95.93           C  
ATOM   3191  CA  ARG I 136      43.839  50.451 -28.152  1.00 98.38           C  
ATOM   3192  CA  VAL I 137      40.542  48.799 -28.872  1.00 92.51           C  
ATOM   3193  CA  GLY I 138      40.600  47.160 -32.246  1.00 25.88           C  
ATOM   3194  CA  ASP I 139      44.151  45.931 -31.909  1.00 28.31           C  
ATOM   3195  CA  PHE I 140      44.683  42.357 -32.990  1.00 45.56           C  
ATOM   3196  CA  ALA I 141      45.426  39.766 -30.366  1.00 31.95           C  
ATOM   3197  CA  VAL I 142      46.259  36.094 -30.299  1.00 91.48           C  
ATOM   3198  CA  ALA I 143      45.711  33.871 -27.326  1.00 37.18           C  
ATOM   3199  CA  VAL I 144      47.832  30.857 -26.637  1.00106.09           C  
ATOM   3200  CA  GLY I 145      47.195  28.289 -23.957  1.00 21.46           C  
ATOM   3201  CA  ASN I 146      45.853  24.826 -23.414  1.00 56.09           C  
ATOM   3202  CA  PRO I 147      42.148  24.718 -23.614  1.00 70.35           C  
ATOM   3203  CA  PHE I 148      40.659  21.541 -22.217  1.00 62.40           C  
ATOM   3204  CA  GLY I 149      44.198  20.293 -21.916  1.00 24.01           C  
ATOM   3205  CA  LEU I 150      44.238  19.543 -25.597  1.00 84.73           C  
ATOM   3206  CA  GLY I 151      47.693  20.969 -26.052  1.00 29.00           C  
ATOM   3207  CA  GLN I 152      49.077  24.256 -27.222  1.00 47.36           C  
ATOM   3208  CA  THR I 153      46.305  26.077 -29.008  1.00 35.43           C  
ATOM   3209  CA  ALA I 154      46.251  29.489 -30.582  1.00 33.73           C  
ATOM   3210  CA  THR I 155      43.151  31.566 -31.114  1.00 97.78           C  
ATOM   3211  CA  SER I 156      42.763  34.954 -32.701  1.00 35.75           C  
ATOM   3212  CA  GLY I 157      40.661  38.001 -31.986  1.00 18.42           C  
ATOM   3213  CA  ILE I 158      40.890  41.712 -31.301  1.00 94.48           C  
ATOM   3214  CA  VAL I 159      41.080  43.720 -28.124  1.00126.36           C  
ATOM   3215  CA  SER I 160      37.478  44.331 -27.277  1.00 48.73           C  
ATOM   3216  CA  ALA I 161      38.071  46.671 -24.386  1.00 47.20           C  
ATOM   3217  CA  LEU I 162      40.605  47.728 -21.824  1.00 99.39           C  
ATOM   3218  CA  GLY I 163      40.626  48.968 -18.295  1.00 32.78           C  
ATOM   3219  CA  ARG I 164      37.666  46.952 -17.297  1.00188.92           C  
ATOM   3220  CA  SER I 165      36.763  46.046 -13.787  1.00144.51           C  
ATOM   3221  CA  GLY I 166      33.872  45.611 -11.463  1.00 43.18           C  
ATOM   3222  CA  LEU I 167      33.752  42.059 -12.696  1.00 48.83           C  
ATOM   3223  CA  ASN I 168      34.508  41.126  -9.115  1.00 65.07           C  
ATOM   3224  CA  LEU I 169      36.586  38.306 -10.464  1.00 44.33           C  
ATOM   3225  CA  GLU I 170      39.598  39.518  -8.516  1.00 84.05           C  
ATOM   3226  CA  GLY I 171      40.471  42.048  -5.854  1.00 32.79           C  
ATOM   3227  CA  LEU I 172      42.458  44.127  -8.276  1.00 71.60           C  
ATOM   3228  CA  GLU I 173      41.246  44.184 -11.792  1.00 93.50           C  
ATOM   3229  CA  ASN I 174      42.077  45.888 -15.047  1.00104.17           C  
ATOM   3230  CA  PHE I 175      41.330  43.324 -17.569  1.00 83.26           C  
ATOM   3231  CA  ILE I 176      42.006  43.631 -21.198  1.00 84.76           C  
ATOM   3232  CA  GLN I 177      38.971  42.150 -22.834  1.00 63.71           C  
ATOM   3233  CA  THR I 178      39.377  40.026 -25.896  1.00133.56           C  
ATOM   3234  CA  ASP I 179      37.156  38.168 -28.351  1.00 65.28           C  
ATOM   3235  CA  ALA I 180      39.827  35.532 -28.850  1.00 45.99           C  
ATOM   3236  CA  SER I 181      38.472  32.187 -27.831  1.00 42.01           C  
ATOM   3237  CA  ILE I 182      39.490  31.518 -24.286  1.00 48.88           C  
ATOM   3238  CA  ASN I 183      38.369  28.407 -22.524  1.00 56.86           C  
ATOM   3239  CA  ARG I 184      39.188  26.555 -19.386  1.00 83.39           C  
ATOM   3240  CA  GLY I 185      42.847  25.691 -19.371  1.00 21.41           C  
ATOM   3241  CA  ASN I 186      43.660  29.030 -20.964  1.00 51.59           C  
ATOM   3242  CA  ALA I 187      44.451  30.594 -17.623  1.00 39.50           C  
ATOM   3243  CA  GLY I 188      48.020  31.709 -17.239  1.00 23.28           C  
ATOM   3244  CA  GLY I 189      48.323  31.636 -20.996  1.00 21.91           C  
ATOM   3245  CA  ALA I 190      49.572  34.457 -23.124  1.00 44.31           C  
ATOM   3246  CA  LEU I 191      47.719  37.019 -25.135  1.00 64.70           C  
ATOM   3247  CA  LEU I 192      49.991  38.337 -27.821  1.00 59.20           C  
ATOM   3248  CA  ASN I 193      50.037  41.147 -30.313  1.00 53.28           C  
ATOM   3249  CA  LEU I 194      50.918  40.770 -33.969  1.00 83.01           C  
ATOM   3250  CA  ASN I 195      54.499  41.310 -32.900  1.00 60.07           C  
ATOM   3251  CA  GLY I 196      54.289  38.202 -30.811  1.00 26.31           C  
ATOM   3252  CA  GLU I 197      54.895  40.356 -27.785  1.00 44.31           C  
ATOM   3253  CA  LEU I 198      53.045  39.690 -24.552  1.00151.40           C  
ATOM   3254  CA  ILE I 199      50.038  41.988 -24.134  1.00112.28           C  
ATOM   3255  CA  GLY I 200      48.647  40.212 -21.082  1.00 33.17           C  
ATOM   3256  CA  ILE I 201      47.984  36.946 -19.272  1.00 94.22           C  
ATOM   3257  CA  ASN I 202      44.567  35.436 -19.849  1.00 79.32           C  
ATOM   3258  CA  THR I 203      42.899  35.244 -16.457  1.00 79.89           C  
ATOM   3259  CA  ALA I 204      39.222  34.528 -16.954  1.00 57.57           C  
ATOM   3260  CA  ILE I 205      36.084  34.541 -19.040  1.00122.33           C  
ATOM   3261  CA  LEU I 206      32.438  35.295 -18.726  1.00 54.53           C  
ATOM   3262  CA  ALA I 207      30.430  32.445 -20.100  1.00 45.42           C  
ATOM   3263  CA  PRO I 208      27.064  31.206 -19.113  1.00 66.80           C  
ATOM   3264  CA  GLY I 209      27.761  27.844 -20.710  1.00 29.78           C  
ATOM   3265  CA  GLY I 210      31.186  27.532 -19.241  1.00 24.07           C  
ATOM   3266  CA  GLY I 211      32.400  27.730 -22.804  1.00 23.26           C  
ATOM   3267  CA  SER I 212      33.918  30.703 -24.567  1.00 54.10           C  
ATOM   3268  CA  VAL I 213      31.277  33.324 -25.280  1.00 58.05           C  
ATOM   3269  CA  GLY I 214      33.843  35.568 -26.875  1.00 35.08           C  
ATOM   3270  CA  ILE I 215      34.280  37.619 -23.755  1.00 43.98           C  
ATOM   3271  CA  GLY I 216      37.631  36.945 -22.163  1.00 20.12           C  
ATOM   3272  CA  PHE I 217      39.747  38.943 -19.779  1.00 43.57           C  
ATOM   3273  CA  ALA I 218      43.481  39.160 -19.355  1.00 33.86           C  
ATOM   3274  CA  ILE I 219      45.865  40.853 -16.964  1.00 70.90           C  
ATOM   3275  CA  PRO I 220      47.781  43.449 -18.816  1.00 83.23           C  
ATOM   3276  CA  SER I 221      51.403  42.751 -19.552  1.00 82.35           C  
ATOM   3277  CA  ASN I 222      52.501  45.826 -17.752  1.00 59.46           C  
ATOM   3278  CA  MET I 223      50.607  44.255 -15.003  1.00103.21           C  
ATOM   3279  CA  ALA I 224      52.276  40.893 -14.990  1.00 49.06           C  
ATOM   3280  CA  ARG I 225      55.661  42.278 -15.784  1.00109.61           C  
ATOM   3281  CA  THR I 226      56.350  44.398 -12.806  1.00 61.67           C  
ATOM   3282  CA  LEU I 227      54.276  42.167 -10.555  1.00109.96           C  
ATOM   3283  CA  ALA I 228      56.426  39.303 -11.664  1.00 46.62           C  
ATOM   3284  CA  GLN I 229      59.516  41.379 -11.278  1.00 81.24           C  
ATOM   3285  CA  GLN I 230      59.479  41.876  -7.578  1.00 87.01           C  
ATOM   3286  CA  LEU I 231      58.480  38.274  -7.174  1.00125.93           C  
ATOM   3287  CA  ILE I 232      61.972  37.639  -8.314  1.00 70.71           C  
ATOM   3288  CA  ASP I 233      63.142  41.062  -7.035  1.00171.27           C  
ATOM   3289  CA  PHE I 234      62.885  43.558  -5.371  1.00152.24           C  
ATOM   3290  CA  GLY I 235      60.022  41.661  -3.928  1.00 48.45           C  
ATOM   3291  CA  GLU I 236      59.304  43.431  -0.775  1.00 70.32           C  
ATOM   3292  CA  ILE I 237      57.402  40.570   0.694  1.00154.90           C  
ATOM   3293  CA  LYS I 238      54.771  42.708   2.235  1.00193.58           C  
ATOM   3294  CA  ARG I 239      52.159  43.301   1.343  1.00193.50           C  
ATOM   3295  CA  GLY I 240      52.905  42.063  -2.140  1.00 63.79           C  
ATOM   3296  CA  LEU I 241      49.379  42.888  -2.994  1.00116.42           C  
ATOM   3297  CA  LEU I 242      46.763  44.909  -1.208  1.00 80.39           C  
ATOM   3298  CA  GLY I 243      44.804  41.902  -0.089  1.00 47.24           C  
ATOM   3299  CA  ILE I 244      41.346  43.239  -0.764  1.00 68.03           C  
ATOM   3300  CA  LYS I 245      38.196  42.336  -2.598  1.00108.89           C  
ATOM   3301  CA  GLY I 246      36.219  44.889  -4.474  1.00 39.16           C  
ATOM   3302  CA  THR I 247      34.034  45.604  -7.426  1.00 76.28           C  
ATOM   3303  CA  GLU I 248      32.785  48.484  -9.507  1.00 60.81           C  
ATOM   3304  CA  MET I 249      31.535  51.404  -7.573  1.00 79.29           C  
ATOM   3305  CA  SER I 250      27.810  50.915  -7.574  1.00 39.26           C  
ATOM   3306  CA  ALA I 251      25.640  53.207  -9.586  1.00 37.59           C  
ATOM   3307  CA  ASP I 252      23.729  54.633  -6.673  1.00102.59           C  
ATOM   3308  CA  ILE I 253      26.857  55.503  -4.781  1.00 78.81           C  
ATOM   3309  CA  ALA I 254      28.429  56.680  -7.976  1.00 31.58           C  
ATOM   3310  CA  LYS I 255      25.641  59.153  -8.420  1.00 75.02           C  
ATOM   3311  CA  ALA I 256      26.042  60.649  -4.985  1.00 44.48           C  
ATOM   3312  CA  PHE I 257      29.808  60.605  -4.747  1.00 93.39           C  
ATOM   3313  CA  ASN I 258      30.593  62.200  -8.087  1.00 86.39           C  
ATOM   3314  CA  LEU I 259      34.231  61.480  -7.497  1.00108.70           C  
ATOM   3315  CA  ASP I 260      37.255  62.129  -9.576  1.00 57.65           C  
ATOM   3316  CA  VAL I 261      36.579  58.525 -10.364  1.00 54.69           C  
ATOM   3317  CA  GLN I 262      33.678  58.000 -12.744  1.00 53.51           C  
ATOM   3318  CA  ARG I 263      33.398  54.767 -10.922  1.00125.82           C  
ATOM   3319  CA  GLY I 264      35.890  53.838  -8.346  1.00 34.51           C  
ATOM   3320  CA  ALA I 265      37.307  50.809  -6.737  1.00 52.13           C  
ATOM   3321  CA  PHE I 266      34.944  49.991  -3.988  1.00147.45           C  
ATOM   3322  CA  VAL I 267      35.983  47.579  -1.351  1.00144.84           C  
ATOM   3323  CA  SER I 268      33.477  45.186   0.109  1.00 72.62           C  
ATOM   3324  CA  GLU I 269      35.911  43.390   2.295  1.00110.50           C  
ATOM   3325  CA  VAL I 270      38.975  43.446   4.476  1.00113.47           C  
ATOM   3326  CA  LEU I 271      41.439  40.606   4.254  1.00 54.96           C  
ATOM   3327  CA  PRO I 272      42.831  39.314   7.450  1.00 72.30           C  
ATOM   3328  CA  GLY I 273      46.501  39.867   8.144  1.00 32.39           C  
ATOM   3329  CA  SER I 274      46.330  41.296   4.750  1.00103.27           C  
ATOM   3330  CA  GLY I 275      47.890  44.188   3.095  1.00 56.56           C  
ATOM   3331  CA  SER I 276      44.716  46.035   3.540  1.00 79.29           C  
ATOM   3332  CA  ALA I 277      44.422  45.279   7.241  1.00 59.96           C  
ATOM   3333  CA  LYS I 278      47.430  46.879   8.957  1.00124.70           C  
ATOM   3334  CA  ALA I 279      47.275  50.190   7.183  1.00 60.03           C  
ATOM   3335  CA  GLY I 280      43.725  50.103   8.228  1.00 47.37           C  
ATOM   3336  CA  VAL I 281      42.026  50.047   4.852  1.00 65.55           C  
ATOM   3337  CA  LYS I 282      38.387  49.654   5.683  1.00120.79           C  
ATOM   3338  CA  ALA I 283      35.428  47.857   4.446  1.00 65.44           C  
ATOM   3339  CA  GLY I 284      33.329  49.848   2.067  1.00 88.57           C  
ATOM   3340  CA  ASP I 285      36.314  51.991   1.241  1.00118.32           C  
ATOM   3341  CA  ILE I 286      36.196  53.587  -2.038  1.00129.68           C  
ATOM   3342  CA  ILE I 287      39.614  53.870  -3.533  1.00 81.30           C  
ATOM   3343  CA  THR I 288      39.675  57.090  -5.493  1.00 81.38           C  
ATOM   3344  CA  SER I 289      43.271  57.082  -6.477  1.00104.80           C  
ATOM   3345  CA  LEU I 290      46.613  55.393  -6.382  1.00 77.01           C  
ATOM   3346  CA  ASN I 291      49.513  57.765  -6.299  1.00273.40           C  
ATOM   3347  CA  GLY I 292      50.276  60.533  -7.318  1.00137.12           C  
ATOM   3348  CA  LYS I 293      47.757  60.870 -10.100  1.00135.45           C  
ATOM   3349  CA  PRO I 294      44.106  60.159 -10.028  1.00 66.76           C  
ATOM   3350  CA  LEU I 295      42.999  56.620 -10.590  1.00123.05           C  
ATOM   3351  CA  ASN I 296      39.931  55.633 -12.514  1.00 85.21           C  
ATOM   3352  CA  SER I 297      37.511  52.820 -12.006  1.00103.96           C  
ATOM   3353  CA  PHE I 298      38.312  49.663 -10.229  1.00100.11           C  
ATOM   3354  CA  ALA I 299      39.440  48.670 -13.672  1.00 44.08           C  
ATOM   3355  CA  GLU I 300      42.163  51.209 -13.665  1.00 92.68           C  
ATOM   3356  CA  LEU I 301      42.986  50.033 -10.228  1.00 68.47           C  
ATOM   3357  CA  ARG I 302      44.352  46.670 -11.061  1.00261.76           C  
ATOM   3358  CA  SER I 303      45.717  48.081 -14.228  1.00 52.95           C  
ATOM   3359  CA  ARG I 304      48.182  50.130 -12.374  1.00115.63           C  
ATOM   3360  CA  ILE I 305      48.615  47.826  -9.382  1.00114.02           C  
ATOM   3361  CA  ALA I 306      48.693  44.693 -11.363  1.00 62.52           C  
ATOM   3362  CA  THR I 307      51.185  46.631 -13.372  1.00 54.79           C  
ATOM   3363  CA  THR I 308      53.260  47.671 -10.407  1.00 48.22           C  
ATOM   3364  CA  GLU I 309      55.715  45.720  -8.341  1.00137.07           C  
ATOM   3365  CA  PRO I 310      54.016  43.628  -5.800  1.00195.17           C  
ATOM   3366  CA  GLY I 311      55.742  44.791  -3.673  1.00128.33           C  
ATOM   3367  CA  THR I 312      56.264  48.440  -4.338  1.00116.69           C  
ATOM   3368  CA  LYS I 313      55.275  50.696  -1.519  1.00 89.70           C  
ATOM   3369  CA  VAL I 314      52.465  52.880  -2.680  1.00 39.07           C  
ATOM   3370  CA  LYS I 315      49.979  55.297  -1.211  1.00 92.58           C  
ATOM   3371  CA  LEU I 316      46.284  54.873  -1.669  1.00 91.57           C  
ATOM   3372  CA  GLY I 317      43.622  57.498  -1.554  1.00 51.44           C  
ATOM   3373  CA  LEU I 318      40.644  55.837  -0.014  1.00256.49           C  
ATOM   3374  CA  LEU I 319      37.303  57.660  -0.177  1.00291.99           C  
ATOM   3375  CA  ARG I 320      35.003  56.769   2.416  1.00336.43           C  
ATOM   3376  CA  ASN I 321      33.647  58.592   5.238  1.00249.47           C  
ATOM   3377  CA  GLY I 322      32.887  61.495   3.006  1.00 62.20           C  
ATOM   3378  CA  LYS I 323      36.095  62.561   4.588  1.00143.98           C  
ATOM   3379  CA  PRO I 324      39.271  62.142   2.651  1.00154.18           C  
ATOM   3380  CA  LEU I 325      42.052  59.715   3.426  1.00146.60           C  
ATOM   3381  CA  GLU I 326      45.593  58.799   2.551  1.00 97.54           C  
ATOM   3382  CA  VAL I 327      47.411  55.635   3.582  1.00105.53           C  
ATOM   3383  CA  GLU I 328      50.644  54.061   2.428  1.00110.88           C  
ATOM   3384  CA  VAL I 329      50.460  50.291   2.333  1.00135.85           C  
ATOM   3385  CA  SER I 340      50.069  22.993  27.557  1.00 55.68           C  
ATOM   3386  CA  ALA I 341      49.484  19.253  27.397  1.00 79.73           C  
ATOM   3387  CA  GLU I 342      46.342  19.560  25.335  1.00 60.35           C  
ATOM   3388  CA  MET I 343      47.869  20.133  21.985  1.00 45.91           C  
ATOM   3389  CA  ILE I 344      50.071  17.108  22.082  1.00 56.82           C  
ATOM   3390  CA  THR I 345      47.542  15.135  24.032  1.00164.33           C  
ATOM   3391  CA  PRO I 346      43.937  15.175  23.095  1.00178.37           C  
ATOM   3392  CA  ALA I 347      41.479  17.125  25.237  1.00 88.61           C  
ATOM   3393  CA  LEU I 348      43.686  16.355  28.209  1.00210.87           C  
ATOM   3394  CA  GLU I 349      44.023  19.757  29.746  1.00141.15           C  
ATOM   3395  CA  GLY I 350      46.861  20.006  32.134  1.00 28.81           C  
ATOM   3396  CA  ALA I 351      50.346  21.260  32.689  1.00 36.12           C  
ATOM   3397  CA  THR I 352      51.979  23.122  29.876  1.00 28.45           C  
ATOM   3398  CA  LEU I 353      54.705  21.422  27.924  1.00 58.21           C  
ATOM   3399  CA  SER I 354      57.984  22.729  26.615  1.00 86.13           C  
ATOM   3400  CA  ASP I 355      60.594  21.303  24.258  1.00 47.56           C  
ATOM   3401  CA  GLY I 356      64.373  21.021  24.768  1.00 49.50           C  
ATOM   3402  CA  GLN I 357      65.846  19.948  28.031  1.00153.43           C  
ATOM   3403  CA  LEU I 358      65.352  23.426  28.665  1.00159.82           C  
ATOM   3404  CA  LYS I 359      68.704  24.474  27.275  1.00161.48           C  
ATOM   3405  CA  ASP I 360      70.599  21.244  27.702  1.00 48.15           C  
ATOM   3406  CA  GLY I 361      70.672  18.185  25.567  1.00 24.94           C  
ATOM   3407  CA  GLY I 362      67.059  17.338  25.213  1.00 37.51           C  
ATOM   3408  CA  LYS I 363      66.189  14.695  27.711  1.00 87.81           C  
ATOM   3409  CA  GLY I 364      62.726  15.191  26.361  1.00 36.37           C  
ATOM   3410  CA  ILE I 365      59.721  17.419  26.684  1.00133.82           C  
ATOM   3411  CA  LYS I 366      59.325  19.387  29.877  1.00101.87           C  
ATOM   3412  CA  ILE I 367      56.054  19.948  31.630  1.00 63.03           C  
ATOM   3413  CA  ASP I 368      56.183  23.497  32.860  1.00 58.54           C  
ATOM   3414  CA  GLU I 369      53.446  23.697  35.414  1.00 86.54           C  
ATOM   3415  CA  VAL I 370      50.593  21.618  36.678  1.00133.10           C  
ATOM   3416  CA  VAL I 371      47.068  22.988  36.359  1.00178.16           C  
ATOM   3417  CA  LYS I 372      46.341  20.129  38.816  1.00177.50           C  
ATOM   3418  CA  GLY I 373      42.595  20.523  38.850  1.00 39.76           C  
ATOM   3419  CA  SER I 374      42.962  19.526  35.178  1.00 44.53           C  
ATOM   3420  CA  PRO I 375      43.016  16.002  33.938  1.00165.44           C  
ATOM   3421  CA  ALA I 376      46.641  16.026  32.909  1.00 49.94           C  
ATOM   3422  CA  ALA I 377      47.001  16.291  36.638  1.00 51.00           C  
ATOM   3423  CA  GLN I 378      44.429  13.609  37.293  1.00 65.99           C  
ATOM   3424  CA  ALA I 379      46.432  10.800  35.749  1.00 74.13           C  
ATOM   3425  CA  GLY I 380      49.695  11.863  37.340  1.00 87.41           C  
ATOM   3426  CA  LEU I 381      51.564  14.448  35.411  1.00 76.79           C  
ATOM   3427  CA  GLN I 382      53.361  16.570  37.977  1.00127.67           C  
ATOM   3428  CA  LYS I 383      55.419  19.610  37.159  1.00128.37           C  
ATOM   3429  CA  ASP I 384      59.144  19.468  36.428  1.00 83.99           C  
ATOM   3430  CA  ASP I 385      58.861  16.034  34.938  1.00 66.51           C  
ATOM   3431  CA  VAL I 386      60.841  15.322  31.788  1.00 62.56           C  
ATOM   3432  CA  ILE I 387      59.380  12.930  29.289  1.00 89.98           C  
ATOM   3433  CA  ILE I 388      62.359  11.088  27.935  1.00117.55           C  
ATOM   3434  CA  GLY I 389      60.582   9.026  25.359  1.00 97.48           C  
ATOM   3435  CA  VAL I 390      57.199   7.610  24.254  1.00183.11           C  
ATOM   3436  CA  ASN I 391      56.267   3.894  24.089  1.00104.74           C  
ATOM   3437  CA  ARG I 392      59.780   2.479  23.893  1.00131.45           C  
ATOM   3438  CA  ASP I 393      60.664   5.429  21.740  1.00 66.05           C  
ATOM   3439  CA  ARG I 394      62.888   8.210  22.866  1.00 77.55           C  
ATOM   3440  CA  VAL I 395      61.320  11.623  22.751  1.00 65.69           C  
ATOM   3441  CA  ASN I 396      63.906  14.283  22.132  1.00 53.05           C  
ATOM   3442  CA  SER I 397      61.321  16.939  21.548  1.00 47.03           C  
ATOM   3443  CA  ILE I 398      57.663  17.694  21.100  1.00 37.41           C  
ATOM   3444  CA  ALA I 399      57.759  16.772  17.454  1.00 26.33           C  
ATOM   3445  CA  GLU I 400      59.065  13.315  18.162  1.00 39.57           C  
ATOM   3446  CA  MET I 401      56.566  12.758  20.924  1.00 46.72           C  
ATOM   3447  CA  ARG I 402      53.851  13.751  18.537  1.00122.45           C  
ATOM   3448  CA  LYS I 403      55.137  11.171  16.100  1.00 64.89           C  
ATOM   3449  CA  VAL I 404      54.606   8.196  18.377  1.00125.99           C  
ATOM   3450  CA  LEU I 405      51.223   9.617  19.249  1.00 54.57           C  
ATOM   3451  CA  ALA I 406      50.577   9.662  15.543  1.00 25.64           C  
ATOM   3452  CA  ALA I 407      50.665   5.893  15.682  1.00 32.00           C  
ATOM   3453  CA  LYS I 408      48.066   6.339  18.379  1.00 96.81           C  
ATOM   3454  CA  PRO I 409      48.623   3.179  20.311  1.00163.63           C  
ATOM   3455  CA  ALA I 410      45.821   2.295  22.644  1.00 26.35           C  
ATOM   3456  CA  ILE I 411      48.338   2.430  25.425  1.00112.60           C  
ATOM   3457  CA  ILE I 412      50.675   5.383  25.535  1.00119.10           C  
ATOM   3458  CA  ALA I 413      53.441   5.004  28.020  1.00 86.55           C  
ATOM   3459  CA  LEU I 414      54.945   8.309  29.267  1.00160.91           C  
ATOM   3460  CA  GLN I 415      58.282   8.203  30.894  1.00223.23           C  
ATOM   3461  CA  ILE I 416      59.185  11.080  32.732  1.00169.07           C  
ATOM   3462  CA  VAL I 417      62.207  11.518  34.848  1.00 76.39           C  
ATOM   3463  CA  ARG I 418      61.341  12.828  38.241  1.00112.08           C  
ATOM   3464  CA  GLY I 419      64.249  13.982  40.309  1.00 28.62           C  
ATOM   3465  CA  ASN I 420      66.915  11.401  39.936  1.00 55.41           C  
ATOM   3466  CA  GLU I 421      64.200   8.852  39.581  1.00 60.95           C  
ATOM   3467  CA  SER I 422      62.378   7.426  36.664  1.00 59.31           C  
ATOM   3468  CA  ILE I 423      58.662   8.248  36.019  1.00104.30           C  
ATOM   3469  CA  TYR I 424      56.031   6.021  34.421  1.00235.93           C  
ATOM   3470  CA  LEU I 425      53.046   7.913  33.308  1.00137.01           C  
ATOM   3471  CA  LEU I 426      50.502   6.103  31.376  1.00236.19           C  
ATOM   3472  CA  MET I 427      47.660   7.761  29.200  1.00203.64           C  
ATOM   3473  CA  ARG I 428      44.164   6.133  28.776  1.00138.43           C  
TER    3474      ARG I 428                                                      
ATOM   3475  CA  PRO J  11     -40.863 -44.219 -43.688  1.00 55.91           C  
ATOM   3476  CA  LEU J  12     -40.330 -40.547 -43.927  1.00110.71           C  
ATOM   3477  CA  PRO J  13     -39.702 -39.632 -47.418  1.00111.92           C  
ATOM   3478  CA  SER J  14     -36.355 -40.396 -48.821  1.00 88.00           C  
ATOM   3479  CA  LEU J  15     -35.018 -36.887 -48.702  1.00 85.70           C  
ATOM   3480  CA  ALA J  16     -32.035 -37.707 -50.826  1.00 37.49           C  
ATOM   3481  CA  PRO J  17     -33.884 -38.134 -54.030  1.00 69.40           C  
ATOM   3482  CA  MET J  18     -35.617 -34.798 -53.698  1.00 34.19           C  
ATOM   3483  CA  LEU J  19     -32.474 -33.144 -52.449  1.00 44.01           C  
ATOM   3484  CA  GLU J  20     -30.200 -34.223 -55.228  1.00 48.35           C  
ATOM   3485  CA  LYS J  21     -32.152 -32.314 -57.822  1.00132.53           C  
ATOM   3486  CA  VAL J  22     -32.736 -29.197 -55.714  1.00111.28           C  
ATOM   3487  CA  LEU J  23     -29.416 -28.711 -53.951  1.00117.24           C  
ATOM   3488  CA  PRO J  24     -27.533 -27.107 -56.765  1.00 66.56           C  
ATOM   3489  CA  ALA J  25     -30.064 -24.290 -56.648  1.00 31.26           C  
ATOM   3490  CA  VAL J  26     -28.876 -23.193 -53.232  1.00 34.34           C  
ATOM   3491  CA  VAL J  27     -25.617 -21.326 -53.174  1.00 36.68           C  
ATOM   3492  CA  SER J  28     -23.233 -19.832 -50.687  1.00 35.70           C  
ATOM   3493  CA  VAL J  29     -22.562 -16.155 -50.795  1.00108.81           C  
ATOM   3494  CA  ARG J  30     -19.295 -14.660 -49.708  1.00 88.25           C  
ATOM   3495  CA  VAL J  31     -18.868 -11.024 -48.859  1.00 45.56           C  
ATOM   3496  CA  GLU J  32     -16.012  -8.616 -48.198  1.00 49.10           C  
ATOM   3497  CA  GLY J  33     -16.200  -5.013 -47.106  1.00 29.05           C  
ATOM   3498  CA  THR J  34     -15.769  -2.296 -44.505  1.00 50.83           C  
ATOM   3499  CA  ALA J  58     -13.165   0.488 -41.763  1.00 48.60           C  
ATOM   3500  CA  GLN J  59     -11.682  -2.858 -40.975  1.00146.13           C  
ATOM   3501  CA  PRO J  60     -11.861  -5.408 -43.644  1.00 74.67           C  
ATOM   3502  CA  PHE J  61     -14.119  -8.301 -42.810  1.00 51.34           C  
ATOM   3503  CA  GLU J  62     -15.376 -11.372 -44.561  1.00 25.16           C  
ATOM   3504  CA  GLY J  63     -18.823 -12.772 -44.135  1.00 22.00           C  
ATOM   3505  CA  LEU J  64     -20.492 -15.924 -45.320  1.00 88.76           C  
ATOM   3506  CA  GLY J  65     -24.136 -16.482 -46.066  1.00 23.59           C  
ATOM   3507  CA  SER J  66     -26.336 -18.357 -48.477  1.00 80.94           C  
ATOM   3508  CA  GLY J  67     -28.657 -17.565 -51.316  1.00 23.25           C  
ATOM   3509  CA  VAL J  68     -31.041 -19.271 -53.681  1.00 60.88           C  
ATOM   3510  CA  ILE J  69     -31.025 -19.177 -57.443  1.00102.17           C  
ATOM   3511  CA  ILE J  70     -34.395 -17.824 -58.480  1.00 85.20           C  
ATOM   3512  CA  ASN J  71     -33.667 -17.509 -62.172  1.00 41.15           C  
ATOM   3513  CA  ALA J  72     -31.035 -19.651 -63.791  1.00 32.52           C  
ATOM   3514  CA  SER J  73     -30.919 -17.768 -67.041  1.00 31.03           C  
ATOM   3515  CA  LYS J  74     -30.662 -14.356 -65.460  1.00128.84           C  
ATOM   3516  CA  GLY J  75     -28.607 -15.616 -62.606  1.00 28.75           C  
ATOM   3517  CA  TYR J  76     -30.739 -13.898 -60.012  1.00 64.67           C  
ATOM   3518  CA  VAL J  77     -30.005 -15.016 -56.489  1.00 36.82           C  
ATOM   3519  CA  LEU J  78     -32.164 -14.133 -53.538  1.00111.65           C  
ATOM   3520  CA  THR J  79     -30.507 -13.517 -50.208  1.00 49.59           C  
ATOM   3521  CA  ASN J  80     -30.951 -11.598 -47.023  1.00 57.48           C  
ATOM   3522  CA  ASN J  81     -30.132  -7.939 -47.062  1.00 56.86           C  
ATOM   3523  CA  HIS J  82     -28.103  -8.194 -43.911  1.00 56.38           C  
ATOM   3524  CA  VAL J  83     -25.825 -10.677 -45.548  1.00 67.82           C  
ATOM   3525  CA  ILE J  84     -25.265  -8.245 -48.427  1.00132.31           C  
ATOM   3526  CA  ASN J  85     -25.452  -4.855 -46.767  1.00124.85           C  
ATOM   3527  CA  GLN J  86     -21.813  -4.285 -45.800  1.00 57.74           C  
ATOM   3528  CA  ALA J  87     -20.495  -6.045 -48.905  1.00 70.22           C  
ATOM   3529  CA  GLN J  88     -18.100  -4.100 -51.022  1.00137.71           C  
ATOM   3530  CA  LYS J  89     -17.687  -7.182 -53.189  1.00 38.81           C  
ATOM   3531  CA  ILE J  90     -19.787 -10.296 -53.456  1.00 44.67           C  
ATOM   3532  CA  SER J  91     -19.097 -13.739 -54.826  1.00 83.30           C  
ATOM   3533  CA  ILE J  92     -21.277 -16.778 -55.022  1.00 56.71           C  
ATOM   3534  CA  GLN J  93     -20.179 -20.360 -54.994  1.00 41.11           C  
ATOM   3535  CA  LEU J  94     -22.049 -23.353 -56.304  1.00 48.50           C  
ATOM   3536  CA  ASN J  95     -22.086 -26.740 -54.644  1.00 44.81           C  
ATOM   3537  CA  ASP J  96     -20.080 -27.978 -57.585  1.00 46.94           C  
ATOM   3538  CA  GLY J  97     -17.307 -25.613 -56.632  1.00 32.70           C  
ATOM   3539  CA  ARG J  98     -17.766 -23.138 -59.432  1.00 74.62           C  
ATOM   3540  CA  GLU J  99     -17.672 -19.567 -58.263  1.00 92.80           C  
ATOM   3541  CA  PHE J 100     -18.976 -16.378 -59.770  1.00 54.07           C  
ATOM   3542  CA  ASP J 101     -19.034 -12.650 -59.162  1.00123.76           C  
ATOM   3543  CA  ALA J 102     -22.300 -11.045 -58.190  1.00 37.65           C  
ATOM   3544  CA  LYS J 103     -23.691  -7.547 -58.152  1.00 36.88           C  
ATOM   3545  CA  LEU J 104     -26.454  -6.291 -55.955  1.00 48.58           C  
ATOM   3546  CA  ILE J 105     -29.525  -5.672 -58.034  1.00103.34           C  
ATOM   3547  CA  GLY J 106     -31.404  -4.162 -55.137  1.00 24.74           C  
ATOM   3548  CA  SER J 107     -32.643  -4.899 -51.666  1.00 98.82           C  
ATOM   3549  CA  ASP J 108     -34.614  -3.441 -48.843  1.00102.19           C  
ATOM   3550  CA  ASP J 109     -33.994  -3.124 -45.137  1.00 64.69           C  
ATOM   3551  CA  GLN J 110     -37.429  -3.521 -43.702  1.00104.28           C  
ATOM   3552  CA  SER J 111     -38.231  -6.986 -45.064  1.00121.31           C  
ATOM   3553  CA  ASP J 112     -34.534  -7.861 -45.272  1.00 76.17           C  
ATOM   3554  CA  ILE J 113     -34.633  -9.218 -48.801  1.00 47.23           C  
ATOM   3555  CA  ALA J 114     -31.962  -8.547 -51.385  1.00 32.59           C  
ATOM   3556  CA  LEU J 115     -31.521  -9.631 -54.962  1.00 96.54           C  
ATOM   3557  CA  LEU J 116     -28.176 -10.356 -56.537  1.00 85.58           C  
ATOM   3558  CA  GLN J 117     -27.250 -11.196 -60.070  1.00115.46           C  
ATOM   3559  CA  ILE J 118     -24.455 -13.519 -61.052  1.00109.43           C  
ATOM   3560  CA  GLN J 119     -22.135 -12.170 -63.664  1.00101.02           C  
ATOM   3561  CA  ASN J 120     -21.957 -14.400 -66.713  1.00 55.67           C  
ATOM   3562  CA  PRO J 121     -23.972 -17.107 -65.086  1.00 67.39           C  
ATOM   3563  CA  SER J 122     -23.748 -20.416 -66.871  1.00 40.40           C  
ATOM   3564  CA  LYS J 123     -25.364 -23.819 -66.494  1.00 48.61           C  
ATOM   3565  CA  LEU J 124     -27.195 -22.906 -63.351  1.00 77.84           C  
ATOM   3566  CA  THR J 125     -30.126 -24.617 -61.707  1.00 96.00           C  
ATOM   3567  CA  GLN J 126     -33.186 -22.804 -60.447  1.00127.99           C  
ATOM   3568  CA  ILE J 127     -35.388 -23.505 -57.491  1.00106.80           C  
ATOM   3569  CA  ALA J 128     -39.120 -23.743 -57.873  1.00 33.88           C  
ATOM   3570  CA  ILE J 129     -41.189 -21.557 -55.626  1.00 71.06           C  
ATOM   3571  CA  ALA J 130     -44.079 -22.866 -53.592  1.00 35.59           C  
ATOM   3572  CA  ASP J 131     -47.078 -21.002 -52.270  1.00 39.08           C  
ATOM   3573  CA  SER J 132     -46.185 -19.964 -48.742  1.00 38.33           C  
ATOM   3574  CA  ASP J 133     -49.733 -19.170 -47.803  1.00 58.42           C  
ATOM   3575  CA  LYS J 134     -50.586 -22.848 -48.180  1.00136.90           C  
ATOM   3576  CA  LEU J 135     -48.226 -23.978 -45.452  1.00 97.14           C  
ATOM   3577  CA  ARG J 136     -49.676 -25.196 -42.189  1.00 69.11           C  
ATOM   3578  CA  VAL J 137     -48.009 -26.089 -38.944  1.00 28.07           C  
ATOM   3579  CA  GLY J 138     -46.695 -29.605 -38.985  1.00 25.78           C  
ATOM   3580  CA  ASP J 139     -45.574 -29.637 -42.557  1.00122.14           C  
ATOM   3581  CA  PHE J 140     -42.073 -30.878 -43.217  1.00 60.39           C  
ATOM   3582  CA  ALA J 141     -39.298 -28.481 -44.028  1.00 31.62           C  
ATOM   3583  CA  VAL J 142     -35.658 -28.748 -44.967  1.00 30.89           C  
ATOM   3584  CA  ALA J 143     -33.190 -25.950 -44.590  1.00 27.38           C  
ATOM   3585  CA  VAL J 144     -30.171 -25.610 -46.799  1.00 29.23           C  
ATOM   3586  CA  GLY J 145     -27.375 -23.140 -46.331  1.00 19.44           C  
ATOM   3587  CA  ASN J 146     -23.851 -22.867 -45.090  1.00 56.22           C  
ATOM   3588  CA  PRO J 147     -23.664 -22.951 -41.385  1.00148.50           C  
ATOM   3589  CA  PHE J 148     -20.332 -21.849 -39.998  1.00 66.06           C  
ATOM   3590  CA  GLY J 149     -19.179 -21.740 -43.582  1.00 25.88           C  
ATOM   3591  CA  LEU J 150     -18.788 -25.496 -43.556  1.00 86.97           C  
ATOM   3592  CA  GLY J 151     -20.295 -25.913 -46.981  1.00 30.93           C  
ATOM   3593  CA  GLN J 152     -23.735 -26.772 -48.195  1.00117.67           C  
ATOM   3594  CA  THR J 153     -25.574 -28.365 -45.335  1.00 40.63           C  
ATOM   3595  CA  ALA J 154     -29.110 -29.629 -45.124  1.00 26.68           C  
ATOM   3596  CA  THR J 155     -31.144 -29.868 -41.959  1.00 30.02           C  
ATOM   3597  CA  SER J 156     -34.638 -31.158 -41.433  1.00 32.64           C  
ATOM   3598  CA  GLY J 157     -37.566 -30.125 -39.298  1.00 20.54           C  
ATOM   3599  CA  ILE J 158     -41.215 -29.137 -39.428  1.00 44.87           C  
ATOM   3600  CA  VAL J 159     -42.947 -25.814 -39.713  1.00 46.65           C  
ATOM   3601  CA  SER J 160     -43.359 -24.744 -36.112  1.00 51.02           C  
ATOM   3602  CA  ALA J 161     -45.493 -21.686 -36.682  1.00 39.29           C  
ATOM   3603  CA  LEU J 162     -46.390 -19.077 -39.234  1.00 61.11           C  
ATOM   3604  CA  GLY J 163     -47.370 -15.465 -39.239  1.00 35.79           C  
ATOM   3605  CA  ARG J 164     -44.883 -14.602 -36.559  1.00234.20           C  
ATOM   3606  CA  SER J 165     -43.800 -11.133 -35.810  1.00 85.25           C  
ATOM   3607  CA  GLY J 166     -43.042  -8.827 -32.970  1.00 34.37           C  
ATOM   3608  CA  LEU J 167     -39.620 -10.431 -33.002  1.00105.14           C  
ATOM   3609  CA  ASN J 168     -38.311  -6.966 -33.761  1.00 65.91           C  
ATOM   3610  CA  LEU J 169     -35.702  -8.490 -35.973  1.00137.03           C  
ATOM   3611  CA  GLU J 170     -36.981  -6.562 -38.970  1.00103.23           C  
ATOM   3612  CA  GLY J 171     -39.294  -3.684 -39.751  1.00 35.65           C  
ATOM   3613  CA  LEU J 172     -41.651  -5.977 -41.560  1.00 92.55           C  
ATOM   3614  CA  GLU J 173     -41.920  -9.466 -40.389  1.00173.56           C  
ATOM   3615  CA  ASN J 174     -43.977 -12.554 -41.015  1.00126.96           C  
ATOM   3616  CA  PHE J 175     -41.636 -15.291 -40.293  1.00123.22           C  
ATOM   3617  CA  ILE J 176     -42.289 -18.901 -40.860  1.00246.29           C  
ATOM   3618  CA  GLN J 177     -40.865 -20.564 -37.827  1.00150.75           C  
ATOM   3619  CA  THR J 178     -39.069 -23.843 -38.127  1.00133.90           C  
ATOM   3620  CA  ASP J 179     -37.264 -26.292 -35.839  1.00 88.50           C  
ATOM   3621  CA  ALA J 180     -34.815 -27.218 -38.584  1.00 45.73           C  
ATOM   3622  CA  SER J 181     -31.385 -26.392 -37.321  1.00 43.57           C  
ATOM   3623  CA  ILE J 182     -30.388 -23.004 -38.550  1.00 44.85           C  
ATOM   3624  CA  ASN J 183     -27.146 -21.420 -37.524  1.00 42.53           C  
ATOM   3625  CA  ARG J 184     -24.993 -18.522 -38.496  1.00 71.46           C  
ATOM   3626  CA  GLY J 185     -24.285 -18.699 -42.183  1.00 23.64           C  
ATOM   3627  CA  ASN J 186     -27.772 -19.996 -42.862  1.00 53.67           C  
ATOM   3628  CA  ALA J 187     -28.993 -16.521 -43.720  1.00 47.93           C  
ATOM   3629  CA  GLY J 188     -30.246 -16.163 -47.252  1.00 24.06           C  
ATOM   3630  CA  GLY J 189     -30.471 -19.925 -47.448  1.00 20.84           C  
ATOM   3631  CA  ALA J 190     -33.499 -21.836 -48.557  1.00 41.28           C  
ATOM   3632  CA  LEU J 191     -36.235 -23.499 -46.578  1.00 65.01           C  
ATOM   3633  CA  LEU J 192     -37.760 -26.185 -48.731  1.00 55.29           C  
ATOM   3634  CA  ASN J 193     -40.782 -28.422 -48.652  1.00 50.27           C  
ATOM   3635  CA  LEU J 194     -40.740 -32.135 -49.375  1.00100.62           C  
ATOM   3636  CA  ASN J 195     -41.200 -31.204 -53.009  1.00 49.46           C  
ATOM   3637  CA  GLY J 196     -37.968 -29.282 -52.923  1.00 23.68           C  
ATOM   3638  CA  GLU J 197     -39.910 -26.122 -53.595  1.00 39.45           C  
ATOM   3639  CA  LEU J 198     -38.907 -22.900 -51.878  1.00126.33           C  
ATOM   3640  CA  ILE J 199     -41.114 -22.179 -48.868  1.00 76.20           C  
ATOM   3641  CA  GLY J 200     -39.057 -19.284 -47.532  1.00 30.07           C  
ATOM   3642  CA  ILE J 201     -35.636 -17.798 -47.014  1.00 77.57           C  
ATOM   3643  CA  ASN J 202     -34.048 -18.365 -43.640  1.00 69.26           C  
ATOM   3644  CA  THR J 203     -33.558 -14.950 -42.101  1.00 90.71           C  
ATOM   3645  CA  ALA J 204     -32.747 -15.396 -38.431  1.00 54.51           C  
ATOM   3646  CA  ILE J 205     -32.888 -17.413 -35.259  1.00 96.90           C  
ATOM   3647  CA  LEU J 206     -33.459 -16.878 -31.591  1.00 58.69           C  
ATOM   3648  CA  ALA J 207     -30.752 -18.466 -29.530  1.00 44.19           C  
ATOM   3649  CA  PRO J 208     -29.305 -17.447 -26.256  1.00141.80           C  
ATOM   3650  CA  GLY J 209     -26.147 -19.403 -26.997  1.00 32.68           C  
ATOM   3651  CA  GLY J 210     -25.783 -18.079 -30.479  1.00 22.40           C  
ATOM   3652  CA  GLY J 211     -26.312 -21.643 -31.575  1.00 24.42           C  
ATOM   3653  CA  SER J 212     -29.466 -23.179 -32.953  1.00 56.25           C  
ATOM   3654  CA  VAL J 213     -32.078 -23.552 -30.230  1.00 66.72           C  
ATOM   3655  CA  GLY J 214     -34.528 -25.030 -32.666  1.00 39.91           C  
ATOM   3656  CA  ILE J 215     -36.327 -21.778 -33.214  1.00 71.40           C  
ATOM   3657  CA  GLY J 216     -35.588 -20.329 -36.606  1.00 30.82           C  
ATOM   3658  CA  PHE J 217     -37.394 -17.799 -38.719  1.00146.22           C  
ATOM   3659  CA  ALA J 218     -37.699 -17.519 -42.466  1.00 39.19           C  
ATOM   3660  CA  ILE J 219     -39.320 -15.039 -44.772  1.00152.64           C  
ATOM   3661  CA  PRO J 220     -42.020 -16.725 -46.650  1.00100.33           C  
ATOM   3662  CA  SER J 221     -41.608 -17.662 -50.268  1.00 43.59           C  
ATOM   3663  CA  ASN J 222     -44.448 -15.515 -51.350  1.00 68.78           C  
ATOM   3664  CA  MET J 223     -42.534 -12.936 -49.528  1.00134.68           C  
ATOM   3665  CA  ALA J 224     -39.298 -13.223 -51.359  1.00 53.82           C  
ATOM   3666  CA  ARG J 225     -40.904 -13.952 -54.669  1.00100.97           C  
ATOM   3667  CA  THR J 226     -42.774 -10.797 -55.317  1.00 64.61           C  
ATOM   3668  CA  LEU J 227     -40.270  -8.682 -53.401  1.00113.18           C  
ATOM   3669  CA  ALA J 228     -37.601 -10.138 -55.599  1.00 44.35           C  
ATOM   3670  CA  GLN J 229     -39.640  -9.604 -58.695  1.00 76.68           C  
ATOM   3671  CA  GLN J 230     -39.971  -5.876 -58.469  1.00 74.56           C  
ATOM   3672  CA  LEU J 231     -36.290  -5.770 -57.712  1.00 51.23           C  
ATOM   3673  CA  ILE J 232     -35.760  -6.938 -61.223  1.00 61.34           C  
ATOM   3674  CA  ASP J 233     -39.069  -5.435 -62.380  1.00166.82           C  
ATOM   3675  CA  PHE J 234     -41.100  -3.365 -62.074  1.00208.36           C  
ATOM   3676  CA  GLY J 235     -38.849  -1.846 -59.507  1.00 42.90           C  
ATOM   3677  CA  GLU J 236     -41.045   1.122 -58.719  1.00 52.99           C  
ATOM   3678  CA  ILE J 237     -38.857   3.411 -56.729  1.00 41.49           C  
ATOM   3679  CA  LYS J 238     -41.539   4.330 -54.296  1.00203.99           C  
ATOM   3680  CA  ARG J 239     -41.946   3.171 -51.755  1.00239.93           C  
ATOM   3681  CA  GLY J 240     -39.480   0.375 -52.296  1.00 55.61           C  
ATOM   3682  CA  LEU J 241     -40.407  -0.491 -48.796  1.00138.96           C  
ATOM   3683  CA  LEU J 242     -41.780   1.293 -45.808  1.00 89.20           C  
ATOM   3684  CA  GLY J 243     -38.495   1.882 -44.134  1.00 57.95           C  
ATOM   3685  CA  ILE J 244     -39.655   1.472 -40.564  1.00 96.84           C  
ATOM   3686  CA  LYS J 245     -38.935  -0.457 -37.428  1.00120.75           C  
ATOM   3687  CA  GLY J 246     -41.653  -2.022 -35.414  1.00 37.21           C  
ATOM   3688  CA  THR J 247     -42.633  -4.860 -33.209  1.00 49.03           C  
ATOM   3689  CA  GLU J 248     -45.646  -6.637 -31.868  1.00 77.94           C  
ATOM   3690  CA  MET J 249     -47.956  -5.077 -29.388  1.00 79.01           C  
ATOM   3691  CA  SER J 250     -46.963  -5.660 -25.795  1.00 83.23           C  
ATOM   3692  CA  ALA J 251     -48.682  -8.002 -23.394  1.00 42.54           C  
ATOM   3693  CA  ASP J 252     -49.577  -5.509 -20.718  1.00 46.64           C  
ATOM   3694  CA  ILE J 253     -51.725  -3.407 -22.965  1.00 89.68           C  
ATOM   3695  CA  ALA J 254     -53.033  -6.591 -24.472  1.00 26.21           C  
ATOM   3696  CA  LYS J 255     -54.183  -7.638 -21.048  1.00123.03           C  
ATOM   3697  CA  ALA J 256     -56.153  -4.486 -20.438  1.00 37.08           C  
ATOM   3698  CA  PHE J 257     -57.500  -3.846 -23.909  1.00 73.31           C  
ATOM   3699  CA  ASN J 258     -58.923  -7.151 -24.958  1.00 63.23           C  
ATOM   3700  CA  LEU J 259     -58.558  -5.603 -28.388  1.00129.97           C  
ATOM   3701  CA  ASP J 260     -59.684  -7.739 -31.308  1.00109.68           C  
ATOM   3702  CA  VAL J 261     -56.343  -7.900 -33.069  1.00 87.12           C  
ATOM   3703  CA  GLN J 262     -53.818  -9.459 -30.799  1.00130.96           C  
ATOM   3704  CA  ARG J 263     -51.240  -6.961 -31.714  1.00172.82           C  
ATOM   3705  CA  GLY J 264     -51.040  -4.744 -34.718  1.00 43.53           C  
ATOM   3706  CA  ALA J 265     -47.832  -3.615 -36.255  1.00 61.05           C  
ATOM   3707  CA  PHE J 266     -46.525  -0.939 -33.968  1.00153.64           C  
ATOM   3708  CA  VAL J 267     -43.638   1.030 -35.062  1.00190.98           C  
ATOM   3709  CA  SER J 268     -41.065   2.409 -32.721  1.00125.17           C  
ATOM   3710  CA  GLU J 269     -39.334   4.392 -35.394  1.00103.87           C  
ATOM   3711  CA  VAL J 270     -39.365   6.539 -38.507  1.00121.79           C  
ATOM   3712  CA  LEU J 271     -36.552   6.237 -40.961  1.00135.37           C  
ATOM   3713  CA  PRO J 272     -35.402   9.532 -42.415  1.00282.64           C  
ATOM   3714  CA  GLY J 273     -35.773   9.845 -46.230  1.00220.11           C  
ATOM   3715  CA  SER J 274     -37.618   6.626 -45.858  1.00149.21           C  
ATOM   3716  CA  GLY J 275     -40.670   5.291 -47.400  1.00 66.36           C  
ATOM   3717  CA  SER J 276     -42.500   5.937 -44.282  1.00 82.01           C  
ATOM   3718  CA  ALA J 277     -41.317   9.474 -43.946  1.00 74.02           C  
ATOM   3719  CA  LYS J 278     -42.772  11.365 -46.891  1.00155.40           C  
ATOM   3720  CA  ALA J 279     -46.154   9.737 -46.823  1.00 73.45           C  
ATOM   3721  CA  GLY J 280     -46.382  10.230 -43.357  1.00 99.40           C  
ATOM   3722  CA  VAL J 281     -46.117   7.637 -40.756  1.00106.30           C  
ATOM   3723  CA  LYS J 282     -43.841   8.353 -37.894  1.00270.92           C  
ATOM   3724  CA  ALA J 283     -43.645   5.821 -35.032  1.00172.55           C  
ATOM   3725  CA  GLY J 284     -46.205   5.087 -32.561  1.00 87.94           C  
ATOM   3726  CA  ASP J 285     -48.449   4.253 -35.295  1.00174.59           C  
ATOM   3727  CA  ILE J 286     -50.431   1.324 -35.055  1.00131.22           C  
ATOM   3728  CA  ILE J 287     -50.497  -0.372 -38.413  1.00 96.37           C  
ATOM   3729  CA  THR J 288     -53.983  -1.702 -38.466  1.00132.62           C  
ATOM   3730  CA  SER J 289     -54.165  -2.835 -42.012  1.00 65.87           C  
ATOM   3731  CA  LEU J 290     -52.565  -3.059 -45.402  1.00 78.04           C  
ATOM   3732  CA  ASN J 291     -54.970  -2.808 -48.271  1.00277.35           C  
ATOM   3733  CA  GLY J 292     -57.848  -3.577 -48.960  1.00136.30           C  
ATOM   3734  CA  LYS J 293     -58.432  -6.352 -46.470  1.00117.68           C  
ATOM   3735  CA  PRO J 294     -57.724  -6.365 -42.806  1.00 63.57           C  
ATOM   3736  CA  LEU J 295     -54.193  -6.737 -41.501  1.00 66.20           C  
ATOM   3737  CA  ASN J 296     -53.302  -8.964 -38.635  1.00 75.24           C  
ATOM   3738  CA  SER J 297     -50.380  -8.735 -36.319  1.00 58.91           C  
ATOM   3739  CA  PHE J 298     -47.034  -7.311 -37.135  1.00110.51           C  
ATOM   3740  CA  ALA J 299     -46.486 -10.838 -38.315  1.00 48.84           C  
ATOM   3741  CA  GLU J 300     -49.067 -10.755 -41.014  1.00 93.46           C  
ATOM   3742  CA  LEU J 301     -47.587  -7.428 -41.893  1.00 66.81           C  
ATOM   3743  CA  ARG J 302     -44.391  -8.639 -43.341  1.00245.36           C  
ATOM   3744  CA  SER J 303     -46.255 -11.636 -44.557  1.00 70.11           C  
ATOM   3745  CA  ARG J 304     -47.954  -9.697 -47.186  1.00180.92           C  
ATOM   3746  CA  ILE J 305     -45.435  -6.944 -47.609  1.00 96.04           C  
ATOM   3747  CA  ALA J 306     -42.534  -9.247 -47.689  1.00 73.53           C  
ATOM   3748  CA  THR J 307     -44.665 -11.098 -50.114  1.00162.56           C  
ATOM   3749  CA  THR J 308     -45.424  -8.147 -52.319  1.00 66.43           C  
ATOM   3750  CA  GLU J 309     -43.253  -6.248 -54.739  1.00 81.21           C  
ATOM   3751  CA  PRO J 310     -40.963  -3.912 -53.042  1.00221.90           C  
ATOM   3752  CA  GLY J 311     -41.822  -1.747 -54.855  1.00119.85           C  
ATOM   3753  CA  THR J 312     -45.528  -1.940 -55.343  1.00112.27           C  
ATOM   3754  CA  LYS J 313     -47.454   1.061 -54.221  1.00 90.60           C  
ATOM   3755  CA  VAL J 314     -49.750   0.168 -51.391  1.00 59.85           C  
ATOM   3756  CA  LYS J 315     -51.850   1.999 -48.861  1.00123.46           C  
ATOM   3757  CA  LEU J 316     -51.632   1.432 -45.146  1.00115.89           C  
ATOM   3758  CA  GLY J 317     -54.242   2.017 -42.506  1.00 54.96           C  
ATOM   3759  CA  LEU J 318     -52.972   3.083 -39.241  1.00148.27           C  
ATOM   3760  CA  LEU J 319     -54.633   4.035 -36.080  1.00136.64           C  
ATOM   3761  CA  ARG J 320     -52.833   6.571 -34.537  1.00274.36           C  
ATOM   3762  CA  ASN J 321     -53.920   8.686 -31.683  1.00190.92           C  
ATOM   3763  CA  GLY J 322     -57.292   7.148 -31.363  1.00 47.80           C  
ATOM   3764  CA  LYS J 323     -58.137   7.695 -34.905  1.00173.58           C  
ATOM   3765  CA  PRO J 324     -57.384   6.129 -38.125  1.00123.52           C  
ATOM   3766  CA  LEU J 325     -55.559   7.018 -41.373  1.00229.06           C  
ATOM   3767  CA  GLU J 326     -55.128   5.737 -44.769  1.00187.51           C  
ATOM   3768  CA  VAL J 327     -52.094   7.055 -46.590  1.00172.32           C  
ATOM   3769  CA  GLU J 328     -50.146   5.825 -49.571  1.00 88.39           C  
ATOM   3770  CA  VAL J 329     -46.770   4.430 -48.801  1.00123.71           C  
ATOM   3771  CA  SER J 340     -22.433  30.096 -47.551  1.00 56.53           C  
ATOM   3772  CA  ALA J 341     -18.690  29.762 -47.026  1.00 75.13           C  
ATOM   3773  CA  GLU J 342     -19.231  27.976 -43.741  1.00 63.78           C  
ATOM   3774  CA  MET J 343     -19.707  24.492 -44.940  1.00 79.33           C  
ATOM   3775  CA  ILE J 344     -16.817  24.530 -47.316  1.00162.67           C  
ATOM   3776  CA  THR J 345     -14.654  26.376 -44.904  1.00 72.37           C  
ATOM   3777  CA  PRO J 346     -14.867  25.696 -41.256  1.00156.86           C  
ATOM   3778  CA  ALA J 347     -16.392  28.208 -38.885  1.00 73.86           C  
ATOM   3779  CA  LEU J 348     -15.672  30.977 -41.378  1.00131.23           C  
ATOM   3780  CA  GLU J 349     -18.936  32.802 -41.570  1.00 92.74           C  
ATOM   3781  CA  GLY J 350     -19.172  34.702 -44.761  1.00 27.98           C  
ATOM   3782  CA  ALA J 351     -20.474  35.094 -48.247  1.00 34.93           C  
ATOM   3783  CA  THR J 352     -22.428  32.218 -49.639  1.00 26.08           C  
ATOM   3784  CA  LEU J 353     -20.905  30.137 -52.352  1.00 48.88           C  
ATOM   3785  CA  SER J 354     -22.348  28.457 -55.400  1.00 86.50           C  
ATOM   3786  CA  ASP J 355     -21.088  25.922 -57.903  1.00 52.79           C  
ATOM   3787  CA  GLY J 356     -20.837  26.185 -61.715  1.00 50.02           C  
ATOM   3788  CA  GLN J 357     -19.576  29.245 -63.459  1.00149.40           C  
ATOM   3789  CA  LEU J 358     -23.011  29.978 -62.898  1.00258.69           C  
ATOM   3790  CA  LYS J 359     -24.205  28.490 -66.157  1.00197.91           C  
ATOM   3791  CA  ASP J 360     -20.984  28.516 -68.156  1.00142.87           C  
ATOM   3792  CA  GLY J 361     -18.070  26.207 -68.106  1.00 36.16           C  
ATOM   3793  CA  GLY J 362     -17.150  26.167 -64.486  1.00 34.84           C  
ATOM   3794  CA  LYS J 363     -14.476  28.705 -63.803  1.00151.54           C  
ATOM   3795  CA  GLY J 364     -14.954  27.541 -60.287  1.00 27.55           C  
ATOM   3796  CA  ILE J 365     -17.005  28.200 -57.195  1.00 73.92           C  
ATOM   3797  CA  LYS J 366     -18.754  31.511 -57.054  1.00128.30           C  
ATOM   3798  CA  ILE J 367     -19.169  33.637 -53.956  1.00 80.23           C  
ATOM   3799  CA  ASP J 368     -22.718  34.892 -54.051  1.00 63.93           C  
ATOM   3800  CA  GLU J 369     -22.708  37.710 -51.576  1.00 91.06           C  
ATOM   3801  CA  VAL J 370     -20.603  38.911 -48.733  1.00158.25           C  
ATOM   3802  CA  VAL J 371     -21.989  39.111 -45.233  1.00198.89           C  
ATOM   3803  CA  LYS J 372     -19.012  41.491 -44.744  1.00168.04           C  
ATOM   3804  CA  GLY J 373     -19.285  41.714 -40.981  1.00 37.30           C  
ATOM   3805  CA  SER J 374     -18.436  37.991 -41.171  1.00 51.75           C  
ATOM   3806  CA  PRO J 375     -14.943  36.690 -41.092  1.00 68.58           C  
ATOM   3807  CA  ALA J 376     -15.120  35.339 -44.614  1.00 44.06           C  
ATOM   3808  CA  ALA J 377     -15.296  39.023 -45.359  1.00 52.49           C  
ATOM   3809  CA  GLN J 378     -12.380  39.878 -43.096  1.00 62.04           C  
ATOM   3810  CA  ALA J 379      -9.716  38.017 -45.079  1.00 64.22           C  
ATOM   3811  CA  GLY J 380     -10.506  39.425 -48.493  1.00 63.35           C  
ATOM   3812  CA  LEU J 381     -13.487  37.481 -49.781  1.00 56.41           C  
ATOM   3813  CA  GLN J 382     -15.558  39.839 -51.901  1.00145.44           C  
ATOM   3814  CA  LYS J 383     -18.686  38.954 -53.779  1.00161.23           C  
ATOM   3815  CA  ASP J 384     -18.498  38.091 -57.440  1.00 66.30           C  
ATOM   3816  CA  ASP J 385     -15.218  36.339 -56.941  1.00 48.29           C  
ATOM   3817  CA  VAL J 386     -14.737  33.064 -58.725  1.00119.04           C  
ATOM   3818  CA  ILE J 387     -12.415  30.583 -57.128  1.00112.41           C  
ATOM   3819  CA  ILE J 388     -10.736  28.972 -60.092  1.00 87.29           C  
ATOM   3820  CA  GLY J 389      -8.241  26.645 -58.419  1.00 75.94           C  
ATOM   3821  CA  VAL J 390      -7.046  25.787 -54.833  1.00 91.95           C  
ATOM   3822  CA  ASN J 391      -3.451  25.257 -53.723  1.00 89.69           C  
ATOM   3823  CA  ARG J 392      -2.200  24.758 -57.252  1.00132.28           C  
ATOM   3824  CA  ASP J 393      -5.126  22.621 -58.250  1.00 78.78           C  
ATOM   3825  CA  ARG J 394      -8.102  23.625 -60.319  1.00 44.17           C  
ATOM   3826  CA  VAL J 395     -11.482  23.877 -58.681  1.00 54.49           C  
ATOM   3827  CA  ASN J 396     -14.258  23.179 -61.116  1.00 46.27           C  
ATOM   3828  CA  SER J 397     -16.890  22.963 -58.441  1.00 39.89           C  
ATOM   3829  CA  ILE J 398     -17.505  22.915 -54.732  1.00 87.11           C  
ATOM   3830  CA  ALA J 399     -16.771  19.231 -54.536  1.00 23.46           C  
ATOM   3831  CA  GLU J 400     -13.322  19.635 -55.993  1.00 34.24           C  
ATOM   3832  CA  MET J 401     -12.649  22.597 -53.761  1.00 36.29           C  
ATOM   3833  CA  ARG J 402     -13.615  20.403 -50.862  1.00 95.67           C  
ATOM   3834  CA  LYS J 403     -11.073  17.896 -52.081  1.00 86.80           C  
ATOM   3835  CA  VAL J 404      -8.245  20.349 -51.697  1.00 35.90           C  
ATOM   3836  CA  LEU J 405      -9.467  21.134 -48.229  1.00171.71           C  
ATOM   3837  CA  ALA J 406      -9.666  17.447 -47.610  1.00 37.49           C  
ATOM   3838  CA  ALA J 407      -5.894  17.536 -47.591  1.00 37.90           C  
ATOM   3839  CA  LYS J 408      -6.380  20.336 -45.093  1.00144.03           C  
ATOM   3840  CA  PRO J 409      -3.121  22.052 -45.676  1.00 80.08           C  
ATOM   3841  CA  ALA J 410      -2.204  24.540 -42.968  1.00 41.16           C  
ATOM   3842  CA  ILE J 411      -1.843  27.022 -45.761  1.00131.14           C  
ATOM   3843  CA  ILE J 412      -4.803  27.415 -48.062  1.00 99.90           C  
ATOM   3844  CA  ALA J 413      -4.107  29.346 -51.179  1.00 96.18           C  
ATOM   3845  CA  LEU J 414      -7.141  30.980 -52.864  1.00157.19           C  
ATOM   3846  CA  GLN J 415      -7.049  32.029 -56.482  1.00225.91           C  
ATOM   3847  CA  ILE J 416     -10.107  33.773 -57.461  1.00 93.34           C  
ATOM   3848  CA  VAL J 417     -10.701  35.910 -60.457  1.00 58.95           C  
ATOM   3849  CA  ARG J 418     -12.024  39.348 -59.738  1.00 89.22           C  
ATOM   3850  CA  GLY J 419     -13.090  41.422 -62.674  1.00 23.08           C  
ATOM   3851  CA  ASN J 420     -10.623  40.800 -65.418  1.00 51.39           C  
ATOM   3852  CA  GLU J 421      -7.764  40.059 -63.080  1.00114.31           C  
ATOM   3853  CA  SER J 422      -6.271  37.261 -61.092  1.00104.13           C  
ATOM   3854  CA  ILE J 423      -6.864  37.356 -57.384  1.00148.84           C  
ATOM   3855  CA  TYR J 424      -5.261  35.692 -54.475  1.00181.21           C  
ATOM   3856  CA  LEU J 425      -6.856  34.940 -51.249  1.00101.05           C  
ATOM   3857  CA  LEU J 426      -5.136  33.353 -48.453  1.00199.15           C  
ATOM   3858  CA  MET J 427      -6.442  31.563 -45.242  1.00 93.71           C  
ATOM   3859  CA  ARG J 428      -4.747  31.134 -41.843  1.00135.67           C  
TER    3860      ARG J 428                                                      
ATOM   3861  CA  PRO K  11     -43.880 -42.870 -40.703  1.00116.59           C  
ATOM   3862  CA  LEU K  12     -40.822 -44.924 -39.983  1.00101.56           C  
ATOM   3863  CA  PRO K  13     -41.565 -48.506 -39.717  1.00201.24           C  
ATOM   3864  CA  SER K  14     -40.584 -49.666 -36.334  1.00117.94           C  
ATOM   3865  CA  LEU K  15     -37.266 -48.446 -35.155  1.00123.90           C  
ATOM   3866  CA  ALA K  16     -37.466 -50.763 -32.173  1.00 44.68           C  
ATOM   3867  CA  PRO K  17     -37.573 -53.977 -34.055  1.00 73.93           C  
ATOM   3868  CA  MET K  18     -34.393 -53.196 -35.909  1.00 47.20           C  
ATOM   3869  CA  LEU K  19     -32.809 -51.901 -32.751  1.00 62.75           C  
ATOM   3870  CA  GLU K  20     -33.499 -54.939 -30.675  1.00 80.84           C  
ATOM   3871  CA  LYS K  21     -31.292 -57.077 -32.840  1.00 82.46           C  
ATOM   3872  CA  VAL K  22     -28.533 -54.510 -33.365  1.00112.84           C  
ATOM   3873  CA  LEU K  23     -28.183 -52.880 -29.966  1.00122.94           C  
ATOM   3874  CA  PRO K  24     -26.188 -55.586 -28.300  1.00 66.91           C  
ATOM   3875  CA  ALA K  25     -23.480 -54.903 -30.859  1.00 34.56           C  
ATOM   3876  CA  VAL K  26     -22.885 -51.419 -29.510  1.00 34.85           C  
ATOM   3877  CA  VAL K  27     -20.976 -51.278 -26.277  1.00 41.12           C  
ATOM   3878  CA  SER K  28     -19.814 -48.766 -23.751  1.00 75.43           C  
ATOM   3879  CA  VAL K  29     -16.128 -48.312 -23.243  1.00 36.56           C  
ATOM   3880  CA  ARG K  30     -14.739 -47.482 -19.843  1.00131.78           C  
ATOM   3881  CA  VAL K  31     -11.269 -46.144 -19.434  1.00 40.01           C  
ATOM   3882  CA  GLU K  32      -8.986 -45.407 -16.531  1.00 40.33           C  
ATOM   3883  CA  GLY K  33      -5.610 -43.793 -16.643  1.00 21.08           C  
ATOM   3884  CA  THR K  34      -3.308 -40.963 -15.657  1.00 40.00           C  
ATOM   3885  CA  ALA K  58      -1.358 -38.067 -13.088  1.00 16.89           C  
ATOM   3886  CA  GLN K  59      -4.305 -38.515 -10.827  1.00 86.86           C  
ATOM   3887  CA  PRO K  60      -6.581 -41.233 -11.882  1.00 63.41           C  
ATOM   3888  CA  PHE K  61      -9.544 -40.297 -13.995  1.00 49.91           C  
ATOM   3889  CA  GLU K  62     -12.276 -42.264 -15.617  1.00 25.82           C  
ATOM   3890  CA  GLY K  63     -13.574 -41.628 -19.083  1.00 17.57           C  
ATOM   3891  CA  LEU K  64     -16.603 -43.002 -20.817  1.00 39.32           C  
ATOM   3892  CA  GLY K  65     -17.070 -43.676 -24.488  1.00 20.26           C  
ATOM   3893  CA  SER K  66     -18.678 -46.184 -26.770  1.00 28.05           C  
ATOM   3894  CA  GLY K  67     -17.551 -48.762 -29.271  1.00 19.85           C  
ATOM   3895  CA  VAL K  68     -18.974 -51.213 -31.730  1.00 95.84           C  
ATOM   3896  CA  ILE K  69     -18.351 -54.925 -31.939  1.00106.00           C  
ATOM   3897  CA  ILE K  70     -16.929 -55.540 -35.369  1.00 93.06           C  
ATOM   3898  CA  ASN K  71     -16.121 -59.203 -34.900  1.00 46.92           C  
ATOM   3899  CA  ALA K  72     -17.978 -61.261 -32.371  1.00 28.85           C  
ATOM   3900  CA  SER K  73     -15.676 -64.224 -32.502  1.00 32.49           C  
ATOM   3901  CA  LYS K  74     -12.480 -62.271 -32.156  1.00 89.21           C  
ATOM   3902  CA  GLY K  75     -14.044 -59.699 -29.904  1.00 25.86           C  
ATOM   3903  CA  TYR K  76     -12.783 -56.756 -31.897  1.00 82.59           C  
ATOM   3904  CA  VAL K  77     -14.370 -53.485 -30.982  1.00 95.93           C  
ATOM   3905  CA  LEU K  78     -13.998 -50.280 -32.949  1.00 87.81           C  
ATOM   3906  CA  THR K  79     -13.691 -47.027 -31.082  1.00 42.29           C  
ATOM   3907  CA  ASN K  80     -12.277 -43.567 -31.400  1.00 58.83           C  
ATOM   3908  CA  ASN K  81      -8.620 -43.182 -30.644  1.00 45.67           C  
ATOM   3909  CA  HIS K  82      -9.297 -40.207 -28.449  1.00 50.60           C  
ATOM   3910  CA  VAL K  83     -11.482 -42.205 -26.171  1.00113.01           C  
ATOM   3911  CA  ILE K  84      -8.727 -44.815 -25.767  1.00135.40           C  
ATOM   3912  CA  ASN K  85      -5.609 -42.664 -25.896  1.00 69.70           C  
ATOM   3913  CA  GLN K  86      -5.061 -41.897 -22.199  1.00 61.55           C  
ATOM   3914  CA  ALA K  87      -6.395 -45.222 -20.947  1.00 66.64           C  
ATOM   3915  CA  GLN K  88      -4.116 -47.347 -18.826  1.00 87.98           C  
ATOM   3916  CA  LYS K  89      -6.840 -49.953 -18.603  1.00 30.41           C  
ATOM   3917  CA  ILE K  90      -9.957 -50.427 -20.644  1.00 40.23           C  
ATOM   3918  CA  SER K  91     -13.163 -52.276 -19.958  1.00 26.39           C  
ATOM   3919  CA  ILE K  92     -16.156 -52.863 -22.156  1.00100.94           C  
ATOM   3920  CA  GLN K  93     -19.690 -53.256 -20.966  1.00108.61           C  
ATOM   3921  CA  LEU K  94     -22.527 -54.797 -22.883  1.00 83.27           C  
ATOM   3922  CA  ASN K  95     -26.076 -53.553 -22.696  1.00 40.76           C  
ATOM   3923  CA  ASP K  96     -26.916 -56.795 -20.938  1.00 49.84           C  
ATOM   3924  CA  GLY K  97     -24.641 -55.763 -18.116  1.00 33.27           C  
ATOM   3925  CA  ARG K  98     -21.824 -58.166 -18.824  1.00 84.55           C  
ATOM   3926  CA  GLU K  99     -18.418 -56.575 -18.690  1.00102.24           C  
ATOM   3927  CA  PHE K 100     -15.076 -57.544 -20.137  1.00 43.33           C  
ATOM   3928  CA  ASP K 101     -11.490 -56.375 -20.185  1.00 39.06           C  
ATOM   3929  CA  ALA K 102     -10.015 -55.099 -23.409  1.00 32.23           C  
ATOM   3930  CA  LYS K 103      -6.595 -54.287 -24.775  1.00142.29           C  
ATOM   3931  CA  LEU K 104      -5.668 -51.976 -27.598  1.00 72.07           C  
ATOM   3932  CA  ILE K 105      -4.887 -53.804 -30.765  1.00108.04           C  
ATOM   3933  CA  GLY K 106      -3.810 -50.588 -32.407  1.00 27.75           C  
ATOM   3934  CA  SER K 107      -5.029 -47.192 -33.459  1.00 48.46           C  
ATOM   3935  CA  ASP K 108      -4.057 -44.145 -35.391  1.00 93.66           C  
ATOM   3936  CA  ASP K 109      -4.221 -40.469 -34.563  1.00 61.47           C  
ATOM   3937  CA  GLN K 110      -4.899 -38.958 -37.934  1.00 96.81           C  
ATOM   3938  CA  SER K 111      -8.188 -40.718 -38.677  1.00 66.80           C  
ATOM   3939  CA  ASP K 112      -8.888 -41.182 -34.968  1.00 72.55           C  
ATOM   3940  CA  ILE K 113      -9.725 -44.865 -35.267  1.00 55.71           C  
ATOM   3941  CA  ALA K 114      -8.695 -47.424 -32.691  1.00 30.21           C  
ATOM   3942  CA  LEU K 115      -9.182 -51.160 -32.496  1.00 83.78           C  
ATOM   3943  CA  LEU K 116      -9.771 -52.887 -29.219  1.00 72.35           C  
ATOM   3944  CA  GLN K 117     -10.006 -56.550 -28.415  1.00 59.68           C  
ATOM   3945  CA  ILE K 118     -12.151 -58.060 -25.728  1.00 48.83           C  
ATOM   3946  CA  GLN K 119     -10.454 -60.568 -23.526  1.00 97.00           C  
ATOM   3947  CA  ASN K 120     -12.199 -63.904 -23.418  1.00 49.82           C  
ATOM   3948  CA  PRO K 121     -15.068 -62.627 -25.468  1.00 62.14           C  
ATOM   3949  CA  SER K 122     -18.111 -64.849 -25.269  1.00 34.99           C  
ATOM   3950  CA  LYS K 123     -21.599 -64.797 -26.747  1.00 43.18           C  
ATOM   3951  CA  LEU K 124     -21.094 -61.503 -28.498  1.00 86.05           C  
ATOM   3952  CA  THR K 125     -23.164 -59.903 -31.200  1.00116.19           C  
ATOM   3953  CA  GLN K 126     -21.584 -58.365 -34.248  1.00 54.32           C  
ATOM   3954  CA  ILE K 127     -22.780 -55.388 -36.215  1.00101.88           C  
ATOM   3955  CA  ALA K 128     -23.020 -55.549 -39.984  1.00 31.09           C  
ATOM   3956  CA  ILE K 129     -21.232 -52.886 -41.951  1.00 97.73           C  
ATOM   3957  CA  ALA K 130     -22.928 -50.943 -44.716  1.00 34.14           C  
ATOM   3958  CA  ASP K 131     -21.249 -49.293 -47.661  1.00 35.14           C  
ATOM   3959  CA  SER K 132     -20.718 -45.700 -46.618  1.00 32.27           C  
ATOM   3960  CA  ASP K 133     -20.087 -44.659 -50.189  1.00 35.73           C  
ATOM   3961  CA  LYS K 134     -23.701 -45.332 -51.058  1.00 62.56           C  
ATOM   3962  CA  LEU K 135     -25.055 -42.993 -48.396  1.00 73.84           C  
ATOM   3963  CA  ARG K 136     -26.640 -39.783 -49.596  1.00 88.54           C  
ATOM   3964  CA  VAL K 137     -28.094 -36.800 -47.830  1.00 85.14           C  
ATOM   3965  CA  GLY K 138     -31.543 -37.382 -46.470  1.00 22.46           C  
ATOM   3966  CA  ASP K 139     -30.869 -40.951 -45.465  1.00 28.67           C  
ATOM   3967  CA  PHE K 140     -32.100 -41.913 -42.028  1.00 53.88           C  
ATOM   3968  CA  ALA K 141     -29.571 -42.510 -39.312  1.00 37.94           C  
ATOM   3969  CA  VAL K 142     -29.646 -43.674 -35.729  1.00 42.89           C  
ATOM   3970  CA  ALA K 143     -26.870 -43.021 -33.295  1.00 30.02           C  
ATOM   3971  CA  VAL K 144     -26.145 -45.309 -30.404  1.00 31.54           C  
ATOM   3972  CA  GLY K 145     -23.690 -44.629 -27.637  1.00 21.68           C  
ATOM   3973  CA  ASN K 146     -23.539 -43.576 -24.048  1.00 65.49           C  
ATOM   3974  CA  PRO K 147     -24.067 -39.902 -23.689  1.00 74.07           C  
ATOM   3975  CA  PHE K 148     -23.100 -38.543 -20.307  1.00 66.86           C  
ATOM   3976  CA  GLY K 149     -22.423 -42.129 -19.361  1.00 31.34           C  
ATOM   3977  CA  LEU K 150     -26.132 -42.593 -18.923  1.00 61.50           C  
ATOM   3978  CA  GLY K 151     -26.146 -46.001 -20.553  1.00 32.69           C  
ATOM   3979  CA  GLN K 152     -26.944 -47.148 -24.036  1.00113.77           C  
ATOM   3980  CA  THR K 153     -28.963 -44.461 -25.676  1.00 40.17           C  
ATOM   3981  CA  ALA K 154     -30.318 -44.254 -29.175  1.00 30.11           C  
ATOM   3982  CA  THR K 155     -31.100 -41.067 -31.031  1.00 35.99           C  
ATOM   3983  CA  SER K 156     -32.337 -40.586 -34.516  1.00116.15           C  
ATOM   3984  CA  GLY K 157     -31.851 -38.156 -37.355  1.00 25.50           C  
ATOM   3985  CA  ILE K 158     -30.920 -38.015 -41.027  1.00 48.45           C  
ATOM   3986  CA  VAL K 159     -27.606 -37.685 -42.776  1.00133.09           C  
ATOM   3987  CA  SER K 160     -27.087 -33.983 -43.077  1.00 49.37           C  
ATOM   3988  CA  ALA K 161     -24.040 -34.090 -45.285  1.00 57.00           C  
ATOM   3989  CA  LEU K 162     -21.096 -36.180 -46.250  1.00111.34           C  
ATOM   3990  CA  GLY K 163     -17.560 -35.714 -47.363  1.00 30.36           C  
ATOM   3991  CA  ARG K 164     -17.036 -32.974 -44.866  1.00210.55           C  
ATOM   3992  CA  SER K 165     -13.672 -31.820 -43.802  1.00 78.65           C  
ATOM   3993  CA  GLY K 166     -11.689 -28.754 -42.985  1.00 38.31           C  
ATOM   3994  CA  LEU K 167     -13.162 -29.028 -39.516  1.00 61.08           C  
ATOM   3995  CA  ASN K 168      -9.557 -29.614 -38.451  1.00 93.79           C  
ATOM   3996  CA  LEU K 169     -10.812 -31.917 -35.787  1.00 49.77           C  
ATOM   3997  CA  GLU K 170      -8.533 -34.628 -37.153  1.00 84.28           C  
ATOM   3998  CA  GLY K 171      -5.685 -35.070 -39.607  1.00 38.72           C  
ATOM   3999  CA  LEU K 172      -7.800 -37.010 -42.039  1.00106.94           C  
ATOM   4000  CA  GLU K 173     -11.391 -36.070 -42.093  1.00 88.55           C  
ATOM   4001  CA  ASN K 174     -14.379 -37.123 -44.131  1.00 91.14           C  
ATOM   4002  CA  PHE K 175     -17.122 -36.932 -41.693  1.00 81.38           C  
ATOM   4003  CA  ILE K 176     -20.646 -37.925 -42.313  1.00 75.71           C  
ATOM   4004  CA  GLN K 177     -22.680 -35.167 -40.773  1.00117.89           C  
ATOM   4005  CA  THR K 178     -25.798 -36.062 -38.869  1.00125.56           C  
ATOM   4006  CA  ASP K 179     -28.527 -34.245 -36.953  1.00 62.69           C  
ATOM   4007  CA  ALA K 180     -28.960 -37.179 -34.584  1.00 39.47           C  
ATOM   4008  CA  SER K 181     -28.215 -35.981 -31.119  1.00 43.67           C  
ATOM   4009  CA  ILE K 182     -24.636 -36.750 -30.293  1.00 96.26           C  
ATOM   4010  CA  ASN K 183     -23.169 -35.805 -26.962  1.00 77.62           C  
ATOM   4011  CA  ARG K 184     -20.049 -36.305 -24.887  1.00 98.78           C  
ATOM   4012  CA  GLY K 185     -20.351 -40.072 -24.289  1.00 59.14           C  
ATOM   4013  CA  ASN K 186     -21.134 -40.786 -27.944  1.00 74.34           C  
ATOM   4014  CA  ALA K 187     -17.582 -41.046 -29.282  1.00 46.32           C  
ATOM   4015  CA  GLY K 188     -16.745 -44.461 -30.649  1.00 24.14           C  
ATOM   4016  CA  GLY K 189     -20.447 -45.165 -30.844  1.00 22.49           C  
ATOM   4017  CA  ALA K 190     -22.266 -46.348 -33.894  1.00 49.95           C  
ATOM   4018  CA  LEU K 191     -24.259 -44.549 -36.540  1.00194.15           C  
ATOM   4019  CA  LEU K 192     -26.706 -46.935 -38.029  1.00 67.68           C  
ATOM   4020  CA  ASN K 193     -28.942 -46.938 -41.051  1.00 73.83           C  
ATOM   4021  CA  LEU K 194     -32.590 -48.028 -41.112  1.00108.57           C  
ATOM   4022  CA  ASN K 195     -31.138 -51.470 -41.283  1.00 81.02           C  
ATOM   4023  CA  GLY K 196     -28.964 -52.551 -38.421  1.00 71.83           C  
ATOM   4024  CA  GLU K 197     -25.947 -51.651 -40.560  1.00 71.85           C  
ATOM   4025  CA  LEU K 198     -23.096 -49.449 -39.427  1.00 70.94           C  
ATOM   4026  CA  ILE K 199     -22.780 -46.275 -41.473  1.00146.82           C  
ATOM   4027  CA  GLY K 200     -20.001 -44.757 -39.407  1.00 28.87           C  
ATOM   4028  CA  ILE K 201     -18.444 -44.192 -36.003  1.00 92.07           C  
ATOM   4029  CA  ASN K 202     -19.528 -41.015 -34.244  1.00 68.32           C  
ATOM   4030  CA  THR K 203     -16.340 -39.039 -33.731  1.00 83.16           C  
ATOM   4031  CA  ALA K 204     -17.242 -35.493 -32.769  1.00 54.07           C  
ATOM   4032  CA  ILE K 205     -19.657 -32.603 -32.760  1.00111.59           C  
ATOM   4033  CA  LEU K 206     -19.709 -28.863 -33.193  1.00114.67           C  
ATOM   4034  CA  ALA K 207     -21.422 -27.198 -30.327  1.00 47.43           C  
ATOM   4035  CA  PRO K 208     -20.806 -23.863 -28.829  1.00 70.92           C  
ATOM   4036  CA  GLY K 209     -22.541 -25.011 -25.656  1.00 36.92           C  
ATOM   4037  CA  GLY K 210     -20.721 -28.287 -25.466  1.00 27.03           C  
ATOM   4038  CA  GLY K 211     -24.104 -29.877 -25.967  1.00 31.93           C  
ATOM   4039  CA  SER K 212     -25.568 -31.302 -29.149  1.00 66.78           C  
ATOM   4040  CA  VAL K 213     -26.415 -28.542 -31.609  1.00 72.47           C  
ATOM   4041  CA  GLY K 214     -27.606 -31.063 -34.124  1.00 37.24           C  
ATOM   4042  CA  ILE K 215     -24.288 -30.967 -35.926  1.00119.08           C  
ATOM   4043  CA  GLY K 216     -22.490 -34.247 -35.420  1.00 23.88           C  
ATOM   4044  CA  PHE K 217     -19.742 -35.914 -37.371  1.00 49.57           C  
ATOM   4045  CA  ALA K 218     -18.914 -39.550 -37.836  1.00 33.49           C  
ATOM   4046  CA  ILE K 219     -16.184 -41.434 -39.610  1.00 69.02           C  
ATOM   4047  CA  PRO K 220     -17.648 -43.398 -42.396  1.00 83.18           C  
ATOM   4048  CA  SER K 221     -18.106 -47.136 -42.109  1.00 35.69           C  
ATOM   4049  CA  ASN K 222     -15.946 -47.741 -45.072  1.00 59.30           C  
ATOM   4050  CA  MET K 223     -13.566 -45.705 -43.131  1.00 97.33           C  
ATOM   4051  CA  ALA K 224     -13.521 -47.663 -39.945  1.00 50.85           C  
ATOM   4052  CA  ARG K 225     -13.857 -50.991 -41.624  1.00 90.80           C  
ATOM   4053  CA  THR K 226     -10.763 -51.148 -43.691  1.00 60.45           C  
ATOM   4054  CA  LEU K 227      -8.779 -49.083 -41.183  1.00113.82           C  
ATOM   4055  CA  ALA K 228      -9.856 -51.523 -38.543  1.00 49.89           C  
ATOM   4056  CA  GLN K 229      -9.047 -54.393 -40.807  1.00133.43           C  
ATOM   4057  CA  GLN K 230      -5.341 -53.992 -41.069  1.00181.52           C  
ATOM   4058  CA  LEU K 231      -5.170 -53.127 -37.428  1.00 57.48           C  
ATOM   4059  CA  ILE K 232      -6.178 -56.731 -37.212  1.00 76.81           C  
ATOM   4060  CA  ASP K 233      -4.535 -57.653 -40.553  1.00177.00           C  
ATOM   4061  CA  PHE K 234      -2.740 -57.054 -42.931  1.00155.24           C  
ATOM   4062  CA  GLY K 235      -1.155 -55.411 -39.973  1.00 51.31           C  
ATOM   4063  CA  GLU K 236       1.587 -53.393 -41.514  1.00114.99           C  
ATOM   4064  CA  ILE K 237       2.214 -50.887 -38.848  1.00147.07           C  
ATOM   4065  CA  LYS K 238       3.064 -48.097 -41.182  1.00214.90           C  
ATOM   4066  CA  ARG K 239       1.564 -45.779 -41.856  1.00311.64           C  
ATOM   4067  CA  GLY K 240      -1.453 -46.813 -39.862  1.00 69.20           C  
ATOM   4068  CA  LEU K 241      -2.195 -43.234 -40.740  1.00185.79           C  
ATOM   4069  CA  LEU K 242      -0.076 -40.547 -42.286  1.00 89.64           C  
ATOM   4070  CA  GLY K 243       0.374 -38.644 -39.081  1.00 50.71           C  
ATOM   4071  CA  ILE K 244      -0.513 -35.153 -40.190  1.00 74.26           C  
ATOM   4072  CA  LYS K 245      -2.858 -32.358 -39.279  1.00 99.55           C  
ATOM   4073  CA  GLY K 246      -4.712 -30.334 -41.821  1.00 41.07           C  
ATOM   4074  CA  THR K 247      -7.853 -28.480 -42.627  1.00137.77           C  
ATOM   4075  CA  GLU K 248      -9.683 -26.993 -45.545  1.00 56.02           C  
ATOM   4076  CA  MET K 249      -7.232 -25.691 -48.063  1.00134.83           C  
ATOM   4077  CA  SER K 250      -5.712 -22.346 -47.302  1.00 90.08           C  
ATOM   4078  CA  ALA K 251      -7.830 -19.578 -48.683  1.00 41.55           C  
ATOM   4079  CA  ASP K 252      -5.038 -17.598 -50.196  1.00 77.76           C  
ATOM   4080  CA  ILE K 253      -3.867 -20.476 -52.320  1.00 58.10           C  
ATOM   4081  CA  ALA K 254      -7.424 -21.414 -53.028  1.00 33.09           C  
ATOM   4082  CA  LYS K 255      -8.010 -18.034 -54.532  1.00 44.23           C  
ATOM   4083  CA  ALA K 256      -5.129 -18.180 -56.949  1.00 37.44           C  
ATOM   4084  CA  PHE K 257      -5.252 -21.866 -57.747  1.00 75.06           C  
ATOM   4085  CA  ASN K 258      -8.851 -22.514 -58.582  1.00125.28           C  
ATOM   4086  CA  LEU K 259      -7.753 -26.098 -58.307  1.00 99.51           C  
ATOM   4087  CA  ASP K 260      -9.870 -28.815 -59.760  1.00 37.89           C  
ATOM   4088  CA  VAL K 261     -10.622 -29.781 -56.218  1.00 27.27           C  
ATOM   4089  CA  GLN K 262     -13.140 -27.558 -54.548  1.00 45.30           C  
ATOM   4090  CA  ARG K 263     -10.862 -27.751 -51.584  1.00147.50           C  
ATOM   4091  CA  GLY K 264      -7.641 -29.599 -51.195  1.00 23.71           C  
ATOM   4092  CA  ALA K 265      -6.326 -31.148 -48.069  1.00 35.08           C  
ATOM   4093  CA  PHE K 266      -3.985 -28.596 -46.697  1.00 81.13           C  
ATOM   4094  CA  VAL K 267      -1.556 -29.606 -44.076  1.00 72.51           C  
ATOM   4095  CA  SER K 268      -0.461 -27.126 -41.466  1.00 60.84           C  
ATOM   4096  CA  GLU K 269       1.769 -29.500 -39.613  1.00 96.34           C  
ATOM   4097  CA  VAL K 270       4.302 -32.283 -39.776  1.00114.47           C  
ATOM   4098  CA  LEU K 271       4.397 -34.988 -37.196  1.00100.27           C  
ATOM   4099  CA  PRO K 272       7.853 -36.065 -36.160  1.00268.51           C  
ATOM   4100  CA  GLY K 273       8.548 -39.778 -36.797  1.00209.27           C  
ATOM   4101  CA  SER K 274       5.179 -39.761 -38.454  1.00139.38           C  
ATOM   4102  CA  GLY K 275       4.290 -41.249 -41.725  1.00 40.91           C  
ATOM   4103  CA  SER K 276       4.109 -37.908 -43.357  1.00 51.63           C  
ATOM   4104  CA  ALA K 277       7.562 -37.005 -42.201  1.00 56.86           C  
ATOM   4105  CA  LYS K 278       9.613 -39.765 -43.803  1.00 88.82           C  
ATOM   4106  CA  ALA K 279       7.376 -39.618 -46.787  1.00 48.11           C  
ATOM   4107  CA  GLY K 280       8.731 -36.182 -46.796  1.00 48.55           C  
ATOM   4108  CA  VAL K 281       5.509 -34.327 -46.880  1.00143.00           C  
ATOM   4109  CA  LYS K 282       5.581 -31.342 -44.745  1.00141.48           C  
ATOM   4110  CA  ALA K 283       3.519 -28.386 -43.925  1.00109.50           C  
ATOM   4111  CA  GLY K 284       2.101 -25.863 -46.237  1.00 46.85           C  
ATOM   4112  CA  ASP K 285       1.389 -28.980 -48.168  1.00102.60           C  
ATOM   4113  CA  ILE K 286      -1.536 -29.269 -50.416  1.00 81.82           C  
ATOM   4114  CA  ILE K 287      -2.717 -32.789 -50.920  1.00 57.96           C  
ATOM   4115  CA  THR K 288      -4.402 -32.760 -54.282  1.00121.14           C  
ATOM   4116  CA  SER K 289      -5.059 -36.419 -54.698  1.00 49.51           C  
ATOM   4117  CA  LEU K 290      -4.774 -39.835 -53.182  1.00115.30           C  
ATOM   4118  CA  ASN K 291      -4.080 -42.668 -55.519  1.00184.06           C  
ATOM   4119  CA  GLY K 292      -4.638 -42.696 -59.260  1.00 57.66           C  
ATOM   4120  CA  LYS K 293      -7.989 -40.956 -59.093  1.00140.12           C  
ATOM   4121  CA  PRO K 294      -8.344 -37.405 -58.058  1.00 62.61           C  
ATOM   4122  CA  LEU K 295      -8.932 -36.454 -54.438  1.00138.13           C  
ATOM   4123  CA  ASN K 296     -11.471 -33.859 -53.511  1.00 79.56           C  
ATOM   4124  CA  SER K 297     -11.443 -31.695 -50.454  1.00 99.54           C  
ATOM   4125  CA  PHE K 298      -9.786 -32.522 -47.196  1.00102.22           C  
ATOM   4126  CA  ALA K 299     -13.136 -34.087 -46.611  1.00 51.39           C  
ATOM   4127  CA  GLU K 300     -12.798 -36.714 -49.241  1.00 97.08           C  
ATOM   4128  CA  LEU K 301      -9.310 -37.248 -47.955  1.00 67.57           C  
ATOM   4129  CA  ARG K 302     -10.236 -38.881 -44.738  1.00150.30           C  
ATOM   4130  CA  SER K 303     -13.089 -40.472 -46.511  1.00 49.90           C  
ATOM   4131  CA  ARG K 304     -10.884 -42.615 -48.558  1.00131.25           C  
ATOM   4132  CA  ILE K 305      -8.012 -42.922 -46.114  1.00 79.91           C  
ATOM   4133  CA  ALA K 306     -10.130 -43.377 -43.103  1.00 65.11           C  
ATOM   4134  CA  THR K 307     -11.713 -45.916 -45.340  1.00 57.03           C  
ATOM   4135  CA  THR K 308      -8.489 -47.560 -46.292  1.00123.14           C  
ATOM   4136  CA  GLU K 309      -6.339 -49.897 -44.280  1.00 95.17           C  
ATOM   4137  CA  PRO K 310      -4.113 -48.147 -41.916  1.00194.27           C  
ATOM   4138  CA  GLY K 311      -1.737 -49.535 -43.039  1.00124.66           C  
ATOM   4139  CA  THR K 312      -2.030 -49.796 -46.764  1.00119.48           C  
ATOM   4140  CA  LYS K 313       0.828 -48.386 -48.744  1.00 60.15           C  
ATOM   4141  CA  VAL K 314      -0.526 -45.541 -50.779  1.00 43.56           C  
ATOM   4142  CA  LYS K 315       0.812 -42.672 -52.812  1.00 88.70           C  
ATOM   4143  CA  LEU K 316      -0.308 -39.115 -52.386  1.00 97.05           C  
ATOM   4144  CA  GLY K 317      -0.086 -36.255 -54.795  1.00 38.34           C  
ATOM   4145  CA  LEU K 318       0.837 -33.036 -53.258  1.00136.59           C  
ATOM   4146  CA  LEU K 319       1.476 -29.679 -54.621  1.00122.46           C  
ATOM   4147  CA  ARG K 320       3.894 -27.646 -52.898  1.00261.82           C  
ATOM   4148  CA  ASN K 321       5.373 -24.414 -54.291  1.00121.43           C  
ATOM   4149  CA  GLY K 322       3.127 -24.536 -57.194  1.00 48.48           C  
ATOM   4150  CA  LYS K 323       4.629 -27.680 -58.389  1.00166.59           C  
ATOM   4151  CA  PRO K 324       3.303 -31.177 -58.500  1.00105.35           C  
ATOM   4152  CA  LEU K 325       4.534 -33.969 -56.195  1.00142.41           C  
ATOM   4153  CA  GLU K 326       4.194 -37.660 -56.063  1.00 98.35           C  
ATOM   4154  CA  VAL K 327       5.295 -39.585 -52.992  1.00 46.57           C  
ATOM   4155  CA  GLU K 328       4.520 -42.875 -51.307  1.00 84.76           C  
ATOM   4156  CA  VAL K 329       3.470 -42.574 -47.733  1.00 50.86           C  
ATOM   4157  CA  SER K 340      28.441 -45.558 -22.712  1.00 39.96           C  
ATOM   4158  CA  ALA K 341      28.329 -45.534 -18.960  1.00 53.81           C  
ATOM   4159  CA  GLU K 342      26.361 -42.330 -19.004  1.00 57.94           C  
ATOM   4160  CA  MET K 343      23.091 -43.865 -20.103  1.00169.51           C  
ATOM   4161  CA  ILE K 344      22.971 -46.487 -17.389  1.00 58.74           C  
ATOM   4162  CA  THR K 345      24.700 -44.273 -14.914  1.00 65.30           C  
ATOM   4163  CA  PRO K 346      23.762 -40.683 -14.587  1.00152.80           C  
ATOM   4164  CA  ALA K 347      25.967 -37.928 -15.936  1.00 73.80           C  
ATOM   4165  CA  LEU K 348      28.969 -40.223 -15.573  1.00 83.37           C  
ATOM   4166  CA  GLU K 349      30.574 -39.989 -18.951  1.00 73.94           C  
ATOM   4167  CA  GLY K 350      32.902 -42.844 -19.493  1.00 26.54           C  
ATOM   4168  CA  ALA K 351      33.572 -46.092 -21.224  1.00 36.16           C  
ATOM   4169  CA  THR K 352      30.767 -47.477 -23.288  1.00 98.26           C  
ATOM   4170  CA  LEU K 353      29.052 -50.593 -22.121  1.00 57.57           C  
ATOM   4171  CA  SER K 354      27.537 -53.542 -23.923  1.00 36.13           C  
ATOM   4172  CA  ASP K 355      25.375 -56.475 -22.851  1.00123.43           C  
ATOM   4173  CA  GLY K 356      25.987 -60.194 -23.219  1.00 52.64           C  
ATOM   4174  CA  GLN K 357      29.163 -61.805 -22.097  1.00190.89           C  
ATOM   4175  CA  LEU K 358      30.192 -60.842 -25.400  1.00256.24           C  
ATOM   4176  CA  LYS K 359      28.711 -63.834 -27.113  1.00138.87           C  
ATOM   4177  CA  ASP K 360      28.811 -66.367 -24.329  1.00126.31           C  
ATOM   4178  CA  GLY K 361      26.800 -66.847 -21.202  1.00 27.15           C  
ATOM   4179  CA  GLY K 362      26.287 -63.391 -19.903  1.00 37.04           C  
ATOM   4180  CA  LYS K 363      28.721 -62.838 -17.108  1.00143.21           C  
ATOM   4181  CA  GLY K 364      27.363 -59.357 -17.188  1.00 36.92           C  
ATOM   4182  CA  ILE K 365      27.647 -56.029 -18.937  1.00138.81           C  
ATOM   4183  CA  LYS K 366      30.949 -55.294 -20.561  1.00 86.81           C  
ATOM   4184  CA  ILE K 367      32.757 -51.994 -20.619  1.00 65.73           C  
ATOM   4185  CA  ASP K 368      33.837 -51.482 -24.197  1.00 62.63           C  
ATOM   4186  CA  GLU K 369      36.457 -48.820 -23.914  1.00 84.71           C  
ATOM   4187  CA  VAL K 370      37.588 -46.251 -21.427  1.00109.14           C  
ATOM   4188  CA  VAL K 371      37.221 -42.630 -22.457  1.00193.42           C  
ATOM   4189  CA  LYS K 372      39.643 -42.164 -19.514  1.00169.29           C  
ATOM   4190  CA  GLY K 373      39.484 -38.393 -19.405  1.00 37.23           C  
ATOM   4191  CA  SER K 374      35.840 -39.086 -18.469  1.00106.76           C  
ATOM   4192  CA  PRO K 375      34.603 -39.484 -14.997  1.00 71.88           C  
ATOM   4193  CA  ALA K 376      33.628 -43.092 -15.496  1.00 52.57           C  
ATOM   4194  CA  ALA K 377      37.367 -43.392 -15.809  1.00 51.63           C  
ATOM   4195  CA  GLN K 378      38.090 -41.331 -12.711  1.00104.53           C  
ATOM   4196  CA  ALA K 379      36.528 -43.751 -10.291  1.00 89.67           C  
ATOM   4197  CA  GLY K 380      38.037 -47.010 -11.385  1.00 76.14           C  
ATOM   4198  CA  LEU K 381      36.222 -48.252 -14.423  1.00112.31           C  
ATOM   4199  CA  GLN K 382      38.787 -49.810 -16.694  1.00 60.01           C  
ATOM   4200  CA  LYS K 383      37.958 -51.263 -20.055  1.00116.42           C  
ATOM   4201  CA  ASP K 384      37.479 -54.988 -20.396  1.00 70.83           C  
ATOM   4202  CA  ASP K 385      35.848 -55.098 -16.999  1.00 56.16           C  
ATOM   4203  CA  VAL K 386      32.846 -57.360 -16.864  1.00 87.52           C  
ATOM   4204  CA  ILE K 387      30.167 -56.274 -14.476  1.00105.02           C  
ATOM   4205  CA  ILE K 388      28.902 -59.444 -12.971  1.00159.81           C  
ATOM   4206  CA  GLY K 389      26.461 -57.791 -10.559  1.00 69.22           C  
ATOM   4207  CA  VAL K 390      25.872 -54.819  -8.365  1.00133.03           C  
ATOM   4208  CA  ASN K 391      24.802 -54.391  -4.793  1.00 87.49           C  
ATOM   4209  CA  ARG K 392      24.679 -58.096  -4.124  1.00109.07           C  
ATOM   4210  CA  ASP K 393      22.581 -58.526  -7.236  1.00 58.34           C  
ATOM   4211  CA  ARG K 394      23.797 -60.321 -10.280  1.00181.87           C  
ATOM   4212  CA  VAL K 395      23.573 -58.439 -13.505  1.00140.32           C  
ATOM   4213  CA  ASN K 396      23.123 -60.632 -16.535  1.00 65.67           C  
ATOM   4214  CA  SER K 397      22.645 -57.708 -18.870  1.00 52.78           C  
ATOM   4215  CA  ILE K 398      22.177 -53.981 -18.879  1.00 80.52           C  
ATOM   4216  CA  ALA K 399      18.487 -54.208 -18.199  1.00 30.14           C  
ATOM   4217  CA  GLU K 400      19.088 -55.924 -14.884  1.00 57.18           C  
ATOM   4218  CA  MET K 401      21.871 -53.530 -14.077  1.00 86.79           C  
ATOM   4219  CA  ARG K 402      19.411 -50.728 -14.558  1.00159.63           C  
ATOM   4220  CA  LYS K 403      17.061 -52.482 -12.202  1.00137.20           C  
ATOM   4221  CA  VAL K 404      19.442 -52.282  -9.294  1.00114.29           C  
ATOM   4222  CA  LEU K 405      19.983 -48.652 -10.178  1.00112.52           C  
ATOM   4223  CA  ALA K 406      16.243 -48.236 -10.110  1.00 28.50           C  
ATOM   4224  CA  ALA K 407      16.444 -48.876  -6.394  1.00 28.34           C  
ATOM   4225  CA  LYS K 408      18.869 -45.984  -6.417  1.00140.84           C  
ATOM   4226  CA  PRO K 409      20.757 -47.146  -3.396  1.00 67.40           C  
ATOM   4227  CA  ALA K 410      22.916 -44.385  -2.001  1.00 22.50           C  
ATOM   4228  CA  ILE K 411      25.906 -46.608  -2.430  1.00 43.29           C  
ATOM   4229  CA  ILE K 412      26.317 -48.812  -5.455  1.00 55.88           C  
ATOM   4230  CA  ALA K 413      28.894 -51.552  -5.659  1.00 62.25           C  
ATOM   4231  CA  LEU K 414      29.483 -52.605  -9.160  1.00148.42           C  
ATOM   4232  CA  GLN K 415      30.536 -56.162  -9.885  1.00186.51           C  
ATOM   4233  CA  ILE K 416      33.011 -57.114 -12.467  1.00255.04           C  
ATOM   4234  CA  VAL K 417      35.814 -59.405 -13.347  1.00157.01           C  
ATOM   4235  CA  ARG K 418      39.134 -57.893 -14.186  1.00186.65           C  
ATOM   4236  CA  GLY K 419      41.828 -60.044 -15.592  1.00 34.39           C  
ATOM   4237  CA  ASN K 420      41.727 -63.180 -13.599  1.00 61.14           C  
ATOM   4238  CA  GLU K 421      40.732 -61.206 -10.631  1.00 84.56           C  
ATOM   4239  CA  SER K 422      37.788 -60.044  -8.785  1.00160.46           C  
ATOM   4240  CA  ILE K 423      38.154 -56.192  -8.286  1.00258.39           C  
ATOM   4241  CA  TYR K 424      36.302 -53.906  -6.149  1.00309.23           C  
ATOM   4242  CA  LEU K 425      34.742 -50.456  -7.441  1.00270.20           C  
ATOM   4243  CA  LEU K 426      32.781 -47.883  -6.084  1.00355.30           C  
ATOM   4244  CA  MET K 427      29.649 -45.597  -6.568  1.00209.06           C  
ATOM   4245  CA  ARG K 428      29.063 -42.318  -4.787  1.00153.95           C  
TER    4246      ARG K 428                                                      
ATOM   4247  CA  PRO L  11     -44.443 -40.790 -46.761  1.00 68.04           C  
ATOM   4248  CA  LEU L  12     -44.775 -39.266 -43.399  1.00 82.91           C  
ATOM   4249  CA  PRO L  13     -48.303 -38.111 -43.265  1.00104.81           C  
ATOM   4250  CA  SER L  14     -48.866 -34.425 -42.983  1.00 44.99           C  
ATOM   4251  CA  LEU L  15     -48.510 -33.419 -39.376  1.00 49.04           C  
ATOM   4252  CA  ALA L  16     -50.574 -30.339 -39.971  1.00 41.32           C  
ATOM   4253  CA  PRO L  17     -53.859 -32.091 -40.229  1.00136.17           C  
ATOM   4254  CA  MET L  18     -53.345 -33.928 -36.964  1.00 37.54           C  
ATOM   4255  CA  LEU L  19     -51.927 -30.847 -35.323  1.00104.21           C  
ATOM   4256  CA  GLU L  20     -54.798 -28.595 -36.219  1.00 76.59           C  
ATOM   4257  CA  LYS L  21     -57.266 -30.457 -34.083  1.00134.63           C  
ATOM   4258  CA  VAL L  22     -54.967 -31.199 -31.149  1.00 52.58           C  
ATOM   4259  CA  LEU L  23     -53.199 -27.870 -30.883  1.00 85.08           C  
ATOM   4260  CA  PRO L  24     -55.831 -26.000 -28.983  1.00 69.71           C  
ATOM   4261  CA  ALA L  25     -55.583 -28.561 -26.205  1.00 32.18           C  
ATOM   4262  CA  VAL L  26     -52.113 -27.421 -25.285  1.00 87.32           C  
ATOM   4263  CA  VAL L  27     -51.923 -24.136 -23.489  1.00 37.09           C  
ATOM   4264  CA  SER L  28     -49.336 -21.800 -22.125  1.00 83.17           C  
ATOM   4265  CA  VAL L  29     -49.222 -21.179 -18.434  1.00 35.12           C  
ATOM   4266  CA  ARG L  30     -48.207 -17.846 -17.058  1.00153.26           C  
ATOM   4267  CA  VAL L  31     -47.059 -17.445 -13.505  1.00 45.92           C  
ATOM   4268  CA  GLU L  32     -46.210 -14.559 -11.248  1.00 39.00           C  
ATOM   4269  CA  GLY L  33     -45.184 -14.433  -7.639  1.00 19.51           C  
ATOM   4270  CA  THR L  34     -42.510 -13.980  -5.007  1.00101.29           C  
ATOM   4271  CA  ALA L  58     -39.289 -11.687  -3.108  1.00 13.30           C  
ATOM   4272  CA  GLN L  59     -38.681  -9.924  -6.362  1.00151.47           C  
ATOM   4273  CA  PRO L  60     -41.761 -10.234  -8.447  1.00152.80           C  
ATOM   4274  CA  PHE L  61     -41.062 -12.262 -11.516  1.00 60.26           C  
ATOM   4275  CA  GLU L  62     -43.010 -13.878 -14.246  1.00 29.23           C  
ATOM   4276  CA  GLY L  63     -42.416 -17.350 -15.502  1.00 21.60           C  
ATOM   4277  CA  LEU L  64     -43.822 -19.080 -18.497  1.00 83.54           C  
ATOM   4278  CA  GLY L  65     -44.520 -22.724 -19.071  1.00 22.59           C  
ATOM   4279  CA  SER L  66     -47.043 -24.913 -20.795  1.00 28.05           C  
ATOM   4280  CA  GLY L  67     -49.856 -27.205 -19.805  1.00 19.39           C  
ATOM   4281  CA  VAL L  68     -52.299 -29.580 -21.373  1.00 96.64           C  
ATOM   4282  CA  ILE L  69     -56.050 -29.593 -21.026  1.00109.07           C  
ATOM   4283  CA  ILE L  70     -56.998 -32.969 -19.636  1.00179.22           C  
ATOM   4284  CA  ASN L  71     -60.669 -32.310 -19.320  1.00 67.97           C  
ATOM   4285  CA  ALA L  72     -62.469 -29.616 -21.196  1.00 31.39           C  
ATOM   4286  CA  SER L  73     -65.548 -29.578 -19.061  1.00 33.98           C  
ATOM   4287  CA  LYS L  74     -63.831 -29.255 -15.736  1.00 85.55           C  
ATOM   4288  CA  GLY L  75     -61.017 -27.219 -17.164  1.00 25.33           C  
ATOM   4289  CA  TYR L  76     -58.300 -29.323 -15.621  1.00 69.07           C  
ATOM   4290  CA  VAL L  77     -54.853 -28.601 -16.967  1.00 39.25           C  
ATOM   4291  CA  LEU L  78     -51.812 -30.728 -16.283  1.00 51.72           C  
ATOM   4292  CA  THR L  79     -48.457 -29.086 -15.862  1.00115.09           C  
ATOM   4293  CA  ASN L  80     -45.139 -29.501 -14.137  1.00 52.12           C  
ATOM   4294  CA  ASN L  81     -44.964 -28.698 -10.471  1.00 41.38           C  
ATOM   4295  CA  HIS L  82     -41.842 -26.664 -10.966  1.00 46.46           C  
ATOM   4296  CA  VAL L  83     -43.602 -24.312 -13.293  1.00 94.65           C  
ATOM   4297  CA  ILE L  84     -46.352 -23.756 -10.696  1.00 76.65           C  
ATOM   4298  CA  ASN L  85     -44.425 -23.879  -7.454  1.00128.94           C  
ATOM   4299  CA  GLN L  86     -43.582 -20.191  -6.937  1.00155.71           C  
ATOM   4300  CA  ALA L  87     -46.822 -18.953  -8.504  1.00 68.64           C  
ATOM   4301  CA  GLN L  88     -48.844 -16.489  -6.513  1.00 47.74           C  
ATOM   4302  CA  LYS L  89     -51.243 -16.262  -9.414  1.00 30.80           C  
ATOM   4303  CA  ILE L  90     -51.588 -18.361 -12.509  1.00 40.64           C  
ATOM   4304  CA  SER L  91     -53.119 -17.624 -15.852  1.00 77.26           C  
ATOM   4305  CA  ILE L  92     -53.649 -19.884 -18.820  1.00 95.32           C  
ATOM   4306  CA  GLN L  93     -53.652 -18.720 -22.395  1.00 33.58           C  
ATOM   4307  CA  LEU L  94     -55.165 -20.562 -25.307  1.00 98.05           C  
ATOM   4308  CA  ASN L  95     -53.669 -20.531 -28.762  1.00 94.20           C  
ATOM   4309  CA  ASP L  96     -56.671 -18.495 -29.826  1.00 51.79           C  
ATOM   4310  CA  GLY L  97     -55.577 -15.730 -27.502  1.00 30.52           C  
ATOM   4311  CA  ARG L  98     -58.216 -16.256 -24.868  1.00195.05           C  
ATOM   4312  CA  GLU L  99     -56.932 -16.100 -21.343  1.00 37.74           C  
ATOM   4313  CA  PHE L 100     -58.279 -17.587 -18.160  1.00 53.26           C  
ATOM   4314  CA  ASP L 101     -57.390 -17.619 -14.496  1.00 36.12           C  
ATOM   4315  CA  ALA L 102     -56.370 -20.878 -12.913  1.00 31.77           C  
ATOM   4316  CA  LYS L 103     -56.043 -22.232  -9.423  1.00148.17           C  
ATOM   4317  CA  LEU L 104     -53.696 -24.930  -8.244  1.00130.82           C  
ATOM   4318  CA  ILE L 105     -55.717 -28.034  -7.553  1.00 62.48           C  
ATOM   4319  CA  GLY L 106     -52.754 -29.960  -6.237  1.00 33.56           C  
ATOM   4320  CA  SER L 107     -49.328 -31.196  -7.175  1.00 60.18           C  
ATOM   4321  CA  ASP L 108     -46.393 -33.133  -5.932  1.00118.82           C  
ATOM   4322  CA  ASP L 109     -42.644 -32.624  -5.930  1.00 71.71           C  
ATOM   4323  CA  GLN L 110     -41.283 -36.090  -6.385  1.00103.66           C  
ATOM   4324  CA  SER L 111     -42.932 -36.850  -9.738  1.00 65.73           C  
ATOM   4325  CA  ASP L 112     -43.159 -33.132 -10.550  1.00 76.57           C  
ATOM   4326  CA  ILE L 113     -46.808 -33.251 -11.629  1.00 98.30           C  
ATOM   4327  CA  ALA L 114     -49.330 -30.545 -10.823  1.00 34.93           C  
ATOM   4328  CA  LEU L 115     -52.978 -30.050 -11.676  1.00 60.35           C  
ATOM   4329  CA  LEU L 116     -54.581 -26.735 -12.429  1.00 70.61           C  
ATOM   4330  CA  GLN L 117     -58.188 -25.816 -12.850  1.00 40.63           C  
ATOM   4331  CA  ILE L 118     -59.331 -23.075 -15.144  1.00 43.93           C  
ATOM   4332  CA  GLN L 119     -61.884 -20.729 -13.735  1.00 97.80           C  
ATOM   4333  CA  ASN L 120     -64.959 -20.387 -15.882  1.00137.11           C  
ATOM   4334  CA  PRO L 121     -63.586 -22.647 -18.536  1.00 68.79           C  
ATOM   4335  CA  SER L 122     -65.542 -22.368 -21.744  1.00 40.61           C  
ATOM   4336  CA  LYS L 123     -65.365 -23.946 -25.181  1.00 48.19           C  
ATOM   4337  CA  LEU L 124     -62.176 -25.745 -24.401  1.00 75.48           C  
ATOM   4338  CA  THR L 125     -60.581 -28.605 -26.250  1.00 99.92           C  
ATOM   4339  CA  GLN L 126     -59.364 -31.748 -24.563  1.00 50.59           C  
ATOM   4340  CA  ILE L 127     -56.387 -33.905 -25.399  1.00102.11           C  
ATOM   4341  CA  ALA L 128     -56.772 -37.638 -25.638  1.00 35.25           C  
ATOM   4342  CA  ILE L 129     -54.373 -39.707 -23.598  1.00184.92           C  
ATOM   4343  CA  ALA L 130     -52.446 -42.566 -25.078  1.00 43.00           C  
ATOM   4344  CA  ASP L 131     -51.164 -45.534 -23.186  1.00 50.07           C  
ATOM   4345  CA  SER L 132     -47.547 -44.746 -22.462  1.00 39.49           C  
ATOM   4346  CA  ASP L 133     -46.588 -48.320 -21.795  1.00 51.98           C  
ATOM   4347  CA  LYS L 134     -47.228 -49.094 -25.458  1.00118.55           C  
ATOM   4348  CA  LEU L 135     -44.504 -46.756 -26.671  1.00 67.25           C  
ATOM   4349  CA  ARG L 136     -41.425 -48.186 -28.303  1.00114.75           C  
ATOM   4350  CA  VAL L 137     -38.239 -46.506 -29.321  1.00 27.44           C  
ATOM   4351  CA  GLY L 138     -38.460 -45.159 -32.821  1.00 26.74           C  
ATOM   4352  CA  ASP L 139     -42.027 -43.994 -32.483  1.00 30.96           C  
ATOM   4353  CA  PHE L 140     -42.658 -40.482 -33.727  1.00 59.04           C  
ATOM   4354  CA  ALA L 141     -43.361 -37.728 -31.270  1.00 34.88           C  
ATOM   4355  CA  VAL L 142     -44.271 -34.075 -31.453  1.00 31.69           C  
ATOM   4356  CA  ALA L 143     -43.672 -31.660 -28.656  1.00 29.74           C  
ATOM   4357  CA  VAL L 144     -45.844 -28.644 -28.136  1.00 27.90           C  
ATOM   4358  CA  GLY L 145     -45.218 -25.874 -25.670  1.00 21.12           C  
ATOM   4359  CA  ASN L 146     -43.928 -22.372 -25.527  1.00 64.67           C  
ATOM   4360  CA  PRO L 147     -40.234 -22.198 -25.763  1.00 71.42           C  
ATOM   4361  CA  PHE L 148     -38.789 -18.878 -24.704  1.00 62.60           C  
ATOM   4362  CA  GLY L 149     -42.358 -17.726 -24.392  1.00 25.55           C  
ATOM   4363  CA  LEU L 150     -42.519 -17.278 -28.126  1.00 90.06           C  
ATOM   4364  CA  GLY L 151     -45.976 -18.759 -28.334  1.00 29.56           C  
ATOM   4365  CA  GLN L 152     -47.239 -22.178 -29.142  1.00 61.96           C  
ATOM   4366  CA  THR L 153     -44.536 -24.008 -30.982  1.00 40.70           C  
ATOM   4367  CA  ALA L 154     -44.436 -27.537 -32.251  1.00 26.34           C  
ATOM   4368  CA  THR L 155     -41.304 -29.559 -32.741  1.00 32.11           C  
ATOM   4369  CA  SER L 156     -40.869 -33.046 -34.072  1.00 34.88           C  
ATOM   4370  CA  GLY L 157     -38.716 -35.998 -33.176  1.00 27.37           C  
ATOM   4371  CA  ILE L 158     -38.759 -39.651 -32.211  1.00132.78           C  
ATOM   4372  CA  VAL L 159     -38.936 -41.467 -28.922  1.00 44.63           C  
ATOM   4373  CA  SER L 160     -35.273 -41.927 -28.104  1.00 48.78           C  
ATOM   4374  CA  ALA L 161     -35.666 -44.066 -25.025  1.00 40.58           C  
ATOM   4375  CA  LEU L 162     -38.051 -44.931 -22.252  1.00 91.18           C  
ATOM   4376  CA  GLY L 163     -37.922 -45.980 -18.676  1.00 35.46           C  
ATOM   4377  CA  ARG L 164     -35.037 -43.793 -17.912  1.00181.26           C  
ATOM   4378  CA  SER L 165     -34.046 -42.592 -14.532  1.00118.25           C  
ATOM   4379  CA  GLY L 166     -31.034 -41.959 -12.412  1.00 35.74           C  
ATOM   4380  CA  LEU L 167     -31.025 -38.488 -13.892  1.00 52.13           C  
ATOM   4381  CA  ASN L 168     -31.596 -37.325 -10.347  1.00 71.69           C  
ATOM   4382  CA  LEU L 169     -33.790 -34.642 -11.797  1.00 51.82           C  
ATOM   4383  CA  GLU L 170     -36.773 -35.887  -9.845  1.00 98.19           C  
ATOM   4384  CA  GLY L 171     -37.479 -38.081  -6.854  1.00 40.74           C  
ATOM   4385  CA  LEU L 172     -39.420 -40.470  -9.017  1.00128.81           C  
ATOM   4386  CA  GLU L 173     -38.307 -40.665 -12.570  1.00 93.96           C  
ATOM   4387  CA  ASN L 174     -39.312 -42.655 -15.619  1.00 96.33           C  
ATOM   4388  CA  PHE L 175     -38.747 -40.246 -18.343  1.00 81.45           C  
ATOM   4389  CA  ILE L 176     -39.542 -40.874 -21.926  1.00 69.07           C  
ATOM   4390  CA  GLN L 177     -36.611 -39.488 -23.816  1.00100.39           C  
ATOM   4391  CA  THR L 178     -37.183 -37.545 -26.992  1.00 52.25           C  
ATOM   4392  CA  ASP L 179     -35.101 -35.865 -29.671  1.00152.87           C  
ATOM   4393  CA  ALA L 180     -37.789 -33.278 -30.292  1.00 42.83           C  
ATOM   4394  CA  SER L 181     -36.462 -29.867 -29.495  1.00 47.35           C  
ATOM   4395  CA  ILE L 182     -37.417 -28.969 -25.977  1.00 97.07           C  
ATOM   4396  CA  ASN L 183     -36.283 -25.707 -24.502  1.00 70.01           C  
ATOM   4397  CA  ARG L 184     -37.115 -23.666 -21.489  1.00126.48           C  
ATOM   4398  CA  GLY L 185     -40.781 -22.843 -21.484  1.00 23.58           C  
ATOM   4399  CA  ASN L 186     -41.535 -26.326 -22.763  1.00 51.63           C  
ATOM   4400  CA  ALA L 187     -42.173 -27.632 -19.283  1.00 41.60           C  
ATOM   4401  CA  GLY L 188     -45.693 -28.803 -18.676  1.00 24.62           C  
ATOM   4402  CA  GLY L 189     -46.125 -29.017 -22.417  1.00 22.47           C  
ATOM   4403  CA  ALA L 190     -47.374 -32.007 -24.297  1.00 43.44           C  
ATOM   4404  CA  LEU L 191     -45.529 -34.743 -26.097  1.00125.74           C  
ATOM   4405  CA  LEU L 192     -47.818 -36.224 -28.652  1.00100.64           C  
ATOM   4406  CA  ASN L 193     -48.098 -39.239 -30.886  1.00 60.69           C  
ATOM   4407  CA  LEU L 194     -48.873 -39.025 -34.581  1.00 45.20           C  
ATOM   4408  CA  ASN L 195     -52.415 -39.636 -33.445  1.00 48.36           C  
ATOM   4409  CA  GLY L 196     -52.227 -36.414 -31.509  1.00 23.77           C  
ATOM   4410  CA  GLU L 197     -52.660 -38.400 -28.329  1.00 49.78           C  
ATOM   4411  CA  LEU L 198     -50.754 -37.443 -25.192  1.00 84.47           C  
ATOM   4412  CA  ILE L 199     -47.635 -39.553 -24.707  1.00237.53           C  
ATOM   4413  CA  GLY L 200     -46.257 -37.590 -21.805  1.00 35.39           C  
ATOM   4414  CA  ILE L 201     -45.593 -34.182 -20.320  1.00 43.33           C  
ATOM   4415  CA  ASN L 202     -42.242 -32.633 -21.130  1.00 87.46           C  
ATOM   4416  CA  THR L 203     -40.482 -32.163 -17.808  1.00 81.95           C  
ATOM   4417  CA  ALA L 204     -36.840 -31.434 -18.473  1.00 53.05           C  
ATOM   4418  CA  ILE L 205     -33.837 -31.514 -20.720  1.00125.64           C  
ATOM   4419  CA  LEU L 206     -30.158 -32.237 -20.385  1.00 67.94           C  
ATOM   4420  CA  ALA L 207     -28.118 -29.605 -22.020  1.00 75.64           C  
ATOM   4421  CA  PRO L 208     -24.857 -28.059 -21.338  1.00321.86           C  
ATOM   4422  CA  GLY L 209     -25.565 -24.738 -22.927  1.00237.83           C  
ATOM   4423  CA  GLY L 210     -29.049 -24.472 -21.533  1.00 45.64           C  
ATOM   4424  CA  GLY L 211     -30.380 -24.989 -25.037  1.00 31.17           C  
ATOM   4425  CA  SER L 212     -31.863 -28.123 -26.516  1.00 67.67           C  
ATOM   4426  CA  VAL L 213     -29.211 -30.750 -27.188  1.00156.34           C  
ATOM   4427  CA  GLY L 214     -31.784 -33.136 -28.499  1.00 43.40           C  
ATOM   4428  CA  ILE L 215     -32.053 -34.944 -25.206  1.00 98.01           C  
ATOM   4429  CA  GLY L 216     -35.369 -34.196 -23.577  1.00 23.06           C  
ATOM   4430  CA  PHE L 217     -37.351 -36.041 -20.961  1.00 46.94           C  
ATOM   4431  CA  ALA L 218     -41.062 -36.302 -20.387  1.00 35.11           C  
ATOM   4432  CA  ILE L 219     -43.273 -37.861 -17.759  1.00 80.69           C  
ATOM   4433  CA  PRO L 220     -45.214 -40.607 -19.330  1.00 96.27           C  
ATOM   4434  CA  SER L 221     -48.894 -40.154 -20.036  1.00 43.94           C  
ATOM   4435  CA  ASN L 222     -49.773 -43.020 -17.843  1.00 61.79           C  
ATOM   4436  CA  MET L 223     -47.828 -41.093 -15.351  1.00123.82           C  
ATOM   4437  CA  ALA L 224     -49.628 -37.837 -15.512  1.00 53.01           C  
ATOM   4438  CA  ARG L 225     -53.006 -39.356 -16.036  1.00102.06           C  
ATOM   4439  CA  THR L 226     -53.479 -41.305 -12.891  1.00 70.62           C  
ATOM   4440  CA  LEU L 227     -51.398 -38.849 -10.838  1.00120.10           C  
ATOM   4441  CA  ALA L 228     -53.659 -36.147 -12.110  1.00 49.35           C  
ATOM   4442  CA  GLN L 229     -56.663 -38.250 -11.370  1.00 88.38           C  
ATOM   4443  CA  GLN L 230     -56.468 -38.449  -7.627  1.00 85.43           C  
ATOM   4444  CA  LEU L 231     -55.367 -34.896  -7.610  1.00 82.94           C  
ATOM   4445  CA  ILE L 232     -58.912 -34.247  -8.650  1.00112.47           C  
ATOM   4446  CA  ASP L 233     -60.051 -37.469  -6.949  1.00184.11           C  
ATOM   4447  CA  PHE L 234     -59.563 -39.390  -4.852  1.00207.51           C  
ATOM   4448  CA  GLY L 235     -56.622 -37.452  -3.631  1.00 52.13           C  
ATOM   4449  CA  GLU L 236     -56.465 -38.952  -0.234  1.00 82.48           C  
ATOM   4450  CA  ILE L 237     -53.949 -36.579   1.086  1.00157.68           C  
ATOM   4451  CA  LYS L 238     -51.590 -39.137   2.517  1.00207.77           C  
ATOM   4452  CA  ARG L 239     -48.991 -39.585   1.983  1.00219.41           C  
ATOM   4453  CA  GLY L 240     -49.105 -37.157  -0.872  1.00125.70           C  
ATOM   4454  CA  LEU L 241     -46.040 -38.323  -2.484  1.00279.73           C  
ATOM   4455  CA  LEU L 242     -43.346 -40.600  -1.557  1.00113.64           C  
ATOM   4456  CA  GLY L 243     -41.415 -37.413  -0.961  1.00 53.67           C  
ATOM   4457  CA  ILE L 244     -37.978 -38.763  -1.517  1.00 91.60           C  
ATOM   4458  CA  LYS L 245     -34.962 -38.160  -3.701  1.00105.33           C  
ATOM   4459  CA  GLY L 246     -33.000 -40.813  -5.440  1.00 37.23           C  
ATOM   4460  CA  THR L 247     -30.969 -41.739  -8.447  1.00139.37           C  
ATOM   4461  CA  GLU L 248     -29.875 -44.729 -10.384  1.00 88.57           C  
ATOM   4462  CA  MET L 249     -28.560 -47.933  -8.956  1.00 85.29           C  
ATOM   4463  CA  SER L 250     -25.156 -49.117  -9.927  1.00 57.39           C  
ATOM   4464  CA  ALA L 251     -23.260 -52.056 -11.257  1.00 45.05           C  
ATOM   4465  CA  ASP L 252     -21.243 -52.214  -8.080  1.00 47.99           C  
ATOM   4466  CA  ILE L 253     -24.251 -53.249  -6.111  1.00 84.50           C  
ATOM   4467  CA  ALA L 254     -25.214 -55.573  -8.890  1.00 30.80           C  
ATOM   4468  CA  LYS L 255     -21.994 -57.474  -8.568  1.00113.00           C  
ATOM   4469  CA  ALA L 256     -22.306 -58.040  -4.867  1.00 38.58           C  
ATOM   4470  CA  PHE L 257     -26.031 -58.480  -4.596  1.00 76.88           C  
ATOM   4471  CA  ASN L 258     -26.980 -61.008  -7.195  1.00 78.00           C  
ATOM   4472  CA  LEU L 259     -30.055 -59.300  -5.929  1.00154.81           C  
ATOM   4473  CA  ASP L 260     -33.708 -59.883  -6.426  1.00 54.34           C  
ATOM   4474  CA  VAL L 261     -33.420 -56.855  -8.632  1.00 51.34           C  
ATOM   4475  CA  GLN L 262     -30.351 -56.149 -10.654  1.00 55.61           C  
ATOM   4476  CA  ARG L 263     -30.560 -52.474  -9.982  1.00 94.16           C  
ATOM   4477  CA  GLY L 264     -33.078 -50.440  -8.118  1.00 23.59           C  
ATOM   4478  CA  ALA L 265     -34.010 -46.898  -7.291  1.00 45.70           C  
ATOM   4479  CA  PHE L 266     -31.664 -45.848  -4.624  1.00122.86           C  
ATOM   4480  CA  VAL L 267     -32.585 -43.245  -2.148  1.00148.36           C  
ATOM   4481  CA  SER L 268     -29.986 -40.773  -1.024  1.00114.41           C  
ATOM   4482  CA  GLU L 269     -32.331 -38.697   1.071  1.00123.93           C  
ATOM   4483  CA  VAL L 270     -35.292 -38.599   3.418  1.00102.61           C  
ATOM   4484  CA  LEU L 271     -37.795 -35.762   3.236  1.00 91.47           C  
ATOM   4485  CA  PRO L 272     -39.191 -34.428   6.427  1.00 77.42           C  
ATOM   4486  CA  GLY L 273     -42.866 -34.824   7.172  1.00 31.14           C  
ATOM   4487  CA  SER L 274     -42.718 -36.634   3.926  1.00 52.64           C  
ATOM   4488  CA  GLY L 275     -44.416 -39.759   2.814  1.00 44.84           C  
ATOM   4489  CA  SER L 276     -41.131 -41.523   2.953  1.00 60.45           C  
ATOM   4490  CA  ALA L 277     -40.289 -40.513   6.490  1.00 54.12           C  
ATOM   4491  CA  LYS L 278     -43.250 -41.909   8.433  1.00115.50           C  
ATOM   4492  CA  ALA L 279     -43.269 -44.885   6.186  1.00 47.06           C  
ATOM   4493  CA  GLY L 280     -39.866 -45.002   7.694  1.00 37.69           C  
ATOM   4494  CA  VAL L 281     -37.903 -45.311   4.531  1.00 59.23           C  
ATOM   4495  CA  LYS L 282     -34.326 -44.280   5.109  1.00121.05           C  
ATOM   4496  CA  ALA L 283     -31.832 -42.598   2.999  1.00 99.96           C  
ATOM   4497  CA  GLY L 284     -29.575 -45.451   1.739  1.00 61.78           C  
ATOM   4498  CA  ASP L 285     -32.634 -47.327   0.605  1.00125.15           C  
ATOM   4499  CA  ILE L 286     -32.741 -49.292  -2.419  1.00122.17           C  
ATOM   4500  CA  ILE L 287     -36.235 -49.652  -3.719  1.00 76.61           C  
ATOM   4501  CA  THR L 288     -36.390 -53.052  -5.353  1.00 66.18           C  
ATOM   4502  CA  SER L 289     -39.999 -53.130  -6.242  1.00 53.79           C  
ATOM   4503  CA  LEU L 290     -43.282 -51.371  -6.122  1.00 82.88           C  
ATOM   4504  CA  ASN L 291     -46.283 -53.434  -5.344  1.00276.22           C  
ATOM   4505  CA  GLY L 292     -46.772 -57.049  -6.181  1.00154.33           C  
ATOM   4506  CA  LYS L 293     -44.674 -57.190  -9.289  1.00165.53           C  
ATOM   4507  CA  PRO L 294     -41.045 -56.450  -9.534  1.00 65.23           C  
ATOM   4508  CA  LEU L 295     -39.853 -52.917 -10.144  1.00148.03           C  
ATOM   4509  CA  ASN L 296     -37.072 -52.099 -12.545  1.00165.33           C  
ATOM   4510  CA  SER L 297     -34.620 -49.269 -12.404  1.00 54.77           C  
ATOM   4511  CA  PHE L 298     -35.326 -46.014 -10.714  1.00111.00           C  
ATOM   4512  CA  ALA L 299     -36.598 -45.224 -14.146  1.00 49.55           C  
ATOM   4513  CA  GLU L 300     -39.340 -47.764 -13.943  1.00123.46           C  
ATOM   4514  CA  LEU L 301     -40.017 -46.380 -10.526  1.00 71.82           C  
ATOM   4515  CA  ARG L 302     -41.381 -43.092 -11.573  1.00162.76           C  
ATOM   4516  CA  SER L 303     -42.907 -44.713 -14.559  1.00 55.00           C  
ATOM   4517  CA  ARG L 304     -45.271 -46.627 -12.444  1.00159.96           C  
ATOM   4518  CA  ILE L 305     -45.595 -44.158  -9.581  1.00 75.58           C  
ATOM   4519  CA  ALA L 306     -45.776 -41.143 -11.720  1.00 70.90           C  
ATOM   4520  CA  THR L 307     -48.315 -43.252 -13.478  1.00 64.14           C  
ATOM   4521  CA  THR L 308     -50.283 -44.083 -10.371  1.00 52.87           C  
ATOM   4522  CA  GLU L 309     -52.556 -41.894  -8.323  1.00 74.15           C  
ATOM   4523  CA  PRO L 310     -50.499 -39.662  -6.184  1.00248.86           C  
ATOM   4524  CA  GLY L 311     -52.483 -40.815  -3.358  1.00205.32           C  
ATOM   4525  CA  THR L 312     -52.688 -44.508  -4.042  1.00 90.48           C  
ATOM   4526  CA  LYS L 313     -51.486 -46.130  -0.847  1.00 78.03           C  
ATOM   4527  CA  VAL L 314     -49.074 -48.616  -2.413  1.00171.78           C  
ATOM   4528  CA  LYS L 315     -46.449 -50.719  -0.696  1.00 77.74           C  
ATOM   4529  CA  LEU L 316     -42.788 -50.597  -1.544  1.00107.21           C  
ATOM   4530  CA  GLY L 317     -40.103 -53.185  -1.252  1.00 49.48           C  
ATOM   4531  CA  LEU L 318     -37.017 -51.461  -0.117  1.00124.51           C  
ATOM   4532  CA  LEU L 319     -33.674 -53.334  -0.257  1.00199.29           C  
ATOM   4533  CA  ARG L 320     -31.191 -52.183   2.021  1.00233.48           C  
ATOM   4534  CA  ASN L 321     -29.098 -53.682   4.490  1.00209.44           C  
ATOM   4535  CA  GLY L 322     -29.267 -57.043   2.813  1.00 52.04           C  
ATOM   4536  CA  LYS L 323     -32.309 -57.722   4.834  1.00187.38           C  
ATOM   4537  CA  PRO L 324     -35.552 -57.524   3.029  1.00147.41           C  
ATOM   4538  CA  LEU L 325     -38.176 -54.894   3.954  1.00151.02           C  
ATOM   4539  CA  GLU L 326     -41.752 -54.109   2.917  1.00113.70           C  
ATOM   4540  CA  VAL L 327     -43.526 -50.895   3.864  1.00125.39           C  
ATOM   4541  CA  GLU L 328     -46.721 -49.030   3.179  1.00 54.10           C  
ATOM   4542  CA  VAL L 329     -45.851 -45.588   1.930  1.00 67.31           C  
ATOM   4543  CA  SER L 340     -44.726 -21.691  25.202  1.00104.52           C  
ATOM   4544  CA  ALA L 341     -44.274 -17.932  25.122  1.00 79.86           C  
ATOM   4545  CA  GLU L 342     -41.193 -18.094  22.951  1.00 61.73           C  
ATOM   4546  CA  MET L 343     -42.763 -18.533  19.591  1.00 42.87           C  
ATOM   4547  CA  ILE L 344     -45.114 -15.644  20.037  1.00115.92           C  
ATOM   4548  CA  THR L 345     -42.533 -13.642  21.867  1.00137.09           C  
ATOM   4549  CA  PRO L 346     -38.973 -13.636  20.751  1.00155.38           C  
ATOM   4550  CA  ALA L 347     -36.371 -15.408  22.856  1.00 72.28           C  
ATOM   4551  CA  LEU L 348     -38.466 -14.944  25.970  1.00 98.88           C  
ATOM   4552  CA  GLU L 349     -38.725 -18.392  27.367  1.00129.16           C  
ATOM   4553  CA  GLY L 350     -41.558 -18.727  29.760  1.00 29.34           C  
ATOM   4554  CA  ALA L 351     -44.978 -20.149  30.344  1.00 38.76           C  
ATOM   4555  CA  THR L 352     -46.611 -22.005  27.516  1.00 96.98           C  
ATOM   4556  CA  LEU L 353     -49.440 -20.348  25.688  1.00 60.43           C  
ATOM   4557  CA  SER L 354     -52.670 -21.765  24.344  1.00 34.81           C  
ATOM   4558  CA  ASP L 355     -55.312 -20.420  21.991  1.00 55.55           C  
ATOM   4559  CA  GLY L 356     -58.953 -20.018  22.666  1.00 46.53           C  
ATOM   4560  CA  GLN L 357     -60.547 -18.958  25.877  1.00166.63           C  
ATOM   4561  CA  LEU L 358     -60.713 -22.580  25.749  1.00232.19           C  
ATOM   4562  CA  LYS L 359     -63.059 -22.773  28.700  1.00128.33           C  
ATOM   4563  CA  ASP L 360     -65.157 -19.718  27.789  1.00 53.27           C  
ATOM   4564  CA  GLY L 361     -65.555 -17.654  24.668  1.00 31.23           C  
ATOM   4565  CA  GLY L 362     -62.092 -16.590  23.646  1.00 38.32           C  
ATOM   4566  CA  LYS L 363     -61.087 -13.809  25.945  1.00 89.70           C  
ATOM   4567  CA  GLY L 364     -57.686 -14.369  24.530  1.00 29.26           C  
ATOM   4568  CA  ILE L 365     -54.570 -16.464  24.701  1.00 63.17           C  
ATOM   4569  CA  LYS L 366     -54.062 -18.431  27.868  1.00 71.54           C  
ATOM   4570  CA  ILE L 367     -50.732 -19.069  29.459  1.00 58.26           C  
ATOM   4571  CA  ASP L 368     -50.637 -22.683  30.498  1.00 61.59           C  
ATOM   4572  CA  GLU L 369     -47.915 -22.762  33.076  1.00 86.78           C  
ATOM   4573  CA  VAL L 370     -45.116 -20.606  34.359  1.00121.13           C  
ATOM   4574  CA  VAL L 371     -41.552 -21.837  33.938  1.00120.37           C  
ATOM   4575  CA  LYS L 372     -40.864 -19.010  36.434  1.00213.94           C  
ATOM   4576  CA  GLY L 373     -37.109 -19.270  36.401  1.00 39.93           C  
ATOM   4577  CA  SER L 374     -37.624 -18.200  32.760  1.00 41.06           C  
ATOM   4578  CA  PRO L 375     -37.824 -14.622  31.695  1.00 74.19           C  
ATOM   4579  CA  ALA L 376     -41.457 -14.766  30.689  1.00 49.50           C  
ATOM   4580  CA  ALA L 377     -41.748 -15.168  34.421  1.00 49.77           C  
ATOM   4581  CA  GLN L 378     -39.304 -12.339  34.962  1.00 58.24           C  
ATOM   4582  CA  ALA L 379     -41.572  -9.706  33.507  1.00 81.26           C  
ATOM   4583  CA  GLY L 380     -44.659 -10.891  35.302  1.00 90.57           C  
ATOM   4584  CA  LEU L 381     -46.452 -13.438  33.310  1.00 71.68           C  
ATOM   4585  CA  GLN L 382     -48.090 -15.691  35.868  1.00 53.47           C  
ATOM   4586  CA  LYS L 383     -49.937 -18.847  34.958  1.00118.88           C  
ATOM   4587  CA  ASP L 384     -53.665 -18.849  34.290  1.00144.69           C  
ATOM   4588  CA  ASP L 385     -53.615 -15.328  32.982  1.00 60.73           C  
ATOM   4589  CA  VAL L 386     -55.594 -14.529  29.863  1.00 59.81           C  
ATOM   4590  CA  ILE L 387     -54.201 -12.079  27.375  1.00 78.79           C  
ATOM   4591  CA  ILE L 388     -57.262 -10.220  26.135  1.00155.65           C  
ATOM   4592  CA  GLY L 389     -55.409  -8.321  23.379  1.00 81.25           C  
ATOM   4593  CA  VAL L 390     -52.221  -6.351  22.672  1.00173.31           C  
ATOM   4594  CA  ASN L 391     -51.738  -2.590  22.389  1.00 95.42           C  
ATOM   4595  CA  ARG L 392     -55.395  -1.550  22.466  1.00237.12           C  
ATOM   4596  CA  ASP L 393     -56.134  -4.374  20.122  1.00 63.78           C  
ATOM   4597  CA  ARG L 394     -58.058  -7.296  21.369  1.00170.81           C  
ATOM   4598  CA  VAL L 395     -56.514 -10.689  20.935  1.00 62.25           C  
ATOM   4599  CA  ASN L 396     -59.031 -13.452  20.499  1.00 64.87           C  
ATOM   4600  CA  SER L 397     -56.339 -16.005  19.788  1.00 39.13           C  
ATOM   4601  CA  ILE L 398     -52.639 -16.406  19.104  1.00 96.15           C  
ATOM   4602  CA  ALA L 399     -52.886 -15.532  15.453  1.00 26.57           C  
ATOM   4603  CA  GLU L 400     -54.332 -12.135  16.250  1.00 46.59           C  
ATOM   4604  CA  MET L 401     -51.789 -11.533  18.953  1.00 38.80           C  
ATOM   4605  CA  ARG L 402     -49.146 -12.345  16.403  1.00 98.01           C  
ATOM   4606  CA  LYS L 403     -50.603  -9.692  14.176  1.00115.30           C  
ATOM   4607  CA  VAL L 404     -50.062  -6.865  16.612  1.00 41.18           C  
ATOM   4608  CA  LEU L 405     -46.590  -8.205  17.253  1.00 48.63           C  
ATOM   4609  CA  ALA L 406     -46.058  -8.089  13.525  1.00 30.54           C  
ATOM   4610  CA  ALA L 407     -46.187  -4.335  13.846  1.00 31.15           C  
ATOM   4611  CA  LYS L 408     -43.417  -4.892  16.349  1.00177.85           C  
ATOM   4612  CA  PRO L 409     -44.068  -1.855  18.403  1.00 74.54           C  
ATOM   4613  CA  ALA L 410     -41.151  -1.164  20.701  1.00 32.62           C  
ATOM   4614  CA  ILE L 411     -43.719  -1.195  23.449  1.00 89.00           C  
ATOM   4615  CA  ILE L 412     -46.116  -4.101  23.454  1.00 99.74           C  
ATOM   4616  CA  ALA L 413     -49.048  -4.010  25.787  1.00 70.20           C  
ATOM   4617  CA  LEU L 414     -50.360  -7.334  27.145  1.00246.58           C  
ATOM   4618  CA  GLN L 415     -53.401  -7.288  29.363  1.00168.34           C  
ATOM   4619  CA  ILE L 416     -54.206 -10.334  31.105  1.00138.86           C  
ATOM   4620  CA  VAL L 417     -57.126 -10.932  33.301  1.00 77.59           C  
ATOM   4621  CA  ARG L 418     -55.906 -12.421  36.484  1.00127.05           C  
ATOM   4622  CA  GLY L 419     -58.480 -13.780  38.841  1.00 24.07           C  
ATOM   4623  CA  ASN L 420     -61.437 -11.520  38.620  1.00 57.50           C  
ATOM   4624  CA  GLU L 421     -59.116  -8.640  38.048  1.00 59.24           C  
ATOM   4625  CA  SER L 422     -57.465  -7.387  34.992  1.00 76.48           C  
ATOM   4626  CA  ILE L 423     -53.656  -7.176  34.891  1.00162.78           C  
ATOM   4627  CA  TYR L 424     -52.069  -5.290  32.130  1.00343.85           C  
ATOM   4628  CA  LEU L 425     -48.497  -6.525  31.577  1.00244.41           C  
ATOM   4629  CA  LEU L 426     -45.588  -5.294  29.748  1.00316.85           C  
ATOM   4630  CA  MET L 427     -42.856  -6.668  27.220  1.00225.73           C  
ATOM   4631  CA  ARG L 428     -39.571  -4.760  26.525  1.00204.89           C  
TER    4632      ARG L 428                                                      
ATOM   4633  CA  LYS M   1       9.575   9.133 -24.201  1.00 50.47           C  
ATOM   4634  CA  VAL M   2      10.785   5.631 -24.586  1.00 99.60           C  
ATOM   4635  CA  PHE M   3       8.178   3.173 -23.502  1.00 63.39           C  
ATOM   4636  CA  GLY M   4       8.989  -0.136 -21.987  1.00 20.55           C  
ATOM   4637  CA  ARG M   5       7.642  -3.092 -23.875  1.00 77.02           C  
ATOM   4638  CA  CYS M   6       4.991  -3.833 -21.296  1.00 30.46           C  
ATOM   4639  CA  GLU M   7       4.378  -0.206 -20.577  1.00 28.17           C  
ATOM   4640  CA  LEU M   8       3.639   0.465 -24.193  1.00 38.34           C  
ATOM   4641  CA  ALA M   9       1.428  -2.566 -24.398  1.00 24.00           C  
ATOM   4642  CA  ALA M  10      -0.521  -1.320 -21.435  1.00 21.26           C  
ATOM   4643  CA  ALA M  11      -0.787   2.119 -22.942  1.00 28.38           C  
ATOM   4644  CA  MET M  12      -1.815   0.688 -26.272  1.00 42.33           C  
ATOM   4645  CA  LYS M  13      -4.369  -1.444 -24.501  1.00 82.86           C  
ATOM   4646  CA  ARG M  14      -5.717   1.532 -22.660  1.00118.14           C  
ATOM   4647  CA  HIS M  15      -5.905   3.345 -25.958  1.00 73.52           C  
ATOM   4648  CA  GLY M  16      -7.976   0.474 -27.247  1.00 28.47           C  
ATOM   4649  CA  LEU M  17      -5.409  -0.685 -29.755  1.00 60.63           C  
ATOM   4650  CA  ASP M  18      -5.555  -4.197 -28.399  1.00 56.30           C  
ATOM   4651  CA  ASN M  19      -7.272  -6.329 -30.977  1.00159.02           C  
ATOM   4652  CA  TYR M  20      -8.108  -3.230 -32.921  1.00 59.67           C  
ATOM   4653  CA  ARG M  21      -8.834  -4.309 -36.448  1.00297.83           C  
ATOM   4654  CA  GLY M  22      -8.258  -7.728 -35.090  1.00 23.26           C  
ATOM   4655  CA  TYR M  23      -4.660  -6.884 -34.500  1.00 65.11           C  
ATOM   4656  CA  SER M  24      -3.462  -8.251 -31.235  1.00 34.54           C  
ATOM   4657  CA  LEU M  25      -1.636  -5.968 -28.891  1.00109.53           C  
ATOM   4658  CA  GLY M  26       1.520  -7.875 -29.613  1.00 26.81           C  
ATOM   4659  CA  ASN M  27       1.239  -6.761 -33.204  1.00 39.52           C  
ATOM   4660  CA  TRP M  28       1.013  -3.152 -32.167  1.00 67.75           C  
ATOM   4661  CA  VAL M  29       3.845  -3.477 -29.724  1.00 29.90           C  
ATOM   4662  CA  CYS M  30       5.894  -5.270 -32.289  1.00 33.20           C  
ATOM   4663  CA  ALA M  31       5.163  -2.586 -34.825  1.00 22.20           C  
ATOM   4664  CA  ALA M  32       6.070   0.055 -32.316  1.00 25.79           C  
ATOM   4665  CA  LYS M  33       9.266  -1.706 -31.475  1.00 94.75           C  
ATOM   4666  CA  PHE M  34      10.457  -1.879 -35.035  1.00 65.06           C  
ATOM   4667  CA  GLU M  35       8.989   1.449 -36.015  1.00 89.12           C  
ATOM   4668  CA  SER M  36      10.485   3.570 -33.302  1.00113.34           C  
ATOM   4669  CA  ASN M  37      11.899   1.184 -30.722  1.00129.15           C  
ATOM   4670  CA  PHE M  38       9.159   2.464 -28.463  1.00 71.79           C  
ATOM   4671  CA  ASN M  39      10.454   5.974 -28.743  1.00 42.63           C  
ATOM   4672  CA  THR M  40       7.584   8.398 -29.064  1.00 38.87           C  
ATOM   4673  CA  GLN M  41      10.099  10.992 -30.236  1.00 68.89           C  
ATOM   4674  CA  ALA M  42      11.330   8.961 -33.205  1.00 51.96           C  
ATOM   4675  CA  THR M  43      11.145  10.870 -36.433  1.00 50.71           C  
ATOM   4676  CA  ASN M  44      12.398   9.636 -39.725  1.00107.92           C  
ATOM   4677  CA  ARG M  45      11.981  11.246 -43.091  1.00168.29           C  
ATOM   4678  CA  ASN M  46      11.154   9.424 -46.252  1.00 78.39           C  
ATOM   4679  CA  THR M  47      12.711   9.441 -49.659  1.00 51.84           C  
ATOM   4680  CA  ASP M  48       9.620  11.174 -50.810  1.00 77.98           C  
ATOM   4681  CA  GLY M  49      10.287  13.888 -48.289  1.00 35.84           C  
ATOM   4682  CA  SER M  50       7.491  12.930 -45.994  1.00 47.46           C  
ATOM   4683  CA  THR M  51       8.470  11.958 -42.516  1.00 44.17           C  
ATOM   4684  CA  ASP M  52       7.370   9.203 -40.194  1.00 44.81           C  
ATOM   4685  CA  TYR M  53       6.642  10.343 -36.718  1.00 60.72           C  
ATOM   4686  CA  GLY M  54       6.230   8.791 -33.357  1.00 35.18           C  
ATOM   4687  CA  ILE M  55       6.140   5.343 -31.920  1.00 58.37           C  
ATOM   4688  CA  LEU M  56       4.007   4.252 -34.867  1.00 94.31           C  
ATOM   4689  CA  GLN M  57       6.158   6.164 -37.346  1.00 76.46           C  
ATOM   4690  CA  ILE M  58       3.009   7.602 -38.847  1.00139.21           C  
ATOM   4691  CA  ASN M  59       3.795   9.109 -42.230  1.00 56.17           C  
ATOM   4692  CA  SER M  60       3.233  12.793 -42.920  1.00 50.73           C  
ATOM   4693  CA  ARG M  61       2.412  11.902 -46.445  1.00175.39           C  
ATOM   4694  CA  TRP M  62      -1.047  10.685 -45.614  1.00113.49           C  
ATOM   4695  CA  TRP M  63      -1.618  10.904 -41.884  1.00120.56           C  
ATOM   4696  CA  CYS M  64      -0.384  14.078 -40.209  1.00 52.17           C  
ATOM   4697  CA  ASN M  65       0.570  17.601 -41.088  1.00 71.84           C  
ATOM   4698  CA  ASP M  66       4.312  18.197 -41.037  1.00 85.74           C  
ATOM   4699  CA  GLY M  67       3.978  21.320 -43.136  1.00 51.90           C  
ATOM   4700  CA  ARG M  68       6.990  19.892 -44.915  1.00153.15           C  
ATOM   4701  CA  THR M  69       5.488  17.156 -47.028  1.00209.99           C  
ATOM   4702  CA  PRO M  70       4.331  17.697 -50.546  1.00170.39           C  
ATOM   4703  CA  GLY M  71       0.958  16.478 -51.834  1.00 65.16           C  
ATOM   4704  CA  SER M  72       0.475  15.040 -48.422  1.00134.18           C  
ATOM   4705  CA  ARG M  73      -2.768  14.899 -46.614  1.00134.97           C  
ATOM   4706  CA  ASN M  74      -3.413  15.012 -42.914  1.00 72.84           C  
ATOM   4707  CA  LEU M  75      -5.988  12.253 -42.614  1.00 52.52           C  
ATOM   4708  CA  CYS M  76      -5.446  11.990 -38.899  1.00 64.84           C  
ATOM   4709  CA  ASN M  77      -6.004  15.733 -38.833  1.00 59.09           C  
ATOM   4710  CA  ILE M  78      -3.234  16.177 -36.367  1.00 49.16           C  
ATOM   4711  CA  PRO M  79       0.054  17.873 -36.496  1.00 72.49           C  
ATOM   4712  CA  CYS M  80       2.779  15.323 -36.927  1.00 37.37           C  
ATOM   4713  CA  SER M  81       4.278  16.767 -33.793  1.00 33.66           C  
ATOM   4714  CA  ALA M  82       1.261  15.407 -31.964  1.00 35.21           C  
ATOM   4715  CA  LEU M  83       2.543  11.971 -32.923  1.00 71.70           C  
ATOM   4716  CA  LEU M  84       5.731  12.751 -30.977  1.00 69.69           C  
ATOM   4717  CA  SER M  85       3.951  13.204 -27.661  1.00102.95           C  
ATOM   4718  CA  SER M  86       4.622  10.993 -24.697  1.00 70.70           C  
ATOM   4719  CA  ASP M  87       0.900  10.494 -24.641  1.00 51.00           C  
ATOM   4720  CA  ILE M  88       0.218   7.740 -27.147  1.00139.54           C  
ATOM   4721  CA  THR M  89      -3.356   8.821 -27.803  1.00 61.69           C  
ATOM   4722  CA  ALA M  90      -2.738  10.833 -30.930  1.00 31.51           C  
ATOM   4723  CA  SER M  91      -0.601   8.075 -32.377  1.00 85.66           C  
ATOM   4724  CA  VAL M  92      -3.134   5.458 -31.434  1.00 42.76           C  
ATOM   4725  CA  ASN M  93      -6.072   7.311 -32.852  1.00 26.15           C  
ATOM   4726  CA  CYS M  94      -4.118   7.951 -35.989  1.00 34.13           C  
ATOM   4727  CA  ALA M  95      -3.028   4.336 -36.048  1.00 32.16           C  
ATOM   4728  CA  LYS M  96      -6.597   3.189 -35.770  1.00 82.84           C  
ATOM   4729  CA  LYS M  97      -7.391   5.267 -38.799  1.00144.33           C  
ATOM   4730  CA  ILE M  98      -4.384   3.924 -40.647  1.00 49.08           C  
ATOM   4731  CA  VAL M  99      -5.221   0.370 -39.792  1.00 93.03           C  
ATOM   4732  CA  SER M 100      -8.776   1.065 -40.937  1.00 77.88           C  
ATOM   4733  CA  ASP M 101      -7.284   2.015 -44.266  1.00 53.22           C  
ATOM   4734  CA  GLY M 102      -7.844  -1.481 -45.608  1.00 32.97           C  
ATOM   4735  CA  ASN M 103      -4.163  -2.237 -45.831  1.00 42.93           C  
ATOM   4736  CA  GLY M 104      -4.356  -3.173 -42.199  1.00 28.68           C  
ATOM   4737  CA  MET M 105      -1.082  -3.336 -40.299  1.00152.13           C  
ATOM   4738  CA  ASN M 106       0.661  -3.760 -43.623  1.00 59.23           C  
ATOM   4739  CA  ALA M 107       0.627   0.016 -43.688  1.00 43.53           C  
ATOM   4740  CA  TRP M 108       3.508  -0.231 -41.284  1.00 61.31           C  
ATOM   4741  CA  VAL M 109       6.295  -1.630 -43.387  1.00 93.19           C  
ATOM   4742  CA  ALA M 110       8.262  -2.642 -40.362  1.00 28.00           C  
ATOM   4743  CA  TRP M 111       5.255  -4.483 -39.097  1.00 54.14           C  
ATOM   4744  CA  ARG M 112       4.878  -6.339 -42.319  1.00168.15           C  
ATOM   4745  CA  ASN M 113       8.518  -7.137 -42.532  1.00 78.19           C  
ATOM   4746  CA  ARG M 114       9.304  -7.866 -38.902  1.00124.65           C  
ATOM   4747  CA  CYS M 115       5.984  -8.372 -37.168  1.00 68.19           C  
ATOM   4748  CA  LYS M 116       3.776 -10.040 -39.690  1.00 78.07           C  
ATOM   4749  CA  GLY M 117       3.481 -13.767 -39.280  1.00 31.29           C  
ATOM   4750  CA  THR M 118       5.732 -13.755 -36.266  1.00103.65           C  
ATOM   4751  CA  ASP M 119       5.017 -14.732 -32.711  1.00 47.02           C  
ATOM   4752  CA  VAL M 120       3.900 -11.240 -31.949  1.00146.82           C  
ATOM   4753  CA  GLN M 121       2.497 -12.487 -28.658  1.00 83.90           C  
ATOM   4754  CA  ALA M 122       6.028 -12.488 -27.344  1.00 36.58           C  
ATOM   4755  CA  TRP M 123       5.891  -8.740 -27.272  1.00 73.10           C  
ATOM   4756  CA  ILE M 124       2.973  -8.888 -24.823  1.00 60.84           C  
ATOM   4757  CA  ARG M 125       4.244 -11.864 -22.814  1.00127.22           C  
ATOM   4758  CA  GLY M 126       5.121 -11.264 -19.209  1.00 21.05           C  
ATOM   4759  CA  CYS M 127       3.248  -8.034 -19.355  1.00 40.40           C  
ATOM   4760  CA  ARG M 128       0.433  -7.378 -16.991  1.00 94.18           C  
ATOM   4761  CA  LEU M 129      -2.191  -5.755 -19.112  1.00 85.76           C  
TER    4762      LEU M 129                                                      
MASTER     1355    0    0    0    0    0    0    6 4749   13    0  418          
END                                                                             
