CNRS Nantes University US2B US2B
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Should you encounter any unexpected behaviour,
please let us know.
elNémo has been hacked on november 27th.
It has been moved away and runs again.
**Still some additional cleaning from time to time**
Sorry for the inconvenience.


***  TRANSPORT PROTEIN 17-DEC-20 7L2L  ***

elNémo ID: 2602200446423711017

Job options:

ID        	=	 2602200446423711017
JOBID     	=	 TRANSPORT PROTEIN 17-DEC-20 7L2L
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


REMARK    File generated by Swiss-PdbViewer  4.00b0
REMARK    http://www.expasy.org/spdbv/
HEADER    TRANSPORT PROTEIN                       17-DEC-20   7L2L              
TITLE     CRYO-EM STRUCTURE OF RTX-BOUND FULL-LENGTH TRPV1 IN O1 STATE          
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TRANSIENT RECEPTOR POTENTIAL CATION CHANNEL SUBFAMILY V    
COMPND   3 MEMBER 1;                                                            
COMPND   4 CHAIN: A, C, D, B;                                                   
COMPND   5 SYNONYM: TRPV1,CAPSAICIN RECEPTOR,OSM-9-LIKE TRP CHANNEL 1,OTRPC1,   
COMPND   6 VANILLOID RECEPTOR 1,VANILLOID RECEPTOR TYPE 1-LIKE;                 
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RATTUS NORVEGICUS;                              
SOURCE   3 ORGANISM_COMMON: RAT;                                                
SOURCE   4 ORGANISM_TAXID: 10116;                                               
SOURCE   5 GENE: TRPV1, VR1, VR1L;                                              
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    TRP CHANNEL, NANODISC, VANILLOID AGONIST, TRANSPORT PROTEIN           
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    K.ZHANG,D.JULIUS,Y.CHENG                                              
REVDAT   3   29-MAY-24 7L2L    1       REMARK                                   
REVDAT   2   13-OCT-21 7L2L    1       JRNL                                     
REVDAT   1   22-SEP-21 7L2L    0                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.42 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 3.420                          
REMARK   3   NUMBER OF PARTICLES               : 29314                          
REMARK   3   CTF CORRECTION METHOD             : NONE                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 7L2L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 17-DEC-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000253209.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : NULL                              
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : FULL-LENGTH TRPV1 IN NANODISC     
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.40                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K2 SUMMIT (4K X 4K)      
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 7040.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, D, B                            
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 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     GLY A    -3                                                      
REMARK 465     ALA A    -2                                                      
REMARK 465     MET A    -1                                                      
REMARK 465     GLY A     0                                                      
REMARK 465     SER A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ARG A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     ASP A     8                                                      
REMARK 465     SER A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 465     GLU A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     GLU A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     PRO A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     GLU A    18                                                      
REMARK 465     ASN A    19                                                      
REMARK 465     SER A    20                                                      
REMARK 465     CYS A    21                                                      
REMARK 465     LEU A    22                                                      
REMARK 465     ASP A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     ARG A    27                                                      
REMARK 465     ASP A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     CYS A    31                                                      
REMARK 465     LYS A    32                                                      
REMARK 465     PRO A    33                                                      
REMARK 465     PRO A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     LYS A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     HIS A    39                                                      
REMARK 465     ILE A    40                                                      
REMARK 465     PHE A    41                                                      
REMARK 465     THR A    42                                                      
REMARK 465     THR A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     SER A    45                                                      
REMARK 465     ARG A    46                                                      
REMARK 465     THR A    47                                                      
REMARK 465     ARG A    48                                                      
REMARK 465     LEU A    49                                                      
REMARK 465     PHE A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     LYS A    52                                                      
REMARK 465     GLY A    53                                                      
REMARK 465     ASP A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     GLU A    56                                                      
REMARK 465     GLU A    57                                                      
REMARK 465     ALA A    58                                                      
REMARK 465     SER A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     LEU A    61                                                      
REMARK 465     ASP A    62                                                      
REMARK 465     CYS A    63                                                      
REMARK 465     PRO A    64                                                      
REMARK 465     TYR A    65                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     GLU A    67                                                      
REMARK 465     GLY A    68                                                      
REMARK 465     GLY A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     CYS A    73                                                      
REMARK 465     PRO A    74                                                      
REMARK 465     ILE A    75                                                      
REMARK 465     ILE A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     VAL A    78                                                      
REMARK 465     SER A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     VAL A    81                                                      
REMARK 465     LEU A    82                                                      
REMARK 465     THR A    83                                                      
REMARK 465     ILE A    84                                                      
REMARK 465     GLN A    85                                                      
REMARK 465     ARG A    86                                                      
REMARK 465     PRO A    87                                                      
REMARK 465     GLY A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     PRO A    91                                                      
REMARK 465     ALA A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     VAL A    94                                                      
REMARK 465     ARG A    95                                                      
REMARK 465     PRO A    96                                                      
REMARK 465     SER A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     GLN A    99                                                      
REMARK 465     ASP A   100                                                      
REMARK 465     SER A   101                                                      
REMARK 465     VAL A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     ALA A   104                                                      
REMARK 465     GLY A   105                                                      
REMARK 465     GLU A   106                                                      
REMARK 465     LYS A   107                                                      
REMARK 465     PRO A   108                                                      
REMARK 465     PRO A   109                                                      
REMARK 465     ARG A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     TYR A   112                                                      
REMARK 465     ASP A   113                                                      
REMARK 465     ARG A   114                                                      
REMARK 465     ARG A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     ILE A   117                                                      
REMARK 465     PHE A   118                                                      
REMARK 465     ASP A   119                                                      
REMARK 465     ALA A   120                                                      
REMARK 465     VAL A   121                                                      
REMARK 465     ALA A   122                                                      
REMARK 465     GLN A   123                                                      
REMARK 465     SER A   124                                                      
REMARK 465     ASN A   125                                                      
REMARK 465     CYS A   126                                                      
REMARK 465     GLN A   127                                                      
REMARK 465     GLU A   128                                                      
REMARK 465     LEU A   129                                                      
REMARK 465     GLU A   130                                                      
REMARK 465     SER A   131                                                      
REMARK 465     LEU A   132                                                      
REMARK 465     LEU A   133                                                      
REMARK 465     PRO A   134                                                      
REMARK 465     PHE A   135                                                      
REMARK 465     LEU A   136                                                      
REMARK 465     GLN A   137                                                      
REMARK 465     ARG A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     LYS A   140                                                      
REMARK 465     LYS A   141                                                      
REMARK 465     ARG A   142                                                      
REMARK 465     LEU A   143                                                      
REMARK 465     THR A   144                                                      
REMARK 465     ASP A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     PHE A   148                                                      
REMARK 465     LYS A   149                                                      
REMARK 465     ASP A   150                                                      
REMARK 465     PRO A   151                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     THR A   153                                                      
REMARK 465     GLY A   154                                                      
REMARK 465     LYS A   155                                                      
REMARK 465     THR A   156                                                      
REMARK 465     CYS A   157                                                      
REMARK 465     LEU A   158                                                      
REMARK 465     LEU A   159                                                      
REMARK 465     LYS A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     MET A   162                                                      
REMARK 465     LEU A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     LEU A   165                                                      
REMARK 465     HIS A   166                                                      
REMARK 465     ASN A   167                                                      
REMARK 465     GLY A   168                                                      
REMARK 465     GLN A   169                                                      
REMARK 465     ASN A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     THR A   172                                                      
REMARK 465     ILE A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     LEU A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     LEU A   177                                                      
REMARK 465     ASP A   178                                                      
REMARK 465     VAL A   179                                                      
REMARK 465     ALA A   180                                                      
REMARK 465     ARG A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     THR A   183                                                      
REMARK 465     ASP A   184                                                      
REMARK 465     SER A   185                                                      
REMARK 465     LEU A   186                                                      
REMARK 465     LYS A   187                                                      
REMARK 465     GLN A   188                                                      
REMARK 465     PHE A   189                                                      
REMARK 465     VAL A   190                                                      
REMARK 465     ASN A   191                                                      
REMARK 465     ALA A   192                                                      
REMARK 465     SER A   193                                                      
REMARK 465     TYR A   194                                                      
REMARK 465     THR A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     SER A   197                                                      
REMARK 465     TYR A   198                                                      
REMARK 465     TYR A   199                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     GLN A   202                                                      
REMARK 465     THR A   203                                                      
REMARK 465     ALA A   204                                                      
REMARK 465     LEU A   205                                                      
REMARK 465     HIS A   206                                                      
REMARK 465     ILE A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     ILE A   209                                                      
REMARK 465     GLU A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     ARG A   212                                                      
REMARK 465     ASN A   213                                                      
REMARK 465     MET A   214                                                      
REMARK 465     THR A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     VAL A   217                                                      
REMARK 465     THR A   218                                                      
REMARK 465     LEU A   219                                                      
REMARK 465     LEU A   220                                                      
REMARK 465     VAL A   221                                                      
REMARK 465     GLU A   222                                                      
REMARK 465     ASN A   223                                                      
REMARK 465     GLY A   224                                                      
REMARK 465     ALA A   225                                                      
REMARK 465     ASP A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     GLN A   228                                                      
REMARK 465     ALA A   229                                                      
REMARK 465     ALA A   230                                                      
REMARK 465     ALA A   231                                                      
REMARK 465     ASN A   232                                                      
REMARK 465     GLY A   233                                                      
REMARK 465     ASP A   234                                                      
REMARK 465     PHE A   235                                                      
REMARK 465     PHE A   236                                                      
REMARK 465     LYS A   237                                                      
REMARK 465     LYS A   238                                                      
REMARK 465     THR A   239                                                      
REMARK 465     LYS A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     ARG A   242                                                      
REMARK 465     PRO A   243                                                      
REMARK 465     GLY A   244                                                      
REMARK 465     PHE A   245                                                      
REMARK 465     TYR A   246                                                      
REMARK 465     PHE A   247                                                      
REMARK 465     GLY A   248                                                      
REMARK 465     GLU A   249                                                      
REMARK 465     LEU A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     LEU A   252                                                      
REMARK 465     SER A   253                                                      
REMARK 465     LEU A   254                                                      
REMARK 465     ALA A   255                                                      
REMARK 465     ALA A   256                                                      
REMARK 465     CYS A   257                                                      
REMARK 465     THR A   258                                                      
REMARK 465     ASN A   259                                                      
REMARK 465     GLN A   260                                                      
REMARK 465     LEU A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     ILE A   263                                                      
REMARK 465     VAL A   264                                                      
REMARK 465     LYS A   265                                                      
REMARK 465     PHE A   266                                                      
REMARK 465     LEU A   267                                                      
REMARK 465     LEU A   268                                                      
REMARK 465     GLN A   269                                                      
REMARK 465     ASN A   270                                                      
REMARK 465     SER A   271                                                      
REMARK 465     TRP A   272                                                      
REMARK 465     GLN A   273                                                      
REMARK 465     PRO A   274                                                      
REMARK 465     ALA A   275                                                      
REMARK 465     ASP A   276                                                      
REMARK 465     ILE A   277                                                      
REMARK 465     SER A   278                                                      
REMARK 465     ALA A   279                                                      
REMARK 465     ARG A   280                                                      
REMARK 465     ASP A   281                                                      
REMARK 465     SER A   282                                                      
REMARK 465     GLY A   602                                                      
REMARK 465     LYS A   603                                                      
REMARK 465     ASN A   604                                                      
REMARK 465     ASN A   605                                                      
REMARK 465     SER A   606                                                      
REMARK 465     LEU A   607                                                      
REMARK 465     PRO A   608                                                      
REMARK 465     MET A   609                                                      
REMARK 465     GLU A   610                                                      
REMARK 465     SER A   611                                                      
REMARK 465     THR A   612                                                      
REMARK 465     PRO A   613                                                      
REMARK 465     HIS A   614                                                      
REMARK 465     LYS A   615                                                      
REMARK 465     CYS A   616                                                      
REMARK 465     ARG A   617                                                      
REMARK 465     GLY A   618                                                      
REMARK 465     SER A   619                                                      
REMARK 465     ALA A   620                                                      
REMARK 465     CYS A   621                                                      
REMARK 465     LYS A   622                                                      
REMARK 465     PRO A   623                                                      
REMARK 465     GLY A   624                                                      
REMARK 465     ASN A   625                                                      
REMARK 465     GLN A   727                                                      
REMARK 465     VAL A   728                                                      
REMARK 465     GLY A   729                                                      
REMARK 465     PHE A   730                                                      
REMARK 465     THR A   731                                                      
REMARK 465     PRO A   732                                                      
REMARK 465     ASP A   733                                                      
REMARK 465     GLY A   734                                                      
REMARK 465     LYS A   735                                                      
REMARK 465     ASP A   736                                                      
REMARK 465     ASP A   737                                                      
REMARK 465     VAL A   747                                                      
REMARK 465     ASN A   748                                                      
REMARK 465     TRP A   749                                                      
REMARK 465     THR A   750                                                      
REMARK 465     THR A   751                                                      
REMARK 465     TRP A   752                                                      
REMARK 465     ASN A   753                                                      
REMARK 465     THR A   754                                                      
REMARK 465     ASN A   755                                                      
REMARK 465     VAL A   756                                                      
REMARK 465     GLY A   757                                                      
REMARK 465     ILE A   758                                                      
REMARK 465     ILE A   759                                                      
REMARK 465     ASN A   760                                                      
REMARK 465     GLU A   761                                                      
REMARK 465     ASP A   762                                                      
REMARK 465     PRO A   763                                                      
REMARK 465     GLY A   764                                                      
REMARK 465     ASN A   765                                                      
REMARK 465     CYS A   766                                                      
REMARK 465     GLU A   767                                                      
REMARK 465     GLY A   768                                                      
REMARK 465     VAL A   769                                                      
REMARK 465     LYS A   770                                                      
REMARK 465     ARG A   771                                                      
REMARK 465     THR A   772                                                      
REMARK 465     LEU A   773                                                      
REMARK 465     SER A   774                                                      
REMARK 465     PHE A   775                                                      
REMARK 465     SER A   776                                                      
REMARK 465     LEU A   777                                                      
REMARK 465     ARG A   778                                                      
REMARK 465     SER A   779                                                      
REMARK 465     GLY A   780                                                      
REMARK 465     ARG A   781                                                      
REMARK 465     VAL A   782                                                      
REMARK 465     SER A   783                                                      
REMARK 465     GLY A   784                                                      
REMARK 465     ARG A   785                                                      
REMARK 465     ASN A   786                                                      
REMARK 465     TRP A   787                                                      
REMARK 465     LYS A   788                                                      
REMARK 465     ASN A   789                                                      
REMARK 465     PHE A   790                                                      
REMARK 465     ALA A   791                                                      
REMARK 465     LEU A   792                                                      
REMARK 465     VAL A   793                                                      
REMARK 465     PRO A   794                                                      
REMARK 465     LEU A   795                                                      
REMARK 465     LEU A   796                                                      
REMARK 465     ARG A   797                                                      
REMARK 465     ASP A   798                                                      
REMARK 465     ALA A   799                                                      
REMARK 465     SER A   800                                                      
REMARK 465     THR A   801                                                      
REMARK 465     ARG A   802                                                      
REMARK 465     ASP A   803                                                      
REMARK 465     ARG A   804                                                      
REMARK 465     HIS A   805                                                      
REMARK 465     ALA A   806                                                      
REMARK 465     THR A   807                                                      
REMARK 465     GLN A   808                                                      
REMARK 465     GLN A   809                                                      
REMARK 465     GLU A   810                                                      
REMARK 465     GLU A   811                                                      
REMARK 465     VAL A   812                                                      
REMARK 465     GLN A   813                                                      
REMARK 465     LEU A   814                                                      
REMARK 465     LYS A   815                                                      
REMARK 465     HIS A   816                                                      
REMARK 465     TYR A   817                                                      
REMARK 465     THR A   818                                                      
REMARK 465     GLY A   819                                                      
REMARK 465     SER A   820                                                      
REMARK 465     LEU A   821                                                      
REMARK 465     LYS A   822                                                      
REMARK 465     PRO A   823                                                      
REMARK 465     GLU A   824                                                      
REMARK 465     ASP A   825                                                      
REMARK 465     ALA A   826                                                      
REMARK 465     GLU A   827                                                      
REMARK 465     VAL A   828                                                      
REMARK 465     PHE A   829                                                      
REMARK 465     LYS A   830                                                      
REMARK 465     ASP A   831                                                      
REMARK 465     SER A   832                                                      
REMARK 465     MET A   833                                                      
REMARK 465     VAL A   834                                                      
REMARK 465     PRO A   835                                                      
REMARK 465     GLY A   836                                                      
REMARK 465     GLU A   837                                                      
REMARK 465     LYS A   838                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     ALA C    -2                                                      
REMARK 465     MET C    -1                                                      
REMARK 465     GLY C     0                                                      
REMARK 465     SER C     1                                                      
REMARK 465     GLU C     2                                                      
REMARK 465     GLN C     3                                                      
REMARK 465     ARG C     4                                                      
REMARK 465     ALA C     5                                                      
REMARK 465     SER C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     ASP C     8                                                      
REMARK 465     SER C     9                                                      
REMARK 465     GLU C    10                                                      
REMARK 465     GLU C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     GLU C    13                                                      
REMARK 465     SER C    14                                                      
REMARK 465     PRO C    15                                                      
REMARK 465     PRO C    16                                                      
REMARK 465     GLN C    17                                                      
REMARK 465     GLU C    18                                                      
REMARK 465     ASN C    19                                                      
REMARK 465     SER C    20                                                      
REMARK 465     CYS C    21                                                      
REMARK 465     LEU C    22                                                      
REMARK 465     ASP C    23                                                      
REMARK 465     PRO C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     ASP C    26                                                      
REMARK 465     ARG C    27                                                      
REMARK 465     ASP C    28                                                      
REMARK 465     PRO C    29                                                      
REMARK 465     ASN C    30                                                      
REMARK 465     CYS C    31                                                      
REMARK 465     LYS C    32                                                      
REMARK 465     PRO C    33                                                      
REMARK 465     PRO C    34                                                      
REMARK 465     PRO C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     LYS C    37                                                      
REMARK 465     PRO C    38                                                      
REMARK 465     HIS C    39                                                      
REMARK 465     ILE C    40                                                      
REMARK 465     PHE C    41                                                      
REMARK 465     THR C    42                                                      
REMARK 465     THR C    43                                                      
REMARK 465     ARG C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     ARG C    46                                                      
REMARK 465     THR C    47                                                      
REMARK 465     ARG C    48                                                      
REMARK 465     LEU C    49                                                      
REMARK 465     PHE C    50                                                      
REMARK 465     GLY C    51                                                      
REMARK 465     LYS C    52                                                      
REMARK 465     GLY C    53                                                      
REMARK 465     ASP C    54                                                      
REMARK 465     SER C    55                                                      
REMARK 465     GLU C    56                                                      
REMARK 465     GLU C    57                                                      
REMARK 465     ALA C    58                                                      
REMARK 465     SER C    59                                                      
REMARK 465     PRO C    60                                                      
REMARK 465     LEU C    61                                                      
REMARK 465     ASP C    62                                                      
REMARK 465     CYS C    63                                                      
REMARK 465     PRO C    64                                                      
REMARK 465     TYR C    65                                                      
REMARK 465     GLU C    66                                                      
REMARK 465     GLU C    67                                                      
REMARK 465     GLY C    68                                                      
REMARK 465     GLY C    69                                                      
REMARK 465     LEU C    70                                                      
REMARK 465     ALA C    71                                                      
REMARK 465     SER C    72                                                      
REMARK 465     CYS C    73                                                      
REMARK 465     PRO C    74                                                      
REMARK 465     ILE C    75                                                      
REMARK 465     ILE C    76                                                      
REMARK 465     THR C    77                                                      
REMARK 465     VAL C    78                                                      
REMARK 465     SER C    79                                                      
REMARK 465     SER C    80                                                      
REMARK 465     VAL C    81                                                      
REMARK 465     LEU C    82                                                      
REMARK 465     THR C    83                                                      
REMARK 465     ILE C    84                                                      
REMARK 465     GLN C    85                                                      
REMARK 465     ARG C    86                                                      
REMARK 465     PRO C    87                                                      
REMARK 465     GLY C    88                                                      
REMARK 465     ASP C    89                                                      
REMARK 465     GLY C    90                                                      
REMARK 465     PRO C    91                                                      
REMARK 465     ALA C    92                                                      
REMARK 465     SER C    93                                                      
REMARK 465     VAL C    94                                                      
REMARK 465     ARG C    95                                                      
REMARK 465     PRO C    96                                                      
REMARK 465     SER C    97                                                      
REMARK 465     SER C    98                                                      
REMARK 465     GLN C    99                                                      
REMARK 465     ASP C   100                                                      
REMARK 465     SER C   101                                                      
REMARK 465     VAL C   102                                                      
REMARK 465     SER C   103                                                      
REMARK 465     ALA C   104                                                      
REMARK 465     GLY C   105                                                      
REMARK 465     GLU C   106                                                      
REMARK 465     LYS C   107                                                      
REMARK 465     PRO C   108                                                      
REMARK 465     PRO C   109                                                      
REMARK 465     ARG C   110                                                      
REMARK 465     LEU C   111                                                      
REMARK 465     TYR C   112                                                      
REMARK 465     ASP C   113                                                      
REMARK 465     ARG C   114                                                      
REMARK 465     ARG C   115                                                      
REMARK 465     SER C   116                                                      
REMARK 465     ILE C   117                                                      
REMARK 465     PHE C   118                                                      
REMARK 465     ASP C   119                                                      
REMARK 465     ALA C   120                                                      
REMARK 465     VAL C   121                                                      
REMARK 465     ALA C   122                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     SER C   124                                                      
REMARK 465     ASN C   125                                                      
REMARK 465     CYS C   126                                                      
REMARK 465     GLN C   127                                                      
REMARK 465     GLU C   128                                                      
REMARK 465     LEU C   129                                                      
REMARK 465     GLU C   130                                                      
REMARK 465     SER C   131                                                      
REMARK 465     LEU C   132                                                      
REMARK 465     LEU C   133                                                      
REMARK 465     PRO C   134                                                      
REMARK 465     PHE C   135                                                      
REMARK 465     LEU C   136                                                      
REMARK 465     GLN C   137                                                      
REMARK 465     ARG C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     LYS C   140                                                      
REMARK 465     LYS C   141                                                      
REMARK 465     ARG C   142                                                      
REMARK 465     LEU C   143                                                      
REMARK 465     THR C   144                                                      
REMARK 465     ASP C   145                                                      
REMARK 465     SER C   146                                                      
REMARK 465     GLU C   147                                                      
REMARK 465     PHE C   148                                                      
REMARK 465     LYS C   149                                                      
REMARK 465     ASP C   150                                                      
REMARK 465     PRO C   151                                                      
REMARK 465     GLU C   152                                                      
REMARK 465     THR C   153                                                      
REMARK 465     GLY C   154                                                      
REMARK 465     LYS C   155                                                      
REMARK 465     THR C   156                                                      
REMARK 465     CYS C   157                                                      
REMARK 465     LEU C   158                                                      
REMARK 465     LEU C   159                                                      
REMARK 465     LYS C   160                                                      
REMARK 465     ALA C   161                                                      
REMARK 465     MET C   162                                                      
REMARK 465     LEU C   163                                                      
REMARK 465     ASN C   164                                                      
REMARK 465     LEU C   165                                                      
REMARK 465     HIS C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     GLY C   168                                                      
REMARK 465     GLN C   169                                                      
REMARK 465     ASN C   170                                                      
REMARK 465     ASP C   171                                                      
REMARK 465     THR C   172                                                      
REMARK 465     ILE C   173                                                      
REMARK 465     ALA C   174                                                      
REMARK 465     LEU C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     LEU C   177                                                      
REMARK 465     ASP C   178                                                      
REMARK 465     VAL C   179                                                      
REMARK 465     ALA C   180                                                      
REMARK 465     ARG C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     THR C   183                                                      
REMARK 465     ASP C   184                                                      
REMARK 465     SER C   185                                                      
REMARK 465     LEU C   186                                                      
REMARK 465     LYS C   187                                                      
REMARK 465     GLN C   188                                                      
REMARK 465     PHE C   189                                                      
REMARK 465     VAL C   190                                                      
REMARK 465     ASN C   191                                                      
REMARK 465     ALA C   192                                                      
REMARK 465     SER C   193                                                      
REMARK 465     TYR C   194                                                      
REMARK 465     THR C   195                                                      
REMARK 465     ASP C   196                                                      
REMARK 465     SER C   197                                                      
REMARK 465     TYR C   198                                                      
REMARK 465     TYR C   199                                                      
REMARK 465     LYS C   200                                                      
REMARK 465     GLY C   201                                                      
REMARK 465     GLN C   202                                                      
REMARK 465     THR C   203                                                      
REMARK 465     ALA C   204                                                      
REMARK 465     LEU C   205                                                      
REMARK 465     HIS C   206                                                      
REMARK 465     ILE C   207                                                      
REMARK 465     ALA C   208                                                      
REMARK 465     ILE C   209                                                      
REMARK 465     GLU C   210                                                      
REMARK 465     ARG C   211                                                      
REMARK 465     ARG C   212                                                      
REMARK 465     ASN C   213                                                      
REMARK 465     MET C   214                                                      
REMARK 465     THR C   215                                                      
REMARK 465     LEU C   216                                                      
REMARK 465     VAL C   217                                                      
REMARK 465     THR C   218                                                      
REMARK 465     LEU C   219                                                      
REMARK 465     LEU C   220                                                      
REMARK 465     VAL C   221                                                      
REMARK 465     GLU C   222                                                      
REMARK 465     ASN C   223                                                      
REMARK 465     GLY C   224                                                      
REMARK 465     ALA C   225                                                      
REMARK 465     ASP C   226                                                      
REMARK 465     VAL C   227                                                      
REMARK 465     GLN C   228                                                      
REMARK 465     ALA C   229                                                      
REMARK 465     ALA C   230                                                      
REMARK 465     ALA C   231                                                      
REMARK 465     ASN C   232                                                      
REMARK 465     GLY C   233                                                      
REMARK 465     ASP C   234                                                      
REMARK 465     PHE C   235                                                      
REMARK 465     PHE C   236                                                      
REMARK 465     LYS C   237                                                      
REMARK 465     LYS C   238                                                      
REMARK 465     THR C   239                                                      
REMARK 465     LYS C   240                                                      
REMARK 465     GLY C   241                                                      
REMARK 465     ARG C   242                                                      
REMARK 465     PRO C   243                                                      
REMARK 465     GLY C   244                                                      
REMARK 465     PHE C   245                                                      
REMARK 465     TYR C   246                                                      
REMARK 465     PHE C   247                                                      
REMARK 465     GLY C   248                                                      
REMARK 465     GLU C   249                                                      
REMARK 465     LEU C   250                                                      
REMARK 465     PRO C   251                                                      
REMARK 465     LEU C   252                                                      
REMARK 465     SER C   253                                                      
REMARK 465     LEU C   254                                                      
REMARK 465     ALA C   255                                                      
REMARK 465     ALA C   256                                                      
REMARK 465     CYS C   257                                                      
REMARK 465     THR C   258                                                      
REMARK 465     ASN C   259                                                      
REMARK 465     GLN C   260                                                      
REMARK 465     LEU C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     ILE C   263                                                      
REMARK 465     VAL C   264                                                      
REMARK 465     LYS C   265                                                      
REMARK 465     PHE C   266                                                      
REMARK 465     LEU C   267                                                      
REMARK 465     LEU C   268                                                      
REMARK 465     GLN C   269                                                      
REMARK 465     ASN C   270                                                      
REMARK 465     SER C   271                                                      
REMARK 465     TRP C   272                                                      
REMARK 465     GLN C   273                                                      
REMARK 465     PRO C   274                                                      
REMARK 465     ALA C   275                                                      
REMARK 465     ASP C   276                                                      
REMARK 465     ILE C   277                                                      
REMARK 465     SER C   278                                                      
REMARK 465     ALA C   279                                                      
REMARK 465     ARG C   280                                                      
REMARK 465     ASP C   281                                                      
REMARK 465     SER C   282                                                      
REMARK 465     GLY C   602                                                      
REMARK 465     LYS C   603                                                      
REMARK 465     ASN C   604                                                      
REMARK 465     ASN C   605                                                      
REMARK 465     SER C   606                                                      
REMARK 465     LEU C   607                                                      
REMARK 465     PRO C   608                                                      
REMARK 465     MET C   609                                                      
REMARK 465     GLU C   610                                                      
REMARK 465     SER C   611                                                      
REMARK 465     THR C   612                                                      
REMARK 465     PRO C   613                                                      
REMARK 465     HIS C   614                                                      
REMARK 465     LYS C   615                                                      
REMARK 465     CYS C   616                                                      
REMARK 465     ARG C   617                                                      
REMARK 465     GLY C   618                                                      
REMARK 465     SER C   619                                                      
REMARK 465     ALA C   620                                                      
REMARK 465     CYS C   621                                                      
REMARK 465     LYS C   622                                                      
REMARK 465     PRO C   623                                                      
REMARK 465     GLY C   624                                                      
REMARK 465     ASN C   625                                                      
REMARK 465     GLN C   727                                                      
REMARK 465     VAL C   728                                                      
REMARK 465     GLY C   729                                                      
REMARK 465     PHE C   730                                                      
REMARK 465     THR C   731                                                      
REMARK 465     PRO C   732                                                      
REMARK 465     ASP C   733                                                      
REMARK 465     GLY C   734                                                      
REMARK 465     LYS C   735                                                      
REMARK 465     ASP C   736                                                      
REMARK 465     ASP C   737                                                      
REMARK 465     VAL C   747                                                      
REMARK 465     ASN C   748                                                      
REMARK 465     TRP C   749                                                      
REMARK 465     THR C   750                                                      
REMARK 465     THR C   751                                                      
REMARK 465     TRP C   752                                                      
REMARK 465     ASN C   753                                                      
REMARK 465     THR C   754                                                      
REMARK 465     ASN C   755                                                      
REMARK 465     VAL C   756                                                      
REMARK 465     GLY C   757                                                      
REMARK 465     ILE C   758                                                      
REMARK 465     ILE C   759                                                      
REMARK 465     ASN C   760                                                      
REMARK 465     GLU C   761                                                      
REMARK 465     ASP C   762                                                      
REMARK 465     PRO C   763                                                      
REMARK 465     GLY C   764                                                      
REMARK 465     ASN C   765                                                      
REMARK 465     CYS C   766                                                      
REMARK 465     GLU C   767                                                      
REMARK 465     GLY C   768                                                      
REMARK 465     VAL C   769                                                      
REMARK 465     LYS C   770                                                      
REMARK 465     ARG C   771                                                      
REMARK 465     THR C   772                                                      
REMARK 465     LEU C   773                                                      
REMARK 465     SER C   774                                                      
REMARK 465     PHE C   775                                                      
REMARK 465     SER C   776                                                      
REMARK 465     LEU C   777                                                      
REMARK 465     ARG C   778                                                      
REMARK 465     SER C   779                                                      
REMARK 465     GLY C   780                                                      
REMARK 465     ARG C   781                                                      
REMARK 465     VAL C   782                                                      
REMARK 465     SER C   783                                                      
REMARK 465     GLY C   784                                                      
REMARK 465     ARG C   785                                                      
REMARK 465     ASN C   786                                                      
REMARK 465     TRP C   787                                                      
REMARK 465     LYS C   788                                                      
REMARK 465     ASN C   789                                                      
REMARK 465     PHE C   790                                                      
REMARK 465     ALA C   791                                                      
REMARK 465     LEU C   792                                                      
REMARK 465     VAL C   793                                                      
REMARK 465     PRO C   794                                                      
REMARK 465     LEU C   795                                                      
REMARK 465     LEU C   796                                                      
REMARK 465     ARG C   797                                                      
REMARK 465     ASP C   798                                                      
REMARK 465     ALA C   799                                                      
REMARK 465     SER C   800                                                      
REMARK 465     THR C   801                                                      
REMARK 465     ARG C   802                                                      
REMARK 465     ASP C   803                                                      
REMARK 465     ARG C   804                                                      
REMARK 465     HIS C   805                                                      
REMARK 465     ALA C   806                                                      
REMARK 465     THR C   807                                                      
REMARK 465     GLN C   808                                                      
REMARK 465     GLN C   809                                                      
REMARK 465     GLU C   810                                                      
REMARK 465     GLU C   811                                                      
REMARK 465     VAL C   812                                                      
REMARK 465     GLN C   813                                                      
REMARK 465     LEU C   814                                                      
REMARK 465     LYS C   815                                                      
REMARK 465     HIS C   816                                                      
REMARK 465     TYR C   817                                                      
REMARK 465     THR C   818                                                      
REMARK 465     GLY C   819                                                      
REMARK 465     SER C   820                                                      
REMARK 465     LEU C   821                                                      
REMARK 465     LYS C   822                                                      
REMARK 465     PRO C   823                                                      
REMARK 465     GLU C   824                                                      
REMARK 465     ASP C   825                                                      
REMARK 465     ALA C   826                                                      
REMARK 465     GLU C   827                                                      
REMARK 465     VAL C   828                                                      
REMARK 465     PHE C   829                                                      
REMARK 465     LYS C   830                                                      
REMARK 465     ASP C   831                                                      
REMARK 465     SER C   832                                                      
REMARK 465     MET C   833                                                      
REMARK 465     VAL C   834                                                      
REMARK 465     PRO C   835                                                      
REMARK 465     GLY C   836                                                      
REMARK 465     GLU C   837                                                      
REMARK 465     LYS C   838                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     ALA D    -2                                                      
REMARK 465     MET D    -1                                                      
REMARK 465     GLY D     0                                                      
REMARK 465     SER D     1                                                      
REMARK 465     GLU D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     ARG D     4                                                      
REMARK 465     ALA D     5                                                      
REMARK 465     SER D     6                                                      
REMARK 465     LEU D     7                                                      
REMARK 465     ASP D     8                                                      
REMARK 465     SER D     9                                                      
REMARK 465     GLU D    10                                                      
REMARK 465     GLU D    11                                                      
REMARK 465     SER D    12                                                      
REMARK 465     GLU D    13                                                      
REMARK 465     SER D    14                                                      
REMARK 465     PRO D    15                                                      
REMARK 465     PRO D    16                                                      
REMARK 465     GLN D    17                                                      
REMARK 465     GLU D    18                                                      
REMARK 465     ASN D    19                                                      
REMARK 465     SER D    20                                                      
REMARK 465     CYS D    21                                                      
REMARK 465     LEU D    22                                                      
REMARK 465     ASP D    23                                                      
REMARK 465     PRO D    24                                                      
REMARK 465     PRO D    25                                                      
REMARK 465     ASP D    26                                                      
REMARK 465     ARG D    27                                                      
REMARK 465     ASP D    28                                                      
REMARK 465     PRO D    29                                                      
REMARK 465     ASN D    30                                                      
REMARK 465     CYS D    31                                                      
REMARK 465     LYS D    32                                                      
REMARK 465     PRO D    33                                                      
REMARK 465     PRO D    34                                                      
REMARK 465     PRO D    35                                                      
REMARK 465     VAL D    36                                                      
REMARK 465     LYS D    37                                                      
REMARK 465     PRO D    38                                                      
REMARK 465     HIS D    39                                                      
REMARK 465     ILE D    40                                                      
REMARK 465     PHE D    41                                                      
REMARK 465     THR D    42                                                      
REMARK 465     THR D    43                                                      
REMARK 465     ARG D    44                                                      
REMARK 465     SER D    45                                                      
REMARK 465     ARG D    46                                                      
REMARK 465     THR D    47                                                      
REMARK 465     ARG D    48                                                      
REMARK 465     LEU D    49                                                      
REMARK 465     PHE D    50                                                      
REMARK 465     GLY D    51                                                      
REMARK 465     LYS D    52                                                      
REMARK 465     GLY D    53                                                      
REMARK 465     ASP D    54                                                      
REMARK 465     SER D    55                                                      
REMARK 465     GLU D    56                                                      
REMARK 465     GLU D    57                                                      
REMARK 465     ALA D    58                                                      
REMARK 465     SER D    59                                                      
REMARK 465     PRO D    60                                                      
REMARK 465     LEU D    61                                                      
REMARK 465     ASP D    62                                                      
REMARK 465     CYS D    63                                                      
REMARK 465     PRO D    64                                                      
REMARK 465     TYR D    65                                                      
REMARK 465     GLU D    66                                                      
REMARK 465     GLU D    67                                                      
REMARK 465     GLY D    68                                                      
REMARK 465     GLY D    69                                                      
REMARK 465     LEU D    70                                                      
REMARK 465     ALA D    71                                                      
REMARK 465     SER D    72                                                      
REMARK 465     CYS D    73                                                      
REMARK 465     PRO D    74                                                      
REMARK 465     ILE D    75                                                      
REMARK 465     ILE D    76                                                      
REMARK 465     THR D    77                                                      
REMARK 465     VAL D    78                                                      
REMARK 465     SER D    79                                                      
REMARK 465     SER D    80                                                      
REMARK 465     VAL D    81                                                      
REMARK 465     LEU D    82                                                      
REMARK 465     THR D    83                                                      
REMARK 465     ILE D    84                                                      
REMARK 465     GLN D    85                                                      
REMARK 465     ARG D    86                                                      
REMARK 465     PRO D    87                                                      
REMARK 465     GLY D    88                                                      
REMARK 465     ASP D    89                                                      
REMARK 465     GLY D    90                                                      
REMARK 465     PRO D    91                                                      
REMARK 465     ALA D    92                                                      
REMARK 465     SER D    93                                                      
REMARK 465     VAL D    94                                                      
REMARK 465     ARG D    95                                                      
REMARK 465     PRO D    96                                                      
REMARK 465     SER D    97                                                      
REMARK 465     SER D    98                                                      
REMARK 465     GLN D    99                                                      
REMARK 465     ASP D   100                                                      
REMARK 465     SER D   101                                                      
REMARK 465     VAL D   102                                                      
REMARK 465     SER D   103                                                      
REMARK 465     ALA D   104                                                      
REMARK 465     GLY D   105                                                      
REMARK 465     GLU D   106                                                      
REMARK 465     LYS D   107                                                      
REMARK 465     PRO D   108                                                      
REMARK 465     PRO D   109                                                      
REMARK 465     ARG D   110                                                      
REMARK 465     LEU D   111                                                      
REMARK 465     TYR D   112                                                      
REMARK 465     ASP D   113                                                      
REMARK 465     ARG D   114                                                      
REMARK 465     ARG D   115                                                      
REMARK 465     SER D   116                                                      
REMARK 465     ILE D   117                                                      
REMARK 465     PHE D   118                                                      
REMARK 465     ASP D   119                                                      
REMARK 465     ALA D   120                                                      
REMARK 465     VAL D   121                                                      
REMARK 465     ALA D   122                                                      
REMARK 465     GLN D   123                                                      
REMARK 465     SER D   124                                                      
REMARK 465     ASN D   125                                                      
REMARK 465     CYS D   126                                                      
REMARK 465     GLN D   127                                                      
REMARK 465     GLU D   128                                                      
REMARK 465     LEU D   129                                                      
REMARK 465     GLU D   130                                                      
REMARK 465     SER D   131                                                      
REMARK 465     LEU D   132                                                      
REMARK 465     LEU D   133                                                      
REMARK 465     PRO D   134                                                      
REMARK 465     PHE D   135                                                      
REMARK 465     LEU D   136                                                      
REMARK 465     GLN D   137                                                      
REMARK 465     ARG D   138                                                      
REMARK 465     SER D   139                                                      
REMARK 465     LYS D   140                                                      
REMARK 465     LYS D   141                                                      
REMARK 465     ARG D   142                                                      
REMARK 465     LEU D   143                                                      
REMARK 465     THR D   144                                                      
REMARK 465     ASP D   145                                                      
REMARK 465     SER D   146                                                      
REMARK 465     GLU D   147                                                      
REMARK 465     PHE D   148                                                      
REMARK 465     LYS D   149                                                      
REMARK 465     ASP D   150                                                      
REMARK 465     PRO D   151                                                      
REMARK 465     GLU D   152                                                      
REMARK 465     THR D   153                                                      
REMARK 465     GLY D   154                                                      
REMARK 465     LYS D   155                                                      
REMARK 465     THR D   156                                                      
REMARK 465     CYS D   157                                                      
REMARK 465     LEU D   158                                                      
REMARK 465     LEU D   159                                                      
REMARK 465     LYS D   160                                                      
REMARK 465     ALA D   161                                                      
REMARK 465     MET D   162                                                      
REMARK 465     LEU D   163                                                      
REMARK 465     ASN D   164                                                      
REMARK 465     LEU D   165                                                      
REMARK 465     HIS D   166                                                      
REMARK 465     ASN D   167                                                      
REMARK 465     GLY D   168                                                      
REMARK 465     GLN D   169                                                      
REMARK 465     ASN D   170                                                      
REMARK 465     ASP D   171                                                      
REMARK 465     THR D   172                                                      
REMARK 465     ILE D   173                                                      
REMARK 465     ALA D   174                                                      
REMARK 465     LEU D   175                                                      
REMARK 465     LEU D   176                                                      
REMARK 465     LEU D   177                                                      
REMARK 465     ASP D   178                                                      
REMARK 465     VAL D   179                                                      
REMARK 465     ALA D   180                                                      
REMARK 465     ARG D   181                                                      
REMARK 465     LYS D   182                                                      
REMARK 465     THR D   183                                                      
REMARK 465     ASP D   184                                                      
REMARK 465     SER D   185                                                      
REMARK 465     LEU D   186                                                      
REMARK 465     LYS D   187                                                      
REMARK 465     GLN D   188                                                      
REMARK 465     PHE D   189                                                      
REMARK 465     VAL D   190                                                      
REMARK 465     ASN D   191                                                      
REMARK 465     ALA D   192                                                      
REMARK 465     SER D   193                                                      
REMARK 465     TYR D   194                                                      
REMARK 465     THR D   195                                                      
REMARK 465     ASP D   196                                                      
REMARK 465     SER D   197                                                      
REMARK 465     TYR D   198                                                      
REMARK 465     TYR D   199                                                      
REMARK 465     LYS D   200                                                      
REMARK 465     GLY D   201                                                      
REMARK 465     GLN D   202                                                      
REMARK 465     THR D   203                                                      
REMARK 465     ALA D   204                                                      
REMARK 465     LEU D   205                                                      
REMARK 465     HIS D   206                                                      
REMARK 465     ILE D   207                                                      
REMARK 465     ALA D   208                                                      
REMARK 465     ILE D   209                                                      
REMARK 465     GLU D   210                                                      
REMARK 465     ARG D   211                                                      
REMARK 465     ARG D   212                                                      
REMARK 465     ASN D   213                                                      
REMARK 465     MET D   214                                                      
REMARK 465     THR D   215                                                      
REMARK 465     LEU D   216                                                      
REMARK 465     VAL D   217                                                      
REMARK 465     THR D   218                                                      
REMARK 465     LEU D   219                                                      
REMARK 465     LEU D   220                                                      
REMARK 465     VAL D   221                                                      
REMARK 465     GLU D   222                                                      
REMARK 465     ASN D   223                                                      
REMARK 465     GLY D   224                                                      
REMARK 465     ALA D   225                                                      
REMARK 465     ASP D   226                                                      
REMARK 465     VAL D   227                                                      
REMARK 465     GLN D   228                                                      
REMARK 465     ALA D   229                                                      
REMARK 465     ALA D   230                                                      
REMARK 465     ALA D   231                                                      
REMARK 465     ASN D   232                                                      
REMARK 465     GLY D   233                                                      
REMARK 465     ASP D   234                                                      
REMARK 465     PHE D   235                                                      
REMARK 465     PHE D   236                                                      
REMARK 465     LYS D   237                                                      
REMARK 465     LYS D   238                                                      
REMARK 465     THR D   239                                                      
REMARK 465     LYS D   240                                                      
REMARK 465     GLY D   241                                                      
REMARK 465     ARG D   242                                                      
REMARK 465     PRO D   243                                                      
REMARK 465     GLY D   244                                                      
REMARK 465     PHE D   245                                                      
REMARK 465     TYR D   246                                                      
REMARK 465     PHE D   247                                                      
REMARK 465     GLY D   248                                                      
REMARK 465     GLU D   249                                                      
REMARK 465     LEU D   250                                                      
REMARK 465     PRO D   251                                                      
REMARK 465     LEU D   252                                                      
REMARK 465     SER D   253                                                      
REMARK 465     LEU D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     ALA D   256                                                      
REMARK 465     CYS D   257                                                      
REMARK 465     THR D   258                                                      
REMARK 465     ASN D   259                                                      
REMARK 465     GLN D   260                                                      
REMARK 465     LEU D   261                                                      
REMARK 465     ALA D   262                                                      
REMARK 465     ILE D   263                                                      
REMARK 465     VAL D   264                                                      
REMARK 465     LYS D   265                                                      
REMARK 465     PHE D   266                                                      
REMARK 465     LEU D   267                                                      
REMARK 465     LEU D   268                                                      
REMARK 465     GLN D   269                                                      
REMARK 465     ASN D   270                                                      
REMARK 465     SER D   271                                                      
REMARK 465     TRP D   272                                                      
REMARK 465     GLN D   273                                                      
REMARK 465     PRO D   274                                                      
REMARK 465     ALA D   275                                                      
REMARK 465     ASP D   276                                                      
REMARK 465     ILE D   277                                                      
REMARK 465     SER D   278                                                      
REMARK 465     ALA D   279                                                      
REMARK 465     ARG D   280                                                      
REMARK 465     ASP D   281                                                      
REMARK 465     SER D   282                                                      
REMARK 465     GLY D   602                                                      
REMARK 465     LYS D   603                                                      
REMARK 465     ASN D   604                                                      
REMARK 465     ASN D   605                                                      
REMARK 465     SER D   606                                                      
REMARK 465     LEU D   607                                                      
REMARK 465     PRO D   608                                                      
REMARK 465     MET D   609                                                      
REMARK 465     GLU D   610                                                      
REMARK 465     SER D   611                                                      
REMARK 465     THR D   612                                                      
REMARK 465     PRO D   613                                                      
REMARK 465     HIS D   614                                                      
REMARK 465     LYS D   615                                                      
REMARK 465     CYS D   616                                                      
REMARK 465     ARG D   617                                                      
REMARK 465     GLY D   618                                                      
REMARK 465     SER D   619                                                      
REMARK 465     ALA D   620                                                      
REMARK 465     CYS D   621                                                      
REMARK 465     LYS D   622                                                      
REMARK 465     PRO D   623                                                      
REMARK 465     GLY D   624                                                      
REMARK 465     ASN D   625                                                      
REMARK 465     GLN D   727                                                      
REMARK 465     VAL D   728                                                      
REMARK 465     GLY D   729                                                      
REMARK 465     PHE D   730                                                      
REMARK 465     THR D   731                                                      
REMARK 465     PRO D   732                                                      
REMARK 465     ASP D   733                                                      
REMARK 465     GLY D   734                                                      
REMARK 465     LYS D   735                                                      
REMARK 465     ASP D   736                                                      
REMARK 465     ASP D   737                                                      
REMARK 465     VAL D   747                                                      
REMARK 465     ASN D   748                                                      
REMARK 465     TRP D   749                                                      
REMARK 465     THR D   750                                                      
REMARK 465     THR D   751                                                      
REMARK 465     TRP D   752                                                      
REMARK 465     ASN D   753                                                      
REMARK 465     THR D   754                                                      
REMARK 465     ASN D   755                                                      
REMARK 465     VAL D   756                                                      
REMARK 465     GLY D   757                                                      
REMARK 465     ILE D   758                                                      
REMARK 465     ILE D   759                                                      
REMARK 465     ASN D   760                                                      
REMARK 465     GLU D   761                                                      
REMARK 465     ASP D   762                                                      
REMARK 465     PRO D   763                                                      
REMARK 465     GLY D   764                                                      
REMARK 465     ASN D   765                                                      
REMARK 465     CYS D   766                                                      
REMARK 465     GLU D   767                                                      
REMARK 465     GLY D   768                                                      
REMARK 465     VAL D   769                                                      
REMARK 465     LYS D   770                                                      
REMARK 465     ARG D   771                                                      
REMARK 465     THR D   772                                                      
REMARK 465     LEU D   773                                                      
REMARK 465     SER D   774                                                      
REMARK 465     PHE D   775                                                      
REMARK 465     SER D   776                                                      
REMARK 465     LEU D   777                                                      
REMARK 465     ARG D   778                                                      
REMARK 465     SER D   779                                                      
REMARK 465     GLY D   780                                                      
REMARK 465     ARG D   781                                                      
REMARK 465     VAL D   782                                                      
REMARK 465     SER D   783                                                      
REMARK 465     GLY D   784                                                      
REMARK 465     ARG D   785                                                      
REMARK 465     ASN D   786                                                      
REMARK 465     TRP D   787                                                      
REMARK 465     LYS D   788                                                      
REMARK 465     ASN D   789                                                      
REMARK 465     PHE D   790                                                      
REMARK 465     ALA D   791                                                      
REMARK 465     LEU D   792                                                      
REMARK 465     VAL D   793                                                      
REMARK 465     PRO D   794                                                      
REMARK 465     LEU D   795                                                      
REMARK 465     LEU D   796                                                      
REMARK 465     ARG D   797                                                      
REMARK 465     ASP D   798                                                      
REMARK 465     ALA D   799                                                      
REMARK 465     SER D   800                                                      
REMARK 465     THR D   801                                                      
REMARK 465     ARG D   802                                                      
REMARK 465     ASP D   803                                                      
REMARK 465     ARG D   804                                                      
REMARK 465     HIS D   805                                                      
REMARK 465     ALA D   806                                                      
REMARK 465     THR D   807                                                      
REMARK 465     GLN D   808                                                      
REMARK 465     GLN D   809                                                      
REMARK 465     GLU D   810                                                      
REMARK 465     GLU D   811                                                      
REMARK 465     VAL D   812                                                      
REMARK 465     GLN D   813                                                      
REMARK 465     LEU D   814                                                      
REMARK 465     LYS D   815                                                      
REMARK 465     HIS D   816                                                      
REMARK 465     TYR D   817                                                      
REMARK 465     THR D   818                                                      
REMARK 465     GLY D   819                                                      
REMARK 465     SER D   820                                                      
REMARK 465     LEU D   821                                                      
REMARK 465     LYS D   822                                                      
REMARK 465     PRO D   823                                                      
REMARK 465     GLU D   824                                                      
REMARK 465     ASP D   825                                                      
REMARK 465     ALA D   826                                                      
REMARK 465     GLU D   827                                                      
REMARK 465     VAL D   828                                                      
REMARK 465     PHE D   829                                                      
REMARK 465     LYS D   830                                                      
REMARK 465     ASP D   831                                                      
REMARK 465     SER D   832                                                      
REMARK 465     MET D   833                                                      
REMARK 465     VAL D   834                                                      
REMARK 465     PRO D   835                                                      
REMARK 465     GLY D   836                                                      
REMARK 465     GLU D   837                                                      
REMARK 465     LYS D   838                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ALA B    -2                                                      
REMARK 465     MET B    -1                                                      
REMARK 465     GLY B     0                                                      
REMARK 465     SER B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     GLN B     3                                                      
REMARK 465     ARG B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     ASP B     8                                                      
REMARK 465     SER B     9                                                      
REMARK 465     GLU B    10                                                      
REMARK 465     GLU B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     GLU B    13                                                      
REMARK 465     SER B    14                                                      
REMARK 465     PRO B    15                                                      
REMARK 465     PRO B    16                                                      
REMARK 465     GLN B    17                                                      
REMARK 465     GLU B    18                                                      
REMARK 465     ASN B    19                                                      
REMARK 465     SER B    20                                                      
REMARK 465     CYS B    21                                                      
REMARK 465     LEU B    22                                                      
REMARK 465     ASP B    23                                                      
REMARK 465     PRO B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     ASP B    26                                                      
REMARK 465     ARG B    27                                                      
REMARK 465     ASP B    28                                                      
REMARK 465     PRO B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     CYS B    31                                                      
REMARK 465     LYS B    32                                                      
REMARK 465     PRO B    33                                                      
REMARK 465     PRO B    34                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     LYS B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     HIS B    39                                                      
REMARK 465     ILE B    40                                                      
REMARK 465     PHE B    41                                                      
REMARK 465     THR B    42                                                      
REMARK 465     THR B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     ARG B    46                                                      
REMARK 465     THR B    47                                                      
REMARK 465     ARG B    48                                                      
REMARK 465     LEU B    49                                                      
REMARK 465     PHE B    50                                                      
REMARK 465     GLY B    51                                                      
REMARK 465     LYS B    52                                                      
REMARK 465     GLY B    53                                                      
REMARK 465     ASP B    54                                                      
REMARK 465     SER B    55                                                      
REMARK 465     GLU B    56                                                      
REMARK 465     GLU B    57                                                      
REMARK 465     ALA B    58                                                      
REMARK 465     SER B    59                                                      
REMARK 465     PRO B    60                                                      
REMARK 465     LEU B    61                                                      
REMARK 465     ASP B    62                                                      
REMARK 465     CYS B    63                                                      
REMARK 465     PRO B    64                                                      
REMARK 465     TYR B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     GLU B    67                                                      
REMARK 465     GLY B    68                                                      
REMARK 465     GLY B    69                                                      
REMARK 465     LEU B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     SER B    72                                                      
REMARK 465     CYS B    73                                                      
REMARK 465     PRO B    74                                                      
REMARK 465     ILE B    75                                                      
REMARK 465     ILE B    76                                                      
REMARK 465     THR B    77                                                      
REMARK 465     VAL B    78                                                      
REMARK 465     SER B    79                                                      
REMARK 465     SER B    80                                                      
REMARK 465     VAL B    81                                                      
REMARK 465     LEU B    82                                                      
REMARK 465     THR B    83                                                      
REMARK 465     ILE B    84                                                      
REMARK 465     GLN B    85                                                      
REMARK 465     ARG B    86                                                      
REMARK 465     PRO B    87                                                      
REMARK 465     GLY B    88                                                      
REMARK 465     ASP B    89                                                      
REMARK 465     GLY B    90                                                      
REMARK 465     PRO B    91                                                      
REMARK 465     ALA B    92                                                      
REMARK 465     SER B    93                                                      
REMARK 465     VAL B    94                                                      
REMARK 465     ARG B    95                                                      
REMARK 465     PRO B    96                                                      
REMARK 465     SER B    97                                                      
REMARK 465     SER B    98                                                      
REMARK 465     GLN B    99                                                      
REMARK 465     ASP B   100                                                      
REMARK 465     SER B   101                                                      
REMARK 465     VAL B   102                                                      
REMARK 465     SER B   103                                                      
REMARK 465     ALA B   104                                                      
REMARK 465     GLY B   105                                                      
REMARK 465     GLU B   106                                                      
REMARK 465     LYS B   107                                                      
REMARK 465     PRO B   108                                                      
REMARK 465     PRO B   109                                                      
REMARK 465     ARG B   110                                                      
REMARK 465     LEU B   111                                                      
REMARK 465     TYR B   112                                                      
REMARK 465     ASP B   113                                                      
REMARK 465     ARG B   114                                                      
REMARK 465     ARG B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     ILE B   117                                                      
REMARK 465     PHE B   118                                                      
REMARK 465     ASP B   119                                                      
REMARK 465     ALA B   120                                                      
REMARK 465     VAL B   121                                                      
REMARK 465     ALA B   122                                                      
REMARK 465     GLN B   123                                                      
REMARK 465     SER B   124                                                      
REMARK 465     ASN B   125                                                      
REMARK 465     CYS B   126                                                      
REMARK 465     GLN B   127                                                      
REMARK 465     GLU B   128                                                      
REMARK 465     LEU B   129                                                      
REMARK 465     GLU B   130                                                      
REMARK 465     SER B   131                                                      
REMARK 465     LEU B   132                                                      
REMARK 465     LEU B   133                                                      
REMARK 465     PRO B   134                                                      
REMARK 465     PHE B   135                                                      
REMARK 465     LEU B   136                                                      
REMARK 465     GLN B   137                                                      
REMARK 465     ARG B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     LYS B   140                                                      
REMARK 465     LYS B   141                                                      
REMARK 465     ARG B   142                                                      
REMARK 465     LEU B   143                                                      
REMARK 465     THR B   144                                                      
REMARK 465     ASP B   145                                                      
REMARK 465     SER B   146                                                      
REMARK 465     GLU B   147                                                      
REMARK 465     PHE B   148                                                      
REMARK 465     LYS B   149                                                      
REMARK 465     ASP B   150                                                      
REMARK 465     PRO B   151                                                      
REMARK 465     GLU B   152                                                      
REMARK 465     THR B   153                                                      
REMARK 465     GLY B   154                                                      
REMARK 465     LYS B   155                                                      
REMARK 465     THR B   156                                                      
REMARK 465     CYS B   157                                                      
REMARK 465     LEU B   158                                                      
REMARK 465     LEU B   159                                                      
REMARK 465     LYS B   160                                                      
REMARK 465     ALA B   161                                                      
REMARK 465     MET B   162                                                      
REMARK 465     LEU B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     LEU B   165                                                      
REMARK 465     HIS B   166                                                      
REMARK 465     ASN B   167                                                      
REMARK 465     GLY B   168                                                      
REMARK 465     GLN B   169                                                      
REMARK 465     ASN B   170                                                      
REMARK 465     ASP B   171                                                      
REMARK 465     THR B   172                                                      
REMARK 465     ILE B   173                                                      
REMARK 465     ALA B   174                                                      
REMARK 465     LEU B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     LEU B   177                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     VAL B   179                                                      
REMARK 465     ALA B   180                                                      
REMARK 465     ARG B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     THR B   183                                                      
REMARK 465     ASP B   184                                                      
REMARK 465     SER B   185                                                      
REMARK 465     LEU B   186                                                      
REMARK 465     LYS B   187                                                      
REMARK 465     GLN B   188                                                      
REMARK 465     PHE B   189                                                      
REMARK 465     VAL B   190                                                      
REMARK 465     ASN B   191                                                      
REMARK 465     ALA B   192                                                      
REMARK 465     SER B   193                                                      
REMARK 465     TYR B   194                                                      
REMARK 465     THR B   195                                                      
REMARK 465     ASP B   196                                                      
REMARK 465     SER B   197                                                      
REMARK 465     TYR B   198                                                      
REMARK 465     TYR B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     GLY B   201                                                      
REMARK 465     GLN B   202                                                      
REMARK 465     THR B   203                                                      
REMARK 465     ALA B   204                                                      
REMARK 465     LEU B   205                                                      
REMARK 465     HIS B   206                                                      
REMARK 465     ILE B   207                                                      
REMARK 465     ALA B   208                                                      
REMARK 465     ILE B   209                                                      
REMARK 465     GLU B   210                                                      
REMARK 465     ARG B   211                                                      
REMARK 465     ARG B   212                                                      
REMARK 465     ASN B   213                                                      
REMARK 465     MET B   214                                                      
REMARK 465     THR B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     VAL B   217                                                      
REMARK 465     THR B   218                                                      
REMARK 465     LEU B   219                                                      
REMARK 465     LEU B   220                                                      
REMARK 465     VAL B   221                                                      
REMARK 465     GLU B   222                                                      
REMARK 465     ASN B   223                                                      
REMARK 465     GLY B   224                                                      
REMARK 465     ALA B   225                                                      
REMARK 465     ASP B   226                                                      
REMARK 465     VAL B   227                                                      
REMARK 465     GLN B   228                                                      
REMARK 465     ALA B   229                                                      
REMARK 465     ALA B   230                                                      
REMARK 465     ALA B   231                                                      
REMARK 465     ASN B   232                                                      
REMARK 465     GLY B   233                                                      
REMARK 465     ASP B   234                                                      
REMARK 465     PHE B   235                                                      
REMARK 465     PHE B   236                                                      
REMARK 465     LYS B   237                                                      
REMARK 465     LYS B   238                                                      
REMARK 465     THR B   239                                                      
REMARK 465     LYS B   240                                                      
REMARK 465     GLY B   241                                                      
REMARK 465     ARG B   242                                                      
REMARK 465     PRO B   243                                                      
REMARK 465     GLY B   244                                                      
REMARK 465     PHE B   245                                                      
REMARK 465     TYR B   246                                                      
REMARK 465     PHE B   247                                                      
REMARK 465     GLY B   248                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     LEU B   250                                                      
REMARK 465     PRO B   251                                                      
REMARK 465     LEU B   252                                                      
REMARK 465     SER B   253                                                      
REMARK 465     LEU B   254                                                      
REMARK 465     ALA B   255                                                      
REMARK 465     ALA B   256                                                      
REMARK 465     CYS B   257                                                      
REMARK 465     THR B   258                                                      
REMARK 465     ASN B   259                                                      
REMARK 465     GLN B   260                                                      
REMARK 465     LEU B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     ILE B   263                                                      
REMARK 465     VAL B   264                                                      
REMARK 465     LYS B   265                                                      
REMARK 465     PHE B   266                                                      
REMARK 465     LEU B   267                                                      
REMARK 465     LEU B   268                                                      
REMARK 465     GLN B   269                                                      
REMARK 465     ASN B   270                                                      
REMARK 465     SER B   271                                                      
REMARK 465     TRP B   272                                                      
REMARK 465     GLN B   273                                                      
REMARK 465     PRO B   274                                                      
REMARK 465     ALA B   275                                                      
REMARK 465     ASP B   276                                                      
REMARK 465     ILE B   277                                                      
REMARK 465     SER B   278                                                      
REMARK 465     ALA B   279                                                      
REMARK 465     ARG B   280                                                      
REMARK 465     ASP B   281                                                      
REMARK 465     SER B   282                                                      
REMARK 465     GLY B   602                                                      
REMARK 465     LYS B   603                                                      
REMARK 465     ASN B   604                                                      
REMARK 465     ASN B   605                                                      
REMARK 465     SER B   606                                                      
REMARK 465     LEU B   607                                                      
REMARK 465     PRO B   608                                                      
REMARK 465     MET B   609                                                      
REMARK 465     GLU B   610                                                      
REMARK 465     SER B   611                                                      
REMARK 465     THR B   612                                                      
REMARK 465     PRO B   613                                                      
REMARK 465     HIS B   614                                                      
REMARK 465     LYS B   615                                                      
REMARK 465     CYS B   616                                                      
REMARK 465     ARG B   617                                                      
REMARK 465     GLY B   618                                                      
REMARK 465     SER B   619                                                      
REMARK 465     ALA B   620                                                      
REMARK 465     CYS B   621                                                      
REMARK 465     LYS B   622                                                      
REMARK 465     PRO B   623                                                      
REMARK 465     GLY B   624                                                      
REMARK 465     ASN B   625                                                      
REMARK 465     GLN B   727                                                      
REMARK 465     VAL B   728                                                      
REMARK 465     GLY B   729                                                      
REMARK 465     PHE B   730                                                      
REMARK 465     THR B   731                                                      
REMARK 465     PRO B   732                                                      
REMARK 465     ASP B   733                                                      
REMARK 465     GLY B   734                                                      
REMARK 465     LYS B   735                                                      
REMARK 465     ASP B   736                                                      
REMARK 465     ASP B   737                                                      
REMARK 465     VAL B   747                                                      
REMARK 465     ASN B   748                                                      
REMARK 465     TRP B   749                                                      
REMARK 465     THR B   750                                                      
REMARK 465     THR B   751                                                      
REMARK 465     TRP B   752                                                      
REMARK 465     ASN B   753                                                      
REMARK 465     THR B   754                                                      
REMARK 465     ASN B   755                                                      
REMARK 465     VAL B   756                                                      
REMARK 465     GLY B   757                                                      
REMARK 465     ILE B   758                                                      
REMARK 465     ILE B   759                                                      
REMARK 465     ASN B   760                                                      
REMARK 465     GLU B   761                                                      
REMARK 465     ASP B   762                                                      
REMARK 465     PRO B   763                                                      
REMARK 465     GLY B   764                                                      
REMARK 465     ASN B   765                                                      
REMARK 465     CYS B   766                                                      
REMARK 465     GLU B   767                                                      
REMARK 465     GLY B   768                                                      
REMARK 465     VAL B   769                                                      
REMARK 465     LYS B   770                                                      
REMARK 465     ARG B   771                                                      
REMARK 465     THR B   772                                                      
REMARK 465     LEU B   773                                                      
REMARK 465     SER B   774                                                      
REMARK 465     PHE B   775                                                      
REMARK 465     SER B   776                                                      
REMARK 465     LEU B   777                                                      
REMARK 465     ARG B   778                                                      
REMARK 465     SER B   779                                                      
REMARK 465     GLY B   780                                                      
REMARK 465     ARG B   781                                                      
REMARK 465     VAL B   782                                                      
REMARK 465     SER B   783                                                      
REMARK 465     GLY B   784                                                      
REMARK 465     ARG B   785                                                      
REMARK 465     ASN B   786                                                      
REMARK 465     TRP B   787                                                      
REMARK 465     LYS B   788                                                      
REMARK 465     ASN B   789                                                      
REMARK 465     PHE B   790                                                      
REMARK 465     ALA B   791                                                      
REMARK 465     LEU B   792                                                      
REMARK 465     VAL B   793                                                      
REMARK 465     PRO B   794                                                      
REMARK 465     LEU B   795                                                      
REMARK 465     LEU B   796                                                      
REMARK 465     ARG B   797                                                      
REMARK 465     ASP B   798                                                      
REMARK 465     ALA B   799                                                      
REMARK 465     SER B   800                                                      
REMARK 465     THR B   801                                                      
REMARK 465     ARG B   802                                                      
REMARK 465     ASP B   803                                                      
REMARK 465     ARG B   804                                                      
REMARK 465     HIS B   805                                                      
REMARK 465     ALA B   806                                                      
REMARK 465     THR B   807                                                      
REMARK 465     GLN B   808                                                      
REMARK 465     GLN B   809                                                      
REMARK 465     GLU B   810                                                      
REMARK 465     GLU B   811                                                      
REMARK 465     VAL B   812                                                      
REMARK 465     GLN B   813                                                      
REMARK 465     LEU B   814                                                      
REMARK 465     LYS B   815                                                      
REMARK 465     HIS B   816                                                      
REMARK 465     TYR B   817                                                      
REMARK 465     THR B   818                                                      
REMARK 465     GLY B   819                                                      
REMARK 465     SER B   820                                                      
REMARK 465     LEU B   821                                                      
REMARK 465     LYS B   822                                                      
REMARK 465     PRO B   823                                                      
REMARK 465     GLU B   824                                                      
REMARK 465     ASP B   825                                                      
REMARK 465     ALA B   826                                                      
REMARK 465     GLU B   827                                                      
REMARK 465     VAL B   828                                                      
REMARK 465     PHE B   829                                                      
REMARK 465     LYS B   830                                                      
REMARK 465     ASP B   831                                                      
REMARK 465     SER B   832                                                      
REMARK 465     MET B   833                                                      
REMARK 465     VAL B   834                                                      
REMARK 465     PRO B   835                                                      
REMARK 465     GLY B   836                                                      
REMARK 465     GLU B   837                                                      
REMARK 465     LYS B   838                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    LEU A   588     OG   SER A   592              1.96            
REMARK 500   O    LEU C   588     OG   SER C   592              1.97            
REMARK 500   O    LEU D   588     OG   SER D   592              1.98            
REMARK 500   OG   SER C   512     OAI  6EU C   901              2.08            
REMARK 500   OG   SER D   512     OAI  6EU D   901              2.08            
REMARK 500   OD1  ASN C   310     OH   TYR C   351              2.10            
REMARK 500   OH   TYR D   441     O    GLY D   548              2.11            
REMARK 500   OG   SER A   512     OAI  6EU A   901              2.11            
REMARK 500   O    LEU B   553     OG1  THR B   556              2.13            
REMARK 500   OG   SER B   512     OAI  6EU B   901              2.14            
REMARK 500   OD1  ASN B   310     OH   TYR B   351              2.17            
REMARK 500   O    GLY B   723     OH   TYR B   738              2.18            
REMARK 500   O    PHE B   517     OG   SER B   520              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A 296       12.99   -142.61                                   
REMARK 500    GLN A 354       52.43   -111.26                                   
REMARK 500    ALA A 373       54.92    -96.01                                   
REMARK 500    GLU A 391       -7.62     69.70                                   
REMARK 500    LYS A 392      -62.35   -107.42                                   
REMARK 500    SER A 404       -4.91     75.32                                   
REMARK 500    LEU A 460       73.57     62.32                                   
REMARK 500    TYR A 627      -11.57     73.85                                   
REMARK 500    LEU A 647       -4.84     69.49                                   
REMARK 500    PHE A 655       68.86     61.55                                   
REMARK 500    THR A 670      -62.92    -92.90                                   
REMARK 500    SER A 711      -76.75    -80.23                                   
REMARK 500    PHE A 712      -23.63     64.18                                   
REMARK 500    ARG A 739       50.35   -140.62                                   
REMARK 500    TRP A 740       63.22     61.42                                   
REMARK 500    ASP C 296       13.02   -142.84                                   
REMARK 500    GLN C 354       40.73   -109.03                                   
REMARK 500    ALA C 373       55.55    -97.74                                   
REMARK 500    GLU C 391       -5.85     70.00                                   
REMARK 500    ASN C 393      115.35   -162.10                                   
REMARK 500    TYR C 401       37.60    -99.12                                   
REMARK 500    SER C 404       -4.85     74.96                                   
REMARK 500    THR C 406      109.07    -45.28                                   
REMARK 500    LEU C 460       75.49     59.97                                   
REMARK 500    GLU C 536       -8.89    -57.38                                   
REMARK 500    TYR C 627      -10.02     74.07                                   
REMARK 500    LEU C 647       -5.33     69.51                                   
REMARK 500    TYR C 653     -178.10   -173.02                                   
REMARK 500    PHE C 655       64.78     62.37                                   
REMARK 500    THR C 670      -63.19    -94.32                                   
REMARK 500    SER C 711      -76.29    -79.34                                   
REMARK 500    PHE C 712      -21.90     65.24                                   
REMARK 500    ARG C 739       51.80   -142.93                                   
REMARK 500    ASP D 296       12.94   -142.56                                   
REMARK 500    GLN D 354       42.99   -107.75                                   
REMARK 500    ALA D 373       54.32    -97.09                                   
REMARK 500    GLU D 391       -5.12     70.03                                   
REMARK 500    ASN D 393      111.14   -161.66                                   
REMARK 500    SER D 404       -7.60     75.55                                   
REMARK 500    THR D 406      109.78    -47.75                                   
REMARK 500    LEU D 460       76.44     59.98                                   
REMARK 500    GLU D 536       -8.70    -56.54                                   
REMARK 500    TYR D 627      -10.91     73.76                                   
REMARK 500    LEU D 647       -5.07     69.82                                   
REMARK 500    PHE D 655       69.63     66.08                                   
REMARK 500    THR D 670      -64.34    -91.71                                   
REMARK 500    SER D 711      -76.83    -78.13                                   
REMARK 500    PHE D 712      -22.87     65.13                                   
REMARK 500    ARG D 739       51.10   -149.24                                   
REMARK 500    ASP B 296       12.60   -142.55                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      67 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-23132   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF RTX-BOUND FULL-LENGTH TRPV1 AT STATE B          
DBREF  7L2L A    2   838  UNP    O35433   TRPV1_RAT        2    838             
DBREF  7L2L C    2   838  UNP    O35433   TRPV1_RAT        2    838             
DBREF  7L2L D    2   838  UNP    O35433   TRPV1_RAT        2    838             
DBREF  7L2L B    2   838  UNP    O35433   TRPV1_RAT        2    838             
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1               
ATOM      1  N   VAL A 283     113.772 176.209 172.289  1.00136.35
ATOM      2  CA  VAL A 283     113.882 175.766 170.906  1.00136.35
ATOM      3  C   VAL A 283     112.590 175.112 170.415  1.00136.35
ATOM      4  O   VAL A 283     112.381 175.002 169.209  1.00136.35
ATOM      5  CB  VAL A 283     115.075 174.799 170.733  1.00136.35
ATOM      6  CG1 VAL A 283     114.826 173.500 171.480  1.00136.35
ATOM      7  CG2 VAL A 283     115.348 174.532 169.250  1.00136.35
ATOM      8  N   GLY A 284     111.726 174.683 171.341  1.00136.76
ATOM      9  CA  GLY A 284     110.521 173.949 171.004  1.00136.76
ATOM     10  C   GLY A 284     110.637 172.441 171.114  1.00136.76
ATOM     11  O   GLY A 284     109.722 171.735 170.667  1.00136.76
ATOM     12  N   ASN A 285     111.742 171.929 171.655  1.00138.19
ATOM     13  CA  ASN A 285     111.969 170.510 171.886  1.00138.19
ATOM     14  C   ASN A 285     111.881 170.189 173.366  1.00138.19
ATOM     15  O   ASN A 285     111.968 171.075 174.218  1.00138.19
ATOM     16  CB  ASN A 285     113.343 170.087 171.378  1.00138.19
ATOM     17  CG  ASN A 285     113.488 170.274 169.897  1.00138.19
ATOM     18  OD1 ASN A 285     112.512 170.526 169.189  1.00138.19
ATOM     19  ND2 ASN A 285     114.713 170.159 169.415  1.00138.19
ATOM     20  N   THR A 286     111.705 168.907 173.663  1.00141.79
ATOM     21  CA  THR A 286     111.776 168.443 175.040  1.00141.79
ATOM     22  C   THR A 286     113.193 167.984 175.362  1.00141.79
ATOM     23  O   THR A 286     114.072 167.917 174.503  1.00141.79
ATOM     24  CB  THR A 286     110.787 167.312 175.332  1.00141.79
ATOM     25  OG1 THR A 286     111.077 166.775 176.628  1.00141.79
ATOM     26  CG2 THR A 286     110.878 166.193 174.321  1.00141.79
ATOM     27  N   VAL A 287     113.401 167.667 176.635  1.00143.44
ATOM     28  CA  VAL A 287     114.719 167.246 177.088  1.00143.44
ATOM     29  C   VAL A 287     115.114 165.926 176.450  1.00143.44
ATOM     30  O   VAL A 287     116.306 165.649 176.273  1.00143.44
ATOM     31  CB  VAL A 287     114.746 167.171 178.631  1.00143.44
ATOM     32  CG1 VAL A 287     113.791 166.097 179.147  1.00143.44
ATOM     33  CG2 VAL A 287     116.161 166.903 179.144  1.00143.44
ATOM     34  N   LEU A 288     114.133 165.079 176.123  1.00143.20
ATOM     35  CA  LEU A 288     114.447 163.753 175.604  1.00143.20
ATOM     36  C   LEU A 288     115.241 163.846 174.318  1.00143.20
ATOM     37  O   LEU A 288     116.152 163.049 174.087  1.00143.20
ATOM     38  CB  LEU A 288     113.171 162.955 175.379  1.00143.20
ATOM     39  CG  LEU A 288     112.380 162.605 176.641  1.00143.20
ATOM     40  CD1 LEU A 288     110.955 162.240 176.301  1.00143.20
ATOM     41  CD2 LEU A 288     113.040 161.477 177.395  1.00143.20
ATOM     42  N   HIS A 289     114.924 164.822 173.477  1.00142.64
ATOM     43  CA  HIS A 289     115.691 165.007 172.253  1.00142.64
ATOM     44  C   HIS A 289     117.055 165.614 172.536  1.00142.64
ATOM     45  O   HIS A 289     118.055 165.195 171.949  1.00142.64
ATOM     46  CB  HIS A 289     114.909 165.886 171.284  1.00142.64
ATOM     47  CG  HIS A 289     113.561 165.347 170.964  1.00142.64
ATOM     48  ND1 HIS A 289     112.448 165.653 171.710  1.00142.64
ATOM     49  CD2 HIS A 289     113.149 164.487 170.006  1.00142.64
ATOM     50  CE1 HIS A 289     111.401 165.021 171.215  1.00142.64
ATOM     51  NE2 HIS A 289     111.799 164.309 170.177  1.00142.64
ATOM     52  N   ALA A 290     117.118 166.602 173.425  1.00142.68
ATOM     53  CA  ALA A 290     118.406 167.204 173.722  1.00142.68
ATOM     54  C   ALA A 290     119.367 166.167 174.269  1.00142.68
ATOM     55  O   ALA A 290     120.563 166.209 173.963  1.00142.68
ATOM     56  CB  ALA A 290     118.237 168.362 174.698  1.00142.68
ATOM     57  N   LEU A 291     118.856 165.199 175.031  1.00143.88
ATOM     58  CA  LEU A 291     119.689 164.086 175.462  1.00143.88
ATOM     59  C   LEU A 291     120.287 163.360 174.273  1.00143.88
ATOM     60  O   LEU A 291     121.416 162.870 174.344  1.00143.88
ATOM     61  CB  LEU A 291     118.868 163.113 176.296  1.00143.88
ATOM     62  CG  LEU A 291     118.423 163.599 177.672  1.00143.88
ATOM     63  CD1 LEU A 291     117.352 162.699 178.237  1.00143.88
ATOM     64  CD2 LEU A 291     119.575 163.622 178.617  1.00143.88
ATOM     65  N   VAL A 292     119.551 163.293 173.171  1.00141.06
ATOM     66  CA  VAL A 292     120.083 162.691 171.959  1.00141.06
ATOM     67  C   VAL A 292     121.142 163.588 171.341  1.00141.06
ATOM     68  O   VAL A 292     122.192 163.118 170.888  1.00141.06
ATOM     69  CB  VAL A 292     118.943 162.417 170.965  1.00141.06
ATOM     70  CG1 VAL A 292     119.493 161.820 169.703  1.00141.06
ATOM     71  CG2 VAL A 292     117.874 161.525 171.584  1.00141.06
ATOM     72  N   GLU A 293     120.856 164.888 171.279  1.00139.40
ATOM     73  CA  GLU A 293     121.760 165.823 170.618  1.00139.40
ATOM     74  C   GLU A 293     123.121 165.849 171.293  1.00139.40
ATOM     75  O   GLU A 293     124.148 166.010 170.626  1.00139.40
ATOM     76  CB  GLU A 293     121.156 167.224 170.615  1.00139.40
ATOM     77  CG  GLU A 293     120.024 167.435 169.637  1.00139.40
ATOM     78  CD  GLU A 293     119.481 168.849 169.693  1.00139.40
ATOM     79  OE1 GLU A 293     120.268 169.785 169.937  1.00139.40
ATOM     80  OE2 GLU A 293     118.261 169.028 169.503  1.00139.40
ATOM     81  N   VAL A 294     123.149 165.718 172.620  1.00139.76
ATOM     82  CA  VAL A 294     124.398 165.860 173.359  1.00139.76
ATOM     83  C   VAL A 294     125.349 164.691 173.164  1.00139.76
ATOM     84  O   VAL A 294     126.528 164.809 173.506  1.00139.76
ATOM     85  CB  VAL A 294     124.139 166.053 174.870  1.00139.76
ATOM     86  CG1 VAL A 294     123.488 167.404 175.128  1.00139.76
ATOM     87  CG2 VAL A 294     123.285 164.928 175.458  1.00139.76
ATOM     88  N   ALA A 295     124.894 163.578 172.606  1.00139.81
ATOM     89  CA  ALA A 295     125.773 162.426 172.526  1.00139.81
ATOM     90  C   ALA A 295     126.828 162.635 171.443  1.00139.81
ATOM     91  O   ALA A 295     126.736 163.550 170.624  1.00139.81
ATOM     92  CB  ALA A 295     124.973 161.153 172.263  1.00139.81
ATOM     93  N   ASP A 296     127.882 161.810 171.487  1.00141.98
ATOM     94  CA  ASP A 296     128.869 161.801 170.412  1.00141.98
ATOM     95  C   ASP A 296     129.402 160.409 170.087  1.00141.98
ATOM     96  O   ASP A 296     130.425 160.309 169.404  1.00141.98
ATOM     97  CB  ASP A 296     130.041 162.735 170.745  1.00141.98
ATOM     98  CG  ASP A 296     130.886 162.244 171.903  1.00141.98
ATOM     99  OD1 ASP A 296     130.485 161.286 172.592  1.00141.98
ATOM    100  OD2 ASP A 296     131.967 162.830 172.133  1.00141.98
ATOM    101  N   ASN A 297     128.775 159.343 170.578  1.00138.00
ATOM    102  CA  ASN A 297     129.165 157.959 170.332  1.00138.00
ATOM    103  C   ASN A 297     130.512 157.583 170.941  1.00138.00
ATOM    104  O   ASN A 297     131.121 156.606 170.494  1.00138.00
ATOM    105  CB  ASN A 297     129.183 157.634 168.833  1.00138.00
ATOM    106  CG  ASN A 297     127.840 157.847 168.181  1.00138.00
ATOM    107  OD1 ASN A 297     126.819 157.413 168.706  1.00138.00
ATOM    108  ND2 ASN A 297     127.829 158.518 167.036  1.00138.00
ATOM    109  N   THR A 298     131.006 158.326 171.930  1.00143.52
ATOM    110  CA  THR A 298     132.132 157.864 172.734  1.00143.52
ATOM    111  C   THR A 298     131.636 157.109 173.970  1.00143.52
ATOM    112  O   THR A 298     130.502 157.285 174.429  1.00143.52
ATOM    113  CB  THR A 298     133.015 159.037 173.155  1.00143.52
ATOM    114  OG1 THR A 298     132.261 159.936 173.976  1.00143.52
ATOM    115  CG2 THR A 298     133.540 159.780 171.930  1.00143.52
ATOM    116  N   VAL A 299     132.524 156.282 174.529  1.00142.53
ATOM    117  CA  VAL A 299     132.112 155.313 175.543  1.00142.53
ATOM    118  C   VAL A 299     131.613 156.026 176.794  1.00142.53
ATOM    119  O   VAL A 299     130.545 155.700 177.332  1.00142.53
ATOM    120  CB  VAL A 299     133.271 154.352 175.873  1.00142.53
ATOM    121  CG1 VAL A 299     132.848 153.364 176.961  1.00142.53
ATOM    122  CG2 VAL A 299     133.759 153.611 174.619  1.00142.53
ATOM    123  N   ASP A 300     132.373 157.013 177.268  1.00141.15
ATOM    124  CA  ASP A 300     131.961 157.734 178.467  1.00141.15
ATOM    125  C   ASP A 300     130.656 158.453 178.203  1.00141.15
ATOM    126  O   ASP A 300     129.713 158.392 179.005  1.00141.15
ATOM    127  CB  ASP A 300     133.031 158.746 178.880  1.00141.15
ATOM    128  CG  ASP A 300     134.431 158.184 178.819  1.00141.15
ATOM    129  OD1 ASP A 300     134.632 157.049 179.290  1.00141.15
ATOM    130  OD2 ASP A 300     135.324 158.872 178.288  1.00141.15
ATOM    131  N   ASN A 301     130.580 159.080 177.034  1.00142.91
ATOM    132  CA  ASN A 301     129.379 159.773 176.612  1.00142.91
ATOM    133  C   ASN A 301     128.208 158.811 176.521  1.00142.91
ATOM    134  O   ASN A 301     127.093 159.131 176.951  1.00142.91
ATOM    135  CB  ASN A 301     129.645 160.429 175.269  1.00142.91
ATOM    136  CG  ASN A 301     128.461 161.143 174.749  1.00142.91
ATOM    137  OD1 ASN A 301     127.583 160.530 174.148  1.00142.91
ATOM    138  ND2 ASN A 301     128.413 162.453 174.968  1.00142.91
ATOM    139  N   THR A 302     128.445 157.621 175.963  1.00143.20
ATOM    140  CA  THR A 302     127.364 156.654 175.811  1.00143.20
ATOM    141  C   THR A 302     126.810 156.229 177.157  1.00143.20
ATOM    142  O   THR A 302     125.589 156.209 177.353  1.00143.20
ATOM    143  CB  THR A 302     127.858 155.428 175.048  1.00143.20
ATOM    144  OG1 THR A 302     128.505 155.841 173.841  1.00143.20
ATOM    145  CG2 THR A 302     126.695 154.498 174.710  1.00143.20
ATOM    146  N   LYS A 303     127.689 155.878 178.093  1.00140.82
ATOM    147  CA  LYS A 303     127.214 155.447 179.400  1.00140.82
ATOM    148  C   LYS A 303     126.474 156.574 180.103  1.00140.82
ATOM    149  O   LYS A 303     125.440 156.345 180.740  1.00140.82
ATOM    150  CB  LYS A 303     128.382 154.969 180.254  1.00140.82
ATOM    151  CG  LYS A 303     129.154 153.788 179.695  1.00140.82
ATOM    152  CD  LYS A 303     130.413 153.573 180.505  1.00140.82
ATOM    153  CE  LYS A 303     131.087 152.281 180.144  1.00140.82
ATOM    154  NZ  LYS A 303     132.278 152.036 180.995  1.00140.82
ATOM    155  N   PHE A 304     126.981 157.801 179.997  1.00142.86
ATOM    156  CA  PHE A 304     126.320 158.907 180.670  1.00142.86
ATOM    157  C   PHE A 304     124.936 159.152 180.089  1.00142.86
ATOM    158  O   PHE A 304     123.970 159.383 180.828  1.00142.86
ATOM    159  CB  PHE A 304     127.172 160.171 180.578  1.00142.86
ATOM    160  CG  PHE A 304     126.514 161.382 181.185  1.00142.86
ATOM    161  CD1 PHE A 304     126.043 161.349 182.484  1.00142.86
ATOM    162  CD2 PHE A 304     126.377 162.548 180.466  1.00142.86
ATOM    163  CE1 PHE A 304     125.445 162.442 183.046  1.00142.86
ATOM    164  CE2 PHE A 304     125.783 163.649 181.028  1.00142.86
ATOM    165  CZ  PHE A 304     125.319 163.595 182.321  1.00142.86
ATOM    166  N   VAL A 305     124.821 159.127 178.763  1.00144.33
ATOM    167  CA  VAL A 305     123.520 159.380 178.156  1.00144.33
ATOM    168  C   VAL A 305     122.558 158.255 178.498  1.00144.33
ATOM    169  O   VAL A 305     121.362 158.488 178.729  1.00144.33
ATOM    170  CB  VAL A 305     123.648 159.584 176.638  1.00144.33
ATOM    171  CG1 VAL A 305     122.267 159.707 176.022  1.00144.33
ATOM    172  CG2 VAL A 305     124.453 160.837 176.333  1.00144.33
ATOM    173  N   THR A 306     123.061 157.023 178.553  1.00140.97
ATOM    174  CA  THR A 306     122.236 155.939 179.055  1.00140.97
ATOM    175  C   THR A 306     121.767 156.236 180.467  1.00140.97
ATOM    176  O   THR A 306     120.597 156.017 180.792  1.00140.97
ATOM    177  CB  THR A 306     123.005 154.623 179.030  1.00140.97
ATOM    178  OG1 THR A 306     123.594 154.429 177.740  1.00140.97
ATOM    179  CG2 THR A 306     122.069 153.463 179.354  1.00140.97
ATOM    180  N   SER A 307     122.663 156.750 181.314  1.00141.64
ATOM    181  CA  SER A 307     122.292 157.034 182.693  1.00141.64
ATOM    182  C   SER A 307     121.162 158.043 182.761  1.00141.64
ATOM    183  O   SER A 307     120.180 157.843 183.486  1.00141.64
ATOM    184  CB  SER A 307     123.495 157.554 183.469  1.00141.64
ATOM    185  OG  SER A 307     123.066 158.281 184.604  1.00141.64
ATOM    186  N   MET A 308     121.282 159.132 182.011  1.00145.65
ATOM    187  CA  MET A 308     120.234 160.145 182.041  1.00145.65
ATOM    188  C   MET A 308     118.918 159.581 181.526  1.00145.65
ATOM    189  O   MET A 308     117.841 159.894 182.063  1.00145.65
ATOM    190  CB  MET A 308     120.647 161.365 181.227  1.00145.65
ATOM    191  CG  MET A 308     121.894 162.038 181.751  1.00145.65
ATOM    192  SD  MET A 308     122.296 163.561 180.877  1.00145.65
ATOM    193  CE  MET A 308     122.929 162.898 179.332  1.00145.65
ATOM    194  N   TYR A 309     118.985 158.743 180.489  1.00142.95
ATOM    195  CA  TYR A 309     117.772 158.092 180.021  1.00142.95
ATOM    196  C   TYR A 309     117.142 157.263 181.122  1.00142.95
ATOM    197  O   TYR A 309     115.933 157.334 181.341  1.00142.95
ATOM    198  CB  TYR A 309     118.066 157.199 178.816  1.00142.95
ATOM    199  CG  TYR A 309     117.762 157.843 177.485  1.00142.95
ATOM    200  CD1 TYR A 309     116.472 158.252 177.159  1.00142.95
ATOM    201  CD2 TYR A 309     118.760 158.030 176.550  1.00142.95
ATOM    202  CE1 TYR A 309     116.196 158.844 175.961  1.00142.95
ATOM    203  CE2 TYR A 309     118.489 158.619 175.347  1.00142.95
ATOM    204  CZ  TYR A 309     117.202 159.023 175.056  1.00142.95
ATOM    205  OH  TYR A 309     116.924 159.620 173.852  1.00142.95
ATOM    206  N   ASN A 310     117.950 156.484 181.832  1.00142.31
ATOM    207  CA  ASN A 310     117.410 155.637 182.884  1.00142.31
ATOM    208  C   ASN A 310     116.713 156.476 183.941  1.00142.31
ATOM    209  O   ASN A 310     115.591 156.161 184.373  1.00142.31
ATOM    210  CB  ASN A 310     118.538 154.818 183.503  1.00142.31
ATOM    211  CG  ASN A 310     119.304 154.022 182.473  1.00142.31
ATOM    212  OD1 ASN A 310     118.964 154.029 181.290  1.00142.31
ATOM    213  ND2 ASN A 310     120.371 153.364 182.911  1.00142.31
ATOM    214  N   GLU A 311     117.341 157.586 184.317  1.00142.34
ATOM    215  CA  GLU A 311     116.770 158.435 185.352  1.00142.34
ATOM    216  C   GLU A 311     115.427 158.989 184.915  1.00142.34
ATOM    217  O   GLU A 311     114.421 158.865 185.633  1.00142.34
ATOM    218  CB  GLU A 311     117.732 159.576 185.672  1.00142.34
ATOM    219  CG  GLU A 311     119.057 159.138 186.279  1.00142.34
ATOM    220  CD  GLU A 311     120.149 160.150 186.045  1.00142.34
ATOM    221  OE1 GLU A 311     119.840 161.359 186.025  1.00142.34
ATOM    222  OE2 GLU A 311     121.312 159.737 185.866  1.00142.34
ATOM    223  N   ILE A 312     115.381 159.573 183.723  1.00143.86
ATOM    224  CA  ILE A 312     114.138 160.213 183.327  1.00143.86
ATOM    225  C   ILE A 312     113.068 159.170 183.049  1.00143.86
ATOM    226  O   ILE A 312     111.879 159.450 183.205  1.00143.86
ATOM    227  CB  ILE A 312     114.349 161.149 182.127  1.00143.86
ATOM    228  CG1 ILE A 312     113.085 161.995 181.903  1.00143.86
ATOM    229  CG2 ILE A 312     114.699 160.350 180.870  1.00143.86
ATOM    230  CD1 ILE A 312     113.272 163.128 180.945  1.00143.86
ATOM    231  N   LEU A 313     113.449 157.967 182.615  1.00141.85
ATOM    232  CA  LEU A 313     112.449 156.929 182.384  1.00141.85
ATOM    233  C   LEU A 313     111.780 156.526 183.687  1.00141.85
ATOM    234  O   LEU A 313     110.547 156.432 183.766  1.00141.85
ATOM    235  CB  LEU A 313     113.093 155.722 181.722  1.00141.85
ATOM    236  CG  LEU A 313     113.522 155.944 180.277  1.00141.85
ATOM    237  CD1 LEU A 313     114.555 154.896 179.908  1.00141.85
ATOM    238  CD2 LEU A 313     112.348 155.906 179.333  1.00141.85
ATOM    239  N   ILE A 314     112.578 156.308 184.736  1.00142.69
ATOM    240  CA  ILE A 314     111.990 155.939 186.021  1.00142.69
ATOM    241  C   ILE A 314     111.107 157.069 186.537  1.00142.69
ATOM    242  O   ILE A 314     109.985 156.841 187.017  1.00142.69
ATOM    243  CB  ILE A 314     113.084 155.577 187.041  1.00142.69
ATOM    244  CG1 ILE A 314     113.896 154.362 186.579  1.00142.69
ATOM    245  CG2 ILE A 314     112.448 155.296 188.401  1.00142.69
ATOM    246  CD1 ILE A 314     115.283 154.298 187.189  1.00142.69
ATOM    247  N   LEU A 315     111.597 158.305 186.438  1.00143.32
ATOM    248  CA  LEU A 315     110.823 159.426 186.956  1.00143.32
ATOM    249  C   LEU A 315     109.536 159.633 186.166  1.00143.32
ATOM    250  O   LEU A 315     108.474 159.875 186.752  1.00143.32
ATOM    251  CB  LEU A 315     111.680 160.687 186.952  1.00143.32
ATOM    252  CG  LEU A 315     112.757 160.727 188.034  1.00143.32
ATOM    253  CD1 LEU A 315     113.677 161.885 187.787  1.00143.32
ATOM    254  CD2 LEU A 315     112.147 160.839 189.413  1.00143.32
ATOM    255  N   GLY A 316     109.605 159.534 184.842  1.00145.17
ATOM    256  CA  GLY A 316     108.406 159.663 184.040  1.00145.17
ATOM    257  C   GLY A 316     107.385 158.597 184.372  1.00145.17
ATOM    258  O   GLY A 316     106.186 158.873 184.454  1.00145.17
ATOM    259  N   ALA A 317     107.849 157.360 184.572  1.00147.45
ATOM    260  CA  ALA A 317     106.932 156.302 184.973  1.00147.45
ATOM    261  C   ALA A 317     106.232 156.655 186.272  1.00147.45
ATOM    262  O   ALA A 317     105.003 156.567 186.369  1.00147.45
ATOM    263  CB  ALA A 317     107.678 154.983 185.151  1.00147.45
ATOM    264  N   LYS A 318     106.992 157.096 187.272  1.00147.33
ATOM    265  CA  LYS A 318     106.389 157.273 188.585  1.00147.33
ATOM    266  C   LYS A 318     105.505 158.503 188.645  1.00147.33
ATOM    267  O   LYS A 318     104.556 158.531 189.435  1.00147.33
ATOM    268  CB  LYS A 318     107.469 157.343 189.674  1.00147.33
ATOM    269  CG  LYS A 318     108.220 156.024 189.935  1.00147.33
ATOM    270  CD  LYS A 318     107.320 154.876 190.432  1.00147.33
ATOM    271  CE  LYS A 318     106.650 155.173 191.770  1.00147.33
ATOM    272  NZ  LYS A 318     105.886 154.000 192.308  1.00147.33
ATOM    273  N   LEU A 319     105.774 159.502 187.811  1.00143.95
ATOM    274  CA  LEU A 319     105.078 160.777 187.917  1.00143.95
ATOM    275  C   LEU A 319     103.896 160.900 186.961  1.00143.95
ATOM    276  O   LEU A 319     102.833 161.384 187.362  1.00143.95
ATOM    277  CB  LEU A 319     106.078 161.910 187.686  1.00143.95
ATOM    278  CG  LEU A 319     107.202 161.952 188.732  1.00143.95
ATOM    279  CD1 LEU A 319     108.337 162.836 188.266  1.00143.95
ATOM    280  CD2 LEU A 319     106.685 162.421 190.082  1.00143.95
ATOM    281  N   HIS A 320     104.045 160.462 185.713  1.00142.25
ATOM    282  CA  HIS A 320     103.005 160.587 184.691  1.00142.25
ATOM    283  C   HIS A 320     102.774 159.226 184.057  1.00142.25
ATOM    284  O   HIS A 320     103.081 159.013 182.877  1.00142.25
ATOM    285  CB  HIS A 320     103.393 161.613 183.629  1.00142.25
ATOM    286  CG  HIS A 320     103.562 162.996 184.164  1.00142.25
ATOM    287  ND1 HIS A 320     102.509 163.871 184.306  1.00142.25
ATOM    288  CD2 HIS A 320     104.661 163.655 184.595  1.00142.25
ATOM    289  CE1 HIS A 320     102.953 165.011 184.800  1.00142.25
ATOM    290  NE2 HIS A 320     104.255 164.906 184.985  1.00142.25
ATOM    291  N   PRO A 321     102.225 158.276 184.816  1.00144.03
ATOM    292  CA  PRO A 321     102.029 156.925 184.272  1.00144.03
ATOM    293  C   PRO A 321     101.058 156.871 183.121  1.00144.03
ATOM    294  O   PRO A 321     101.059 155.883 182.378  1.00144.03
ATOM    295  CB  PRO A 321     101.503 156.137 185.476  1.00144.03
ATOM    296  CG  PRO A 321     100.867 157.164 186.345  1.00144.03
ATOM    297  CD  PRO A 321     101.658 158.414 186.169  1.00144.03
ATOM    298  N   THR A 322     100.212 157.889 182.961  1.00143.84
ATOM    299  CA  THR A 322      99.241 157.923 181.878  1.00143.84
ATOM    300  C   THR A 322      99.849 158.354 180.556  1.00143.84
ATOM    301  O   THR A 322      99.348 157.947 179.505  1.00143.84
ATOM    302  CB  THR A 322      98.104 158.885 182.223  1.00143.84
ATOM    303  OG1 THR A 322      98.602 160.227 182.220  1.00143.84
ATOM    304  CG2 THR A 322      97.517 158.565 183.593  1.00143.84
ATOM    305  N   LEU A 323     100.933 159.122 180.584  1.00141.71
ATOM    306  CA  LEU A 323     101.492 159.755 179.398  1.00141.71
ATOM    307  C   LEU A 323     102.772 159.041 178.998  1.00141.71
ATOM    308  O   LEU A 323     103.621 158.757 179.850  1.00141.71
ATOM    309  CB  LEU A 323     101.769 161.236 179.660  1.00141.71
ATOM    310  CG  LEU A 323     102.443 162.042 178.548  1.00141.71
ATOM    311  CD1 LEU A 323     101.602 162.046 177.284  1.00141.71
ATOM    312  CD2 LEU A 323     102.709 163.455 179.034  1.00141.71
ATOM    313  N   LYS A 324     102.901 158.749 177.706  1.00143.51
ATOM    314  CA  LYS A 324     104.101 158.124 177.182  1.00143.51
ATOM    315  C   LYS A 324     105.136 159.174 176.810  1.00143.51
ATOM    316  O   LYS A 324     104.819 160.214 176.228  1.00143.51
ATOM    317  CB  LYS A 324     103.767 157.272 175.964  1.00143.51
ATOM    318  CG  LYS A 324     102.901 156.063 176.290  1.00143.51
ATOM    319  CD  LYS A 324     102.647 155.209 175.053  1.00143.51
ATOM    320  CE  LYS A 324     101.781 153.992 175.363  1.00143.51
ATOM    321  NZ  LYS A 324     100.381 154.346 175.695  1.00143.51
ATOM    322  N   LEU A 325     106.394 158.876 177.134  1.00144.11
ATOM    323  CA  LEU A 325     107.473 159.817 176.870  1.00144.11
ATOM    324  C   LEU A 325     107.889 159.787 175.405  1.00144.11
ATOM    325  O   LEU A 325     107.804 160.801 174.705  1.00144.11
ATOM    326  CB  LEU A 325     108.686 159.493 177.744  1.00144.11
ATOM    327  CG  LEU A 325     108.669 159.746 179.252  1.00144.11
ATOM    328  CD1 LEU A 325     109.867 159.055 179.909  1.00144.11
ATOM    329  CD2 LEU A 325     108.681 161.230 179.565  1.00144.11
ATOM    330  N   GLU A 326     108.316 158.620 174.922  1.00143.75
ATOM    331  CA  GLU A 326     109.041 158.550 173.662  1.00143.75
ATOM    332  C   GLU A 326     108.183 158.924 172.465  1.00143.75
ATOM    333  O   GLU A 326     108.729 159.228 171.405  1.00143.75
ATOM    334  CB  GLU A 326     109.615 157.152 173.459  1.00143.75
ATOM    335  CG  GLU A 326     110.725 156.793 174.428  1.00143.75
ATOM    336  CD  GLU A 326     110.197 156.247 175.743  1.00143.75
ATOM    337  OE1 GLU A 326     109.041 156.558 176.094  1.00143.75
ATOM    338  OE2 GLU A 326     110.929 155.499 176.422  1.00143.75
ATOM    339  N   GLU A 327     106.860 158.917 172.595  1.00144.63
ATOM    340  CA  GLU A 327     106.049 159.467 171.518  1.00144.63
ATOM    341  C   GLU A 327     106.286 160.956 171.336  1.00144.63
ATOM    342  O   GLU A 327     106.007 161.489 170.258  1.00144.63
ATOM    343  CB  GLU A 327     104.555 159.207 171.772  1.00144.63
ATOM    344  CG  GLU A 327     103.929 159.941 172.964  1.00144.63
ATOM    345  CD  GLU A 327     102.419 159.794 173.003  1.00144.63
ATOM    346  OE1 GLU A 327     101.865 159.116 172.117  1.00144.63
ATOM    347  OE2 GLU A 327     101.782 160.363 173.918  1.00144.63
ATOM    348  N   ILE A 328     106.797 161.633 172.361  1.00144.43
ATOM    349  CA  ILE A 328     106.830 163.085 172.361  1.00144.43
ATOM    350  C   ILE A 328     107.792 163.559 171.288  1.00144.43
ATOM    351  O   ILE A 328     108.988 163.248 171.321  1.00144.43
ATOM    352  CB  ILE A 328     107.230 163.610 173.746  1.00144.43
ATOM    353  CG1 ILE A 328     106.155 163.265 174.782  1.00144.43
ATOM    354  CG2 ILE A 328     107.446 165.105 173.692  1.00144.43
ATOM    355  CD1 ILE A 328     106.652 163.305 176.210  1.00144.43
ATOM    356  N   THR A 329     107.276 164.338 170.351  1.00142.72
ATOM    357  CA  THR A 329     108.022 164.743 169.177  1.00142.72
ATOM    358  C   THR A 329     108.718 166.069 169.420  1.00142.72
ATOM    359  O   THR A 329     108.279 166.898 170.218  1.00142.72
ATOM    360  CB  THR A 329     107.098 164.871 167.969  1.00142.72
ATOM    361  OG1 THR A 329     106.076 165.836 168.248  1.00142.72
ATOM    362  CG2 THR A 329     106.461 163.543 167.643  1.00142.72
ATOM    363  N   ASN A 330     109.816 166.258 168.704  1.00142.93
ATOM    364  CA  ASN A 330     110.460 167.559 168.639  1.00142.93
ATOM    365  C   ASN A 330     109.672 168.417 167.663  1.00142.93
ATOM    366  O   ASN A 330     108.674 167.986 167.077  1.00142.93
ATOM    367  CB  ASN A 330     111.922 167.430 168.222  1.00142.93
ATOM    368  CG  ASN A 330     112.087 166.713 166.909  1.00142.93
ATOM    369  OD1 ASN A 330     111.130 166.168 166.371  1.00142.93
ATOM    370  ND2 ASN A 330     113.301 166.707 166.384  1.00142.93
ATOM    371  N   ARG A 331     110.135 169.645 167.462  1.00142.03
ATOM    372  CA  ARG A 331     109.434 170.561 166.579  1.00142.03
ATOM    373  C   ARG A 331     109.331 170.029 165.158  1.00142.03
ATOM    374  O   ARG A 331     108.375 170.369 164.454  1.00142.03
ATOM    375  CB  ARG A 331     110.140 171.915 166.592  1.00142.03
ATOM    376  CG  ARG A 331     111.616 171.869 166.192  1.00142.03
ATOM    377  CD  ARG A 331     112.300 173.189 166.501  1.00142.03
ATOM    378  NE  ARG A 331     111.629 174.317 165.857  1.00142.03
ATOM    379  CZ  ARG A 331     111.983 175.593 165.994  1.00142.03
ATOM    380  NH1 ARG A 331     113.011 175.938 166.754  1.00142.03
ATOM    381  NH2 ARG A 331     111.301 176.529 165.353  1.00142.03
ATOM    382  N   LYS A 332     110.254 169.167 164.740  1.00139.54
ATOM    383  CA  LYS A 332     110.243 168.581 163.409  1.00139.54
ATOM    384  C   LYS A 332     109.441 167.293 163.339  1.00139.54
ATOM    385  O   LYS A 332     109.537 166.575 162.340  1.00139.54
ATOM    386  CB  LYS A 332     111.670 168.312 162.945  1.00139.54
ATOM    387  CG  LYS A 332     112.529 169.546 162.898  1.00139.54
ATOM    388  CD  LYS A 332     113.915 169.211 162.415  1.00139.54
ATOM    389  CE  LYS A 332     114.786 170.445 162.338  1.00139.54
ATOM    390  NZ  LYS A 332     116.133 170.125 161.797  1.00139.54
ATOM    391  N   GLY A 333     108.674 166.970 164.375  1.00139.37
ATOM    392  CA  GLY A 333     107.870 165.769 164.336  1.00139.37
ATOM    393  C   GLY A 333     108.681 164.499 164.376  1.00139.37
ATOM    394  O   GLY A 333     108.283 163.503 163.768  1.00139.37
ATOM    395  N   LEU A 334     109.808 164.507 165.078  1.00139.78
ATOM    396  CA  LEU A 334     110.682 163.349 165.204  1.00139.78
ATOM    397  C   LEU A 334     110.746 162.946 166.662  1.00139.78
ATOM    398  O   LEU A 334     110.971 163.790 167.531  1.00139.78
ATOM    399  CB  LEU A 334     112.094 163.645 164.701  1.00139.78
ATOM    400  CG  LEU A 334     112.266 164.039 163.234  1.00139.78
ATOM    401  CD1 LEU A 334     113.709 164.416 162.944  1.00139.78
ATOM    402  CD2 LEU A 334     111.841 162.919 162.324  1.00139.78
ATOM    403  N   THR A 335     110.551 161.671 166.925  1.00140.71
ATOM    404  CA  THR A 335     110.675 161.176 168.278  1.00140.71
ATOM    405  C   THR A 335     112.148 161.037 168.637  1.00140.71
ATOM    406  O   THR A 335     113.007 161.064 167.754  1.00140.71
ATOM    407  CB  THR A 335     109.971 159.837 168.425  1.00140.71
ATOM    408  OG1 THR A 335     110.739 158.813 167.788  1.00140.71
ATOM    409  CG2 THR A 335     108.572 159.895 167.816  1.00140.71
ATOM    410  N   PRO A 336     112.472 160.926 169.931  1.00140.90
ATOM    411  CA  PRO A 336     113.885 160.804 170.321  1.00140.90
ATOM    412  C   PRO A 336     114.586 159.640 169.669  1.00140.90
ATOM    413  O   PRO A 336     115.774 159.735 169.330  1.00140.90
ATOM    414  CB  PRO A 336     113.806 160.626 171.840  1.00140.90
ATOM    415  CG  PRO A 336     112.518 161.239 172.225  1.00140.90
ATOM    416  CD  PRO A 336     111.591 160.942 171.112  1.00140.90
ATOM    417  N   LEU A 337     113.867 158.542 169.458  1.00135.19
ATOM    418  CA  LEU A 337     114.441 157.402 168.759  1.00135.19
ATOM    419  C   LEU A 337     114.843 157.780 167.345  1.00135.19
ATOM    420  O   LEU A 337     115.988 157.568 166.934  1.00135.19
ATOM    421  CB  LEU A 337     113.425 156.263 168.731  1.00135.19
ATOM    422  CG  LEU A 337     113.784 155.029 167.907  1.00135.19
ATOM    423  CD1 LEU A 337     115.013 154.381 168.477  1.00135.19
ATOM    424  CD2 LEU A 337     112.634 154.064 167.900  1.00135.19
ATOM    425  N   ALA A 338     113.910 158.349 166.589  1.00134.25
ATOM    426  CA  ALA A 338     114.216 158.733 165.224  1.00134.25
ATOM    427  C   ALA A 338     115.268 159.824 165.184  1.00134.25
ATOM    428  O   ALA A 338     115.945 159.979 164.173  1.00134.25
ATOM    429  CB  ALA A 338     112.948 159.184 164.507  1.00134.25
ATOM    430  N   LEU A 339     115.406 160.605 166.251  1.00137.82
ATOM    431  CA  LEU A 339     116.481 161.586 166.284  1.00137.82
ATOM    432  C   LEU A 339     117.829 160.908 166.427  1.00137.82
ATOM    433  O   LEU A 339     118.786 161.259 165.728  1.00137.82
ATOM    434  CB  LEU A 339     116.283 162.575 167.426  1.00137.82
ATOM    435  CG  LEU A 339     117.351 163.670 167.530  1.00137.82
ATOM    436  CD1 LEU A 339     117.451 164.475 166.243  1.00137.82
ATOM    437  CD2 LEU A 339     117.019 164.572 168.687  1.00137.82
ATOM    438  N   ALA A 340     117.935 159.958 167.357  1.00136.59
ATOM    439  CA  ALA A 340     119.196 159.246 167.517  1.00136.59
ATOM    440  C   ALA A 340     119.545 158.521 166.234  1.00136.59
ATOM    441  O   ALA A 340     120.714 158.455 165.838  1.00136.59
ATOM    442  CB  ALA A 340     119.113 158.267 168.685  1.00136.59
ATOM    443  N   ALA A 341     118.525 157.999 165.557  1.00132.34
ATOM    444  CA  ALA A 341     118.726 157.356 164.268  1.00132.34
ATOM    445  C   ALA A 341     119.152 158.360 163.209  1.00132.34
ATOM    446  O   ALA A 341     120.076 158.103 162.434  1.00132.34
ATOM    447  CB  ALA A 341     117.446 156.641 163.852  1.00132.34
ATOM    448  N   SER A 342     118.478 159.503 163.149  1.00129.27
ATOM    449  CA  SER A 342     118.714 160.439 162.061  1.00129.27
ATOM    450  C   SER A 342     120.124 161.009 162.115  1.00129.27
ATOM    451  O   SER A 342     120.780 161.162 161.079  1.00129.27
ATOM    452  CB  SER A 342     117.679 161.559 162.102  1.00129.27
ATOM    453  OG  SER A 342     117.972 162.529 161.120  1.00129.27
ATOM    454  N   SER A 343     120.608 161.323 163.313  1.00131.59
ATOM    455  CA  SER A 343     121.890 161.994 163.452  1.00131.59
ATOM    456  C   SER A 343     123.072 161.041 163.457  1.00131.59
ATOM    457  O   SER A 343     124.215 161.505 163.447  1.00131.59
ATOM    458  CB  SER A 343     121.898 162.823 164.729  1.00131.59
ATOM    459  OG  SER A 343     121.427 162.055 165.816  1.00131.59
ATOM    460  N   GLY A 344     122.835 159.736 163.446  1.00126.90
ATOM    461  CA  GLY A 344     123.928 158.785 163.460  1.00126.90
ATOM    462  C   GLY A 344     124.413 158.432 164.844  1.00126.90
ATOM    463  O   GLY A 344     125.549 157.971 165.003  1.00126.90
ATOM    464  N   LYS A 345     123.571 158.609 165.854  1.00134.22
ATOM    465  CA  LYS A 345     123.964 158.398 167.238  1.00134.22
ATOM    466  C   LYS A 345     123.737 156.924 167.515  1.00134.22
ATOM    467  O   LYS A 345     122.710 156.519 168.053  1.00134.22
ATOM    468  CB  LYS A 345     123.163 159.287 168.177  1.00134.22
ATOM    469  CG  LYS A 345     123.352 160.775 167.940  1.00134.22
ATOM    470  CD  LYS A 345     124.721 161.246 168.364  1.00134.22
ATOM    471  CE  LYS A 345     124.798 162.755 168.361  1.00134.22
ATOM    472  NZ  LYS A 345     124.348 163.344 167.072  1.00134.22
ATOM    473  N   ILE A 346     124.724 156.117 167.153  1.00127.26
ATOM    474  CA  ILE A 346     124.544 154.677 167.216  1.00127.26
ATOM    475  C   ILE A 346     124.459 154.189 168.652  1.00127.26
ATOM    476  O   ILE A 346     123.755 153.217 168.927  1.00127.26
ATOM    477  CB  ILE A 346     125.673 153.978 166.448  1.00127.26
ATOM    478  CG1 ILE A 346     125.296 152.526 166.186  1.00127.26
ATOM    479  CG2 ILE A 346     126.984 154.058 167.222  1.00127.26
ATOM    480  CD1 ILE A 346     126.241 151.811 165.278  1.00127.26
ATOM    481  N   GLY A 347     125.176 154.817 169.584  1.00135.12
ATOM    482  CA  GLY A 347     125.146 154.341 170.957  1.00135.12
ATOM    483  C   GLY A 347     123.779 154.490 171.592  1.00135.12
ATOM    484  O   GLY A 347     123.250 153.547 172.186  1.00135.12
ATOM    485  N   VAL A 348     123.174 155.665 171.444  1.00137.67
ATOM    486  CA  VAL A 348     121.873 155.898 172.055  1.00137.67
ATOM    487  C   VAL A 348     120.836 154.986 171.435  1.00137.67
ATOM    488  O   VAL A 348     119.991 154.413 172.130  1.00137.67
ATOM    489  CB  VAL A 348     121.470 157.369 171.898  1.00137.67
ATOM    490  CG1 VAL A 348     120.085 157.598 172.470  1.00137.67
ATOM    491  CG2 VAL A 348     122.509 158.290 172.535  1.00137.67
ATOM    492  N   LEU A 349     120.875 154.857 170.115  1.00133.46
ATOM    493  CA  LEU A 349     119.946 153.985 169.418  1.00133.46
ATOM    494  C   LEU A 349     120.113 152.552 169.881  1.00133.46
ATOM    495  O   LEU A 349     119.134 151.866 170.201  1.00133.46
ATOM    496  CB  LEU A 349     120.206 154.100 167.921  1.00133.46
ATOM    497  CG  LEU A 349     119.315 153.343 166.956  1.00133.46
ATOM    498  CD1 LEU A 349     117.883 153.702 167.166  1.00133.46
ATOM    499  CD2 LEU A 349     119.745 153.688 165.558  1.00133.46
ATOM    500  N   ALA A 350     121.364 152.097 169.943  1.00133.02
ATOM    501  CA  ALA A 350     121.655 150.737 170.359  1.00133.02
ATOM    502  C   ALA A 350     121.123 150.487 171.751  1.00133.02
ATOM    503  O   ALA A 350     120.631 149.396 172.049  1.00133.02
ATOM    504  CB  ALA A 350     123.161 150.492 170.299  1.00133.02
ATOM    505  N   TYR A 351     121.199 151.491 172.617  1.00138.25
ATOM    506  CA  TYR A 351     120.543 151.368 173.908  1.00138.25
ATOM    507  C   TYR A 351     119.036 151.250 173.752  1.00138.25
ATOM    508  O   TYR A 351     118.425 150.302 174.255  1.00138.25
ATOM    509  CB  TYR A 351     120.879 152.563 174.783  1.00138.25
ATOM    510  CG  TYR A 351     119.890 152.737 175.885  1.00138.25
ATOM    511  CD1 TYR A 351     119.819 151.834 176.918  1.00138.25
ATOM    512  CD2 TYR A 351     119.026 153.804 175.890  1.00138.25
ATOM    513  CE1 TYR A 351     118.918 151.996 177.924  1.00138.25
ATOM    514  CE2 TYR A 351     118.124 153.973 176.884  1.00138.25
ATOM    515  CZ  TYR A 351     118.071 153.074 177.901  1.00138.25
ATOM    516  OH  TYR A 351     117.156 153.269 178.900  1.00138.25
ATOM    517  N   ILE A 352     118.421 152.199 173.039  1.00137.89
ATOM    518  CA  ILE A 352     116.966 152.356 173.106  1.00137.89
ATOM    519  C   ILE A 352     116.269 151.150 172.507  1.00137.89
ATOM    520  O   ILE A 352     115.292 150.640 173.061  1.00137.89
ATOM    521  CB  ILE A 352     116.512 153.650 172.409  1.00137.89
ATOM    522  CG1 ILE A 352     116.982 154.874 173.187  1.00137.89
ATOM    523  CG2 ILE A 352     114.989 153.672 172.327  1.00137.89
ATOM    524  CD1 ILE A 352     116.897 156.159 172.413  1.00137.89
ATOM    525  N   LEU A 353     116.735 150.696 171.351  1.00132.73
ATOM    526  CA  LEU A 353     116.143 149.502 170.778  1.00132.73
ATOM    527  C   LEU A 353     116.347 148.290 171.674  1.00132.73
ATOM    528  O   LEU A 353     115.508 147.390 171.665  1.00132.73
ATOM    529  CB  LEU A 353     116.722 149.247 169.384  1.00132.73
ATOM    530  CG  LEU A 353     116.496 150.330 168.316  1.00132.73
ATOM    531  CD1 LEU A 353     117.438 150.130 167.165  1.00132.73
ATOM    532  CD2 LEU A 353     115.068 150.351 167.805  1.00132.73
ATOM    533  N   GLN A 354     117.410 148.272 172.478  1.00134.80
ATOM    534  CA  GLN A 354     117.780 147.126 173.303  1.00134.80
ATOM    535  C   GLN A 354     117.589 147.418 174.784  1.00134.80
ATOM    536  O   GLN A 354     118.515 147.271 175.579  1.00134.80
ATOM    537  CB  GLN A 354     119.224 146.707 173.042  1.00134.80
ATOM    538  CG  GLN A 354     119.503 146.231 171.630  1.00134.80
ATOM    539  CD  GLN A 354     120.869 145.589 171.505  1.00134.80
ATOM    540  OE1 GLN A 354     121.892 146.248 171.663  1.00134.80
ATOM    541  NE2 GLN A 354     120.890 144.293 171.234  1.00134.80
ATOM    542  N   ARG A 355     116.404 147.875 175.153  1.00140.05
ATOM    543  CA  ARG A 355     116.110 148.315 176.509  1.00140.05
ATOM    544  C   ARG A 355     114.987 147.463 177.087  1.00140.05
ATOM    545  O   ARG A 355     113.846 147.526 176.617  1.00140.05
ATOM    546  CB  ARG A 355     115.729 149.785 176.473  1.00140.05
ATOM    547  CG  ARG A 355     115.476 150.422 177.802  1.00140.05
ATOM    548  CD  ARG A 355     114.947 151.804 177.574  1.00140.05
ATOM    549  NE  ARG A 355     113.632 151.782 176.948  1.00140.05
ATOM    550  CZ  ARG A 355     113.056 152.832 176.378  1.00140.05
ATOM    551  NH1 ARG A 355     113.664 154.012 176.336  1.00140.05
ATOM    552  NH2 ARG A 355     111.857 152.703 175.840  1.00140.05
ATOM    553  N   GLU A 356     115.299 146.692 178.122  1.00144.00
ATOM    554  CA  GLU A 356     114.320 145.871 178.822  1.00144.00
ATOM    555  C   GLU A 356     114.076 146.481 180.189  1.00144.00
ATOM    556  O   GLU A 356     115.023 146.695 180.953  1.00144.00
ATOM    557  CB  GLU A 356     114.794 144.424 178.965  1.00144.00
ATOM    558  CG  GLU A 356     113.817 143.537 179.770  1.00144.00
ATOM    559  CD  GLU A 356     113.920 142.045 179.452  1.00144.00
ATOM    560  OE1 GLU A 356     114.623 141.665 178.490  1.00144.00
ATOM    561  OE2 GLU A 356     113.269 141.248 180.158  1.00144.00
ATOM    562  N   ILE A 357     112.813 146.755 180.490  1.00144.63
ATOM    563  CA  ILE A 357     112.396 147.280 181.783  1.00144.63
ATOM    564  C   ILE A 357     111.432 146.271 182.381  1.00144.63
ATOM    565  O   ILE A 357     110.404 145.950 181.774  1.00144.63
ATOM    566  CB  ILE A 357     111.763 148.672 181.662  1.00144.63
ATOM    567  CG1 ILE A 357     112.800 149.664 181.118  1.00144.63
ATOM    568  CG2 ILE A 357     111.286 149.148 183.016  1.00144.63
ATOM    569  CD1 ILE A 357     112.224 150.957 180.613  1.00144.63
ATOM    570  N   HIS A 358     111.770 145.776 183.572  1.00148.92
ATOM    571  CA  HIS A 358     111.177 144.588 184.178  1.00148.92
ATOM    572  C   HIS A 358     110.844 144.824 185.651  1.00148.92
ATOM    573  O   HIS A 358     110.671 143.871 186.418  1.00148.92
ATOM    574  CB  HIS A 358     112.142 143.413 184.039  1.00148.92
ATOM    575  CG  HIS A 358     113.513 143.727 184.556  1.00148.92
ATOM    576  ND1 HIS A 358     113.835 143.647 185.893  1.00148.92
ATOM    577  CD2 HIS A 358     114.622 144.185 183.929  1.00148.92
ATOM    578  CE1 HIS A 358     115.094 144.011 186.063  1.00148.92
ATOM    579  NE2 HIS A 358     115.594 144.343 184.886  1.00148.92
ATOM    580  N   GLU A 359     110.750 146.088 186.055  1.00150.97
ATOM    581  CA  GLU A 359     110.587 146.518 187.427  1.00150.97
ATOM    582  C   GLU A 359     109.119 146.760 187.723  1.00150.97
ATOM    583  O   GLU A 359     108.288 146.772 186.811  1.00150.97
ATOM    584  CB  GLU A 359     111.381 147.806 187.673  1.00150.97
ATOM    585  CG  GLU A 359     112.878 147.666 187.505  1.00150.97
ATOM    586  CD  GLU A 359     113.489 146.697 188.489  1.00150.97
ATOM    587  OE1 GLU A 359     112.849 146.413 189.521  1.00150.97
ATOM    588  OE2 GLU A 359     114.605 146.210 188.225  1.00150.97
ATOM    589  N   PRO A 360     108.746 146.910 188.993  1.00151.48
ATOM    590  CA  PRO A 360     107.363 147.294 189.294  1.00151.48
ATOM    591  C   PRO A 360     107.032 148.673 188.739  1.00151.48
ATOM    592  O   PRO A 360     107.826 149.609 188.840  1.00151.48
ATOM    593  CB  PRO A 360     107.312 147.279 190.828  1.00151.48
ATOM    594  CG  PRO A 360     108.489 146.466 191.255  1.00151.48
ATOM    595  CD  PRO A 360     109.529 146.685 190.223  1.00151.48
ATOM    596  N   GLU A 361     105.840 148.790 188.150  1.00152.37
ATOM    597  CA  GLU A 361     105.267 150.052 187.671  1.00152.37
ATOM    598  C   GLU A 361     106.090 150.717 186.567  1.00152.37
ATOM    599  O   GLU A 361     105.846 151.883 186.234  1.00152.37
ATOM    600  CB  GLU A 361     105.092 151.060 188.811  1.00152.37
ATOM    601  CG  GLU A 361     104.242 150.637 189.976  1.00152.37
ATOM    602  CD  GLU A 361     104.077 151.783 190.961  1.00152.37
ATOM    603  OE1 GLU A 361     103.263 152.688 190.680  1.00152.37
ATOM    604  OE2 GLU A 361     104.779 151.800 191.993  1.00152.37
ATOM    605  N   CYS A 362     107.059 150.011 185.984  1.00150.25
ATOM    606  CA  CYS A 362     107.875 150.520 184.887  1.00150.25
ATOM    607  C   CYS A 362     107.921 149.579 183.696  1.00150.25
ATOM    608  O   CYS A 362     108.383 150.001 182.628  1.00150.25
ATOM    609  CB  CYS A 362     109.309 150.797 185.362  1.00150.25
ATOM    610  SG  CYS A 362     109.392 151.982 186.717  1.00150.25
ATOM    611  N   ARG A 363     107.456 148.328 183.845  1.00146.72
ATOM    612  CA  ARG A 363     107.517 147.337 182.779  1.00146.72
ATOM    613  C   ARG A 363     106.939 147.869 181.484  1.00146.72
ATOM    614  O   ARG A 363     107.491 147.622 180.405  1.00146.72
ATOM    615  CB  ARG A 363     106.756 146.080 183.210  1.00146.72
ATOM    616  CG  ARG A 363     106.633 145.001 182.143  1.00146.72
ATOM    617  CD  ARG A 363     105.940 143.772 182.668  1.00146.72
ATOM    618  NE  ARG A 363     106.073 142.668 181.725  1.00146.72
ATOM    619  CZ  ARG A 363     107.132 141.861 181.637  1.00146.72
ATOM    620  NH1 ARG A 363     108.180 142.000 182.434  1.00146.72
ATOM    621  NH2 ARG A 363     107.148 140.895 180.734  1.00146.72
ATOM    622  N   HIS A 364     105.868 148.653 181.576  1.00145.61
ATOM    623  CA  HIS A 364     105.176 149.125 180.388  1.00145.61
ATOM    624  C   HIS A 364     106.049 149.989 179.503  1.00145.61
ATOM    625  O   HIS A 364     105.686 150.205 178.342  1.00145.61
ATOM    626  CB  HIS A 364     103.920 149.907 180.779  1.00145.61
ATOM    627  CG  HIS A 364     104.184 151.140 181.594  1.00145.61
ATOM    628  ND1 HIS A 364     104.762 151.103 182.845  1.00145.61
ATOM    629  CD2 HIS A 364     103.899 152.443 181.354  1.00145.61
ATOM    630  CE1 HIS A 364     104.844 152.330 183.328  1.00145.61
ATOM    631  NE2 HIS A 364     104.324 153.161 182.445  1.00145.61
ATOM    632  N   LEU A 365     107.189 150.461 180.000  1.00146.34
ATOM    633  CA  LEU A 365     108.101 151.291 179.232  1.00146.34
ATOM    634  C   LEU A 365     109.208 150.490 178.557  1.00146.34
ATOM    635  O   LEU A 365     110.142 151.084 178.012  1.00146.34
ATOM    636  CB  LEU A 365     108.705 152.363 180.139  1.00146.34
ATOM    637  CG  LEU A 365     107.700 153.289 180.835  1.00146.34
ATOM    638  CD1 LEU A 365     108.438 154.279 181.701  1.00146.34
ATOM    639  CD2 LEU A 365     106.809 154.014 179.829  1.00146.34
ATOM    640  N   SER A 366     109.133 149.163 178.587  1.00144.19
ATOM    641  CA  SER A 366     110.159 148.343 177.962  1.00144.19
ATOM    642  C   SER A 366     110.055 148.375 176.440  1.00144.19
ATOM    643  O   SER A 366     108.970 148.503 175.866  1.00144.19
ATOM    644  CB  SER A 366     110.043 146.901 178.442  1.00144.19
ATOM    645  OG  SER A 366     111.061 146.097 177.873  1.00144.19
ATOM    646  N   ARG A 367     111.209 148.238 175.789  1.00138.48
ATOM    647  CA  ARG A 367     111.291 148.073 174.344  1.00138.48
ATOM    648  C   ARG A 367     111.442 146.625 173.929  1.00138.48
ATOM    649  O   ARG A 367     110.973 146.255 172.848  1.00138.48
ATOM    650  CB  ARG A 367     112.472 148.874 173.788  1.00138.48
ATOM    651  CG  ARG A 367     112.803 148.645 172.323  1.00138.48
ATOM    652  CD  ARG A 367     111.653 148.932 171.384  1.00138.48
ATOM    653  NE  ARG A 367     111.260 150.336 171.384  1.00138.48
ATOM    654  CZ  ARG A 367     110.514 150.917 170.446  1.00138.48
ATOM    655  NH1 ARG A 367     110.218 152.202 170.560  1.00138.48
ATOM    656  NH2 ARG A 367     110.064 150.240 169.395  1.00138.48
ATOM    657  N   LYS A 368     112.113 145.809 174.737  1.00140.23
ATOM    658  CA  LYS A 368     112.193 144.383 174.470  1.00140.23
ATOM    659  C   LYS A 368     112.108 143.606 175.773  1.00140.23
ATOM    660  O   LYS A 368     112.366 144.132 176.856  1.00140.23
ATOM    661  CB  LYS A 368     113.471 144.020 173.715  1.00140.23
ATOM    662  CG  LYS A 368     114.743 144.163 174.511  1.00140.23
ATOM    663  CD  LYS A 368     115.256 142.826 175.013  1.00140.23
ATOM    664  CE  LYS A 368     116.667 142.978 175.533  1.00140.23
ATOM    665  NZ  LYS A 368     117.117 141.825 176.362  1.00140.23
ATOM    666  N   PHE A 369     111.732 142.340 175.636  1.00143.13
ATOM    667  CA  PHE A 369     111.639 141.388 176.733  1.00143.13
ATOM    668  C   PHE A 369     112.412 140.145 176.318  1.00143.13
ATOM    669  O   PHE A 369     112.730 139.964 175.145  1.00143.13
ATOM    670  CB  PHE A 369     110.176 141.032 177.063  1.00143.13
ATOM    671  CG  PHE A 369     109.253 142.229 177.183  1.00143.13
ATOM    672  CD1 PHE A 369     108.693 142.813 176.055  1.00143.13
ATOM    673  CD2 PHE A 369     108.927 142.754 178.424  1.00143.13
ATOM    674  CE1 PHE A 369     107.847 143.902 176.165  1.00143.13
ATOM    675  CE2 PHE A 369     108.078 143.841 178.534  1.00143.13
ATOM    676  CZ  PHE A 369     107.537 144.412 177.404  1.00143.13
ATOM    677  N   THR A 370     112.715 139.278 177.278  1.00144.43
ATOM    678  CA  THR A 370     113.370 138.000 177.001  1.00144.43
ATOM    679  C   THR A 370     112.393 136.892 177.356  1.00144.43
ATOM    680  O   THR A 370     111.871 136.850 178.475  1.00144.43
ATOM    681  CB  THR A 370     114.676 137.833 177.777  1.00144.43
ATOM    682  OG1 THR A 370     115.556 138.933 177.507  1.00144.43
ATOM    683  CG2 THR A 370     115.360 136.530 177.369  1.00144.43
ATOM    684  N   GLU A 371     112.136 136.010 176.396  1.00146.30
ATOM    685  CA  GLU A 371     111.246 134.880 176.629  1.00146.30
ATOM    686  C   GLU A 371     112.000 133.676 177.194  1.00146.30
ATOM    687  O   GLU A 371     111.678 133.186 178.283  1.00146.30
ATOM    688  CB  GLU A 371     110.555 134.519 175.317  1.00146.30
ATOM    689  CG  GLU A 371     109.515 133.427 175.403  1.00146.30
ATOM    690  CD  GLU A 371     108.991 133.084 174.043  1.00146.30
ATOM    691  OE1 GLU A 371     109.472 133.696 173.068  1.00146.30
ATOM    692  OE2 GLU A 371     108.107 132.211 173.943  1.00146.30
ATOM    693  N   TRP A 372     113.008 133.198 176.464  1.00148.78
ATOM    694  CA  TRP A 372     113.733 131.972 176.773  1.00148.78
ATOM    695  C   TRP A 372     115.151 132.350 177.160  1.00148.78
ATOM    696  O   TRP A 372     115.906 132.857 176.324  1.00148.78
ATOM    697  CB  TRP A 372     113.754 131.025 175.566  1.00148.78
ATOM    698  CG  TRP A 372     112.400 130.495 175.148  1.00148.78
ATOM    699  CD1 TRP A 372     111.592 130.973 174.155  1.00148.78
ATOM    700  CD2 TRP A 372     111.708 129.378 175.715  1.00148.78
ATOM    701  NE1 TRP A 372     110.447 130.232 174.075  1.00148.78
ATOM    702  CE2 TRP A 372     110.493 129.244 175.022  1.00148.78
ATOM    703  CE3 TRP A 372     111.997 128.482 176.746  1.00148.78
ATOM    704  CZ2 TRP A 372     109.569 128.246 175.325  1.00148.78
ATOM    705  CZ3 TRP A 372     111.075 127.492 177.047  1.00148.78
ATOM    706  CH2 TRP A 372     109.881 127.381 176.339  1.00148.78
ATOM    707  N   ALA A 373     115.509 132.101 178.417  1.00146.66
ATOM    708  CA  ALA A 373     116.834 132.452 178.936  1.00146.66
ATOM    709  C   ALA A 373     117.776 131.253 178.869  1.00146.66
ATOM    710  O   ALA A 373     118.395 130.854 179.853  1.00146.66
ATOM    711  CB  ALA A 373     116.716 132.984 180.363  1.00146.66
ATOM    712  N   TYR A 374     117.906 130.692 177.672  1.00144.54
ATOM    713  CA  TYR A 374     118.884 129.639 177.488  1.00144.54
ATOM    714  C   TYR A 374     120.283 130.241 177.557  1.00144.54
ATOM    715  O   TYR A 374     120.473 131.448 177.391  1.00144.54
ATOM    716  CB  TYR A 374     118.675 128.914 176.156  1.00144.54
ATOM    717  CG  TYR A 374     117.488 127.970 176.123  1.00144.54
ATOM    718  CD1 TYR A 374     117.407 126.882 176.987  1.00144.54
ATOM    719  CD2 TYR A 374     116.464 128.148 175.203  1.00144.54
ATOM    720  CE1 TYR A 374     116.331 126.016 176.948  1.00144.54
ATOM    721  CE2 TYR A 374     115.391 127.290 175.157  1.00144.54
ATOM    722  CZ  TYR A 374     115.329 126.227 176.031  1.00144.54
ATOM    723  OH  TYR A 374     114.256 125.376 175.982  1.00144.54
ATOM    724  N   GLY A 375     121.262 129.387 177.841  1.00142.67
ATOM    725  CA  GLY A 375     122.620 129.824 178.058  1.00142.67
ATOM    726  C   GLY A 375     123.194 130.603 176.897  1.00142.67
ATOM    727  O   GLY A 375     123.439 131.808 176.991  1.00142.67
ATOM    728  N   PRO A 376     123.403 129.928 175.765  1.00143.87
ATOM    729  CA  PRO A 376     124.075 130.584 174.635  1.00143.87
ATOM    730  C   PRO A 376     123.182 131.486 173.809  1.00143.87
ATOM    731  O   PRO A 376     123.697 132.414 173.172  1.00143.87
ATOM    732  CB  PRO A 376     124.559 129.401 173.792  1.00143.87
ATOM    733  CG  PRO A 376     123.495 128.360 174.023  1.00143.87
ATOM    734  CD  PRO A 376     123.073 128.523 175.466  1.00143.87
ATOM    735  N   VAL A 377     121.875 131.247 173.800  1.00143.41
ATOM    736  CA  VAL A 377     120.938 131.961 172.940  1.00143.41
ATOM    737  C   VAL A 377     119.787 132.443 173.798  1.00143.41
ATOM    738  O   VAL A 377     119.420 131.795 174.783  1.00143.41
ATOM    739  CB  VAL A 377     120.393 131.087 171.784  1.00143.41
ATOM    740  CG1 VAL A 377     121.491 130.735 170.798  1.00143.41
ATOM    741  CG2 VAL A 377     119.702 129.817 172.319  1.00143.41
ATOM    742  N   HIS A 378     119.216 133.581 173.416  1.00144.00
ATOM    743  CA  HIS A 378     118.034 134.145 174.047  1.00144.00
ATOM    744  C   HIS A 378     116.924 134.241 173.011  1.00144.00
ATOM    745  O   HIS A 378     117.192 134.461 171.829  1.00144.00
ATOM    746  CB  HIS A 378     118.335 135.532 174.631  1.00144.00
ATOM    747  CG  HIS A 378     119.291 135.511 175.786  1.00144.00
ATOM    748  ND1 HIS A 378     119.853 136.656 176.309  1.00144.00
ATOM    749  CD2 HIS A 378     119.776 134.485 176.525  1.00144.00
ATOM    750  CE1 HIS A 378     120.649 136.336 177.313  1.00144.00
ATOM    751  NE2 HIS A 378     120.619 135.025 177.466  1.00144.00
ATOM    752  N   SER A 379     115.679 134.048 173.444  1.00143.70
ATOM    753  CA  SER A 379     114.522 134.405 172.620  1.00143.70
ATOM    754  C   SER A 379     114.026 135.780 173.056  1.00143.70
ATOM    755  O   SER A 379     113.173 135.924 173.933  1.00143.70
ATOM    756  CB  SER A 379     113.427 133.361 172.734  1.00143.70
ATOM    757  OG  SER A 379     113.883 132.082 172.334  1.00143.70
ATOM    758  N   SER A 380     114.614 136.809 172.453  1.00137.27
ATOM    759  CA  SER A 380     114.200 138.177 172.702  1.00137.27
ATOM    760  C   SER A 380     112.963 138.522 171.880  1.00137.27
ATOM    761  O   SER A 380     112.750 137.997 170.789  1.00137.27
ATOM    762  CB  SER A 380     115.343 139.120 172.365  1.00137.27
ATOM    763  OG  SER A 380     116.535 138.671 172.981  1.00137.27
ATOM    764  N   LEU A 381     112.134 139.404 172.430  1.00137.63
ATOM    765  CA  LEU A 381     110.924 139.889 171.783  1.00137.63
ATOM    766  C   LEU A 381     110.957 141.408 171.766  1.00137.63
ATOM    767  O   LEU A 381     111.007 142.032 172.829  1.00137.63
ATOM    768  CB  LEU A 381     109.679 139.411 172.528  1.00137.63
ATOM    769  CG  LEU A 381     109.550 137.905 172.742  1.00137.63
ATOM    770  CD1 LEU A 381     108.358 137.589 173.614  1.00137.63
ATOM    771  CD2 LEU A 381     109.434 137.182 171.429  1.00137.63
ATOM    772  N   TYR A 382     110.879 141.994 170.570  1.00133.72
ATOM    773  CA  TYR A 382     111.049 143.423 170.349  1.00133.72
ATOM    774  C   TYR A 382     109.754 144.063 169.881  1.00133.72
ATOM    775  O   TYR A 382     108.959 143.443 169.169  1.00133.72
ATOM    776  CB  TYR A 382     112.116 143.701 169.307  1.00133.72
ATOM    777  CG  TYR A 382     113.505 143.441 169.787  1.00133.72
ATOM    778  CD1 TYR A 382     114.027 142.170 169.775  1.00133.72
ATOM    779  CD2 TYR A 382     114.296 144.473 170.257  1.00133.72
ATOM    780  CE1 TYR A 382     115.304 141.930 170.221  1.00133.72
ATOM    781  CE2 TYR A 382     115.573 144.247 170.703  1.00133.72
ATOM    782  CZ  TYR A 382     116.076 142.977 170.683  1.00133.72
ATOM    783  OH  TYR A 382     117.358 142.755 171.126  1.00133.72
ATOM    784  N   ASP A 383     109.565 145.311 170.283  1.00135.27
ATOM    785  CA  ASP A 383     108.471 146.140 169.805  1.00135.27
ATOM    786  C   ASP A 383     108.912 146.842 168.527  1.00135.27
ATOM    787  O   ASP A 383     110.051 147.303 168.431  1.00135.27
ATOM    788  CB  ASP A 383     108.082 147.151 170.883  1.00135.27
ATOM    789  CG  ASP A 383     106.818 147.890 170.562  1.00135.27
ATOM    790  OD1 ASP A 383     106.757 148.521 169.498  1.00135.27
ATOM    791  OD2 ASP A 383     105.875 147.839 171.378  1.00135.27
ATOM    792  N   LEU A 384     108.022 146.892 167.541  1.00130.96
ATOM    793  CA  LEU A 384     108.275 147.576 166.282  1.00130.96
ATOM    794  C   LEU A 384     107.537 148.896 166.173  1.00130.96
ATOM    795  O   LEU A 384     107.264 149.345 165.056  1.00130.96
ATOM    796  CB  LEU A 384     107.894 146.675 165.110  1.00130.96
ATOM    797  CG  LEU A 384     108.450 145.247 165.133  1.00130.96
ATOM    798  CD1 LEU A 384     108.054 144.496 163.866  1.00130.96
ATOM    799  CD2 LEU A 384     109.952 145.228 165.318  1.00130.96
ATOM    800  N   SER A 385     107.187 149.516 167.298  1.00134.91
ATOM    801  CA  SER A 385     106.502 150.802 167.268  1.00134.91
ATOM    802  C   SER A 385     107.369 151.833 166.576  1.00134.91
ATOM    803  O   SER A 385     108.467 152.150 167.040  1.00134.91
ATOM    804  CB  SER A 385     106.170 151.269 168.685  1.00134.91
ATOM    805  OG  SER A 385     105.255 150.387 169.313  1.00134.91
ATOM    806  N   CYS A 386     106.873 152.350 165.462  1.00133.84
ATOM    807  CA  CYS A 386     107.569 153.375 164.704  1.00133.84
ATOM    808  C   CYS A 386     108.939 152.901 164.224  1.00133.84
ATOM    809  O   CYS A 386     109.847 153.708 164.018  1.00133.84
ATOM    810  CB  CYS A 386     107.709 154.657 165.529  1.00133.84
ATOM    811  SG  CYS A 386     106.156 155.296 166.178  1.00133.84
ATOM    812  N   ILE A 387     109.100 151.599 164.032  1.00129.86
ATOM    813  CA  ILE A 387     110.333 151.029 163.510  1.00129.86
ATOM    814  C   ILE A 387     110.210 150.731 162.031  1.00129.86
ATOM    815  O   ILE A 387     111.105 151.047 161.252  1.00129.86
ATOM    816  CB  ILE A 387     110.710 149.758 164.297  1.00129.86
ATOM    817  CG1 ILE A 387     110.809 150.052 165.795  1.00129.86
ATOM    818  CG2 ILE A 387     111.991 149.197 163.763  1.00129.86
ATOM    819  CD1 ILE A 387     111.828 151.093 166.194  1.00129.86
ATOM    820  N   ASP A 388     109.112 150.095 161.634  1.00130.21
ATOM    821  CA  ASP A 388     108.742 149.909 160.238  1.00130.21
ATOM    822  C   ASP A 388     107.448 150.627 159.900  1.00130.21
ATOM    823  O   ASP A 388     107.303 151.139 158.789  1.00130.21
ATOM    824  CB  ASP A 388     108.602 148.415 159.912  1.00130.21
ATOM    825  CG  ASP A 388     107.443 147.765 160.638  1.00130.21
ATOM    826  OD1 ASP A 388     107.023 148.313 161.677  1.00130.21
ATOM    827  OD2 ASP A 388     106.946 146.721 160.169  1.00130.21
ATOM    828  N   THR A 389     106.483 150.627 160.818  1.00132.44
ATOM    829  CA  THR A 389     105.231 151.353 160.656  1.00132.44
ATOM    830  C   THR A 389     105.222 152.528 161.621  1.00132.44
ATOM    831  O   THR A 389     105.176 152.334 162.842  1.00132.44
ATOM    832  CB  THR A 389     104.035 150.432 160.895  1.00132.44
ATOM    833  OG1 THR A 389     104.103 149.331 159.980  1.00132.44
ATOM    834  CG2 THR A 389     102.720 151.174 160.675  1.00132.44
ATOM    835  N   CYS A 390     105.297 153.738 161.065  1.00135.45
ATOM    836  CA  CYS A 390     105.183 154.977 161.823  1.00135.45
ATOM    837  C   CYS A 390     104.152 155.908 161.209  1.00135.45
ATOM    838  O   CYS A 390     103.465 156.634 161.934  1.00135.45
ATOM    839  CB  CYS A 390     106.523 155.703 161.885  1.00135.45
ATOM    840  SG  CYS A 390     106.440 157.240 162.790  1.00135.45
ATOM    841  N   GLU A 391     104.085 155.927 159.871  1.00138.99
ATOM    842  CA  GLU A 391     103.266 156.787 159.009  1.00138.99
ATOM    843  C   GLU A 391     103.707 158.252 159.005  1.00138.99
ATOM    844  O   GLU A 391     103.183 159.030 158.195  1.00138.99
ATOM    845  CB  GLU A 391     101.767 156.735 159.351  1.00138.99
ATOM    846  CG  GLU A 391     101.094 155.417 159.005  1.00138.99
ATOM    847  CD  GLU A 391      99.609 155.432 159.291  1.00138.99
ATOM    848  OE1 GLU A 391      99.190 156.108 160.252  1.00138.99
ATOM    849  OE2 GLU A 391      98.854 154.770 158.552  1.00138.99
ATOM    850  N   LYS A 392     104.651 158.655 159.861  1.00137.50
ATOM    851  CA  LYS A 392     105.332 159.941 159.781  1.00137.50
ATOM    852  C   LYS A 392     106.760 159.755 159.307  1.00137.50
ATOM    853  O   LYS A 392     107.128 160.230 158.229  1.00137.50
ATOM    854  CB  LYS A 392     105.340 160.641 161.157  1.00137.50
ATOM    855  CG  LYS A 392     103.974 160.956 161.737  1.00137.50
ATOM    856  CD  LYS A 392     104.062 161.449 163.189  1.00137.50
ATOM    857  CE  LYS A 392     102.665 161.653 163.782  1.00137.50
ATOM    858  NZ  LYS A 392     102.673 162.035 165.221  1.00137.50
ATOM    859  N   ASN A 393     107.560 159.034 160.081  1.00135.64
ATOM    860  CA  ASN A 393     108.915 158.678 159.700  1.00135.64
ATOM    861  C   ASN A 393     109.397 157.583 160.648  1.00135.64
ATOM    862  O   ASN A 393     109.374 157.768 161.869  1.00135.64
ATOM    863  CB  ASN A 393     109.805 159.909 159.761  1.00135.64
ATOM    864  CG  ASN A 393     109.759 160.565 161.108  1.00135.64
ATOM    865  OD1 ASN A 393     110.551 160.244 161.993  1.00135.64
ATOM    866  ND2 ASN A 393     108.789 161.449 161.300  1.00135.64
ATOM    867  N   SER A 394     109.828 156.449 160.116  1.00129.76
ATOM    868  CA  SER A 394     110.249 155.321 160.928  1.00129.76
ATOM    869  C   SER A 394     111.771 155.250 161.022  1.00129.76
ATOM    870  O   SER A 394     112.500 155.961 160.332  1.00129.76
ATOM    871  CB  SER A 394     109.690 154.034 160.348  1.00129.76
ATOM    872  OG  SER A 394     110.434 153.629 159.215  1.00129.76
ATOM    873  N   VAL A 395     112.250 154.366 161.896  1.00126.46
ATOM    874  CA  VAL A 395     113.687 154.259 162.119  1.00126.46
ATOM    875  C   VAL A 395     114.386 153.831 160.846  1.00126.46
ATOM    876  O   VAL A 395     115.438 154.367 160.485  1.00126.46
ATOM    877  CB  VAL A 395     113.993 153.285 163.264  1.00126.46
ATOM    878  CG1 VAL A 395     115.488 153.114 163.391  1.00126.46
ATOM    879  CG2 VAL A 395     113.402 153.796 164.562  1.00126.46
ATOM    880  N   LEU A 396     113.823 152.851 160.153  1.00120.99
ATOM    881  CA  LEU A 396     114.404 152.440 158.886  1.00120.99
ATOM    882  C   LEU A 396     114.336 153.573 157.872  1.00120.99
ATOM    883  O   LEU A 396     115.245 153.745 157.058  1.00120.99
ATOM    884  CB  LEU A 396     113.690 151.197 158.369  1.00120.99
ATOM    885  CG  LEU A 396     113.654 149.966 159.280  1.00120.99
ATOM    886  CD1 LEU A 396     112.591 149.005 158.821  1.00120.99
ATOM    887  CD2 LEU A 396     114.991 149.279 159.319  1.00120.99
ATOM    888  N   GLU A 397     113.271 154.366 157.916  1.00122.36
ATOM    889  CA  GLU A 397     113.135 155.460 156.966  1.00122.36
ATOM    890  C   GLU A 397     114.183 156.535 157.210  1.00122.36
ATOM    891  O   GLU A 397     114.847 156.989 156.277  1.00122.36
ATOM    892  CB  GLU A 397     111.726 156.026 157.061  1.00122.36
ATOM    893  CG  GLU A 397     110.682 155.084 156.455  1.00122.36
ATOM    894  CD  GLU A 397     109.278 155.261 157.005  1.00122.36
ATOM    895  OE1 GLU A 397     109.072 156.130 157.869  1.00122.36
ATOM    896  OE2 GLU A 397     108.371 154.524 156.569  1.00122.36
ATOM    897  N   VAL A 398     114.361 156.941 158.464  1.00125.67
ATOM    898  CA  VAL A 398     115.310 158.009 158.770  1.00125.67
ATOM    899  C   VAL A 398     116.754 157.542 158.645  1.00125.67
ATOM    900  O   VAL A 398     117.642 158.348 158.358  1.00125.67
ATOM    901  CB  VAL A 398     115.046 158.590 160.167  1.00125.67
ATOM    902  CG1 VAL A 398     113.651 159.143 160.242  1.00125.67
ATOM    903  CG2 VAL A 398     115.284 157.565 161.252  1.00125.67
ATOM    904  N   ILE A 399     117.035 156.267 158.905  1.00121.61
ATOM    905  CA  ILE A 399     118.385 155.767 158.667  1.00121.61
ATOM    906  C   ILE A 399     118.635 155.634 157.179  1.00121.61
ATOM    907  O   ILE A 399     119.665 156.071 156.660  1.00121.61
ATOM    908  CB  ILE A 399     118.608 154.423 159.377  1.00121.61
ATOM    909  CG1 ILE A 399     118.557 154.626 160.881  1.00121.61
ATOM    910  CG2 ILE A 399     119.938 153.819 158.938  1.00121.61
ATOM    911  CD1 ILE A 399     118.520 153.357 161.702  1.00121.61
ATOM    912  N   ALA A 400     117.711 155.008 156.474  1.00112.61
ATOM    913  CA  ALA A 400     117.951 154.726 155.074  1.00112.61
ATOM    914  C   ALA A 400     117.972 156.003 154.258  1.00112.61
ATOM    915  O   ALA A 400     118.835 156.177 153.393  1.00112.61
ATOM    916  CB  ALA A 400     116.886 153.771 154.559  1.00112.61
ATOM    917  N   TYR A 401     117.052 156.916 154.539  1.00107.39
ATOM    918  CA  TYR A 401     116.928 158.175 153.819  1.00107.39
ATOM    919  C   TYR A 401     117.495 159.327 154.636  1.00107.39
ATOM    920  O   TYR A 401     116.947 160.428 154.657  1.00107.39
ATOM    921  CB  TYR A 401     115.478 158.437 153.457  1.00107.39
ATOM    922  CG  TYR A 401     114.909 157.407 152.535  1.00107.39
ATOM    923  CD1 TYR A 401     115.333 157.319 151.220  1.00107.39
ATOM    924  CD2 TYR A 401     113.936 156.524 152.971  1.00107.39
ATOM    925  CE1 TYR A 401     114.807 156.384 150.367  1.00107.39
ATOM    926  CE2 TYR A 401     113.402 155.577 152.124  1.00107.39
ATOM    927  CZ  TYR A 401     113.844 155.511 150.825  1.00107.39
ATOM    928  OH  TYR A 401     113.302 154.576 149.983  1.00107.39
ATOM    929  N   SER A 402     118.598 159.080 155.328  1.00115.62
ATOM    930  CA  SER A 402     119.271 160.149 156.033  1.00115.62
ATOM    931  C   SER A 402     119.921 161.093 155.026  1.00115.62
ATOM    932  O   SER A 402     119.896 160.872 153.812  1.00115.62
ATOM    933  CB  SER A 402     120.315 159.581 156.984  1.00115.62
ATOM    934  OG  SER A 402     121.444 159.116 156.266  1.00115.62
ATOM    935  N   SER A 403     120.532 162.154 155.544  1.00115.43
ATOM    936  CA  SER A 403     121.134 163.176 154.699  1.00115.43
ATOM    937  C   SER A 403     122.475 162.763 154.112  1.00115.43
ATOM    938  O   SER A 403     123.075 163.568 153.393  1.00115.43
ATOM    939  CB  SER A 403     121.310 164.462 155.503  1.00115.43
ATOM    940  OG  SER A 403     122.277 164.277 156.522  1.00115.43
ATOM    941  N   SER A 404     122.977 161.569 154.414  1.00110.26
ATOM    942  CA  SER A 404     124.239 161.021 153.947  1.00110.26
ATOM    943  C   SER A 404     125.435 161.645 154.659  1.00110.26
ATOM    944  O   SER A 404     126.559 161.214 154.411  1.00110.26
ATOM    945  CB  SER A 404     124.443 161.180 152.430  1.00110.26
ATOM    946  OG  SER A 404     124.941 162.469 152.145  1.00110.26
ATOM    947  N   GLU A 405     125.248 162.649 155.519  1.00119.29
ATOM    948  CA  GLU A 405     126.292 163.082 156.439  1.00119.29
ATOM    949  C   GLU A 405     126.343 162.238 157.701  1.00119.29
ATOM    950  O   GLU A 405     127.389 162.197 158.359  1.00119.29
ATOM    951  CB  GLU A 405     126.073 164.545 156.839  1.00119.29
ATOM    952  CG  GLU A 405     126.344 165.530 155.726  1.00119.29
ATOM    953  CD  GLU A 405     126.334 166.964 156.199  1.00119.29
ATOM    954  OE1 GLU A 405     125.941 167.203 157.358  1.00119.29
ATOM    955  OE2 GLU A 405     126.720 167.855 155.415  1.00119.29
ATOM    956  N   THR A 406     125.231 161.568 158.029  1.00118.87
ATOM    957  CA  THR A 406     125.016 160.742 159.202  1.00118.87
ATOM    958  C   THR A 406     126.227 159.839 159.392  1.00118.87
ATOM    959  O   THR A 406     126.453 158.953 158.560  1.00118.87
ATOM    960  CB  THR A 406     123.737 159.935 159.009  1.00118.87
ATOM    961  OG1 THR A 406     122.656 160.833 158.744  1.00118.87
ATOM    962  CG2 THR A 406     123.405 159.159 160.239  1.00118.87
ATOM    963  N   PRO A 407     127.047 160.040 160.432  1.00121.69
ATOM    964  CA  PRO A 407     128.367 159.392 160.437  1.00121.69
ATOM    965  C   PRO A 407     128.327 157.881 160.463  1.00121.69
ATOM    966  O   PRO A 407     129.300 157.263 160.016  1.00121.69
ATOM    967  CB  PRO A 407     129.033 159.933 161.711  1.00121.69
ATOM    968  CG  PRO A 407     128.288 161.130 162.073  1.00121.69
ATOM    969  CD  PRO A 407     126.893 160.931 161.598  1.00121.69
ATOM    970  N   ASN A 408     127.244 157.267 160.945  1.00121.47
ATOM    971  CA  ASN A 408     127.258 155.847 161.274  1.00121.47
ATOM    972  C   ASN A 408     126.166 155.057 160.574  1.00121.47
ATOM    973  O   ASN A 408     125.891 153.927 160.980  1.00121.47
ATOM    974  CB  ASN A 408     127.131 155.663 162.782  1.00121.47
ATOM    975  CG  ASN A 408     128.259 156.304 163.530  1.00121.47
ATOM    976  OD1 ASN A 408     129.353 155.750 163.617  1.00121.47
ATOM    977  ND2 ASN A 408     128.001 157.480 164.086  1.00121.47
ATOM    978  N   ARG A 409     125.577 155.597 159.504  1.00113.29
ATOM    979  CA  ARG A 409     124.495 154.901 158.805  1.00113.29
ATOM    980  C   ARG A 409     124.918 153.516 158.330  1.00113.29
ATOM    981  O   ARG A 409     124.080 152.621 158.191  1.00113.29
ATOM    982  CB  ARG A 409     124.016 155.750 157.621  1.00113.29
ATOM    983  CG  ARG A 409     125.110 156.131 156.623  1.00113.29
ATOM    984  CD  ARG A 409     124.620 157.102 155.549  1.00113.29
ATOM    985  NE  ARG A 409     125.692 157.429 154.604  1.00113.29
ATOM    986  CZ  ARG A 409     126.687 158.292 154.841  1.00113.29
ATOM    987  NH1 ARG A 409     126.769 158.945 155.994  1.00113.29
ATOM    988  NH2 ARG A 409     127.611 158.512 153.917  1.00113.29
ATOM    989  N   HIS A 410     126.214 153.319 158.103  1.00109.70
ATOM    990  CA  HIS A 410     126.724 152.028 157.660  1.00109.70
ATOM    991  C   HIS A 410     126.621 150.968 158.746  1.00109.70
ATOM    992  O   HIS A 410     126.074 149.885 158.516  1.00109.70
ATOM    993  CB  HIS A 410     128.170 152.212 157.236  1.00109.70
ATOM    994  CG  HIS A 410     128.321 153.091 156.045  1.00109.70
ATOM    995  ND1 HIS A 410     128.421 154.460 156.147  1.00109.70
ATOM    996  CD2 HIS A 410     128.342 152.806 154.723  1.00109.70
ATOM    997  CE1 HIS A 410     128.524 154.980 154.939  1.00109.70
ATOM    998  NE2 HIS A 410     128.480 153.997 154.057  1.00109.70
ATOM    999  N   ASP A 411     127.155 151.256 159.927  1.00116.04
ATOM   1000  CA  ASP A 411     127.110 150.318 161.036  1.00116.04
ATOM   1001  C   ASP A 411     125.808 150.393 161.813  1.00116.04
ATOM   1002  O   ASP A 411     125.568 149.536 162.668  1.00116.04
ATOM   1003  CB  ASP A 411     128.269 150.575 162.007  1.00116.04
ATOM   1004  CG  ASP A 411     129.624 150.190 161.435  1.00116.04
ATOM   1005  OD1 ASP A 411     129.868 148.987 161.203  1.00116.04
ATOM   1006  OD2 ASP A 411     130.450 151.102 161.226  1.00116.04
ATOM   1007  N   MET A 412     124.978 151.406 161.559  1.00122.37
ATOM   1008  CA  MET A 412     123.791 151.595 162.381  1.00122.37
ATOM   1009  C   MET A 412     122.814 150.445 162.222  1.00122.37
ATOM   1010  O   MET A 412     122.103 150.100 163.172  1.00122.37
ATOM   1011  CB  MET A 412     123.103 152.911 162.030  1.00122.37
ATOM   1012  CG  MET A 412     122.037 153.285 163.007  1.00122.37
ATOM   1013  SD  MET A 412     121.572 155.010 162.891  1.00122.37
ATOM   1014  CE  MET A 412     122.674 155.729 164.081  1.00122.37
ATOM   1015  N   LEU A 413     122.766 149.835 161.042  1.00114.58
ATOM   1016  CA  LEU A 413     121.866 148.708 160.857  1.00114.58
ATOM   1017  C   LEU A 413     122.349 147.455 161.569  1.00114.58
ATOM   1018  O   LEU A 413     121.543 146.551 161.794  1.00114.58
ATOM   1019  CB  LEU A 413     121.683 148.426 159.370  1.00114.58
ATOM   1020  CG  LEU A 413     121.120 149.597 158.570  1.00114.58
ATOM   1021  CD1 LEU A 413     121.243 149.284 157.116  1.00114.58
ATOM   1022  CD2 LEU A 413     119.690 149.897 158.940  1.00114.58
ATOM   1023  N   LEU A 414     123.609 147.404 161.991  1.00115.27
ATOM   1024  CA  LEU A 414     124.104 146.244 162.714  1.00115.27
ATOM   1025  C   LEU A 414     123.500 146.113 164.100  1.00115.27
ATOM   1026  O   LEU A 414     123.730 145.098 164.761  1.00115.27
ATOM   1027  CB  LEU A 414     125.624 146.309 162.856  1.00115.27
ATOM   1028  CG  LEU A 414     126.478 146.284 161.589  1.00115.27
ATOM   1029  CD1 LEU A 414     127.920 146.619 161.930  1.00115.27
ATOM   1030  CD2 LEU A 414     126.414 144.939 160.919  1.00115.27
ATOM   1031  N   VAL A 415     122.775 147.121 164.574  1.00124.99
ATOM   1032  CA  VAL A 415     122.036 146.993 165.823  1.00124.99
ATOM   1033  C   VAL A 415     120.976 145.915 165.641  1.00124.99
ATOM   1034  O   VAL A 415     120.145 145.995 164.730  1.00124.99
ATOM   1035  CB  VAL A 415     121.414 148.333 166.223  1.00124.99
ATOM   1036  CG1 VAL A 415     120.579 148.164 167.468  1.00124.99
ATOM   1037  CG2 VAL A 415     122.491 149.391 166.406  1.00124.99
ATOM   1038  N   GLU A 416     121.001 144.913 166.520  1.00130.71
ATOM   1039  CA  GLU A 416     120.375 143.608 166.332  1.00130.71
ATOM   1040  C   GLU A 416     118.963 143.663 165.761  1.00130.71
ATOM   1041  O   GLU A 416     118.712 143.011 164.741  1.00130.71
ATOM   1042  CB  GLU A 416     120.378 142.834 167.657  1.00130.71
ATOM   1043  CG  GLU A 416     119.721 141.440 167.622  1.00130.71
ATOM   1044  CD  GLU A 416     119.600 140.820 168.992  1.00130.71
ATOM   1045  OE1 GLU A 416     120.639 140.488 169.593  1.00130.71
ATOM   1046  OE2 GLU A 416     118.459 140.664 169.469  1.00130.71
ATOM   1047  N   PRO A 417     118.009 144.367 166.378  1.00128.89
ATOM   1048  CA  PRO A 417     116.632 144.301 165.860  1.00128.89
ATOM   1049  C   PRO A 417     116.486 144.811 164.444  1.00128.89
ATOM   1050  O   PRO A 417     115.724 144.219 163.675  1.00128.89
ATOM   1051  CB  PRO A 417     115.838 145.156 166.848  1.00128.89
ATOM   1052  CG  PRO A 417     116.835 146.021 167.479  1.00128.89
ATOM   1053  CD  PRO A 417     118.088 145.229 167.563  1.00128.89
ATOM   1054  N   LEU A 418     117.231 145.846 164.047  1.00124.17
ATOM   1055  CA  LEU A 418     117.124 146.335 162.674  1.00124.17
ATOM   1056  C   LEU A 418     117.675 145.330 161.686  1.00124.17
ATOM   1057  O   LEU A 418     117.041 145.041 160.666  1.00124.17
ATOM   1058  CB  LEU A 418     117.885 147.634 162.519  1.00124.17
ATOM   1059  CG  LEU A 418     117.369 148.778 163.360  1.00124.17
ATOM   1060  CD1 LEU A 418     118.363 149.904 163.264  1.00124.17
ATOM   1061  CD2 LEU A 418     116.015 149.202 162.875  1.00124.17
ATOM   1062  N   ASN A 419     118.871 144.821 161.958  1.00121.95
ATOM   1063  CA  ASN A 419     119.457 143.818 161.093  1.00121.95
ATOM   1064  C   ASN A 419     118.531 142.630 160.960  1.00121.95
ATOM   1065  O   ASN A 419     118.323 142.107 159.861  1.00121.95
ATOM   1066  CB  ASN A 419     120.799 143.389 161.667  1.00121.95
ATOM   1067  CG  ASN A 419     121.439 142.317 160.862  1.00121.95
ATOM   1068  OD1 ASN A 419     121.706 142.495 159.675  1.00121.95
ATOM   1069  ND2 ASN A 419     121.705 141.184 161.494  1.00121.95
ATOM   1070  N   ARG A 420     117.911 142.236 162.063  1.00125.94
ATOM   1071  CA  ARG A 420     117.004 141.105 162.016  1.00125.94
ATOM   1072  C   ARG A 420     115.751 141.428 161.215  1.00125.94
ATOM   1073  O   ARG A 420     115.279 140.591 160.441  1.00125.94
ATOM   1074  CB  ARG A 420     116.660 140.669 163.437  1.00125.94
ATOM   1075  CG  ARG A 420     117.741 139.807 164.076  1.00125.94
ATOM   1076  CD  ARG A 420     117.639 138.373 163.592  1.00125.94
ATOM   1077  NE  ARG A 420     118.552 137.471 164.287  1.00125.94
ATOM   1078  CZ  ARG A 420     118.834 136.230 163.886  1.00125.94
ATOM   1079  NH1 ARG A 420     118.293 135.736 162.779  1.00125.94
ATOM   1080  NH2 ARG A 420     119.674 135.483 164.592  1.00125.94
ATOM   1081  N   LEU A 421     115.203 142.631 161.372  1.00122.34
ATOM   1082  CA  LEU A 421     114.020 142.992 160.606  1.00122.34
ATOM   1083  C   LEU A 421     114.312 142.996 159.125  1.00122.34
ATOM   1084  O   LEU A 421     113.524 142.483 158.327  1.00122.34
ATOM   1085  CB  LEU A 421     113.527 144.370 161.000  1.00122.34
ATOM   1086  CG  LEU A 421     112.888 144.501 162.361  1.00122.34
ATOM   1087  CD1 LEU A 421     112.897 145.953 162.781  1.00122.34
ATOM   1088  CD2 LEU A 421     111.495 143.978 162.310  1.00122.34
ATOM   1089  N   LEU A 422     115.427 143.595 158.737  1.00113.82
ATOM   1090  CA  LEU A 422     115.730 143.682 157.323  1.00113.82
ATOM   1091  C   LEU A 422     115.993 142.309 156.756  1.00113.82
ATOM   1092  O   LEU A 422     115.542 141.998 155.656  1.00113.82
ATOM   1093  CB  LEU A 422     116.924 144.589 157.088  1.00113.82
ATOM   1094  CG  LEU A 422     116.712 146.045 157.476  1.00113.82
ATOM   1095  CD1 LEU A 422     118.013 146.789 157.326  1.00113.82
ATOM   1096  CD2 LEU A 422     115.638 146.674 156.637  1.00113.82
ATOM   1097  N   GLN A 423     116.689 141.456 157.504  1.00112.15
ATOM   1098  CA  GLN A 423     116.930 140.113 157.004  1.00112.15
ATOM   1099  C   GLN A 423     115.624 139.353 156.854  1.00112.15
ATOM   1100  O   GLN A 423     115.381 138.714 155.819  1.00112.15
ATOM   1101  CB  GLN A 423     117.883 139.376 157.941  1.00112.15
ATOM   1102  CG  GLN A 423     118.302 138.007 157.451  1.00112.15
ATOM   1103  CD  GLN A 423     118.988 138.048 156.103  1.00112.15
ATOM   1104  OE1 GLN A 423     119.644 139.031 155.758  1.00112.15
ATOM   1105  NE2 GLN A 423     118.829 136.983 155.324  1.00112.15
ATOM   1106  N   ASP A 424     114.752 139.456 157.854  1.00115.70
ATOM   1107  CA  ASP A 424     113.483 138.751 157.804  1.00115.70
ATOM   1108  C   ASP A 424     112.628 139.232 156.649  1.00115.70
ATOM   1109  O   ASP A 424     112.062 138.425 155.913  1.00115.70
ATOM   1110  CB  ASP A 424     112.721 138.936 159.103  1.00115.70
ATOM   1111  CG  ASP A 424     111.247 138.701 158.922  1.00115.70
ATOM   1112  OD1 ASP A 424     110.893 137.635 158.372  1.00115.70
ATOM   1113  OD2 ASP A 424     110.444 139.575 159.318  1.00115.70
ATOM   1114  N   LYS A 425     112.475 140.542 156.502  1.00111.47
ATOM   1115  CA  LYS A 425     111.583 141.034 155.467  1.00111.47
ATOM   1116  C   LYS A 425     112.204 140.848 154.097  1.00111.47
ATOM   1117  O   LYS A 425     111.489 140.722 153.096  1.00111.47
ATOM   1118  CB  LYS A 425     111.224 142.493 155.725  1.00111.47
ATOM   1119  CG  LYS A 425     110.261 143.109 154.717  1.00111.47
ATOM   1120  CD  LYS A 425     108.908 142.413 154.682  1.00111.47
ATOM   1121  CE  LYS A 425     108.007 142.992 153.625  1.00111.47
ATOM   1122  NZ  LYS A 425     106.673 142.377 153.706  1.00111.47
ATOM   1123  N   TRP A 426     113.531 140.851 154.024  1.00102.81
ATOM   1124  CA  TRP A 426     114.178 140.515 152.774  1.00102.81
ATOM   1125  C   TRP A 426     113.772 139.128 152.350  1.00102.81
ATOM   1126  O   TRP A 426     113.178 138.936 151.286  1.00102.81
ATOM   1127  CB  TRP A 426     115.688 140.588 152.911  1.00102.81
ATOM   1128  CG  TRP A 426     116.338 140.141 151.666  1.00102.81
ATOM   1129  CD1 TRP A 426     117.019 138.989 151.468  1.00102.81
ATOM   1130  CD2 TRP A 426     116.351 140.833 150.432  1.00102.81
ATOM   1131  NE1 TRP A 426     117.465 138.922 150.181  1.00102.81
ATOM   1132  CE2 TRP A 426     117.064 140.050 149.524  1.00102.81
ATOM   1133  CE3 TRP A 426     115.826 142.044 150.003  1.00102.81
ATOM   1134  CZ2 TRP A 426     117.274 140.440 148.219  1.00102.81
ATOM   1135  CZ3 TRP A 426     116.032 142.428 148.705  1.00102.81
ATOM   1136  CH2 TRP A 426     116.748 141.634 147.829  1.00102.81
ATOM   1137  N   ASP A 427     114.039 138.152 153.210  1.00107.74
ATOM   1138  CA  ASP A 427     113.764 136.773 152.842  1.00107.74
ATOM   1139  C   ASP A 427     112.281 136.544 152.636  1.00107.74
ATOM   1140  O   ASP A 427     111.875 135.889 151.671  1.00107.74
ATOM   1141  CB  ASP A 427     114.278 135.840 153.925  1.00107.74
ATOM   1142  CG  ASP A 427     115.700 136.124 154.294  1.00107.74
ATOM   1143  OD1 ASP A 427     116.488 136.432 153.382  1.00107.74
ATOM   1144  OD2 ASP A 427     116.029 136.055 155.493  1.00107.74
ATOM   1145  N   ARG A 428     111.466 137.122 153.505  1.00108.34
ATOM   1146  CA  ARG A 428     110.081 136.711 153.620  1.00108.34
ATOM   1147  C   ARG A 428     109.278 137.151 152.412  1.00108.34
ATOM   1148  O   ARG A 428     108.526 136.355 151.841  1.00108.34
ATOM   1149  CB  ARG A 428     109.499 137.278 154.912  1.00108.34
ATOM   1150  CG  ARG A 428     108.069 136.891 155.187  1.00108.34
ATOM   1151  CD  ARG A 428     107.607 137.438 156.531  1.00108.34
ATOM   1152  NE  ARG A 428     108.284 136.826 157.679  1.00108.34
ATOM   1153  CZ  ARG A 428     107.912 135.695 158.282  1.00108.34
ATOM   1154  NH1 ARG A 428     106.862 134.998 157.866  1.00108.34
ATOM   1155  NH2 ARG A 428     108.601 135.250 159.321  1.00108.34
ATOM   1156  N   PHE A 429     109.406 138.418 152.021  1.00106.95
ATOM   1157  CA  PHE A 429     108.648 138.944 150.894  1.00106.95
ATOM   1158  C   PHE A 429     109.528 139.629 149.870  1.00106.95
ATOM   1159  O   PHE A 429     109.350 139.433 148.668  1.00106.95
ATOM   1160  CB  PHE A 429     107.603 139.934 151.391  1.00106.95
ATOM   1161  CG  PHE A 429     106.737 140.506 150.305  1.00106.95
ATOM   1162  CD1 PHE A 429     105.896 139.695 149.569  1.00106.95
ATOM   1163  CD2 PHE A 429     106.748 141.859 150.037  1.00106.95
ATOM   1164  CE1 PHE A 429     105.096 140.222 148.583  1.00106.95
ATOM   1165  CE2 PHE A 429     105.946 142.388 149.053  1.00106.95
ATOM   1166  CZ  PHE A 429     105.120 141.568 148.327  1.00106.95
ATOM   1167  N   VAL A 430     110.494 140.418 150.329  1.00104.21
ATOM   1168  CA  VAL A 430     111.089 141.396 149.427  1.00104.21
ATOM   1169  C   VAL A 430     112.080 140.743 148.481  1.00104.21
ATOM   1170  O   VAL A 430     112.300 141.239 147.379  1.00104.21
ATOM   1171  CB  VAL A 430     111.743 142.548 150.201  1.00104.21
ATOM   1172  CG1 VAL A 430     112.383 143.515 149.232  1.00104.21
ATOM   1173  CG2 VAL A 430     110.736 143.259 151.044  1.00104.21
ATOM   1174  N   LYS A 431     112.742 139.674 148.910  1.00 98.80
ATOM   1175  CA  LYS A 431     113.748 139.048 148.062  1.00 98.80
ATOM   1176  C   LYS A 431     113.163 138.649 146.720  1.00 98.80
ATOM   1177  O   LYS A 431     113.709 138.983 145.663  1.00 98.80
ATOM   1178  CB  LYS A 431     114.332 137.831 148.764  1.00 98.80
ATOM   1179  CG  LYS A 431     115.394 137.138 147.978  1.00 98.80
ATOM   1180  CD  LYS A 431     116.138 136.111 148.802  1.00 98.80
ATOM   1181  CE  LYS A 431     115.302 134.877 149.031  1.00 98.80
ATOM   1182  NZ  LYS A 431     116.089 133.833 149.724  1.00 98.80
ATOM   1183  N   ARG A 432     112.026 137.962 146.742  1.00 97.88
ATOM   1184  CA  ARG A 432     111.437 137.496 145.496  1.00 97.88
ATOM   1185  C   ARG A 432     110.980 138.665 144.654  1.00 97.88
ATOM   1186  O   ARG A 432     111.163 138.665 143.436  1.00 97.88
ATOM   1187  CB  ARG A 432     110.266 136.554 145.772  1.00 97.88
ATOM   1188  CG  ARG A 432     110.603 135.302 146.598  1.00 97.88
ATOM   1189  CD  ARG A 432     111.641 134.413 145.923  1.00 97.88
ATOM   1190  NE  ARG A 432     111.919 133.198 146.685  1.00 97.88
ATOM   1191  CZ  ARG A 432     112.911 132.345 146.422  1.00 97.88
ATOM   1192  NH1 ARG A 432     113.749 132.555 145.413  1.00 97.88
ATOM   1193  NH2 ARG A 432     113.068 131.270 147.179  1.00 97.88
ATOM   1194  N   ILE A 433     110.392 139.678 145.284  1.00 92.55
ATOM   1195  CA  ILE A 433     109.917 140.816 144.513  1.00 92.55
ATOM   1196  C   ILE A 433     111.083 141.564 143.912  1.00 92.55
ATOM   1197  O   ILE A 433     110.993 142.082 142.799  1.00 92.55
ATOM   1198  CB  ILE A 433     109.047 141.740 145.374  1.00 92.55
ATOM   1199  CG1 ILE A 433     107.831 140.987 145.905  1.00 92.55
ATOM   1200  CG2 ILE A 433     108.625 142.938 144.568  1.00 92.55
ATOM   1201  CD1 ILE A 433     106.917 140.368 144.847  1.00 92.55
ATOM   1202  N   PHE A 434     112.185 141.663 144.641  1.00 87.96
ATOM   1203  CA  PHE A 434     113.351 142.327 144.089  1.00 87.96
ATOM   1204  C   PHE A 434     113.873 141.573 142.894  1.00 87.96
ATOM   1205  O   PHE A 434     114.242 142.175 141.889  1.00 87.96
ATOM   1206  CB  PHE A 434     114.457 142.457 145.113  1.00 87.96
ATOM   1207  CG  PHE A 434     115.689 143.045 144.551  1.00 87.96
ATOM   1208  CD1 PHE A 434     115.713 144.360 144.173  1.00 87.96
ATOM   1209  CD2 PHE A 434     116.814 142.293 144.373  1.00 87.96
ATOM   1210  CE1 PHE A 434     116.845 144.922 143.649  1.00 87.96
ATOM   1211  CE2 PHE A 434     117.955 142.851 143.845  1.00 87.96
ATOM   1212  CZ  PHE A 434     117.967 144.168 143.479  1.00 87.96
ATOM   1213  N   TYR A 435     113.952 140.253 142.992  1.00 86.81
ATOM   1214  CA  TYR A 435     114.422 139.506 141.836  1.00 86.81
ATOM   1215  C   TYR A 435     113.455 139.641 140.681  1.00 86.81
ATOM   1216  O   TYR A 435     113.864 139.640 139.522  1.00 86.81
ATOM   1217  CB  TYR A 435     114.629 138.046 142.176  1.00 86.81
ATOM   1218  CG  TYR A 435     115.849 137.799 142.991  1.00 86.81
ATOM   1219  CD1 TYR A 435     117.107 138.010 142.474  1.00 86.81
ATOM   1220  CD2 TYR A 435     115.747 137.329 144.271  1.00 86.81
ATOM   1221  CE1 TYR A 435     118.216 137.777 143.222  1.00 86.81
ATOM   1222  CE2 TYR A 435     116.844 137.097 145.018  1.00 86.81
ATOM   1223  CZ  TYR A 435     118.074 137.316 144.499  1.00 86.81
ATOM   1224  OH  TYR A 435     119.167 137.064 145.290  1.00 86.81
ATOM   1225  N   PHE A 436     112.165 139.744 140.970  1.00 80.75
ATOM   1226  CA  PHE A 436     111.210 139.946 139.894  1.00 80.75
ATOM   1227  C   PHE A 436     111.425 141.297 139.253  1.00 80.75
ATOM   1228  O   PHE A 436     111.342 141.440 138.034  1.00 80.75
ATOM   1229  CB  PHE A 436     109.780 139.816 140.404  1.00 80.75
ATOM   1230  CG  PHE A 436     108.757 140.070 139.355  1.00 80.75
ATOM   1231  CD1 PHE A 436     108.484 139.119 138.401  1.00 80.75
ATOM   1232  CD2 PHE A 436     108.080 141.259 139.313  1.00 80.75
ATOM   1233  CE1 PHE A 436     107.556 139.348 137.429  1.00 80.75
ATOM   1234  CE2 PHE A 436     107.150 141.494 138.344  1.00 80.75
ATOM   1235  CZ  PHE A 436     106.887 140.535 137.399  1.00 80.75
ATOM   1236  N   ASN A 437     111.662 142.312 140.068  1.00 79.63
ATOM   1237  CA  ASN A 437     111.936 143.632 139.530  1.00 79.63
ATOM   1238  C   ASN A 437     113.174 143.611 138.674  1.00 79.63
ATOM   1239  O   ASN A 437     113.193 144.183 137.587  1.00 79.63
ATOM   1240  CB  ASN A 437     112.126 144.622 140.658  1.00 79.63
ATOM   1241  CG  ASN A 437     110.847 145.235 141.099  1.00 79.63
ATOM   1242  OD1 ASN A 437     110.091 145.771 140.290  1.00 79.63
ATOM   1243  ND2 ASN A 437     110.582 145.162 142.394  1.00 79.63
ATOM   1244  N   PHE A 438     114.221 142.957 139.156  1.00 73.28
ATOM   1245  CA  PHE A 438     115.443 142.853 138.383  1.00 73.28
ATOM   1246  C   PHE A 438     115.183 142.116 137.090  1.00 73.28
ATOM   1247  O   PHE A 438     115.647 142.519 136.028  1.00 73.28
ATOM   1248  CB  PHE A 438     116.509 142.140 139.196  1.00 73.28
ATOM   1249  CG  PHE A 438     117.717 141.787 138.408  1.00 73.28
ATOM   1250  CD1 PHE A 438     118.442 142.753 137.777  1.00 73.28
ATOM   1251  CD2 PHE A 438     118.139 140.490 138.314  1.00 73.28
ATOM   1252  CE1 PHE A 438     119.555 142.442 137.059  1.00 73.28
ATOM   1253  CE2 PHE A 438     119.254 140.172 137.593  1.00 73.28
ATOM   1254  CZ  PHE A 438     119.958 141.151 136.963  1.00 73.28
ATOM   1255  N   PHE A 439     114.417 141.039 137.162  1.00 73.29
ATOM   1256  CA  PHE A 439     114.123 140.255 135.978  1.00 73.29
ATOM   1257  C   PHE A 439     113.330 141.059 134.968  1.00 73.29
ATOM   1258  O   PHE A 439     113.589 140.989 133.768  1.00 73.29
ATOM   1259  CB  PHE A 439     113.363 139.000 136.366  1.00 73.29
ATOM   1260  CG  PHE A 439     112.894 138.222 135.201  1.00 73.29
ATOM   1261  CD1 PHE A 439     113.799 137.619 134.357  1.00 73.29
ATOM   1262  CD2 PHE A 439     111.555 138.100 134.937  1.00 73.29
ATOM   1263  CE1 PHE A 439     113.374 136.903 133.277  1.00 73.29
ATOM   1264  CE2 PHE A 439     111.129 137.383 133.863  1.00 73.29
ATOM   1265  CZ  PHE A 439     112.039 136.785 133.029  1.00 73.29
ATOM   1266  N   VAL A 440     112.330 141.799 135.424  1.00 70.81
ATOM   1267  CA  VAL A 440     111.546 142.587 134.488  1.00 70.81
ATOM   1268  C   VAL A 440     112.386 143.703 133.923  1.00 70.81
ATOM   1269  O   VAL A 440     112.200 144.109 132.779  1.00 70.81
ATOM   1270  CB  VAL A 440     110.278 143.139 135.137  1.00 70.81
ATOM   1271  CG1 VAL A 440     109.591 144.070 134.170  1.00 70.81
ATOM   1272  CG2 VAL A 440     109.375 142.026 135.484  1.00 70.81
ATOM   1273  N   TYR A 441     113.283 144.262 134.723  1.00 68.02
ATOM   1274  CA  TYR A 441     114.178 145.252 134.157  1.00 68.02
ATOM   1275  C   TYR A 441     115.048 144.614 133.092  1.00 68.02
ATOM   1276  O   TYR A 441     115.281 145.208 132.042  1.00 68.02
ATOM   1277  CB  TYR A 441     115.028 145.910 135.231  1.00 68.02
ATOM   1278  CG  TYR A 441     115.921 146.934 134.620  1.00 68.02
ATOM   1279  CD1 TYR A 441     115.434 148.149 134.216  1.00 68.02
ATOM   1280  CD2 TYR A 441     117.238 146.664 134.395  1.00 68.02
ATOM   1281  CE1 TYR A 441     116.244 149.064 133.636  1.00 68.02
ATOM   1282  CE2 TYR A 441     118.043 147.569 133.820  1.00 68.02
ATOM   1283  CZ  TYR A 441     117.547 148.757 133.436  1.00 68.02
ATOM   1284  OH  TYR A 441     118.407 149.630 132.861  1.00 68.02
ATOM   1285  N   CYS A 442     115.516 143.396 133.331  1.00 67.92
ATOM   1286  CA  CYS A 442     116.272 142.689 132.310  1.00 67.92
ATOM   1287  C   CYS A 442     115.436 142.473 131.062  1.00 67.92
ATOM   1288  O   CYS A 442     115.937 142.603 129.944  1.00 67.92
ATOM   1289  CB  CYS A 442     116.766 141.355 132.848  1.00 67.92
ATOM   1290  SG  CYS A 442     118.124 141.464 134.004  1.00 67.92
ATOM   1291  N   LEU A 443     114.168 142.118 131.227  1.00 67.81
ATOM   1292  CA  LEU A 443     113.317 141.910 130.066  1.00 67.81
ATOM   1293  C   LEU A 443     113.076 143.210 129.337  1.00 67.81
ATOM   1294  O   LEU A 443     113.045 143.250 128.105  1.00 67.81
ATOM   1295  CB  LEU A 443     111.988 141.309 130.480  1.00 67.81
ATOM   1296  CG  LEU A 443     111.951 139.832 130.824  1.00 67.81
ATOM   1297  CD1 LEU A 443     110.548 139.505 131.244  1.00 67.81
ATOM   1298  CD2 LEU A 443     112.383 138.970 129.664  1.00 67.81
ATOM   1299  N   TYR A 444     112.876 144.279 130.083  1.00 66.73
ATOM   1300  CA  TYR A 444     112.725 145.576 129.465  1.00 66.73
ATOM   1301  C   TYR A 444     113.960 145.913 128.669  1.00 66.73
ATOM   1302  O   TYR A 444     113.872 146.423 127.556  1.00 66.73
ATOM   1303  CB  TYR A 444     112.475 146.627 130.527  1.00 66.73
ATOM   1304  CG  TYR A 444     112.743 148.015 130.056  1.00 66.73
ATOM   1305  CD1 TYR A 444     112.051 148.559 129.005  1.00 66.73
ATOM   1306  CD2 TYR A 444     113.682 148.791 130.681  1.00 66.73
ATOM   1307  CE1 TYR A 444     112.307 149.821 128.595  1.00 66.73
ATOM   1308  CE2 TYR A 444     113.934 150.051 130.274  1.00 66.73
ATOM   1309  CZ  TYR A 444     113.244 150.561 129.230  1.00 66.73
ATOM   1310  OH  TYR A 444     113.495 151.839 128.819  1.00 66.73
ATOM   1311  N   MET A 445     115.126 145.626 129.223  1.00 64.66
ATOM   1312  CA  MET A 445     116.342 145.997 128.533  1.00 64.66
ATOM   1313  C   MET A 445     116.563 145.135 127.319  1.00 64.66
ATOM   1314  O   MET A 445     117.072 145.615 126.313  1.00 64.66
ATOM   1315  CB  MET A 445     117.540 145.900 129.457  1.00 64.66
ATOM   1316  CG  MET A 445     117.651 147.013 130.470  1.00 64.66
ATOM   1317  SD  MET A 445     117.620 148.703 129.841  1.00 64.66
ATOM   1318  CE  MET A 445     118.520 148.612 128.299  1.00 64.66
ATOM   1319  N   ILE A 446     116.182 143.872 127.378  1.00 65.31
ATOM   1320  CA  ILE A 446     116.305 143.034 126.201  1.00 65.31
ATOM   1321  C   ILE A 446     115.368 143.519 125.112  1.00 65.31
ATOM   1322  O   ILE A 446     115.742 143.569 123.940  1.00 65.31
ATOM   1323  CB  ILE A 446     116.036 141.574 126.560  1.00 65.31
ATOM   1324  CG1 ILE A 446     117.113 141.048 127.488  1.00 65.31
ATOM   1325  CG2 ILE A 446     115.986 140.743 125.322  1.00 65.31
ATOM   1326  CD1 ILE A 446     116.652 139.889 128.321  1.00 65.31
ATOM   1327  N   ILE A 447     114.134 143.871 125.467  1.00 67.14
ATOM   1328  CA  ILE A 447     113.202 144.356 124.454  1.00 67.14
ATOM   1329  C   ILE A 447     113.696 145.668 123.886  1.00 67.14
ATOM   1330  O   ILE A 447     113.632 145.906 122.679  1.00 67.14
ATOM   1331  CB  ILE A 447     111.791 144.511 125.030  1.00 67.14
ATOM   1332  CG1 ILE A 447     111.217 143.162 125.404  1.00 67.14
ATOM   1333  CG2 ILE A 447     110.890 145.182 124.023  1.00 67.14
ATOM   1334  CD1 ILE A 447     110.126 143.256 126.417  1.00 67.14
ATOM   1335  N   PHE A 448     114.168 146.551 124.753  1.00 64.24
ATOM   1336  CA  PHE A 448     114.667 147.832 124.295  1.00 64.24
ATOM   1337  C   PHE A 448     115.845 147.630 123.371  1.00 64.24
ATOM   1338  O   PHE A 448     115.929 148.254 122.314  1.00 64.24
ATOM   1339  CB  PHE A 448     115.057 148.670 125.502  1.00 64.24
ATOM   1340  CG  PHE A 448     115.583 150.037 125.180  1.00 64.24
ATOM   1341  CD1 PHE A 448     115.322 150.675 123.993  1.00 64.24
ATOM   1342  CD2 PHE A 448     116.339 150.690 126.106  1.00 64.24
ATOM   1343  CE1 PHE A 448     115.815 151.901 123.746  1.00 64.24
ATOM   1344  CE2 PHE A 448     116.818 151.916 125.856  1.00 64.24
ATOM   1345  CZ  PHE A 448     116.562 152.522 124.673  1.00 64.24
ATOM   1346  N   THR A 449     116.776 146.773 123.766  1.00 61.63
ATOM   1347  CA  THR A 449     117.954 146.552 122.957  1.00 61.63
ATOM   1348  C   THR A 449     117.578 145.955 121.624  1.00 61.63
ATOM   1349  O   THR A 449     118.117 146.347 120.589  1.00 61.63
ATOM   1350  CB  THR A 449     118.918 145.639 123.686  1.00 61.63
ATOM   1351  OG1 THR A 449     119.222 146.184 124.967  1.00 61.63
ATOM   1352  CG2 THR A 449     120.170 145.512 122.911  1.00 61.63
ATOM   1353  N   ALA A 450     116.660 144.997 121.628  1.00 62.64
ATOM   1354  CA  ALA A 450     116.252 144.373 120.383  1.00 62.64
ATOM   1355  C   ALA A 450     115.576 145.378 119.474  1.00 62.64
ATOM   1356  O   ALA A 450     115.856 145.434 118.276  1.00 62.64
ATOM   1357  CB  ALA A 450     115.325 143.211 120.688  1.00 62.64
ATOM   1358  N   ALA A 451     114.692 146.193 120.033  1.00 67.35
ATOM   1359  CA  ALA A 451     114.018 147.211 119.249  1.00 67.35
ATOM   1360  C   ALA A 451     115.008 148.200 118.675  1.00 67.35
ATOM   1361  O   ALA A 451     114.926 148.567 117.501  1.00 67.35
ATOM   1362  CB  ALA A 451     113.010 147.935 120.127  1.00 67.35
ATOM   1363  N   ALA A 452     115.963 148.630 119.483  1.00 64.43
ATOM   1364  CA  ALA A 452     116.901 149.633 119.023  1.00 64.43
ATOM   1365  C   ALA A 452     117.793 149.068 117.944  1.00 64.43
ATOM   1366  O   ALA A 452     118.013 149.709 116.916  1.00 64.43
ATOM   1367  CB  ALA A 452     117.732 150.136 120.191  1.00 64.43
ATOM   1368  N   TYR A 453     118.305 147.862 118.159  1.00 63.54
ATOM   1369  CA  TYR A 453     119.237 147.269 117.216  1.00 63.54
ATOM   1370  C   TYR A 453     118.603 147.144 115.854  1.00 63.54
ATOM   1371  O   TYR A 453     119.233 147.453 114.843  1.00 63.54
ATOM   1372  CB  TYR A 453     119.681 145.905 117.729  1.00 63.54
ATOM   1373  CG  TYR A 453     120.580 145.116 116.809  1.00 63.54
ATOM   1374  CD1 TYR A 453     120.058 144.314 115.814  1.00 63.54
ATOM   1375  CD2 TYR A 453     121.945 145.130 116.969  1.00 63.54
ATOM   1376  CE1 TYR A 453     120.865 143.594 114.991  1.00 63.54
ATOM   1377  CE2 TYR A 453     122.763 144.402 116.144  1.00 63.54
ATOM   1378  CZ  TYR A 453     122.215 143.637 115.162  1.00 63.54
ATOM   1379  OH  TYR A 453     123.015 142.904 114.330  1.00 63.54
ATOM   1380  N   TYR A 454     117.349 146.698 115.810  1.00 65.98
ATOM   1381  CA  TYR A 454     116.628 146.510 114.560  1.00 65.98
ATOM   1382  C   TYR A 454     115.852 147.731 114.165  1.00 65.98
ATOM   1383  O   TYR A 454     114.854 147.609 113.455  1.00 65.98
ATOM   1384  CB  TYR A 454     115.700 145.302 114.659  1.00 65.98
ATOM   1385  CG  TYR A 454     116.470 144.034 114.807  1.00 65.98
ATOM   1386  CD1 TYR A 454     117.125 143.484 113.730  1.00 65.98
ATOM   1387  CD2 TYR A 454     116.569 143.407 116.017  1.00 65.98
ATOM   1388  CE1 TYR A 454     117.844 142.344 113.853  1.00 65.98
ATOM   1389  CE2 TYR A 454     117.282 142.264 116.153  1.00 65.98
ATOM   1390  CZ  TYR A 454     117.922 141.733 115.069  1.00 65.98
ATOM   1391  OH  TYR A 454     118.646 140.575 115.207  1.00 65.98
ATOM   1392  N   ARG A 455     116.283 148.907 114.601  1.00 68.93
ATOM   1393  CA  ARG A 455     115.595 150.112 114.209  1.00 68.93
ATOM   1394  C   ARG A 455     115.612 150.208 112.691  1.00 68.93
ATOM   1395  O   ARG A 455     116.533 149.707 112.050  1.00 68.93
ATOM   1396  CB  ARG A 455     116.260 151.342 114.812  1.00 68.93
ATOM   1397  CG  ARG A 455     117.700 151.574 114.397  1.00 68.93
ATOM   1398  CD  ARG A 455     118.208 152.849 115.020  1.00 68.93
ATOM   1399  NE  ARG A 455     119.554 153.214 114.616  1.00 68.93
ATOM   1400  CZ  ARG A 455     119.882 153.677 113.418  1.00 68.93
ATOM   1401  NH1 ARG A 455     118.978 153.814 112.466  1.00 68.93
ATOM   1402  NH2 ARG A 455     121.136 153.990 113.161  1.00 68.93
ATOM   1403  N   PRO A 456     114.599 150.796 112.085  1.00 78.13
ATOM   1404  CA  PRO A 456     114.629 150.963 110.638  1.00 78.13
ATOM   1405  C   PRO A 456     115.684 151.975 110.254  1.00 78.13
ATOM   1406  O   PRO A 456     116.079 152.835 111.040  1.00 78.13
ATOM   1407  CB  PRO A 456     113.230 151.472 110.315  1.00 78.13
ATOM   1408  CG  PRO A 456     112.886 152.222 111.517  1.00 78.13
ATOM   1409  CD  PRO A 456     113.430 151.462 112.664  1.00 78.13
ATOM   1410  N   VAL A 457     116.140 151.852 109.018  1.00 77.11
ATOM   1411  CA  VAL A 457     117.191 152.696 108.489  1.00 77.11
ATOM   1412  C   VAL A 457     116.649 153.710 107.507  1.00 77.11
ATOM   1413  O   VAL A 457     117.427 154.445 106.902  1.00 77.11
ATOM   1414  CB  VAL A 457     118.296 151.856 107.837  1.00 77.11
ATOM   1415  CG1 VAL A 457     118.949 150.962 108.871  1.00 77.11
ATOM   1416  CG2 VAL A 457     117.754 151.020 106.674  1.00 77.11
ATOM   1417  N   GLU A 458     115.334 153.779 107.334  1.00 83.69
ATOM   1418  CA  GLU A 458     114.784 154.726 106.387  1.00 83.69
ATOM   1419  C   GLU A 458     115.046 156.139 106.877  1.00 83.69
ATOM   1420  O   GLU A 458     115.140 156.401 108.074  1.00 83.69
ATOM   1421  CB  GLU A 458     113.286 154.506 106.219  1.00 83.69
ATOM   1422  CG  GLU A 458     112.917 153.127 105.722  1.00 83.69
ATOM   1423  CD  GLU A 458     111.418 152.920 105.629  1.00 83.69
ATOM   1424  OE1 GLU A 458     110.661 153.772 106.127  1.00 83.69
ATOM   1425  OE2 GLU A 458     110.991 151.902 105.053  1.00 83.69
ATOM   1426  N   GLY A 459     115.185 157.050 105.949  1.00 80.59
ATOM   1427  CA  GLY A 459     115.346 158.423 106.339  1.00 80.59
ATOM   1428  C   GLY A 459     114.055 158.973 106.881  1.00 80.59
ATOM   1429  O   GLY A 459     112.989 158.404 106.666  1.00 80.59
ATOM   1430  N   LEU A 460     114.159 160.091 107.587  1.00 79.88
ATOM   1431  CA  LEU A 460     112.968 160.850 107.929  1.00 79.88
ATOM   1432  C   LEU A 460     111.988 160.073 108.812  1.00 79.88
ATOM   1433  O   LEU A 460     110.937 159.632 108.330  1.00 79.88
ATOM   1434  CB  LEU A 460     112.268 161.290 106.639  1.00 79.88
ATOM   1435  CG  LEU A 460     113.150 161.850 105.525  1.00 79.88
ATOM   1436  CD1 LEU A 460     112.297 162.144 104.303  1.00 79.88
ATOM   1437  CD2 LEU A 460     113.884 163.078 106.014  1.00 79.88
ATOM   1438  N   PRO A 461     112.282 159.874 110.093  1.00 76.88
ATOM   1439  CA  PRO A 461     111.294 159.274 111.000  1.00 76.88
ATOM   1440  C   PRO A 461     110.053 160.140 111.113  1.00 76.88
ATOM   1441  O   PRO A 461     110.015 161.256 110.580  1.00 76.88
ATOM   1442  CB  PRO A 461     112.043 159.205 112.335  1.00 76.88
ATOM   1443  CG  PRO A 461     113.050 160.254 112.246  1.00 76.88
ATOM   1444  CD  PRO A 461     113.462 160.354 110.823  1.00 76.88
ATOM   1445  N   PRO A 462     108.975 159.634 111.714  1.00 75.55
ATOM   1446  CA  PRO A 462     108.649 158.275 112.116  1.00 75.55
ATOM   1447  C   PRO A 462     108.344 157.456 110.889  1.00 75.55
ATOM   1448  O   PRO A 462     108.121 158.042 109.840  1.00 75.55
ATOM   1449  CB  PRO A 462     107.421 158.461 112.976  1.00 75.55
ATOM   1450  CG  PRO A 462     106.772 159.617 112.391  1.00 75.55
ATOM   1451  CD  PRO A 462     107.861 160.542 112.004  1.00 75.55
ATOM   1452  N   TYR A 463     108.343 156.137 111.013  1.00 80.50
ATOM   1453  CA  TYR A 463     108.278 155.243 109.872  1.00 80.50
ATOM   1454  C   TYR A 463     106.996 154.433 109.892  1.00 80.50
ATOM   1455  O   TYR A 463     106.494 154.056 110.952  1.00 80.50
ATOM   1456  CB  TYR A 463     109.485 154.317 109.863  1.00 80.50
ATOM   1457  CG  TYR A 463     110.755 155.088 110.048  1.00 80.50
ATOM   1458  CD1 TYR A 463     111.261 155.853 109.024  1.00 80.50
ATOM   1459  CD2 TYR A 463     111.416 155.089 111.257  1.00 80.50
ATOM   1460  CE1 TYR A 463     112.395 156.562 109.184  1.00 80.50
ATOM   1461  CE2 TYR A 463     112.562 155.788 111.422  1.00 80.50
ATOM   1462  CZ  TYR A 463     113.046 156.532 110.383  1.00 80.50
ATOM   1463  OH  TYR A 463     114.192 157.263 110.535  1.00 80.50
ATOM   1464  N   LYS A 464     106.469 154.177 108.702  1.00 90.96
ATOM   1465  CA  LYS A 464     105.204 153.475 108.589  1.00 90.96
ATOM   1466  C   LYS A 464     105.376 152.027 109.001  1.00 90.96
ATOM   1467  O   LYS A 464     106.345 151.368 108.623  1.00 90.96
ATOM   1468  CB  LYS A 464     104.685 153.556 107.159  1.00 90.96
ATOM   1469  CG  LYS A 464     103.290 153.006 106.982  1.00 90.96
ATOM   1470  CD  LYS A 464     102.811 153.196 105.559  1.00 90.96
ATOM   1471  CE  LYS A 464     101.484 152.508 105.324  1.00 90.96
ATOM   1472  NZ  LYS A 464     101.023 152.699 103.921  1.00 90.96
ATOM   1473  N   LEU A 465     104.425 151.533 109.778  1.00 92.47
ATOM   1474  CA  LEU A 465     104.442 150.138 110.173  1.00 92.47
ATOM   1475  C   LEU A 465     104.129 149.270 108.969  1.00 92.47
ATOM   1476  O   LEU A 465     103.087 149.434 108.334  1.00 92.47
ATOM   1477  CB  LEU A 465     103.413 149.893 111.270  1.00 92.47
ATOM   1478  CG  LEU A 465     103.341 148.486 111.866  1.00 92.47
ATOM   1479  CD1 LEU A 465     104.605 148.227 112.641  1.00 92.47
ATOM   1480  CD2 LEU A 465     102.115 148.313 112.744  1.00 92.47
ATOM   1481  N   LYS A 466     105.011 148.329 108.673  1.00 95.24
ATOM   1482  CA  LYS A 466     104.741 147.373 107.619  1.00 95.24
ATOM   1483  C   LYS A 466     103.974 146.196 108.190  1.00 95.24
ATOM   1484  O   LYS A 466     104.175 145.789 109.335  1.00 95.24
ATOM   1485  CB  LYS A 466     106.039 146.894 106.982  1.00 95.24
ATOM   1486  CG  LYS A 466     106.821 147.998 106.296  1.00 95.24
ATOM   1487  CD  LYS A 466     108.104 147.469 105.675  1.00 95.24
ATOM   1488  CE  LYS A 466     108.960 148.596 105.132  1.00 95.24
ATOM   1489  NZ  LYS A 466     109.411 149.553 106.178  1.00 95.24
ATOM   1490  N   ASN A 467     103.109 145.618 107.365  1.00 95.89
ATOM   1491  CA  ASN A 467     102.239 144.558 107.854  1.00 95.89
ATOM   1492  C   ASN A 467     102.986 143.272 108.174  1.00 95.89
ATOM   1493  O   ASN A 467     102.379 142.338 108.705  1.00 95.89
ATOM   1494  CB  ASN A 467     101.138 144.281 106.834  1.00 95.89
ATOM   1495  CG  ASN A 467     100.378 145.529 106.462  1.00 95.89
ATOM   1496  OD1 ASN A 467     100.444 146.536 107.164  1.00 95.89
ATOM   1497  ND2 ASN A 467      99.652 145.472 105.356  1.00 95.89
ATOM   1498  N   THR A 468     104.269 143.179 107.836  1.00 95.81
ATOM   1499  CA  THR A 468     105.048 142.007 108.201  1.00 95.81
ATOM   1500  C   THR A 468     105.203 141.950 109.715  1.00 95.81
ATOM   1501  O   THR A 468     105.253 142.981 110.391  1.00 95.81
ATOM   1502  CB  THR A 468     106.409 142.025 107.498  1.00 95.81
ATOM   1503  OG1 THR A 468     107.097 140.804 107.769  1.00 95.81
ATOM   1504  CG2 THR A 468     107.267 143.192 107.950  1.00 95.81
ATOM   1505  N   VAL A 469     105.228 140.728 110.248  1.00 94.39
ATOM   1506  CA  VAL A 469     105.197 140.534 111.695  1.00 94.39
ATOM   1507  C   VAL A 469     106.466 141.048 112.347  1.00 94.39
ATOM   1508  O   VAL A 469     106.450 141.439 113.520  1.00 94.39
ATOM   1509  CB  VAL A 469     104.969 139.048 112.017  1.00 94.39
ATOM   1510  CG1 VAL A 469     106.217 138.242 111.694  1.00 94.39
ATOM   1511  CG2 VAL A 469     104.540 138.857 113.478  1.00 94.39
ATOM   1512  N   GLY A 470     107.591 141.010 111.628  1.00 95.45
ATOM   1513  CA  GLY A 470     108.817 141.537 112.186  1.00 95.45
ATOM   1514  C   GLY A 470     108.665 142.989 112.574  1.00 95.45
ATOM   1515  O   GLY A 470     109.056 143.390 113.668  1.00 95.45
ATOM   1516  N   ASP A 471     108.016 143.774 111.731  1.00 93.69
ATOM   1517  CA  ASP A 471     107.775 145.159 112.077  1.00 93.69
ATOM   1518  C   ASP A 471     106.775 145.281 113.206  1.00 93.69
ATOM   1519  O   ASP A 471     106.860 146.216 114.001  1.00 93.69
ATOM   1520  CB  ASP A 471     107.276 145.913 110.853  1.00 93.69
ATOM   1521  CG  ASP A 471     108.383 146.319 109.950  1.00 93.69
ATOM   1522  OD1 ASP A 471     109.030 147.337 110.246  1.00 93.69
ATOM   1523  OD2 ASP A 471     108.628 145.608 108.961  1.00 93.69
ATOM   1524  N   TYR A 472     105.813 144.372 113.290  1.00 93.06
ATOM   1525  CA  TYR A 472     104.896 144.420 114.416  1.00 93.06
ATOM   1526  C   TYR A 472     105.636 144.220 115.722  1.00 93.06
ATOM   1527  O   TYR A 472     105.430 144.968 116.682  1.00 93.06
ATOM   1528  CB  TYR A 472     103.816 143.363 114.259  1.00 93.06
ATOM   1529  CG  TYR A 472     102.678 143.780 113.381  1.00 93.06
ATOM   1530  CD1 TYR A 472     101.650 144.548 113.882  1.00 93.06
ATOM   1531  CD2 TYR A 472     102.623 143.397 112.051  1.00 93.06
ATOM   1532  CE1 TYR A 472     100.597 144.924 113.089  1.00 93.06
ATOM   1533  CE2 TYR A 472     101.571 143.770 111.255  1.00 93.06
ATOM   1534  CZ  TYR A 472     100.564 144.530 111.772  1.00 93.06
ATOM   1535  OH  TYR A 472      99.523 144.896 110.951  1.00 93.06
ATOM   1536  N   PHE A 473     106.515 143.227 115.774  1.00 89.45
ATOM   1537  CA  PHE A 473     107.332 143.054 116.963  1.00 89.45
ATOM   1538  C   PHE A 473     108.188 144.276 117.207  1.00 89.45
ATOM   1539  O   PHE A 473     108.373 144.686 118.351  1.00 89.45
ATOM   1540  CB  PHE A 473     108.242 141.845 116.830  1.00 89.45
ATOM   1541  CG  PHE A 473     107.560 140.548 117.005  1.00 89.45
ATOM   1542  CD1 PHE A 473     107.074 140.170 118.233  1.00 89.45
ATOM   1543  CD2 PHE A 473     107.447 139.682 115.948  1.00 89.45
ATOM   1544  CE1 PHE A 473     106.461 138.957 118.396  1.00 89.45
ATOM   1545  CE2 PHE A 473     106.840 138.472 116.102  1.00 89.45
ATOM   1546  CZ  PHE A 473     106.343 138.106 117.328  1.00 89.45
ATOM   1547  N   ARG A 474     108.749 144.851 116.146  1.00 84.93
ATOM   1548  CA  ARG A 474     109.615 146.007 116.317  1.00 84.93
ATOM   1549  C   ARG A 474     108.857 147.152 116.960  1.00 84.93
ATOM   1550  O   ARG A 474     109.308 147.735 117.947  1.00 84.93
ATOM   1551  CB  ARG A 474     110.187 146.433 114.971  1.00 84.93
ATOM   1552  CG  ARG A 474     110.950 147.741 114.985  1.00 84.93
ATOM   1553  CD  ARG A 474     111.557 147.988 113.639  1.00 84.93
ATOM   1554  NE  ARG A 474     110.542 148.253 112.619  1.00 84.93
ATOM   1555  CZ  ARG A 474     109.945 149.426 112.420  1.00 84.93
ATOM   1556  NH1 ARG A 474     110.240 150.483 113.164  1.00 84.93
ATOM   1557  NH2 ARG A 474     109.036 149.551 111.468  1.00 84.93
ATOM   1558  N   VAL A 475     107.695 147.489 116.414  1.00 85.18
ATOM   1559  CA  VAL A 475     106.980 148.633 116.948  1.00 85.18
ATOM   1560  C   VAL A 475     106.456 148.308 118.327  1.00 85.18
ATOM   1561  O   VAL A 475     106.388 149.185 119.193  1.00 85.18
ATOM   1562  CB  VAL A 475     105.871 149.090 115.992  1.00 85.18
ATOM   1563  CG1 VAL A 475     104.660 148.190 116.077  1.00 85.18
ATOM   1564  CG2 VAL A 475     105.493 150.511 116.285  1.00 85.18
ATOM   1565  N   THR A 476     106.075 147.058 118.568  1.00 82.05
ATOM   1566  CA  THR A 476     105.675 146.684 119.913  1.00 82.05
ATOM   1567  C   THR A 476     106.826 146.864 120.873  1.00 82.05
ATOM   1568  O   THR A 476     106.644 147.342 121.997  1.00 82.05
ATOM   1569  CB  THR A 476     105.203 145.243 119.944  1.00 82.05
ATOM   1570  OG1 THR A 476     104.037 145.097 119.129  1.00 82.05
ATOM   1571  CG2 THR A 476     104.888 144.846 121.356  1.00 82.05
ATOM   1572  N   GLY A 477     108.016 146.462 120.451  1.00 77.62
ATOM   1573  CA  GLY A 477     109.173 146.636 121.290  1.00 77.62
ATOM   1574  C   GLY A 477     109.428 148.095 121.559  1.00 77.62
ATOM   1575  O   GLY A 477     109.761 148.477 122.671  1.00 77.62
ATOM   1576  N   GLU A 478     109.260 148.927 120.545  1.00 78.82
ATOM   1577  CA  GLU A 478     109.467 150.352 120.727  1.00 78.82
ATOM   1578  C   GLU A 478     108.471 150.915 121.718  1.00 78.82
ATOM   1579  O   GLU A 478     108.823 151.740 122.564  1.00 78.82
ATOM   1580  CB  GLU A 478     109.347 151.056 119.384  1.00 78.82
ATOM   1581  CG  GLU A 478     110.493 150.731 118.455  1.00 78.82
ATOM   1582  CD  GLU A 478     110.167 150.881 116.992  1.00 78.82
ATOM   1583  OE1 GLU A 478     109.034 151.280 116.655  1.00 78.82
ATOM   1584  OE2 GLU A 478     111.069 150.604 116.168  1.00 78.82
ATOM   1585  N   ILE A 479     107.220 150.484 121.624  1.00 77.13
ATOM   1586  CA  ILE A 479     106.192 151.005 122.513  1.00 77.13
ATOM   1587  C   ILE A 479     106.479 150.586 123.942  1.00 77.13
ATOM   1588  O   ILE A 479     106.373 151.389 124.871  1.00 77.13
ATOM   1589  CB  ILE A 479     104.807 150.548 122.034  1.00 77.13
ATOM   1590  CG1 ILE A 479     104.463 151.231 120.710  1.00 77.13
ATOM   1591  CG2 ILE A 479     103.767 150.874 123.052  1.00 77.13
ATOM   1592  CD1 ILE A 479     103.456 150.498 119.891  1.00 77.13
ATOM   1593  N   LEU A 480     106.867 149.330 124.140  1.00 75.28
ATOM   1594  CA  LEU A 480     107.267 148.889 125.468  1.00 75.28
ATOM   1595  C   LEU A 480     108.508 149.616 125.937  1.00 75.28
ATOM   1596  O   LEU A 480     108.633 149.922 127.121  1.00 75.28
ATOM   1597  CB  LEU A 480     107.525 147.392 125.475  1.00 75.28
ATOM   1598  CG  LEU A 480     106.310 146.529 125.178  1.00 75.28
ATOM   1599  CD1 LEU A 480     106.748 145.133 124.870  1.00 75.28
ATOM   1600  CD2 LEU A 480     105.362 146.534 126.353  1.00 75.28
ATOM   1601  N   SER A 481     109.441 149.883 125.030  1.00 73.26
ATOM   1602  CA  SER A 481     110.652 150.599 125.391  1.00 73.26
ATOM   1603  C   SER A 481     110.320 151.978 125.917  1.00 73.26
ATOM   1604  O   SER A 481     110.762 152.374 127.001  1.00 73.26
ATOM   1605  CB  SER A 481     111.554 150.716 124.177  1.00 73.26
ATOM   1606  OG  SER A 481     111.744 149.454 123.588  1.00 73.26
ATOM   1607  N   VAL A 482     109.499 152.707 125.171  1.00 73.15
ATOM   1608  CA  VAL A 482     109.081 154.034 125.591  1.00 73.15
ATOM   1609  C   VAL A 482     108.307 153.945 126.884  1.00 73.15
ATOM   1610  O   VAL A 482     108.405 154.827 127.735  1.00 73.15
ATOM   1611  CB  VAL A 482     108.239 154.704 124.499  1.00 73.15
ATOM   1612  CG1 VAL A 482     107.748 156.025 124.991  1.00 73.15
ATOM   1613  CG2 VAL A 482     109.029 154.880 123.232  1.00 73.15
ATOM   1614  N   SER A 483     107.479 152.911 127.024  1.00 73.74
ATOM   1615  CA  SER A 483     106.682 152.742 128.229  1.00 73.74
ATOM   1616  C   SER A 483     107.566 152.598 129.443  1.00 73.74
ATOM   1617  O   SER A 483     107.308 153.193 130.490  1.00 73.74
ATOM   1618  CB  SER A 483     105.791 151.520 128.086  1.00 73.74
ATOM   1619  OG  SER A 483     105.177 151.228 129.320  1.00 73.74
ATOM   1620  N   GLY A 484     108.608 151.790 129.325  1.00 73.98
ATOM   1621  CA  GLY A 484     109.579 151.710 130.393  1.00 73.98
ATOM   1622  C   GLY A 484     110.225 153.051 130.647  1.00 73.98
ATOM   1623  O   GLY A 484     110.444 153.441 131.794  1.00 73.98
ATOM   1624  N   GLY A 485     110.513 153.788 129.580  1.00 72.64
ATOM   1625  CA  GLY A 485     111.078 155.112 129.756  1.00 72.64
ATOM   1626  C   GLY A 485     110.172 156.016 130.559  1.00 72.64
ATOM   1627  O   GLY A 485     110.604 156.656 131.516  1.00 72.64
ATOM   1628  N   VAL A 486     108.895 156.044 130.203  1.00 73.59
ATOM   1629  CA  VAL A 486     107.942 156.896 130.893  1.00 73.59
ATOM   1630  C   VAL A 486     107.801 156.465 132.336  1.00 73.59
ATOM   1631  O   VAL A 486     107.690 157.299 133.240  1.00 73.59
ATOM   1632  CB  VAL A 486     106.589 156.873 130.172  1.00 73.59
ATOM   1633  CG1 VAL A 486     105.589 157.593 130.984  1.00 73.59
ATOM   1634  CG2 VAL A 486     106.703 157.526 128.820  1.00 73.59
ATOM   1635  N   TYR A 487     107.746 155.159 132.574  1.00 74.62
ATOM   1636  CA  TYR A 487     107.604 154.681 133.938  1.00 74.62
ATOM   1637  C   TYR A 487     108.775 155.119 134.785  1.00 74.62
ATOM   1638  O   TYR A 487     108.600 155.569 135.918  1.00 74.62
ATOM   1639  CB  TYR A 487     107.480 153.169 133.978  1.00 74.62
ATOM   1640  CG  TYR A 487     107.631 152.674 135.369  1.00 74.62
ATOM   1641  CD1 TYR A 487     106.641 152.874 136.289  1.00 74.62
ATOM   1642  CD2 TYR A 487     108.766 152.024 135.771  1.00 74.62
ATOM   1643  CE1 TYR A 487     106.774 152.440 137.577  1.00 74.62
ATOM   1644  CE2 TYR A 487     108.911 151.591 137.052  1.00 74.62
ATOM   1645  CZ  TYR A 487     107.908 151.789 137.951  1.00 74.62
ATOM   1646  OH  TYR A 487     108.052 151.353 139.242  1.00 74.62
ATOM   1647  N   PHE A 488     109.986 154.973 134.265  1.00 71.74
ATOM   1648  CA  PHE A 488     111.137 155.384 135.055  1.00 71.74
ATOM   1649  C   PHE A 488     111.152 156.881 135.250  1.00 71.74
ATOM   1650  O   PHE A 488     111.520 157.357 136.327  1.00 71.74
ATOM   1651  CB  PHE A 488     112.429 154.921 134.403  1.00 71.74
ATOM   1652  CG  PHE A 488     112.703 153.482 134.601  1.00 71.74
ATOM   1653  CD1 PHE A 488     112.991 152.996 135.848  1.00 71.74
ATOM   1654  CD2 PHE A 488     112.671 152.617 133.549  1.00 71.74
ATOM   1655  CE1 PHE A 488     113.231 151.682 136.037  1.00 71.74
ATOM   1656  CE2 PHE A 488     112.913 151.302 133.734  1.00 71.74
ATOM   1657  CZ  PHE A 488     113.195 150.830 134.977  1.00 71.74
ATOM   1658  N   PHE A 489     110.739 157.626 134.228  1.00 73.72
ATOM   1659  CA  PHE A 489     110.618 159.071 134.347  1.00 73.72
ATOM   1660  C   PHE A 489     109.730 159.436 135.521  1.00 73.72
ATOM   1661  O   PHE A 489     110.106 160.239 136.384  1.00 73.72
ATOM   1662  CB  PHE A 489     110.046 159.622 133.052  1.00 73.72
ATOM   1663  CG  PHE A 489     109.937 161.091 133.013  1.00 73.72
ATOM   1664  CD1 PHE A 489     111.055 161.873 132.953  1.00 73.72
ATOM   1665  CD2 PHE A 489     108.710 161.694 132.975  1.00 73.72
ATOM   1666  CE1 PHE A 489     110.952 163.235 132.891  1.00 73.72
ATOM   1667  CE2 PHE A 489     108.604 163.046 132.907  1.00 73.72
ATOM   1668  CZ  PHE A 489     109.727 163.819 132.863  1.00 73.72
ATOM   1669  N   PHE A 490     108.561 158.818 135.595  1.00 76.47
ATOM   1670  CA  PHE A 490     107.642 159.200 136.646  1.00 76.47
ATOM   1671  C   PHE A 490     108.095 158.685 138.001  1.00 76.47
ATOM   1672  O   PHE A 490     107.858 159.347 139.014  1.00 76.47
ATOM   1673  CB  PHE A 490     106.234 158.731 136.310  1.00 76.47
ATOM   1674  CG  PHE A 490     105.534 159.596 135.296  1.00 76.47
ATOM   1675  CD1 PHE A 490     105.283 160.933 135.546  1.00 76.47
ATOM   1676  CD2 PHE A 490     105.112 159.070 134.095  1.00 76.47
ATOM   1677  CE1 PHE A 490     104.645 161.716 134.613  1.00 76.47
ATOM   1678  CE2 PHE A 490     104.465 159.855 133.167  1.00 76.47
ATOM   1679  CZ  PHE A 490     104.235 161.173 133.426  1.00 76.47
ATOM   1680  N   ARG A 491     108.767 157.540 138.061  1.00 81.34
ATOM   1681  CA  ARG A 491     109.323 157.127 139.344  1.00 81.34
ATOM   1682  C   ARG A 491     110.350 158.128 139.823  1.00 81.34
ATOM   1683  O   ARG A 491     110.407 158.451 141.012  1.00 81.34
ATOM   1684  CB  ARG A 491     109.976 155.753 139.263  1.00 81.34
ATOM   1685  CG  ARG A 491     109.043 154.613 139.078  1.00 81.34
ATOM   1686  CD  ARG A 491     108.364 154.225 140.366  1.00 81.34
ATOM   1687  NE  ARG A 491     109.250 153.492 141.263  1.00 81.34
ATOM   1688  CZ  ARG A 491     108.912 153.056 142.477  1.00 81.34
ATOM   1689  NH1 ARG A 491     107.698 153.273 142.973  1.00 81.34
ATOM   1690  NH2 ARG A 491     109.797 152.396 143.207  1.00 81.34
ATOM   1691  N   GLY A 492     111.184 158.619 138.912  1.00 79.11
ATOM   1692  CA  GLY A 492     112.184 159.589 139.305  1.00 79.11
ATOM   1693  C   GLY A 492     111.559 160.869 139.806  1.00 79.11
ATOM   1694  O   GLY A 492     112.004 161.444 140.802  1.00 79.11
ATOM   1695  N   ILE A 493     110.522 161.339 139.120  1.00 79.15
ATOM   1696  CA  ILE A 493     109.856 162.547 139.580  1.00 79.15
ATOM   1697  C   ILE A 493     109.257 162.316 140.954  1.00 79.15
ATOM   1698  O   ILE A 493     109.373 163.166 141.835  1.00 79.15
ATOM   1699  CB  ILE A 493     108.794 163.011 138.577  1.00 79.15
ATOM   1700  CG1 ILE A 493     109.468 163.522 137.322  1.00 79.15
ATOM   1701  CG2 ILE A 493     107.954 164.105 139.207  1.00 79.15
ATOM   1702  CD1 ILE A 493     108.550 163.701 136.137  1.00 79.15
ATOM   1703  N   GLN A 494     108.581 161.183 141.151  1.00 84.65
ATOM   1704  CA  GLN A 494     108.004 160.905 142.461  1.00 84.65
ATOM   1705  C   GLN A 494     109.082 160.901 143.522  1.00 84.65
ATOM   1706  O   GLN A 494     108.897 161.442 144.616  1.00 84.65
ATOM   1707  CB  GLN A 494     107.285 159.564 142.456  1.00 84.65
ATOM   1708  CG  GLN A 494     106.010 159.549 141.672  1.00 84.65
ATOM   1709  CD  GLN A 494     105.480 158.144 141.447  1.00 84.65
ATOM   1710  OE1 GLN A 494     105.936 157.186 142.072  1.00 84.65
ATOM   1711  NE2 GLN A 494     104.507 158.018 140.551  1.00 84.65
ATOM   1712  N   TYR A 495     110.229 160.324 143.193  1.00 82.38
ATOM   1713  CA  TYR A 495     111.334 160.264 144.130  1.00 82.38
ATOM   1714  C   TYR A 495     111.786 161.660 144.522  1.00 82.38
ATOM   1715  O   TYR A 495     111.845 161.999 145.708  1.00 82.38
ATOM   1716  CB  TYR A 495     112.477 159.483 143.499  1.00 82.38
ATOM   1717  CG  TYR A 495     113.684 159.394 144.373  1.00 82.38
ATOM   1718  CD1 TYR A 495     113.771 158.442 145.353  1.00 82.38
ATOM   1719  CD2 TYR A 495     114.735 160.266 144.220  1.00 82.38
ATOM   1720  CE1 TYR A 495     114.869 158.355 146.149  1.00 82.38
ATOM   1721  CE2 TYR A 495     115.828 160.191 145.011  1.00 82.38
ATOM   1722  CZ  TYR A 495     115.892 159.234 145.976  1.00 82.38
ATOM   1723  OH  TYR A 495     116.995 159.151 146.780  1.00 82.38
ATOM   1724  N   PHE A 496     112.079 162.496 143.534  1.00 81.92
ATOM   1725  CA  PHE A 496     112.619 163.812 143.841  1.00 81.92
ATOM   1726  C   PHE A 496     111.573 164.706 144.490  1.00 81.92
ATOM   1727  O   PHE A 496     111.909 165.553 145.322  1.00 81.92
ATOM   1728  CB  PHE A 496     113.173 164.459 142.577  1.00 81.92
ATOM   1729  CG  PHE A 496     114.343 163.733 141.977  1.00 81.92
ATOM   1730  CD1 PHE A 496     115.424 163.359 142.747  1.00 81.92
ATOM   1731  CD2 PHE A 496     114.358 163.431 140.632  1.00 81.92
ATOM   1732  CE1 PHE A 496     116.479 162.699 142.190  1.00 81.92
ATOM   1733  CE2 PHE A 496     115.412 162.768 140.075  1.00 81.92
ATOM   1734  CZ  PHE A 496     116.473 162.403 140.851  1.00 81.92
ATOM   1735  N   LEU A 497     110.303 164.554 144.118  1.00 86.06
ATOM   1736  CA  LEU A 497     109.256 165.340 144.754  1.00 86.06
ATOM   1737  C   LEU A 497     109.092 164.954 146.207  1.00 86.06
ATOM   1738  O   LEU A 497     108.877 165.815 147.064  1.00 86.06
ATOM   1739  CB  LEU A 497     107.928 165.152 144.030  1.00 86.06
ATOM   1740  CG  LEU A 497     107.760 165.769 142.648  1.00 86.06
ATOM   1741  CD1 LEU A 497     106.354 165.507 142.173  1.00 86.06
ATOM   1742  CD2 LEU A 497     108.043 167.244 142.658  1.00 86.06
ATOM   1743  N   GLN A 498     109.169 163.662 146.504  1.00 87.62
ATOM   1744  CA  GLN A 498     109.048 163.239 147.886  1.00 87.62
ATOM   1745  C   GLN A 498     110.254 163.660 148.697  1.00 87.62
ATOM   1746  O   GLN A 498     110.105 164.058 149.855  1.00 87.62
ATOM   1747  CB  GLN A 498     108.887 161.735 147.949  1.00 87.62
ATOM   1748  CG  GLN A 498     107.563 161.249 147.448  1.00 87.62
ATOM   1749  CD  GLN A 498     107.583 159.772 147.116  1.00 87.62
ATOM   1750  OE1 GLN A 498     108.557 159.072 147.394  1.00 87.62
ATOM   1751  NE2 GLN A 498     106.502 159.288 146.516  1.00 87.62
ATOM   1752  N   ARG A 499     111.448 163.603 148.109  1.00 89.48
ATOM   1753  CA  ARG A 499     112.664 163.813 148.874  1.00 89.48
ATOM   1754  C   ARG A 499     113.130 165.251 148.863  1.00 89.48
ATOM   1755  O   ARG A 499     113.671 165.713 149.872  1.00 89.48
ATOM   1756  CB  ARG A 499     113.791 162.923 148.349  1.00 89.48
ATOM   1757  CG  ARG A 499     113.849 161.551 149.003  1.00 89.48
ATOM   1758  CD  ARG A 499     112.617 160.725 148.675  1.00 89.48
ATOM   1759  NE  ARG A 499     112.508 159.512 149.467  1.00 89.48
ATOM   1760  CZ  ARG A 499     111.474 158.676 149.402  1.00 89.48
ATOM   1761  NH1 ARG A 499     110.461 158.903 148.576  1.00 89.48
ATOM   1762  NH2 ARG A 499     111.449 157.601 150.166  1.00 89.48
ATOM   1763  N   ARG A 500     112.883 165.977 147.784  1.00 89.22
ATOM   1764  CA  ARG A 500     113.355 167.345 147.627  1.00 89.22
ATOM   1765  C   ARG A 500     114.854 167.470 147.944  1.00 89.22
ATOM   1766  O   ARG A 500     115.250 168.284 148.769  1.00 89.22
ATOM   1767  CB  ARG A 500     112.550 168.285 148.516  1.00 89.22
ATOM   1768  CG  ARG A 500     111.043 168.280 148.301  1.00 89.22
ATOM   1769  CD  ARG A 500     110.657 169.039 147.049  1.00 89.22
ATOM   1770  NE  ARG A 500     109.216 169.007 146.826  1.00 89.22
ATOM   1771  CZ  ARG A 500     108.596 169.622 145.821  1.00 89.22
ATOM   1772  NH1 ARG A 500     109.281 170.331 144.935  1.00 89.22
ATOM   1773  NH2 ARG A 500     107.280 169.531 145.704  1.00 89.22
ATOM   1774  N   PRO A 501     115.705 166.667 147.307  1.00 85.08
ATOM   1775  CA  PRO A 501     117.138 166.799 147.575  1.00 85.08
ATOM   1776  C   PRO A 501     117.667 168.126 147.063  1.00 85.08
ATOM   1777  O   PRO A 501     117.071 168.773 146.202  1.00 85.08
ATOM   1778  CB  PRO A 501     117.757 165.622 146.817  1.00 85.08
ATOM   1779  CG  PRO A 501     116.797 165.311 145.768  1.00 85.08
ATOM   1780  CD  PRO A 501     115.444 165.626 146.303  1.00 85.08
ATOM   1781  N   SER A 502     118.797 168.537 147.621  1.00 86.69
ATOM   1782  CA  SER A 502     119.466 169.758 147.201  1.00 86.69
ATOM   1783  C   SER A 502     120.572 169.442 146.208  1.00 86.69
ATOM   1784  O   SER A 502     121.079 168.322 146.133  1.00 86.69
ATOM   1785  CB  SER A 502     120.058 170.500 148.394  1.00 86.69
ATOM   1786  OG  SER A 502     121.204 169.824 148.876  1.00 86.69
ATOM   1787  N   LEU A 503     120.948 170.469 145.449  1.00 89.49
ATOM   1788  CA  LEU A 503     122.001 170.324 144.452  1.00 89.49
ATOM   1789  C   LEU A 503     123.331 169.969 145.097  1.00 89.49
ATOM   1790  O   LEU A 503     124.070 169.120 144.585  1.00 89.49
ATOM   1791  CB  LEU A 503     122.134 171.618 143.657  1.00 89.49
ATOM   1792  CG  LEU A 503     120.881 172.003 142.880  1.00 89.49
ATOM   1793  CD1 LEU A 503     120.933 173.469 142.470  1.00 89.49
ATOM   1794  CD2 LEU A 503     120.722 171.090 141.681  1.00 89.49
ATOM   1795  N   LYS A 504     123.655 170.609 146.220  1.00 87.72
ATOM   1796  CA  LYS A 504     124.956 170.388 146.835  1.00 87.72
ATOM   1797  C   LYS A 504     125.146 168.933 147.235  1.00 87.72
ATOM   1798  O   LYS A 504     126.283 168.459 147.305  1.00 87.72
ATOM   1799  CB  LYS A 504     125.135 171.312 148.038  1.00 87.72
ATOM   1800  CG  LYS A 504     125.422 172.758 147.660  1.00 87.72
ATOM   1801  CD  LYS A 504     125.714 173.617 148.877  1.00 87.72
ATOM   1802  CE  LYS A 504     125.767 175.091 148.506  1.00 87.72
ATOM   1803  NZ  LYS A 504     125.811 175.996 149.693  1.00 87.72
ATOM   1804  N   SER A 505     124.056 168.212 147.502  1.00 85.95
ATOM   1805  CA  SER A 505     124.107 166.785 147.792  1.00 85.95
ATOM   1806  C   SER A 505     123.131 165.998 146.928  1.00 85.95
ATOM   1807  O   SER A 505     122.610 164.966 147.356  1.00 85.95
ATOM   1808  CB  SER A 505     123.856 166.553 149.284  1.00 85.95
ATOM   1809  OG  SER A 505     125.068 166.693 150.004  1.00 85.95
ATOM   1810  N   LEU A 506     122.860 166.465 145.715  1.00 82.89
ATOM   1811  CA  LEU A 506     121.980 165.699 144.848  1.00 82.89
ATOM   1812  C   LEU A 506     122.601 164.359 144.487  1.00 82.89
ATOM   1813  O   LEU A 506     121.907 163.345 144.471  1.00 82.89
ATOM   1814  CB  LEU A 506     121.655 166.488 143.583  1.00 82.89
ATOM   1815  CG  LEU A 506     120.678 165.837 142.594  1.00 82.89
ATOM   1816  CD1 LEU A 506     119.329 165.700 143.233  1.00 82.89
ATOM   1817  CD2 LEU A 506     120.559 166.602 141.295  1.00 82.89
ATOM   1818  N   PHE A 507     123.905 164.333 144.199  1.00 77.94
ATOM   1819  CA  PHE A 507     124.575 163.119 143.753  1.00 77.94
ATOM   1820  C   PHE A 507     125.176 162.290 144.872  1.00 77.94
ATOM   1821  O   PHE A 507     125.289 161.074 144.717  1.00 77.94
ATOM   1822  CB  PHE A 507     125.705 163.456 142.790  1.00 77.94
ATOM   1823  CG  PHE A 507     125.251 164.069 141.528  1.00 77.94
ATOM   1824  CD1 PHE A 507     124.909 163.282 140.455  1.00 77.94
ATOM   1825  CD2 PHE A 507     125.177 165.437 141.403  1.00 77.94
ATOM   1826  CE1 PHE A 507     124.495 163.849 139.287  1.00 77.94
ATOM   1827  CE2 PHE A 507     124.762 166.010 140.234  1.00 77.94
ATOM   1828  CZ  PHE A 507     124.416 165.215 139.175  1.00 77.94
ATOM   1829  N   VAL A 508     125.586 162.908 145.980  1.00 86.57
ATOM   1830  CA  VAL A 508     126.213 162.153 147.060  1.00 86.57
ATOM   1831  C   VAL A 508     125.268 161.084 147.567  1.00 86.57
ATOM   1832  O   VAL A 508     125.689 159.969 147.887  1.00 86.57
ATOM   1833  CB  VAL A 508     126.656 163.090 148.204  1.00 86.57
ATOM   1834  CG1 VAL A 508     127.664 164.131 147.716  1.00 86.57
ATOM   1835  CG2 VAL A 508     125.464 163.765 148.867  1.00 86.57
ATOM   1836  N   ASP A 509     123.994 161.402 147.644  1.00 88.31
ATOM   1837  CA  ASP A 509     122.924 160.448 147.815  1.00 88.31
ATOM   1838  C   ASP A 509     122.168 160.390 146.498  1.00 88.31
ATOM   1839  O   ASP A 509     122.504 161.095 145.551  1.00 88.31
ATOM   1840  CB  ASP A 509     122.028 160.872 148.979  1.00 88.31
ATOM   1841  CG  ASP A 509     121.540 159.703 149.807  1.00 88.31
ATOM   1842  OD1 ASP A 509     121.597 158.545 149.345  1.00 88.31
ATOM   1843  OD2 ASP A 509     121.067 159.949 150.933  1.00 88.31
ATOM   1844  N   SER A 510     121.166 159.525 146.420  1.00 80.00
ATOM   1845  CA  SER A 510     120.216 159.549 145.315  1.00 80.00
ATOM   1846  C   SER A 510     120.872 159.346 143.964  1.00 80.00
ATOM   1847  O   SER A 510     120.339 159.787 142.950  1.00 80.00
ATOM   1848  CB  SER A 510     119.445 160.867 145.304  1.00 80.00
ATOM   1849  OG  SER A 510     118.912 161.139 146.586  1.00 80.00
ATOM   1850  N   TYR A 511     122.032 158.698 143.928  1.00 72.68
ATOM   1851  CA  TYR A 511     122.779 158.592 142.684  1.00 72.68
ATOM   1852  C   TYR A 511     122.049 157.723 141.676  1.00 72.68
ATOM   1853  O   TYR A 511     121.883 158.095 140.504  1.00 72.68
ATOM   1854  CB  TYR A 511     124.156 158.023 142.973  1.00 72.68
ATOM   1855  CG  TYR A 511     124.941 157.773 141.739  1.00 72.68
ATOM   1856  CD1 TYR A 511     125.257 158.796 140.891  1.00 72.68
ATOM   1857  CD2 TYR A 511     125.370 156.514 141.422  1.00 72.68
ATOM   1858  CE1 TYR A 511     125.971 158.572 139.767  1.00 72.68
ATOM   1859  CE2 TYR A 511     126.089 156.284 140.308  1.00 72.68
ATOM   1860  CZ  TYR A 511     126.388 157.319 139.482  1.00 72.68
ATOM   1861  OH  TYR A 511     127.101 157.101 138.340  1.00 72.68
ATOM   1862  N   SER A 512     121.595 156.557 142.123  1.00 73.99
ATOM   1863  CA  SER A 512     120.944 155.623 141.223  1.00 73.99
ATOM   1864  C   SER A 512     119.682 156.209 140.638  1.00 73.99
ATOM   1865  O   SER A 512     119.383 156.008 139.459  1.00 73.99
ATOM   1866  CB  SER A 512     120.622 154.350 141.970  1.00 73.99
ATOM   1867  OG  SER A 512     121.812 153.639 142.198  1.00 73.99
ATOM   1868  N   GLU A 513     118.924 156.919 141.450  1.00 77.78
ATOM   1869  CA  GLU A 513     117.673 157.456 140.967  1.00 77.78
ATOM   1870  C   GLU A 513     117.938 158.480 139.899  1.00 77.78
ATOM   1871  O   GLU A 513     117.204 158.571 138.913  1.00 77.78
ATOM   1872  CB  GLU A 513     116.901 158.059 142.116  1.00 77.78
ATOM   1873  CG  GLU A 513     116.351 157.010 143.045  1.00 77.78
ATOM   1874  CD  GLU A 513     117.384 156.442 144.005  1.00 77.78
ATOM   1875  OE1 GLU A 513     118.560 156.867 143.939  1.00 77.78
ATOM   1876  OE2 GLU A 513     117.023 155.556 144.808  1.00 77.78
ATOM   1877  N   ILE A 514     119.014 159.234 140.060  1.00 75.03
ATOM   1878  CA  ILE A 514     119.379 160.213 139.052  1.00 75.03
ATOM   1879  C   ILE A 514     119.721 159.514 137.758  1.00 75.03
ATOM   1880  O   ILE A 514     119.361 159.975 136.676  1.00 75.03
ATOM   1881  CB  ILE A 514     120.543 161.077 139.543  1.00 75.03
ATOM   1882  CG1 ILE A 514     120.087 161.908 140.735  1.00 75.03
ATOM   1883  CG2 ILE A 514     120.997 161.977 138.431  1.00 75.03
ATOM   1884  CD1 ILE A 514     121.173 162.322 141.629  1.00 75.03
ATOM   1885  N   LEU A 515     120.462 158.414 137.845  1.00 69.43
ATOM   1886  CA  LEU A 515     120.847 157.726 136.618  1.00 69.43
ATOM   1887  C   LEU A 515     119.649 157.126 135.909  1.00 69.43
ATOM   1888  O   LEU A 515     119.547 157.199 134.683  1.00 69.43
ATOM   1889  CB  LEU A 515     121.865 156.641 136.920  1.00 69.43
ATOM   1890  CG  LEU A 515     123.274 157.083 137.264  1.00 69.43
ATOM   1891  CD1 LEU A 515     124.091 155.863 137.589  1.00 69.43
ATOM   1892  CD2 LEU A 515     123.852 157.836 136.121  1.00 69.43
ATOM   1893  N   PHE A 516     118.744 156.512 136.653  1.00 69.80
ATOM   1894  CA  PHE A 516     117.545 155.986 136.019  1.00 69.80
ATOM   1895  C   PHE A 516     116.740 157.107 135.404  1.00 69.80
ATOM   1896  O   PHE A 516     116.238 156.991 134.279  1.00 69.80
ATOM   1897  CB  PHE A 516     116.686 155.246 137.028  1.00 69.80
ATOM   1898  CG  PHE A 516     117.091 153.841 137.251  1.00 69.80
ATOM   1899  CD1 PHE A 516     116.828 152.885 136.306  1.00 69.80
ATOM   1900  CD2 PHE A 516     117.704 153.471 138.414  1.00 69.80
ATOM   1901  CE1 PHE A 516     117.189 151.606 136.509  1.00 69.80
ATOM   1902  CE2 PHE A 516     118.065 152.193 138.618  1.00 69.80
ATOM   1903  CZ  PHE A 516     117.805 151.256 137.667  1.00 69.80
ATOM   1904  N   PHE A 517     116.630 158.210 136.125  1.00 71.67
ATOM   1905  CA  PHE A 517     115.877 159.333 135.621  1.00 71.67
ATOM   1906  C   PHE A 517     116.493 159.862 134.344  1.00 71.67
ATOM   1907  O   PHE A 517     115.782 160.168 133.388  1.00 71.67
ATOM   1908  CB  PHE A 517     115.818 160.415 136.686  1.00 71.67
ATOM   1909  CG  PHE A 517     114.903 161.513 136.347  1.00 71.67
ATOM   1910  CD1 PHE A 517     113.558 161.303 136.327  1.00 71.67
ATOM   1911  CD2 PHE A 517     115.383 162.752 136.037  1.00 71.67
ATOM   1912  CE1 PHE A 517     112.716 162.291 136.010  1.00 71.67
ATOM   1913  CE2 PHE A 517     114.539 163.747 135.715  1.00 71.67
ATOM   1914  CZ  PHE A 517     113.199 163.519 135.704  1.00 71.67
ATOM   1915  N   VAL A 518     117.817 159.953 134.300  1.00 67.40
ATOM   1916  CA  VAL A 518     118.487 160.492 133.126  1.00 67.40
ATOM   1917  C   VAL A 518     118.333 159.552 131.945  1.00 67.40
ATOM   1918  O   VAL A 518     118.197 159.993 130.798  1.00 67.40
ATOM   1919  CB  VAL A 518     119.958 160.778 133.452  1.00 67.40
ATOM   1920  CG1 VAL A 518     120.760 161.085 132.205  1.00 67.40
ATOM   1921  CG2 VAL A 518     120.044 161.921 134.415  1.00 67.40
ATOM   1922  N   GLN A 519     118.383 158.246 132.193  1.00 67.80
ATOM   1923  CA  GLN A 519     118.068 157.303 131.130  1.00 67.80
ATOM   1924  C   GLN A 519     116.707 157.611 130.559  1.00 67.80
ATOM   1925  O   GLN A 519     116.529 157.690 129.341  1.00 67.80
ATOM   1926  CB  GLN A 519     118.088 155.873 131.649  1.00 67.80
ATOM   1927  CG  GLN A 519     117.787 154.821 130.600  1.00 67.80
ATOM   1928  CD  GLN A 519     117.302 153.561 131.197  1.00 67.80
ATOM   1929  OE1 GLN A 519     117.604 153.251 132.339  1.00 67.80
ATOM   1930  NE2 GLN A 519     116.534 152.812 130.430  1.00 67.80
ATOM   1931  N   SER A 520     115.729 157.772 131.432  1.00 69.73
ATOM   1932  CA  SER A 520     114.389 158.026 130.947  1.00 69.73
ATOM   1933  C   SER A 520     114.319 159.342 130.196  1.00 69.73
ATOM   1934  O   SER A 520     113.614 159.436 129.193  1.00 69.73
ATOM   1935  CB  SER A 520     113.427 158.014 132.118  1.00 69.73
ATOM   1936  OG  SER A 520     113.920 158.831 133.161  1.00 69.73
ATOM   1937  N   LEU A 521     115.061 160.350 130.648  1.00 68.34
ATOM   1938  CA  LEU A 521     115.071 161.635 129.964  1.00 68.34
ATOM   1939  C   LEU A 521     115.569 161.471 128.547  1.00 68.34
ATOM   1940  O   LEU A 521     114.996 162.026 127.605  1.00 68.34
ATOM   1941  CB  LEU A 521     115.963 162.630 130.702  1.00 68.34
ATOM   1942  CG  LEU A 521     115.551 163.191 132.059  1.00 68.34
ATOM   1943  CD1 LEU A 521     116.648 164.064 132.610  1.00 68.34
ATOM   1944  CD2 LEU A 521     114.284 163.983 131.932  1.00 68.34
ATOM   1945  N   PHE A 522     116.636 160.702 128.377  1.00 65.48
ATOM   1946  CA  PHE A 522     117.139 160.452 127.038  1.00 65.48
ATOM   1947  C   PHE A 522     116.140 159.667 126.216  1.00 65.48
ATOM   1948  O   PHE A 522     115.998 159.906 125.018  1.00 65.48
ATOM   1949  CB  PHE A 522     118.453 159.705 127.101  1.00 65.48
ATOM   1950  CG  PHE A 522     119.630 160.585 127.188  1.00 65.48
ATOM   1951  CD1 PHE A 522     120.115 160.981 128.396  1.00 65.48
ATOM   1952  CD2 PHE A 522     120.255 161.013 126.053  1.00 65.48
ATOM   1953  CE1 PHE A 522     121.202 161.774 128.479  1.00 65.48
ATOM   1954  CE2 PHE A 522     121.345 161.822 126.129  1.00 65.48
ATOM   1955  CZ  PHE A 522     121.818 162.201 127.346  1.00 65.48
ATOM   1956  N   MET A 523     115.457 158.709 126.827  1.00 67.53
ATOM   1957  CA  MET A 523     114.461 157.957 126.080  1.00 67.53
ATOM   1958  C   MET A 523     113.380 158.887 125.564  1.00 67.53
ATOM   1959  O   MET A 523     112.987 158.825 124.394  1.00 67.53
ATOM   1960  CB  MET A 523     113.854 156.876 126.963  1.00 67.53
ATOM   1961  CG  MET A 523     112.802 156.040 126.287  1.00 67.53
ATOM   1962  SD  MET A 523     113.448 154.967 125.012  1.00 67.53
ATOM   1963  CE  MET A 523     113.733 153.511 125.988  1.00 67.53
ATOM   1964  N   LEU A 524     112.899 159.774 126.424  1.00 68.64
ATOM   1965  CA  LEU A 524     111.832 160.677 126.029  1.00 68.64
ATOM   1966  C   LEU A 524     112.299 161.635 124.956  1.00 68.64
ATOM   1967  O   LEU A 524     111.571 161.898 123.996  1.00 68.64
ATOM   1968  CB  LEU A 524     111.342 161.444 127.237  1.00 68.64
ATOM   1969  CG  LEU A 524     110.732 160.560 128.310  1.00 68.64
ATOM   1970  CD1 LEU A 524     110.546 161.355 129.573  1.00 68.64
ATOM   1971  CD2 LEU A 524     109.429 159.973 127.837  1.00 68.64
ATOM   1972  N   VAL A 525     113.508 162.171 125.103  1.00 66.05
ATOM   1973  CA  VAL A 525     114.055 163.024 124.062  1.00 66.05
ATOM   1974  C   VAL A 525     114.117 162.260 122.757  1.00 66.05
ATOM   1975  O   VAL A 525     113.887 162.818 121.677  1.00 66.05
ATOM   1976  CB  VAL A 525     115.440 163.543 124.470  1.00 66.05
ATOM   1977  CG1 VAL A 525     116.128 164.201 123.294  1.00 66.05
ATOM   1978  CG2 VAL A 525     115.322 164.504 125.616  1.00 66.05
ATOM   1979  N   SER A 526     114.442 160.975 122.829  1.00 68.29
ATOM   1980  CA  SER A 526     114.454 160.182 121.618  1.00 68.29
ATOM   1981  C   SER A 526     113.064 160.085 121.030  1.00 68.29
ATOM   1982  O   SER A 526     112.905 160.112 119.813  1.00 68.29
ATOM   1983  CB  SER A 526     115.014 158.797 121.881  1.00 68.29
ATOM   1984  OG  SER A 526     115.401 158.223 120.651  1.00 68.29
ATOM   1985  N   VAL A 527     112.042 159.971 121.870  1.00 68.61
ATOM   1986  CA  VAL A 527     110.683 159.936 121.334  1.00 68.61
ATOM   1987  C   VAL A 527     110.366 161.232 120.621  1.00 68.61
ATOM   1988  O   VAL A 527     109.841 161.233 119.502  1.00 68.61
ATOM   1989  CB  VAL A 527     109.658 159.682 122.443  1.00 68.61
ATOM   1990  CG1 VAL A 527     108.260 159.788 121.875  1.00 68.61
ATOM   1991  CG2 VAL A 527     109.875 158.353 123.069  1.00 68.61
ATOM   1992  N   VAL A 528     110.667 162.353 121.270  1.00 68.54
ATOM   1993  CA  VAL A 528     110.343 163.662 120.715  1.00 68.54
ATOM   1994  C   VAL A 528     111.009 163.834 119.365  1.00 68.54
ATOM   1995  O   VAL A 528     110.378 164.244 118.386  1.00 68.54
ATOM   1996  CB  VAL A 528     110.768 164.768 121.687  1.00 68.54
ATOM   1997  CG1 VAL A 528     110.644 166.118 121.028  1.00 68.54
ATOM   1998  CG2 VAL A 528     109.948 164.685 122.935  1.00 68.54
ATOM   1999  N   LEU A 529     112.292 163.510 119.289  1.00 67.46
ATOM   2000  CA  LEU A 529     112.974 163.602 118.011  1.00 67.46
ATOM   2001  C   LEU A 529     112.414 162.594 117.028  1.00 67.46
ATOM   2002  O   LEU A 529     112.337 162.872 115.833  1.00 67.46
ATOM   2003  CB  LEU A 529     114.459 163.406 118.220  1.00 67.46
ATOM   2004  CG  LEU A 529     115.075 164.574 118.974  1.00 67.46
ATOM   2005  CD1 LEU A 529     116.317 164.133 119.671  1.00 67.46
ATOM   2006  CD2 LEU A 529     115.374 165.718 118.044  1.00 67.46
ATOM   2007  N   TYR A 530     112.005 161.425 117.512  1.00 70.67
ATOM   2008  CA  TYR A 530     111.523 160.384 116.619  1.00 70.67
ATOM   2009  C   TYR A 530     110.277 160.836 115.901  1.00 70.67
ATOM   2010  O   TYR A 530     110.072 160.513 114.727  1.00 70.67
ATOM   2011  CB  TYR A 530     111.244 159.097 117.383  1.00 70.67
ATOM   2012  CG  TYR A 530     110.583 158.058 116.518  1.00 70.67
ATOM   2013  CD1 TYR A 530     111.307 157.344 115.595  1.00 70.67
ATOM   2014  CD2 TYR A 530     109.232 157.810 116.609  1.00 70.67
ATOM   2015  CE1 TYR A 530     110.707 156.406 114.800  1.00 70.67
ATOM   2016  CE2 TYR A 530     108.624 156.876 115.817  1.00 70.67
ATOM   2017  CZ  TYR A 530     109.362 156.178 114.912  1.00 70.67
ATOM   2018  OH  TYR A 530     108.746 155.246 114.114  1.00 70.67
ATOM   2019  N   PHE A 531     109.401 161.528 116.610  1.00 70.87
ATOM   2020  CA  PHE A 531     108.223 162.086 115.975  1.00 70.87
ATOM   2021  C   PHE A 531     108.443 163.488 115.450  1.00 70.87
ATOM   2022  O   PHE A 531     107.627 163.953 114.655  1.00 70.87
ATOM   2023  CB  PHE A 531     107.066 162.065 116.949  1.00 70.87
ATOM   2024  CG  PHE A 531     106.585 160.699 117.255  1.00 70.87
ATOM   2025  CD1 PHE A 531     106.017 159.923 116.270  1.00 70.87
ATOM   2026  CD2 PHE A 531     106.702 160.184 118.516  1.00 70.87
ATOM   2027  CE1 PHE A 531     105.578 158.673 116.537  1.00 70.87
ATOM   2028  CE2 PHE A 531     106.266 158.929 118.785  1.00 70.87
ATOM   2029  CZ  PHE A 531     105.700 158.172 117.793  1.00 70.87
ATOM   2030  N   SER A 532     109.525 164.157 115.824  1.00 71.41
ATOM   2031  CA  SER A 532     109.853 165.443 115.232  1.00 71.41
ATOM   2032  C   SER A 532     110.579 165.308 113.916  1.00 71.41
ATOM   2033  O   SER A 532     111.182 166.281 113.462  1.00 71.41
ATOM   2034  CB  SER A 532     110.707 166.275 116.175  1.00 71.41
ATOM   2035  OG  SER A 532     110.063 166.443 117.417  1.00 71.41
ATOM   2036  N   GLN A 533     110.571 164.126 113.314  1.00 75.23
ATOM   2037  CA  GLN A 533     111.129 163.931 111.989  1.00 75.23
ATOM   2038  C   GLN A 533     112.608 164.285 111.955  1.00 75.23
ATOM   2039  O   GLN A 533     113.087 164.942 111.030  1.00 75.23
ATOM   2040  CB  GLN A 533     110.349 164.732 110.956  1.00 75.23
ATOM   2041  CG  GLN A 533     108.865 164.466 110.972  1.00 75.23
ATOM   2042  CD  GLN A 533     108.157 165.201 109.865  1.00 75.23
ATOM   2043  OE1 GLN A 533     108.777 165.618 108.887  1.00 75.23
ATOM   2044  NE2 GLN A 533     106.855 165.384 110.016  1.00 75.23
ATOM   2045  N   ARG A 534     113.327 163.846 112.982  1.00 72.96
ATOM   2046  CA  ARG A 534     114.762 164.034 113.110  1.00 72.96
ATOM   2047  C   ARG A 534     115.429 162.677 113.216  1.00 72.96
ATOM   2048  O   ARG A 534     115.001 161.835 114.004  1.00 72.96
ATOM   2049  CB  ARG A 534     115.103 164.857 114.345  1.00 72.96
ATOM   2050  CG  ARG A 534     114.459 166.205 114.394  1.00 72.96
ATOM   2051  CD  ARG A 534     114.853 167.076 113.220  1.00 72.96
ATOM   2052  NE  ARG A 534     116.293 167.277 113.146  1.00 72.96
ATOM   2053  CZ  ARG A 534     116.904 167.965 112.190  1.00 72.96
ATOM   2054  NH1 ARG A 534     118.221 168.095 112.215  1.00 72.96
ATOM   2055  NH2 ARG A 534     116.213 168.522 111.203  1.00 72.96
ATOM   2056  N   LYS A 535     116.474 162.467 112.426  1.00 69.61
ATOM   2057  CA  LYS A 535     117.280 161.268 112.580  1.00 69.61
ATOM   2058  C   LYS A 535     117.986 161.234 113.925  1.00 69.61
ATOM   2059  O   LYS A 535     118.216 160.153 114.477  1.00 69.61
ATOM   2060  CB  LYS A 535     118.281 161.219 111.445  1.00 69.61
ATOM   2061  CG  LYS A 535     118.871 159.877 111.142  1.00 69.61
ATOM   2062  CD  LYS A 535     119.810 160.041 109.960  1.00 69.61
ATOM   2063  CE  LYS A 535     120.789 158.905 109.803  1.00 69.61
ATOM   2064  NZ  LYS A 535     121.947 159.353 108.972  1.00 69.61
ATOM   2065  N   GLU A 536     118.243 162.394 114.517  1.00 69.92
ATOM   2066  CA  GLU A 536     119.026 162.472 115.736  1.00 69.92
ATOM   2067  C   GLU A 536     118.423 161.723 116.899  1.00 69.92
ATOM   2068  O   GLU A 536     119.073 161.647 117.942  1.00 69.92
ATOM   2069  CB  GLU A 536     119.192 163.923 116.171  1.00 69.92
ATOM   2070  CG  GLU A 536     120.250 164.698 115.436  1.00 69.92
ATOM   2071  CD  GLU A 536     119.850 165.037 114.020  1.00 69.92
ATOM   2072  OE1 GLU A 536     119.210 164.190 113.369  1.00 69.92
ATOM   2073  OE2 GLU A 536     120.175 166.153 113.560  1.00 69.92
ATOM   2074  N   TYR A 537     117.204 161.203 116.785  1.00 67.73
ATOM   2075  CA  TYR A 537     116.679 160.398 117.871  1.00 67.73
ATOM   2076  C   TYR A 537     117.595 159.239 118.180  1.00 67.73
ATOM   2077  O   TYR A 537     117.714 158.848 119.347  1.00 67.73
ATOM   2078  CB  TYR A 537     115.298 159.878 117.538  1.00 67.73
ATOM   2079  CG  TYR A 537     115.290 158.697 116.627  1.00 67.73
ATOM   2080  CD1 TYR A 537     115.596 158.837 115.299  1.00 67.73
ATOM   2081  CD2 TYR A 537     114.963 157.447 117.094  1.00 67.73
ATOM   2082  CE1 TYR A 537     115.581 157.778 114.460  1.00 67.73
ATOM   2083  CE2 TYR A 537     114.942 156.381 116.264  1.00 67.73
ATOM   2084  CZ  TYR A 537     115.254 156.551 114.945  1.00 67.73
ATOM   2085  OH  TYR A 537     115.238 155.481 114.094  1.00 67.73
ATOM   2086  N   VAL A 538     118.293 158.712 117.165  1.00 65.53
ATOM   2087  CA  VAL A 538     119.216 157.619 117.424  1.00 65.53
ATOM   2088  C   VAL A 538     120.253 158.070 118.416  1.00 65.53
ATOM   2089  O   VAL A 538     120.493 157.404 119.422  1.00 65.53
ATOM   2090  CB  VAL A 538     119.878 157.131 116.132  1.00 65.53
ATOM   2091  CG1 VAL A 538     120.874 156.059 116.456  1.00 65.53
ATOM   2092  CG2 VAL A 538     118.853 156.645 115.164  1.00 65.53
ATOM   2093  N   ALA A 539     120.788 159.266 118.208  1.00 64.80
ATOM   2094  CA  ALA A 539     121.815 159.787 119.090  1.00 64.80
ATOM   2095  C   ALA A 539     121.338 159.832 120.523  1.00 64.80
ATOM   2096  O   ALA A 539     122.135 159.700 121.447  1.00 64.80
ATOM   2097  CB  ALA A 539     122.239 161.175 118.634  1.00 64.80
ATOM   2098  N   SER A 540     120.047 160.011 120.733  1.00 65.60
ATOM   2099  CA  SER A 540     119.553 160.032 122.095  1.00 65.60
ATOM   2100  C   SER A 540     119.322 158.633 122.607  1.00 65.60
ATOM   2101  O   SER A 540     119.742 158.297 123.718  1.00 65.60
ATOM   2102  CB  SER A 540     118.271 160.823 122.141  1.00 65.60
ATOM   2103  OG  SER A 540     118.405 161.942 121.290  1.00 65.60
ATOM   2104  N   MET A 541     118.708 157.798 121.772  1.00 65.04
ATOM   2105  CA  MET A 541     118.269 156.482 122.210  1.00 65.04
ATOM   2106  C   MET A 541     119.436 155.685 122.725  1.00 65.04
ATOM   2107  O   MET A 541     119.369 155.099 123.807  1.00 65.04
ATOM   2108  CB  MET A 541     117.621 155.759 121.044  1.00 65.04
ATOM   2109  CG  MET A 541     117.241 154.334 121.295  1.00 65.04
ATOM   2110  SD  MET A 541     116.266 153.703 119.937  1.00 65.04
ATOM   2111  CE  MET A 541     117.486 153.664 118.655  1.00 65.04
ATOM   2112  N   VAL A 542     120.547 155.725 121.992  1.00 62.35
ATOM   2113  CA  VAL A 542     121.695 154.916 122.346  1.00 62.35
ATOM   2114  C   VAL A 542     122.208 155.289 123.716  1.00 62.35
ATOM   2115  O   VAL A 542     122.579 154.406 124.486  1.00 62.35
ATOM   2116  CB  VAL A 542     122.805 155.030 121.298  1.00 62.35
ATOM   2117  CG1 VAL A 542     122.310 154.587 119.936  1.00 62.35
ATOM   2118  CG2 VAL A 542     123.352 156.413 121.250  1.00 62.35
ATOM   2119  N   PHE A 543     122.197 156.566 124.082  1.00 61.75
ATOM   2120  CA  PHE A 543     122.679 156.872 125.417  1.00 61.75
ATOM   2121  C   PHE A 543     121.761 156.258 126.440  1.00 61.75
ATOM   2122  O   PHE A 543     122.226 155.575 127.358  1.00 61.75
ATOM   2123  CB  PHE A 543     122.809 158.366 125.634  1.00 61.75
ATOM   2124  CG  PHE A 543     124.028 158.930 125.036  1.00 61.75
ATOM   2125  CD1 PHE A 543     125.238 158.797 125.656  1.00 61.75
ATOM   2126  CD2 PHE A 543     123.969 159.576 123.844  1.00 61.75
ATOM   2127  CE1 PHE A 543     126.357 159.302 125.095  1.00 61.75
ATOM   2128  CE2 PHE A 543     125.080 160.088 123.280  1.00 61.75
ATOM   2129  CZ  PHE A 543     126.279 159.956 123.904  1.00 61.75
ATOM   2130  N   SER A 544     120.457 156.367 126.214  1.00 63.57
ATOM   2131  CA  SER A 544     119.527 155.670 127.079  1.00 63.57
ATOM   2132  C   SER A 544     119.829 154.190 127.079  1.00 63.57
ATOM   2133  O   SER A 544     119.966 153.576 128.142  1.00 63.57
ATOM   2134  CB  SER A 544     118.108 155.901 126.624  1.00 63.57
ATOM   2135  OG  SER A 544     117.244 155.241 127.507  1.00 63.57
ATOM   2136  N   LEU A 545     120.075 153.638 125.898  1.00 60.02
ATOM   2137  CA  LEU A 545     120.412 152.230 125.794  1.00 60.02
ATOM   2138  C   LEU A 545     121.694 151.934 126.541  1.00 60.02
ATOM   2139  O   LEU A 545     121.728 151.046 127.395  1.00 60.02
ATOM   2140  CB  LEU A 545     120.529 151.864 124.331  1.00 60.02
ATOM   2141  CG  LEU A 545     120.765 150.445 123.905  1.00 60.02
ATOM   2142  CD1 LEU A 545     119.821 149.547 124.582  1.00 60.02
ATOM   2143  CD2 LEU A 545     120.599 150.385 122.413  1.00 60.02
ATOM   2144  N   ALA A 546     122.727 152.746 126.316  1.00 57.69
ATOM   2145  CA  ALA A 546     123.973 152.565 127.040  1.00 57.69
ATOM   2146  C   ALA A 546     123.749 152.739 128.520  1.00 57.69
ATOM   2147  O   ALA A 546     124.360 152.051 129.335  1.00 57.69
ATOM   2148  CB  ALA A 546     125.004 153.565 126.564  1.00 57.69
ATOM   2149  N   MET A 547     122.880 153.661 128.890  1.00 62.73
ATOM   2150  CA  MET A 547     122.593 153.820 130.299  1.00 62.73
ATOM   2151  C   MET A 547     121.727 152.695 130.794  1.00 62.73
ATOM   2152  O   MET A 547     121.920 152.212 131.913  1.00 62.73
ATOM   2153  CB  MET A 547     121.932 155.158 130.549  1.00 62.73
ATOM   2154  CG  MET A 547     122.911 156.241 130.493  1.00 62.73
ATOM   2155  SD  MET A 547     122.336 157.696 131.287  1.00 62.73
ATOM   2156  CE  MET A 547     121.634 158.410 129.832  1.00 62.73
ATOM   2157  N   GLY A 548     120.790 152.248 129.964  1.00 61.33
ATOM   2158  CA  GLY A 548     119.849 151.262 130.428  1.00 61.33
ATOM   2159  C   GLY A 548     120.562 150.018 130.879  1.00 61.33
ATOM   2160  O   GLY A 548     120.440 149.610 132.033  1.00 61.33
ATOM   2161  N   TRP A 549     121.450 149.517 130.038  1.00 59.16
ATOM   2162  CA  TRP A 549     122.232 148.364 130.418  1.00 59.16
ATOM   2163  C   TRP A 549     123.069 148.662 131.628  1.00 59.16
ATOM   2164  O   TRP A 549     123.076 147.886 132.583  1.00 59.16
ATOM   2165  CB  TRP A 549     123.111 147.944 129.266  1.00 59.16
ATOM   2166  CG  TRP A 549     122.374 147.174 128.341  1.00 59.16
ATOM   2167  CD1 TRP A 549     121.973 147.536 127.113  1.00 59.16
ATOM   2168  CD2 TRP A 549     121.881 145.873 128.567  1.00 59.16
ATOM   2169  NE1 TRP A 549     121.264 146.525 126.538  1.00 59.16
ATOM   2170  CE2 TRP A 549     121.195 145.488 127.426  1.00 59.16
ATOM   2171  CE3 TRP A 549     121.958 144.990 129.636  1.00 59.16
ATOM   2172  CZ2 TRP A 549     120.595 144.266 127.320  1.00 59.16
ATOM   2173  CZ3 TRP A 549     121.376 143.792 129.526  1.00 59.16
ATOM   2174  CH2 TRP A 549     120.703 143.428 128.385  1.00 59.16
ATOM   2175  N   THR A 550     123.717 149.814 131.644  1.00 61.07
ATOM   2176  CA  THR A 550     124.587 150.113 132.763  1.00 61.07
ATOM   2177  C   THR A 550     123.791 150.227 134.044  1.00 61.07
ATOM   2178  O   THR A 550     124.272 149.852 135.119  1.00 61.07
ATOM   2179  CB  THR A 550     125.362 151.380 132.488  1.00 61.07
ATOM   2180  OG1 THR A 550     126.206 151.159 131.359  1.00 61.07
ATOM   2181  CG2 THR A 550     126.205 151.733 133.673  1.00 61.07
ATOM   2182  N   ASN A 551     122.537 150.645 133.947  1.00 66.12
ATOM   2183  CA  ASN A 551     121.786 150.777 135.177  1.00 66.12
ATOM   2184  C   ASN A 551     121.507 149.448 135.825  1.00 66.12
ATOM   2185  O   ASN A 551     121.093 149.436 136.981  1.00 66.12
ATOM   2186  CB  ASN A 551     120.466 151.474 134.922  1.00 66.12
ATOM   2187  CG  ASN A 551     120.634 152.873 134.501  1.00 66.12
ATOM   2188  OD1 ASN A 551     121.563 153.540 134.918  1.00 66.12
ATOM   2189  ND2 ASN A 551     119.728 153.346 133.660  1.00 66.12
ATOM   2190  N   MET A 552     121.739 148.334 135.137  1.00 65.37
ATOM   2191  CA  MET A 552     121.581 147.049 135.783  1.00 65.37
ATOM   2192  C   MET A 552     122.445 146.930 137.007  1.00 65.37
ATOM   2193  O   MET A 552     122.064 146.225 137.940  1.00 65.37
ATOM   2194  CB  MET A 552     121.932 145.922 134.840  1.00 65.37
ATOM   2195  CG  MET A 552     120.877 145.641 133.896  1.00 65.37
ATOM   2196  SD  MET A 552     121.256 144.207 132.960  1.00 65.37
ATOM   2197  CE  MET A 552     119.644 143.952 132.292  1.00 65.37
ATOM   2198  N   LEU A 553     123.556 147.655 137.068  1.00 65.66
ATOM   2199  CA  LEU A 553     124.387 147.565 138.252  1.00 65.66
ATOM   2200  C   LEU A 553     123.654 148.015 139.495  1.00 65.66
ATOM   2201  O   LEU A 553     124.058 147.646 140.598  1.00 65.66
ATOM   2202  CB  LEU A 553     125.641 148.392 138.077  1.00 65.66
ATOM   2203  CG  LEU A 553     126.509 148.006 136.906  1.00 65.66
ATOM   2204  CD1 LEU A 553     127.575 149.047 136.759  1.00 65.66
ATOM   2205  CD2 LEU A 553     127.097 146.647 137.129  1.00 65.66
ATOM   2206  N   TYR A 554     122.598 148.805 139.340  1.00 71.47
ATOM   2207  CA  TYR A 554     121.788 149.190 140.477  1.00 71.47
ATOM   2208  C   TYR A 554     121.348 147.976 141.245  1.00 71.47
ATOM   2209  O   TYR A 554     121.419 147.952 142.474  1.00 71.47
ATOM   2210  CB  TYR A 554     120.571 149.964 140.009  1.00 71.47
ATOM   2211  CG  TYR A 554     119.464 149.993 141.006  1.00 71.47
ATOM   2212  CD1 TYR A 554     119.591 150.688 142.185  1.00 71.47
ATOM   2213  CD2 TYR A 554     118.284 149.338 140.759  1.00 71.47
ATOM   2214  CE1 TYR A 554     118.582 150.728 143.079  1.00 71.47
ATOM   2215  CE2 TYR A 554     117.270 149.365 141.654  1.00 71.47
ATOM   2216  CZ  TYR A 554     117.427 150.057 142.819  1.00 71.47
ATOM   2217  OH  TYR A 554     116.402 150.091 143.720  1.00 71.47
ATOM   2218  N   TYR A 555     120.919 146.942 140.533  1.00 72.83
ATOM   2219  CA  TYR A 555     120.447 145.748 141.215  1.00 72.83
ATOM   2220  C   TYR A 555     121.595 144.995 141.830  1.00 72.83
ATOM   2221  O   TYR A 555     121.435 144.360 142.866  1.00 72.83
ATOM   2222  CB  TYR A 555     119.704 144.859 140.244  1.00 72.83
ATOM   2223  CG  TYR A 555     118.596 145.603 139.594  1.00 72.83
ATOM   2224  CD1 TYR A 555     117.427 145.845 140.260  1.00 72.83
ATOM   2225  CD2 TYR A 555     118.739 146.105 138.334  1.00 72.83
ATOM   2226  CE1 TYR A 555     116.434 146.539 139.676  1.00 72.83
ATOM   2227  CE2 TYR A 555     117.746 146.782 137.746  1.00 72.83
ATOM   2228  CZ  TYR A 555     116.602 147.000 138.412  1.00 72.83
ATOM   2229  OH  TYR A 555     115.613 147.695 137.793  1.00 72.83
ATOM   2230  N   THR A 556     122.760 145.084 141.221  1.00 76.21
ATOM   2231  CA  THR A 556     123.898 144.415 141.774  1.00 76.21
ATOM   2232  C   THR A 556     124.246 144.959 143.149  1.00 76.21
ATOM   2233  O   THR A 556     124.860 144.254 143.943  1.00 76.21
ATOM   2234  CB  THR A 556     125.050 144.544 140.794  1.00 76.21
ATOM   2235  OG1 THR A 556     124.733 143.780 139.645  1.00 76.21
ATOM   2236  CG2 THR A 556     126.302 144.033 141.354  1.00 76.21
ATOM   2237  N   ARG A 557     123.847 146.173 143.459  1.00 80.05
ATOM   2238  CA  ARG A 557     123.898 146.645 144.823  1.00 80.05
ATOM   2239  C   ARG A 557     122.879 145.863 145.624  1.00 80.05
ATOM   2240  O   ARG A 557     121.784 145.565 145.150  1.00 80.05
ATOM   2241  CB  ARG A 557     123.569 148.116 144.904  1.00 80.05
ATOM   2242  CG  ARG A 557     124.375 148.966 143.955  1.00 80.05
ATOM   2243  CD  ARG A 557     124.014 150.417 144.054  1.00 80.05
ATOM   2244  NE  ARG A 557     124.085 150.932 145.413  1.00 80.05
ATOM   2245  CZ  ARG A 557     123.941 152.206 145.745  1.00 80.05
ATOM   2246  NH1 ARG A 557     123.747 153.137 144.827  1.00 80.05
ATOM   2247  NH2 ARG A 557     124.005 152.552 147.016  1.00 80.05
ATOM   2248  N   GLY A 558     123.240 145.509 146.832  1.00 88.64
ATOM   2249  CA  GLY A 558     122.419 144.658 147.655  1.00 88.64
ATOM   2250  C   GLY A 558     122.796 143.201 147.618  1.00 88.64
ATOM   2251  O   GLY A 558     122.214 142.422 148.363  1.00 88.64
ATOM   2252  N   PHE A 559     123.764 142.835 146.791  1.00 84.22
ATOM   2253  CA  PHE A 559     124.412 141.537 146.830  1.00 84.22
ATOM   2254  C   PHE A 559     125.763 141.797 147.452  1.00 84.22
ATOM   2255  O   PHE A 559     126.520 142.592 146.915  1.00 84.22
ATOM   2256  CB  PHE A 559     124.546 140.914 145.452  1.00 84.22
ATOM   2257  CG  PHE A 559     123.248 140.574 144.819  1.00 84.22
ATOM   2258  CD1 PHE A 559     122.387 141.556 144.411  1.00 84.22
ATOM   2259  CD2 PHE A 559     122.928 139.268 144.574  1.00 84.22
ATOM   2260  CE1 PHE A 559     121.210 141.249 143.813  1.00 84.22
ATOM   2261  CE2 PHE A 559     121.754 138.958 143.963  1.00 84.22
ATOM   2262  CZ  PHE A 559     120.883 139.963 143.583  1.00 84.22
ATOM   2263  N   GLN A 560     126.020 141.191 148.612  1.00 90.42
ATOM   2264  CA  GLN A 560     127.230 141.476 149.360  1.00 90.42
ATOM   2265  C   GLN A 560     128.462 141.258 148.502  1.00 90.42
ATOM   2266  O   GLN A 560     129.325 142.134 148.407  1.00 90.42
ATOM   2267  CB  GLN A 560     127.275 140.597 150.602  1.00 90.42
ATOM   2268  CG  GLN A 560     128.561 140.674 151.417  1.00 90.42
ATOM   2269  CD  GLN A 560     128.961 142.092 151.771  1.00 90.42
ATOM   2270  OE1 GLN A 560     129.293 142.908 150.905  1.00 90.42
ATOM   2271  NE2 GLN A 560     128.972 142.388 153.046  1.00 90.42
ATOM   2272  N   GLN A 561     128.519 140.137 147.801  1.00 81.46
ATOM   2273  CA  GLN A 561     129.641 139.905 146.909  1.00 81.46
ATOM   2274  C   GLN A 561     129.582 140.835 145.717  1.00 81.46
ATOM   2275  O   GLN A 561     130.425 141.723 145.579  1.00 81.46
ATOM   2276  CB  GLN A 561     129.678 138.441 146.469  1.00 81.46
ATOM   2277  CG  GLN A 561     130.966 138.024 145.803  1.00 81.46
ATOM   2278  CD  GLN A 561     131.086 136.517 145.716  1.00 81.46
ATOM   2279  OE1 GLN A 561     130.679 135.807 146.635  1.00 81.46
ATOM   2280  NE2 GLN A 561     131.652 136.020 144.620  1.00 81.46
ATOM   2281  N   MET A 562     128.557 140.711 144.894  1.00 78.66
ATOM   2282  CA  MET A 562     128.623 141.333 143.587  1.00 78.66
ATOM   2283  C   MET A 562     128.381 142.820 143.620  1.00 78.66
ATOM   2284  O   MET A 562     128.778 143.502 142.681  1.00 78.66
ATOM   2285  CB  MET A 562     127.610 140.708 142.643  1.00 78.66
ATOM   2286  CG  MET A 562     127.962 139.323 142.244  1.00 78.66
ATOM   2287  SD  MET A 562     126.820 138.708 141.018  1.00 78.66
ATOM   2288  CE  MET A 562     127.527 139.434 139.567  1.00 78.66
ATOM   2289  N   GLY A 563     127.814 143.344 144.688  1.00 81.85
ATOM   2290  CA  GLY A 563     127.602 144.768 144.764  1.00 81.85
ATOM   2291  C   GLY A 563     128.816 145.586 145.115  1.00 81.85
ATOM   2292  O   GLY A 563     128.714 146.810 145.194  1.00 81.85
ATOM   2293  N   ILE A 564     129.960 144.956 145.340  1.00 79.95
ATOM   2294  CA  ILE A 564     131.140 145.717 145.708  1.00 79.95
ATOM   2295  C   ILE A 564     131.559 146.636 144.573  1.00 79.95
ATOM   2296  O   ILE A 564     132.038 147.744 144.812  1.00 79.95
ATOM   2297  CB  ILE A 564     132.271 144.760 146.128  1.00 79.95
ATOM   2298  CG1 ILE A 564     133.367 145.503 146.881  1.00 79.95
ATOM   2299  CG2 ILE A 564     132.888 144.090 144.936  1.00 79.95
ATOM   2300  CD1 ILE A 564     132.991 145.900 148.285  1.00 79.95
ATOM   2301  N   TYR A 565     131.414 146.198 143.328  1.00 74.32
ATOM   2302  CA  TYR A 565     131.857 147.037 142.221  1.00 74.32
ATOM   2303  C   TYR A 565     130.912 148.199 141.964  1.00 74.32
ATOM   2304  O   TYR A 565     131.362 149.337 141.788  1.00 74.32
ATOM   2305  CB  TYR A 565     131.988 146.219 140.958  1.00 74.32
ATOM   2306  CG  TYR A 565     133.287 145.506 140.858  1.00 74.32
ATOM   2307  CD1 TYR A 565     133.545 144.412 141.647  1.00 74.32
ATOM   2308  CD2 TYR A 565     134.251 145.913 139.967  1.00 74.32
ATOM   2309  CE1 TYR A 565     134.736 143.737 141.564  1.00 74.32
ATOM   2310  CE2 TYR A 565     135.447 145.248 139.870  1.00 74.32
ATOM   2311  CZ  TYR A 565     135.687 144.151 140.678  1.00 74.32
ATOM   2312  OH  TYR A 565     136.873 143.453 140.610  1.00 74.32
ATOM   2313  N   ALA A 566     129.608 147.938 141.948  1.00 73.59
ATOM   2314  CA  ALA A 566     128.662 149.001 141.654  1.00 73.59
ATOM   2315  C   ALA A 566     128.777 150.116 142.671  1.00 73.59
ATOM   2316  O   ALA A 566     128.908 151.283 142.299  1.00 73.59
ATOM   2317  CB  ALA A 566     127.251 148.450 141.633  1.00 73.59
ATOM   2318  N   VAL A 567     128.861 149.762 143.948  1.00 78.50
ATOM   2319  CA  VAL A 567     129.100 150.756 144.982  1.00 78.50
ATOM   2320  C   VAL A 567     130.356 151.544 144.670  1.00 78.50
ATOM   2321  O   VAL A 567     130.355 152.777 144.698  1.00 78.50
ATOM   2322  CB  VAL A 567     129.212 150.065 146.347  1.00 78.50
ATOM   2323  CG1 VAL A 567     130.056 150.870 147.337  1.00 78.50
ATOM   2324  CG2 VAL A 567     127.848 149.801 146.900  1.00 78.50
ATOM   2325  N   MET A 568     131.440 150.848 144.341  1.00 76.63
ATOM   2326  CA  MET A 568     132.681 151.561 144.111  1.00 76.63
ATOM   2327  C   MET A 568     132.559 152.480 142.921  1.00 76.63
ATOM   2328  O   MET A 568     133.011 153.624 142.985  1.00 76.63
ATOM   2329  CB  MET A 568     133.821 150.582 143.937  1.00 76.63
ATOM   2330  CG  MET A 568     134.234 149.951 145.233  1.00 76.63
ATOM   2331  SD  MET A 568     135.384 148.625 144.952  1.00 76.63
ATOM   2332  CE  MET A 568     136.834 149.558 144.515  1.00 76.63
ATOM   2333  N   ILE A 569     131.863 152.057 141.876  1.00 68.91
ATOM   2334  CA  ILE A 569     131.756 152.937 140.725  1.00 68.91
ATOM   2335  C   ILE A 569     130.924 154.156 141.078  1.00 68.91
ATOM   2336  O   ILE A 569     131.079 155.223 140.484  1.00 68.91
ATOM   2337  CB  ILE A 569     131.186 152.195 139.521  1.00 68.91
ATOM   2338  CG1 ILE A 569     132.150 151.101 139.088  1.00 68.91
ATOM   2339  CG2 ILE A 569     130.951 153.159 138.396  1.00 68.91
ATOM   2340  CD1 ILE A 569     131.499 150.016 138.334  1.00 68.91
ATOM   2341  N   GLU A 570     129.994 154.011 142.012  1.00 75.88
ATOM   2342  CA  GLU A 570     129.302 155.187 142.505  1.00 75.88
ATOM   2343  C   GLU A 570     130.290 156.117 143.168  1.00 75.88
ATOM   2344  O   GLU A 570     130.377 157.290 142.814  1.00 75.88
ATOM   2345  CB  GLU A 570     128.183 154.783 143.462  1.00 75.88
ATOM   2346  CG  GLU A 570     127.485 155.911 144.171  1.00 75.88
ATOM   2347  CD  GLU A 570     126.321 155.440 145.020  1.00 75.88
ATOM   2348  OE1 GLU A 570     126.015 154.231 145.018  1.00 75.88
ATOM   2349  OE2 GLU A 570     125.718 156.287 145.710  1.00 75.88
ATOM   2350  N   LYS A 571     131.080 155.603 144.099  1.00 80.36
ATOM   2351  CA  LYS A 571     131.978 156.487 144.822  1.00 80.36
ATOM   2352  C   LYS A 571     133.034 157.049 143.895  1.00 80.36
ATOM   2353  O   LYS A 571     133.207 158.270 143.806  1.00 80.36
ATOM   2354  CB  LYS A 571     132.623 155.752 145.972  1.00 80.36
ATOM   2355  CG  LYS A 571     131.659 155.398 147.044  1.00 80.36
ATOM   2356  CD  LYS A 571     132.362 154.685 148.158  1.00 80.36
ATOM   2357  CE  LYS A 571     131.414 154.395 149.289  1.00 80.36
ATOM   2358  NZ  LYS A 571     132.090 153.638 150.375  1.00 80.36
ATOM   2359  N   MET A 572     133.682 156.183 143.128  1.00 75.51
ATOM   2360  CA  MET A 572     134.823 156.631 142.351  1.00 75.51
ATOM   2361  C   MET A 572     134.424 157.679 141.334  1.00 75.51
ATOM   2362  O   MET A 572     135.135 158.667 141.156  1.00 75.51
ATOM   2363  CB  MET A 572     135.481 155.463 141.647  1.00 75.51
ATOM   2364  CG  MET A 572     136.704 155.883 140.927  1.00 75.51
ATOM   2365  SD  MET A 572     137.854 154.578 140.543  1.00 75.51
ATOM   2366  CE  MET A 572     139.111 155.596 139.783  1.00 75.51
ATOM   2367  N   ILE A 573     133.297 157.501 140.661  1.00 69.78
ATOM   2368  CA  ILE A 573     132.875 158.545 139.744  1.00 69.78
ATOM   2369  C   ILE A 573     132.566 159.817 140.509  1.00 69.78
ATOM   2370  O   ILE A 573     133.007 160.902 140.127  1.00 69.78
ATOM   2371  CB  ILE A 573     131.687 158.084 138.889  1.00 69.78
ATOM   2372  CG1 ILE A 573     132.206 157.182 137.784  1.00 69.78
ATOM   2373  CG2 ILE A 573     130.948 159.282 138.292  1.00 69.78
ATOM   2374  CD1 ILE A 573     131.164 156.448 137.054  1.00 69.78
ATOM   2375  N   LEU A 574     131.814 159.716 141.600  1.00 75.39
ATOM   2376  CA  LEU A 574     131.371 160.938 142.255  1.00 75.39
ATOM   2377  C   LEU A 574     132.519 161.607 142.969  1.00 75.39
ATOM   2378  O   LEU A 574     132.714 162.816 142.849  1.00 75.39
ATOM   2379  CB  LEU A 574     130.245 160.650 143.240  1.00 75.39
ATOM   2380  CG  LEU A 574     128.921 160.153 142.675  1.00 75.39
ATOM   2381  CD1 LEU A 574     127.941 160.031 143.802  1.00 75.39
ATOM   2382  CD2 LEU A 574     128.377 161.042 141.573  1.00 75.39
ATOM   2383  N   ARG A 575     133.315 160.834 143.675  1.00 80.74
ATOM   2384  CA  ARG A 575     134.388 161.411 144.451  1.00 80.74
ATOM   2385  C   ARG A 575     135.605 161.705 143.589  1.00 80.74
ATOM   2386  O   ARG A 575     136.095 162.833 143.568  1.00 80.74
ATOM   2387  CB  ARG A 575     134.761 160.461 145.575  1.00 80.74
ATOM   2388  CG  ARG A 575     135.620 161.098 146.625  1.00 80.74
ATOM   2389  CD  ARG A 575     135.865 160.139 147.763  1.00 80.74
ATOM   2390  NE  ARG A 575     136.546 158.942 147.280  1.00 80.74
ATOM   2391  CZ  ARG A 575     136.477 157.736 147.837  1.00 80.74
ATOM   2392  NH1 ARG A 575     135.739 157.514 148.919  1.00 80.74
ATOM   2393  NH2 ARG A 575     137.155 156.740 147.287  1.00 80.74
ATOM   2394  N   ASP A 576     136.079 160.712 142.851  1.00 78.87
ATOM   2395  CA  ASP A 576     137.438 160.710 142.344  1.00 78.87
ATOM   2396  C   ASP A 576     137.578 161.017 140.866  1.00 78.87
ATOM   2397  O   ASP A 576     138.673 161.371 140.436  1.00 78.87
ATOM   2398  CB  ASP A 576     138.079 159.357 142.628  1.00 78.87
ATOM   2399  CG  ASP A 576     138.175 159.073 144.100  1.00 78.87
ATOM   2400  OD1 ASP A 576     138.020 160.028 144.882  1.00 78.87
ATOM   2401  OD2 ASP A 576     138.402 157.909 144.486  1.00 78.87
ATOM   2402  N   LEU A 577     136.549 160.867 140.053  1.00 70.84
ATOM   2403  CA  LEU A 577     136.772 161.129 138.644  1.00 70.84
ATOM   2404  C   LEU A 577     137.005 162.600 138.369  1.00 70.84
ATOM   2405  O   LEU A 577     137.723 162.930 137.426  1.00 70.84
ATOM   2406  CB  LEU A 577     135.601 160.651 137.806  1.00 70.84
ATOM   2407  CG  LEU A 577     135.788 160.784 136.296  1.00 70.84
ATOM   2408  CD1 LEU A 577     136.871 159.870 135.829  1.00 70.84
ATOM   2409  CD2 LEU A 577     134.512 160.442 135.630  1.00 70.84
ATOM   2410  N   CYS A 578     136.366 163.496 139.118  1.00 73.09
ATOM   2411  CA  CYS A 578     136.443 164.908 138.767  1.00 73.09
ATOM   2412  C   CYS A 578     137.873 165.407 138.830  1.00 73.09
ATOM   2413  O   CYS A 578     138.352 166.063 137.899  1.00 73.09
ATOM   2414  CB  CYS A 578     135.567 165.748 139.680  1.00 73.09
ATOM   2415  SG  CYS A 578     135.810 167.518 139.412  1.00 73.09
ATOM   2416  N   ARG A 579     138.584 165.087 139.912  1.00 76.10
ATOM   2417  CA  ARG A 579     139.933 165.611 140.052  1.00 76.10
ATOM   2418  C   ARG A 579     140.857 165.037 138.996  1.00 76.10
ATOM   2419  O   ARG A 579     141.592 165.784 138.335  1.00 76.10
ATOM   2420  CB  ARG A 579     140.464 165.339 141.451  1.00 76.10
ATOM   2421  CG  ARG A 579     140.677 163.906 141.833  1.00 76.10
ATOM   2422  CD  ARG A 579     141.335 163.830 143.160  1.00 76.10
ATOM   2423  NE  ARG A 579     140.406 164.085 144.241  1.00 76.10
ATOM   2424  CZ  ARG A 579     139.770 163.150 144.942  1.00 76.10
ATOM   2425  NH1 ARG A 579     139.922 161.862 144.697  1.00 76.10
ATOM   2426  NH2 ARG A 579     138.951 163.511 145.913  1.00 76.10
ATOM   2427  N   PHE A 580     140.802 163.725 138.788  1.00 70.48
ATOM   2428  CA  PHE A 580     141.693 163.121 137.822  1.00 70.48
ATOM   2429  C   PHE A 580     141.404 163.668 136.454  1.00 70.48
ATOM   2430  O   PHE A 580     142.322 163.918 135.686  1.00 70.48
ATOM   2431  CB  PHE A 580     141.578 161.604 137.803  1.00 70.48
ATOM   2432  CG  PHE A 580     142.215 160.966 136.582  1.00 70.48
ATOM   2433  CD1 PHE A 580     143.576 160.799 136.497  1.00 70.48
ATOM   2434  CD2 PHE A 580     141.448 160.536 135.522  1.00 70.48
ATOM   2435  CE1 PHE A 580     144.143 160.225 135.391  1.00 70.48
ATOM   2436  CE2 PHE A 580     142.024 159.968 134.421  1.00 70.48
ATOM   2437  CZ  PHE A 580     143.369 159.821 134.360  1.00 70.48
ATOM   2438  N   MET A 581     140.139 163.838 136.111  1.00 68.49
ATOM   2439  CA  MET A 581     139.865 164.252 134.751  1.00 68.49
ATOM   2440  C   MET A 581     140.144 165.721 134.544  1.00 68.49
ATOM   2441  O   MET A 581     140.478 166.109 133.430  1.00 68.49
ATOM   2442  CB  MET A 581     138.447 163.911 134.353  1.00 68.49
ATOM   2443  CG  MET A 581     138.233 162.435 134.163  1.00 68.49
ATOM   2444  SD  MET A 581     139.216 161.634 132.888  1.00 68.49
ATOM   2445  CE  MET A 581     138.754 162.583 131.456  1.00 68.49
ATOM   2446  N   PHE A 582     140.058 166.557 135.573  1.00 67.02
ATOM   2447  CA  PHE A 582     140.532 167.918 135.371  1.00 67.02
ATOM   2448  C   PHE A 582     142.016 167.916 135.089  1.00 67.02
ATOM   2449  O   PHE A 582     142.480 168.556 134.145  1.00 67.02
ATOM   2450  CB  PHE A 582     140.259 168.810 136.568  1.00 67.02
ATOM   2451  CG  PHE A 582     140.799 170.198 136.397  1.00 67.02
ATOM   2452  CD1 PHE A 582     140.185 171.088 135.546  1.00 67.02
ATOM   2453  CD2 PHE A 582     141.940 170.602 137.056  1.00 67.02
ATOM   2454  CE1 PHE A 582     140.684 172.350 135.377  1.00 67.02
ATOM   2455  CE2 PHE A 582     142.438 171.867 136.882  1.00 67.02
ATOM   2456  CZ  PHE A 582     141.813 172.736 136.049  1.00 67.02
ATOM   2457  N   VAL A 583     142.784 167.194 135.899  1.00 64.70
ATOM   2458  CA  VAL A 583     144.229 167.190 135.708  1.00 64.70
ATOM   2459  C   VAL A 583     144.575 166.566 134.375  1.00 64.70
ATOM   2460  O   VAL A 583     145.417 167.066 133.625  1.00 64.70
ATOM   2461  CB  VAL A 583     144.914 166.453 136.861  1.00 64.70
ATOM   2462  CG1 VAL A 583     146.372 166.310 136.572  1.00 64.70
ATOM   2463  CG2 VAL A 583     144.662 167.207 138.135  1.00 64.70
ATOM   2464  N   TYR A 584     143.945 165.455 134.072  1.00 62.02
ATOM   2465  CA  TYR A 584     144.236 164.767 132.841  1.00 62.02
ATOM   2466  C   TYR A 584     143.882 165.623 131.657  1.00 62.02
ATOM   2467  O   TYR A 584     144.579 165.607 130.651  1.00 62.02
ATOM   2468  CB  TYR A 584     143.471 163.461 132.771  1.00 62.02
ATOM   2469  CG  TYR A 584     143.734 162.794 131.482  1.00 62.02
ATOM   2470  CD1 TYR A 584     144.915 162.158 131.282  1.00 62.02
ATOM   2471  CD2 TYR A 584     142.829 162.828 130.461  1.00 62.02
ATOM   2472  CE1 TYR A 584     145.192 161.574 130.130  1.00 62.02
ATOM   2473  CE2 TYR A 584     143.100 162.241 129.296  1.00 62.02
ATOM   2474  CZ  TYR A 584     144.292 161.615 129.133  1.00 62.02
ATOM   2475  OH  TYR A 584     144.609 160.996 127.958  1.00 62.02
ATOM   2476  N   LEU A 585     142.761 166.322 131.720  1.00 62.27
ATOM   2477  CA  LEU A 585     142.382 167.144 130.593  1.00 62.27
ATOM   2478  C   LEU A 585     143.286 168.340 130.480  1.00 62.27
ATOM   2479  O   LEU A 585     143.543 168.804 129.379  1.00 62.27
ATOM   2480  CB  LEU A 585     140.940 167.571 130.728  1.00 62.27
ATOM   2481  CG  LEU A 585     139.956 166.441 130.480  1.00 62.27
ATOM   2482  CD1 LEU A 585     138.591 166.820 130.995  1.00 62.27
ATOM   2483  CD2 LEU A 585     139.882 166.086 129.025  1.00 62.27
ATOM   2484  N   VAL A 586     143.816 168.822 131.595  1.00 59.73
ATOM   2485  CA  VAL A 586     144.815 169.873 131.530  1.00 59.73
ATOM   2486  C   VAL A 586     146.020 169.386 130.755  1.00 59.73
ATOM   2487  O   VAL A 586     146.500 170.065 129.855  1.00 59.73
ATOM   2488  CB  VAL A 586     145.185 170.313 132.950  1.00 59.73
ATOM   2489  CG1 VAL A 586     146.441 171.059 132.970  1.00 59.73
ATOM   2490  CG2 VAL A 586     144.097 171.160 133.503  1.00 59.73
ATOM   2491  N   PHE A 587     146.508 168.190 131.069  1.00 60.27
ATOM   2492  CA  PHE A 587     147.674 167.679 130.361  1.00 60.27
ATOM   2493  C   PHE A 587     147.353 167.364 128.917  1.00 60.27
ATOM   2494  O   PHE A 587     148.087 167.767 128.013  1.00 60.27
ATOM   2495  CB  PHE A 587     148.214 166.437 131.033  1.00 60.27
ATOM   2496  CG  PHE A 587     148.954 166.711 132.272  1.00 60.27
ATOM   2497  CD1 PHE A 587     150.134 167.375 132.244  1.00 60.27
ATOM   2498  CD2 PHE A 587     148.484 166.285 133.470  1.00 60.27
ATOM   2499  CE1 PHE A 587     150.808 167.621 133.384  1.00 60.27
ATOM   2500  CE2 PHE A 587     149.171 166.530 134.614  1.00 60.27
ATOM   2501  CZ  PHE A 587     150.331 167.193 134.565  1.00 60.27
ATOM   2502  N   LEU A 588     146.262 166.657 128.678  1.00 59.44
ATOM   2503  CA  LEU A 588     145.906 166.298 127.321  1.00 59.44
ATOM   2504  C   LEU A 588     145.724 167.544 126.498  1.00 59.44
ATOM   2505  O   LEU A 588     146.316 167.676 125.435  1.00 59.44
ATOM   2506  CB  LEU A 588     144.635 165.456 127.320  1.00 59.44
ATOM   2507  CG  LEU A 588     143.906 165.212 126.006  1.00 59.44
ATOM   2508  CD1 LEU A 588     144.822 164.678 124.987  1.00 59.44
ATOM   2509  CD2 LEU A 588     142.799 164.244 126.237  1.00 59.44
ATOM   2510  N   PHE A 589     144.997 168.517 127.024  1.00 60.60
ATOM   2511  CA  PHE A 589     144.703 169.710 126.261  1.00 60.60
ATOM   2512  C   PHE A 589     145.926 170.583 126.097  1.00 60.60
ATOM   2513  O   PHE A 589     146.148 171.136 125.022  1.00 60.60
ATOM   2514  CB  PHE A 589     143.600 170.495 126.932  1.00 60.60
ATOM   2515  CG  PHE A 589     143.128 171.614 126.115  1.00 60.60
ATOM   2516  CD1 PHE A 589     142.359 171.383 125.012  1.00 60.60
ATOM   2517  CD2 PHE A 589     143.469 172.900 126.419  1.00 60.60
ATOM   2518  CE1 PHE A 589     141.931 172.417 124.237  1.00 60.60
ATOM   2519  CE2 PHE A 589     143.040 173.937 125.631  1.00 60.60
ATOM   2520  CZ  PHE A 589     142.276 173.694 124.543  1.00 60.60
ATOM   2521  N   GLY A 590     146.720 170.745 127.148  1.00 59.14
ATOM   2522  CA  GLY A 590     147.899 171.570 127.034  1.00 59.14
ATOM   2523  C   GLY A 590     148.855 171.044 125.994  1.00 59.14
ATOM   2524  O   GLY A 590     149.233 171.756 125.063  1.00 59.14
ATOM   2525  N   PHE A 591     149.211 169.775 126.095  1.00 57.36
ATOM   2526  CA  PHE A 591     150.107 169.250 125.088  1.00 57.36
ATOM   2527  C   PHE A 591     149.428 169.126 123.740  1.00 57.36
ATOM   2528  O   PHE A 591     150.102 169.159 122.714  1.00 57.36
ATOM   2529  CB  PHE A 591     150.659 167.923 125.530  1.00 57.36
ATOM   2530  CG  PHE A 591     151.639 168.039 126.604  1.00 57.36
ATOM   2531  CD1 PHE A 591     151.243 168.130 127.895  1.00 57.36
ATOM   2532  CD2 PHE A 591     152.958 168.062 126.326  1.00 57.36
ATOM   2533  CE1 PHE A 591     152.143 168.211 128.886  1.00 57.36
ATOM   2534  CE2 PHE A 591     153.858 168.163 127.312  1.00 57.36
ATOM   2535  CZ  PHE A 591     153.450 168.223 128.597  1.00 57.36
ATOM   2536  N   SER A 592     148.111 168.980 123.710  1.00 61.51
ATOM   2537  CA  SER A 592     147.409 168.959 122.443  1.00 61.51
ATOM   2538  C   SER A 592     147.574 170.270 121.721  1.00 61.51
ATOM   2539  O   SER A 592     147.809 170.303 120.510  1.00 61.51
ATOM   2540  CB  SER A 592     145.939 168.692 122.688  1.00 61.51
ATOM   2541  OG  SER A 592     145.787 167.598 123.548  1.00 61.51
ATOM   2542  N   THR A 593     147.452 171.365 122.451  1.00 61.38
ATOM   2543  CA  THR A 593     147.640 172.661 121.839  1.00 61.38
ATOM   2544  C   THR A 593     149.083 172.850 121.441  1.00 61.38
ATOM   2545  O   THR A 593     149.367 173.428 120.392  1.00 61.38
ATOM   2546  CB  THR A 593     147.212 173.728 122.800  1.00 61.38
ATOM   2547  OG1 THR A 593     147.690 173.375 124.090  1.00 61.38
ATOM   2548  CG2 THR A 593     145.732 173.795 122.832  1.00 61.38
ATOM   2549  N   ALA A 594     150.005 172.330 122.242  1.00 59.76
ATOM   2550  CA  ALA A 594     151.405 172.386 121.860  1.00 59.76
ATOM   2551  C   ALA A 594     151.647 171.697 120.535  1.00 59.76
ATOM   2552  O   ALA A 594     152.184 172.301 119.606  1.00 59.76
ATOM   2553  CB  ALA A 594     152.253 171.739 122.933  1.00 59.76
ATOM   2554  N   VAL A 595     151.210 170.456 120.400  1.00 59.71
ATOM   2555  CA  VAL A 595     151.543 169.711 119.195  1.00 59.71
ATOM   2556  C   VAL A 595     150.797 170.267 118.004  1.00 59.71
ATOM   2557  O   VAL A 595     151.334 170.316 116.899  1.00 59.71
ATOM   2558  CB  VAL A 595     151.262 168.216 119.370  1.00 59.71
ATOM   2559  CG1 VAL A 595     151.556 167.509 118.096  1.00 59.71
ATOM   2560  CG2 VAL A 595     152.087 167.626 120.468  1.00 59.71
ATOM   2561  N   VAL A 596     149.541 170.657 118.184  1.00 61.11
ATOM   2562  CA  VAL A 596     148.795 171.155 117.042  1.00 61.11
ATOM   2563  C   VAL A 596     149.335 172.496 116.611  1.00 61.11
ATOM   2564  O   VAL A 596     149.277 172.844 115.428  1.00 61.11
ATOM   2565  CB  VAL A 596     147.307 171.211 117.374  1.00 61.11
ATOM   2566  CG1 VAL A 596     147.026 172.320 118.281  1.00 61.11
ATOM   2567  CG2 VAL A 596     146.521 171.338 116.139  1.00 61.11
ATOM   2568  N   THR A 597     149.847 173.289 117.548  1.00 62.04
ATOM   2569  CA  THR A 597     150.564 174.490 117.165  1.00 62.04
ATOM   2570  C   THR A 597     151.764 174.141 116.336  1.00 62.04
ATOM   2571  O   THR A 597     152.013 174.753 115.298  1.00 62.04
ATOM   2572  CB  THR A 597     151.046 175.229 118.392  1.00 62.04
ATOM   2573  OG1 THR A 597     149.942 175.600 119.211  1.00 62.04
ATOM   2574  CG2 THR A 597     151.776 176.437 117.980  1.00 62.04
ATOM   2575  N   LEU A 598     152.520 173.157 116.795  1.00 61.63
ATOM   2576  CA  LEU A 598     153.795 172.843 116.180  1.00 61.63
ATOM   2577  C   LEU A 598     153.621 172.382 114.746  1.00 61.63
ATOM   2578  O   LEU A 598     154.373 172.796 113.865  1.00 61.63
ATOM   2579  CB  LEU A 598     154.492 171.784 117.012  1.00 61.63
ATOM   2580  CG  LEU A 598     155.875 171.352 116.597  1.00 61.63
ATOM   2581  CD1 LEU A 598     156.785 172.510 116.600  1.00 61.63
ATOM   2582  CD2 LEU A 598     156.356 170.307 117.555  1.00 61.63
ATOM   2583  N   ILE A 599     152.635 171.563 114.483  1.00 65.04
ATOM   2584  CA  ILE A 599     152.492 171.003 113.150  1.00 65.04
ATOM   2585  C   ILE A 599     151.794 171.995 112.245  1.00 65.04
ATOM   2586  O   ILE A 599     151.024 172.848 112.685  1.00 65.04
ATOM   2587  CB  ILE A 599     151.756 169.655 113.177  1.00 65.04
ATOM   2588  CG1 ILE A 599     150.295 169.807 113.557  1.00 65.04
ATOM   2589  CG2 ILE A 599     152.420 168.735 114.146  1.00 65.04
ATOM   2590  CD1 ILE A 599     149.563 168.507 113.515  1.00 65.04
ATOM   2591  N   GLU A 600     152.047 171.845 110.958  1.00 70.64
ATOM   2592  CA  GLU A 600     151.494 172.715 109.943  1.00 70.64
ATOM   2593  C   GLU A 600     151.518 171.953 108.637  1.00 70.64
ATOM   2594  O   GLU A 600     152.226 170.956 108.508  1.00 70.64
ATOM   2595  CB  GLU A 600     152.286 174.011 109.814  1.00 70.64
ATOM   2596  CG  GLU A 600     153.718 173.801 109.384  1.00 70.64
ATOM   2597  CD  GLU A 600     154.618 174.970 109.735  1.00 70.64
ATOM   2598  OE1 GLU A 600     154.798 175.243 110.940  1.00 70.64
ATOM   2599  OE2 GLU A 600     155.148 175.609 108.803  1.00 70.64
ATOM   2600  N   ASP A 601     150.731 172.415 107.683  1.00 74.73
ATOM   2601  CA  ASP A 601     150.700 171.803 106.373  1.00 74.73
ATOM   2602  C   ASP A 601     150.103 172.821 105.422  1.00 74.73
ATOM   2603  O   ASP A 601     149.495 173.793 105.866  1.00 74.73
ATOM   2604  CB  ASP A 601     149.880 170.508 106.386  1.00 74.73
ATOM   2605  CG  ASP A 601     150.199 169.591 105.209  1.00 74.73
ATOM   2606  OD1 ASP A 601     151.393 169.441 104.862  1.00 74.73
ATOM   2607  OD2 ASP A 601     149.255 168.992 104.652  1.00 74.73
ATOM   2608  N   SER A 626     144.453 167.095 107.472  1.00 71.45
ATOM   2609  CA  SER A 626     144.987 165.912 108.131  1.00 71.45
ATOM   2610  C   SER A 626     145.847 166.320 109.308  1.00 71.45
ATOM   2611  O   SER A 626     146.921 166.876 109.131  1.00 71.45
ATOM   2612  CB  SER A 626     145.800 165.063 107.156  1.00 71.45
ATOM   2613  OG  SER A 626     144.966 164.451 106.189  1.00 71.45
ATOM   2614  N   TYR A 627     145.327 166.069 110.507  1.00 68.71
ATOM   2615  CA  TYR A 627     145.986 166.301 111.791  1.00 68.71
ATOM   2616  C   TYR A 627     146.065 167.763 112.180  1.00 68.71
ATOM   2617  O   TYR A 627     146.315 168.073 113.344  1.00 68.71
ATOM   2618  CB  TYR A 627     147.404 165.726 111.816  1.00 68.71
ATOM   2619  CG  TYR A 627     147.458 164.279 111.450  1.00 68.71
ATOM   2620  CD1 TYR A 627     147.110 163.305 112.362  1.00 68.71
ATOM   2621  CD2 TYR A 627     147.851 163.886 110.183  1.00 68.71
ATOM   2622  CE1 TYR A 627     147.150 161.988 112.025  1.00 68.71
ATOM   2623  CE2 TYR A 627     147.894 162.572 109.833  1.00 68.71
ATOM   2624  CZ  TYR A 627     147.543 161.623 110.754  1.00 68.71
ATOM   2625  OH  TYR A 627     147.593 160.297 110.396  1.00 68.71
ATOM   2626  N   ASN A 628     145.769 168.674 111.270  1.00 69.22
ATOM   2627  CA  ASN A 628     145.980 170.062 111.622  1.00 69.22
ATOM   2628  C   ASN A 628     144.933 170.582 112.586  1.00 69.22
ATOM   2629  O   ASN A 628     145.065 171.714 113.050  1.00 69.22
ATOM   2630  CB  ASN A 628     146.004 170.926 110.369  1.00 69.22
ATOM   2631  CG  ASN A 628     146.707 172.239 110.596  1.00 69.22
ATOM   2632  OD1 ASN A 628     146.072 173.265 110.824  1.00 69.22
ATOM   2633  ND2 ASN A 628     148.028 172.210 110.560  1.00 69.22
ATOM   2634  N   SER A 629     143.888 169.820 112.864  1.00 62.34
ATOM   2635  CA  SER A 629     142.854 170.271 113.767  1.00 62.34
ATOM   2636  C   SER A 629     143.207 169.911 115.194  1.00 62.34
ATOM   2637  O   SER A 629     143.931 168.954 115.452  1.00 62.34
ATOM   2638  CB  SER A 629     141.518 169.649 113.388  1.00 62.34
ATOM   2639  OG  SER A 629     141.559 168.247 113.528  1.00 62.34
ATOM   2640  N   LEU A 630     142.690 170.701 116.123  1.00 60.06
ATOM   2641  CA  LEU A 630     142.918 170.409 117.520  1.00 60.06
ATOM   2642  C   LEU A 630     142.234 169.136 117.927  1.00 60.06
ATOM   2643  O   LEU A 630     142.710 168.441 118.816  1.00 60.06
ATOM   2644  CB  LEU A 630     142.421 171.549 118.386  1.00 60.06
ATOM   2645  CG  LEU A 630     142.413 171.313 119.896  1.00 60.06
ATOM   2646  CD1 LEU A 630     143.746 170.906 120.422  1.00 60.06
ATOM   2647  CD2 LEU A 630     141.975 172.568 120.555  1.00 60.06
ATOM   2648  N   TYR A 631     141.093 168.827 117.336  1.00 59.71
ATOM   2649  CA  TYR A 631     140.390 167.616 117.735  1.00 59.71
ATOM   2650  C   TYR A 631     141.199 166.378 117.389  1.00 59.71
ATOM   2651  O   TYR A 631     141.346 165.469 118.212  1.00 59.71
ATOM   2652  CB  TYR A 631     139.023 167.553 117.077  1.00 59.71
ATOM   2653  CG  TYR A 631     138.381 166.230 117.301  1.00 59.71
ATOM   2654  CD1 TYR A 631     137.813 165.925 118.512  1.00 59.71
ATOM   2655  CD2 TYR A 631     138.353 165.276 116.309  1.00 59.71
ATOM   2656  CE1 TYR A 631     137.233 164.728 118.724  1.00 59.71
ATOM   2657  CE2 TYR A 631     137.780 164.080 116.520  1.00 59.71
ATOM   2658  CZ  TYR A 631     137.224 163.816 117.726  1.00 59.71
ATOM   2659  OH  TYR A 631     136.640 162.614 117.943  1.00 59.71
ATOM   2660  N   SER A 632     141.714 166.316 116.163  1.00 58.93
ATOM   2661  CA  SER A 632     142.446 165.131 115.753  1.00 58.93
ATOM   2662  C   SER A 632     143.664 164.926 116.625  1.00 58.93
ATOM   2663  O   SER A 632     143.947 163.806 117.051  1.00 58.93
ATOM   2664  CB  SER A 632     142.856 165.238 114.296  1.00 58.93
ATOM   2665  OG  SER A 632     141.731 165.424 113.469  1.00 58.93
ATOM   2666  N   THR A 633     144.389 165.990 116.922  1.00 59.08
ATOM   2667  CA  THR A 633     145.538 165.822 117.788  1.00 59.08
ATOM   2668  C   THR A 633     145.112 165.476 119.202  1.00 59.08
ATOM   2669  O   THR A 633     145.832 164.776 119.915  1.00 59.08
ATOM   2670  CB  THR A 633     146.400 167.060 117.761  1.00 59.08
ATOM   2671  OG1 THR A 633     146.946 167.199 116.452  1.00 59.08
ATOM   2672  CG2 THR A 633     147.511 166.914 118.716  1.00 59.08
ATOM   2673  N   CYS A 634     143.960 165.963 119.641  1.00 61.03
ATOM   2674  CA  CYS A 634     143.476 165.542 120.948  1.00 61.03
ATOM   2675  C   CYS A 634     143.243 164.044 120.980  1.00 61.03
ATOM   2676  O   CYS A 634     143.590 163.381 121.956  1.00 61.03
ATOM   2677  CB  CYS A 634     142.199 166.281 121.315  1.00 61.03
ATOM   2678  SG  CYS A 634     142.456 167.729 122.345  1.00 61.03
ATOM   2679  N   LEU A 635     142.668 163.485 119.918  1.00 58.47
ATOM   2680  CA  LEU A 635     142.502 162.036 119.875  1.00 58.47
ATOM   2681  C   LEU A 635     143.832 161.321 119.809  1.00 58.47
ATOM   2682  O   LEU A 635     144.031 160.318 120.495  1.00 58.47
ATOM   2683  CB  LEU A 635     141.671 161.615 118.683  1.00 58.47
ATOM   2684  CG  LEU A 635     140.172 161.810 118.772  1.00 58.47
ATOM   2685  CD1 LEU A 635     139.570 161.241 117.497  1.00 58.47
ATOM   2686  CD2 LEU A 635     139.573 161.176 120.004  1.00 58.47
ATOM   2687  N   GLU A 636     144.745 161.802 118.976  1.00 58.52
ATOM   2688  CA  GLU A 636     146.017 161.121 118.818  1.00 58.52
ATOM   2689  C   GLU A 636     146.778 161.089 120.115  1.00 58.52
ATOM   2690  O   GLU A 636     147.493 160.128 120.379  1.00 58.52
ATOM   2691  CB  GLU A 636     146.841 161.810 117.754  1.00 58.52
ATOM   2692  CG  GLU A 636     146.275 161.678 116.384  1.00 58.52
ATOM   2693  CD  GLU A 636     146.473 160.308 115.807  1.00 58.52
ATOM   2694  OE1 GLU A 636     147.028 159.440 116.505  1.00 58.52
ATOM   2695  OE2 GLU A 636     146.071 160.095 114.647  1.00 58.52
ATOM   2696  N   LEU A 637     146.650 162.126 120.930  1.00 57.64
ATOM   2697  CA  LEU A 637     147.317 162.124 122.220  1.00 57.64
ATOM   2698  C   LEU A 637     146.506 161.390 123.254  1.00 57.64
ATOM   2699  O   LEU A 637     147.035 160.999 124.289  1.00 57.64
ATOM   2700  CB  LEU A 637     147.579 163.535 122.705  1.00 57.64
ATOM   2701  CG  LEU A 637     148.953 164.050 122.344  1.00 57.64
ATOM   2702  CD1 LEU A 637     149.073 164.172 120.862  1.00 57.64
ATOM   2703  CD2 LEU A 637     149.136 165.344 122.998  1.00 57.64
ATOM   2704  N   PHE A 638     145.210 161.270 123.049  1.00 55.66
ATOM   2705  CA  PHE A 638     144.445 160.431 123.942  1.00 55.66
ATOM   2706  C   PHE A 638     144.876 158.992 123.799  1.00 55.66
ATOM   2707  O   PHE A 638     145.013 158.272 124.788  1.00 55.66
ATOM   2708  CB  PHE A 638     142.968 160.566 123.646  1.00 55.66
ATOM   2709  CG  PHE A 638     142.131 159.650 124.436  1.00 55.66
ATOM   2710  CD1 PHE A 638     142.088 159.738 125.803  1.00 55.66
ATOM   2711  CD2 PHE A 638     141.393 158.694 123.818  1.00 55.66
ATOM   2712  CE1 PHE A 638     141.323 158.888 126.530  1.00 55.66
ATOM   2713  CE2 PHE A 638     140.626 157.845 124.534  1.00 55.66
ATOM   2714  CZ  PHE A 638     140.585 157.935 125.890  1.00 55.66
ATOM   2715  N   LYS A 639     145.138 158.574 122.565  1.00 53.37
ATOM   2716  CA  LYS A 639     145.435 157.184 122.279  1.00 53.37
ATOM   2717  C   LYS A 639     146.646 156.689 123.026  1.00 53.37
ATOM   2718  O   LYS A 639     146.796 155.487 123.219  1.00 53.37
ATOM   2719  CB  LYS A 639     145.661 156.999 120.803  1.00 53.37
ATOM   2720  CG  LYS A 639     144.425 157.021 120.037  1.00 53.37
ATOM   2721  CD  LYS A 639     144.731 156.835 118.610  1.00 53.37
ATOM   2722  CE  LYS A 639     143.506 156.979 117.788  1.00 53.37
ATOM   2723  NZ  LYS A 639     143.910 157.152 116.393  1.00 53.37
ATOM   2724  N   PHE A 640     147.536 157.578 123.432  1.00 56.00
ATOM   2725  CA  PHE A 640     148.606 157.145 124.305  1.00 56.00
ATOM   2726  C   PHE A 640     148.052 156.644 125.611  1.00 56.00
ATOM   2727  O   PHE A 640     148.634 155.757 126.220  1.00 56.00
ATOM   2728  CB  PHE A 640     149.587 158.276 124.547  1.00 56.00
ATOM   2729  CG  PHE A 640     150.381 158.605 123.356  1.00 56.00
ATOM   2730  CD1 PHE A 640     149.896 159.449 122.416  1.00 56.00
ATOM   2731  CD2 PHE A 640     151.581 158.027 123.151  1.00 56.00
ATOM   2732  CE1 PHE A 640     150.602 159.728 121.317  1.00 56.00
ATOM   2733  CE2 PHE A 640     152.273 158.302 122.053  1.00 56.00
ATOM   2734  CZ  PHE A 640     151.782 159.155 121.132  1.00 56.00
ATOM   2735  N   THR A 641     146.919 157.162 126.039  1.00 56.84
ATOM   2736  CA  THR A 641     146.356 156.703 127.290  1.00 56.84
ATOM   2737  C   THR A 641     145.846 155.281 127.180  1.00 56.84
ATOM   2738  O   THR A 641     145.864 154.541 128.164  1.00 56.84
ATOM   2739  CB  THR A 641     145.242 157.635 127.719  1.00 56.84
ATOM   2740  OG1 THR A 641     145.650 158.985 127.486  1.00 56.84
ATOM   2741  CG2 THR A 641     144.909 157.438 129.180  1.00 56.84
ATOM   2742  N   ILE A 642     145.360 154.889 126.008  1.00 54.81
ATOM   2743  CA  ILE A 642     144.851 153.542 125.787  1.00 54.81
ATOM   2744  C   ILE A 642     145.871 152.656 125.075  1.00 54.81
ATOM   2745  O   ILE A 642     145.491 151.708 124.416  1.00 54.81
ATOM   2746  CB  ILE A 642     143.514 153.547 125.033  1.00 54.81
ATOM   2747  CG1 ILE A 642     143.623 154.233 123.678  1.00 54.81
ATOM   2748  CG2 ILE A 642     142.482 154.228 125.841  1.00 54.81
ATOM   2749  CD1 ILE A 642     142.478 153.986 122.775  1.00 54.81
ATOM   2750  N   GLY A 643     147.151 152.968 125.171  1.00 52.47
ATOM   2751  CA  GLY A 643     148.146 152.059 124.663  1.00 52.47
ATOM   2752  C   GLY A 643     148.125 151.897 123.172  1.00 52.47
ATOM   2753  O   GLY A 643     148.596 150.885 122.668  1.00 52.47
ATOM   2754  N   MET A 644     147.589 152.869 122.446  1.00 53.49
ATOM   2755  CA  MET A 644     147.627 152.852 120.992  1.00 53.49
ATOM   2756  C   MET A 644     148.172 154.157 120.439  1.00 53.49
ATOM   2757  O   MET A 644     147.882 154.516 119.301  1.00 53.49
ATOM   2758  CB  MET A 644     146.245 152.558 120.426  1.00 53.49
ATOM   2759  CG  MET A 644     145.900 151.119 120.473  1.00 53.49
ATOM   2760  SD  MET A 644     146.740 150.153 119.230  1.00 53.49
ATOM   2761  CE  MET A 644     145.895 150.690 117.764  1.00 53.49
ATOM   2762  N   GLY A 645     148.987 154.861 121.210  1.00 56.53
ATOM   2763  CA  GLY A 645     149.582 156.070 120.713  1.00 56.53
ATOM   2764  C   GLY A 645     150.716 155.757 119.765  1.00 56.53
ATOM   2765  O   GLY A 645     151.601 154.960 120.062  1.00 56.53
ATOM   2766  N   ASP A 646     150.683 156.392 118.605  1.00 62.07
ATOM   2767  CA  ASP A 646     151.668 156.051 117.597  1.00 62.07
ATOM   2768  C   ASP A 646     153.016 156.693 117.861  1.00 62.07
ATOM   2769  O   ASP A 646     154.039 156.129 117.471  1.00 62.07
ATOM   2770  CB  ASP A 646     151.163 156.442 116.213  1.00 62.07
ATOM   2771  CG  ASP A 646     150.136 155.463 115.662  1.00 62.07
ATOM   2772  OD1 ASP A 646     150.162 154.270 116.034  1.00 62.07
ATOM   2773  OD2 ASP A 646     149.294 155.883 114.838  1.00 62.07
ATOM   2774  N   LEU A 647     153.053 157.894 118.424  1.00 58.25
ATOM   2775  CA  LEU A 647     154.303 158.547 118.807  1.00 58.25
ATOM   2776  C   LEU A 647     155.158 158.990 117.632  1.00 58.25
ATOM   2777  O   LEU A 647     156.192 159.623 117.827  1.00 58.25
ATOM   2778  CB  LEU A 647     155.129 157.632 119.703  1.00 58.25
ATOM   2779  CG  LEU A 647     156.226 158.221 120.578  1.00 58.25
ATOM   2780  CD1 LEU A 647     155.754 159.306 121.458  1.00 58.25
ATOM   2781  CD2 LEU A 647     156.761 157.143 121.445  1.00 58.25
ATOM   2782  N   GLU A 648     154.765 158.672 116.421  1.00 65.29
ATOM   2783  CA  GLU A 648     155.142 159.447 115.275  1.00 65.29
ATOM   2784  C   GLU A 648     153.957 159.280 114.334  1.00 65.29
ATOM   2785  O   GLU A 648     153.960 158.446 113.431  1.00 65.29
ATOM   2786  CB  GLU A 648     156.437 158.946 114.650  1.00 65.29
ATOM   2787  CG  GLU A 648     156.979 159.835 113.558  1.00 65.29
ATOM   2788  CD  GLU A 648     158.159 159.216 112.834  1.00 65.29
ATOM   2789  OE1 GLU A 648     158.336 157.981 112.916  1.00 65.29
ATOM   2790  OE2 GLU A 648     158.914 159.967 112.180  1.00 65.29
ATOM   2791  N   PHE A 649     152.948 160.120 114.536  1.00 64.50
ATOM   2792  CA  PHE A 649     151.708 160.008 113.793  1.00 64.50
ATOM   2793  C   PHE A 649     151.595 161.025 112.685  1.00 64.50
ATOM   2794  O   PHE A 649     150.656 160.939 111.896  1.00 64.50
ATOM   2795  CB  PHE A 649     150.490 160.124 114.716  1.00 64.50
ATOM   2796  CG  PHE A 649     150.442 161.365 115.554  1.00 64.50
ATOM   2797  CD1 PHE A 649     149.924 162.531 115.058  1.00 64.50
ATOM   2798  CD2 PHE A 649     150.845 161.340 116.863  1.00 64.50
ATOM   2799  CE1 PHE A 649     149.854 163.648 115.831  1.00 64.50
ATOM   2800  CE2 PHE A 649     150.768 162.461 117.638  1.00 64.50
ATOM   2801  CZ  PHE A 649     150.275 163.611 117.120  1.00 64.50
ATOM   2802  N   THR A 650     152.512 161.979 112.609  1.00 68.10
ATOM   2803  CA  THR A 650     152.538 162.933 111.523  1.00 68.10
ATOM   2804  C   THR A 650     153.975 163.180 111.122  1.00 68.10
ATOM   2805  O   THR A 650     154.877 163.173 111.956  1.00 68.10
ATOM   2806  CB  THR A 650     151.891 164.251 111.905  1.00 68.10
ATOM   2807  OG1 THR A 650     151.912 165.116 110.771  1.00 68.10
ATOM   2808  CG2 THR A 650     152.640 164.914 113.031  1.00 68.10
ATOM   2809  N   GLU A 651     154.176 163.360 109.821  1.00 76.77
ATOM   2810  CA  GLU A 651     155.411 163.892 109.275  1.00 76.77
ATOM   2811  C   GLU A 651     155.263 165.321 108.790  1.00 76.77
ATOM   2812  O   GLU A 651     156.274 165.964 108.504  1.00 76.77
ATOM   2813  CB  GLU A 651     155.899 163.012 108.119  1.00 76.77
ATOM   2814  CG  GLU A 651     156.193 161.569 108.542  1.00 76.77
ATOM   2815  CD  GLU A 651     156.832 160.736 107.443  1.00 76.77
ATOM   2816  OE1 GLU A 651     156.942 161.227 106.296  1.00 76.77
ATOM   2817  OE2 GLU A 651     157.226 159.585 107.724  1.00 76.77
ATOM   2818  N   ASN A 652     154.030 165.830 108.708  1.00 74.30
ATOM   2819  CA  ASN A 652     153.751 167.180 108.230  1.00 74.30
ATOM   2820  C   ASN A 652     153.898 168.151 109.384  1.00 74.30
ATOM   2821  O   ASN A 652     152.929 168.629 109.963  1.00 74.30
ATOM   2822  CB  ASN A 652     152.356 167.254 107.647  1.00 74.30
ATOM   2823  CG  ASN A 652     152.211 166.431 106.414  1.00 74.30
ATOM   2824  OD1 ASN A 652     153.180 166.195 105.696  1.00 74.30
ATOM   2825  ND2 ASN A 652     150.993 165.996 106.140  1.00 74.30
ATOM   2826  N   TYR A 653     155.138 168.448 109.712  1.00 68.96
ATOM   2827  CA  TYR A 653     155.463 169.354 110.802  1.00 68.96
ATOM   2828  C   TYR A 653     156.957 169.608 110.751  1.00 68.96
ATOM   2829  O   TYR A 653     157.683 169.005 109.960  1.00 68.96
ATOM   2830  CB  TYR A 653     155.067 168.767 112.139  1.00 68.96
ATOM   2831  CG  TYR A 653     155.960 167.660 112.523  1.00 68.96
ATOM   2832  CD1 TYR A 653     155.916 166.453 111.866  1.00 68.96
ATOM   2833  CD2 TYR A 653     156.854 167.808 113.536  1.00 68.96
ATOM   2834  CE1 TYR A 653     156.747 165.434 112.210  1.00 68.96
ATOM   2835  CE2 TYR A 653     157.679 166.798 113.877  1.00 68.96
ATOM   2836  CZ  TYR A 653     157.622 165.603 113.217  1.00 68.96
ATOM   2837  OH  TYR A 653     158.444 164.557 113.538  1.00 68.96
ATOM   2838  N   ASP A 654     157.415 170.476 111.628  1.00 68.88
ATOM   2839  CA  ASP A 654     158.800 170.889 111.653  1.00 68.88
ATOM   2840  C   ASP A 654     159.326 170.721 113.070  1.00 68.88
ATOM   2841  O   ASP A 654     158.561 170.695 114.032  1.00 68.88
ATOM   2842  CB  ASP A 654     158.910 172.331 111.160  1.00 68.88
ATOM   2843  CG  ASP A 654     160.141 172.565 110.346  1.00 68.88
ATOM   2844  OD1 ASP A 654     161.242 172.263 110.857  1.00 68.88
ATOM   2845  OD2 ASP A 654     160.008 173.042 109.198  1.00 68.88
ATOM   2846  N   PHE A 655     160.648 170.633 113.209  1.00 66.07
ATOM   2847  CA  PHE A 655     161.291 170.387 114.500  1.00 66.07
ATOM   2848  C   PHE A 655     160.864 169.039 115.082  1.00 66.07
ATOM   2849  O   PHE A 655     160.155 168.940 116.080  1.00 66.07
ATOM   2850  CB  PHE A 655     160.997 171.521 115.478  1.00 66.07
ATOM   2851  CG  PHE A 655     161.016 172.858 114.846  1.00 66.07
ATOM   2852  CD1 PHE A 655     162.191 173.388 114.366  1.00 66.07
ATOM   2853  CD2 PHE A 655     159.855 173.575 114.712  1.00 66.07
ATOM   2854  CE1 PHE A 655     162.203 174.603 113.779  1.00 66.07
ATOM   2855  CE2 PHE A 655     159.862 174.789 114.128  1.00 66.07
ATOM   2856  CZ  PHE A 655     161.034 175.311 113.659  1.00 66.07
ATOM   2857  N   LYS A 656     161.333 168.000 114.401  1.00 66.86
ATOM   2858  CA  LYS A 656     161.146 166.634 114.866  1.00 66.86
ATOM   2859  C   LYS A 656     161.561 166.478 116.314  1.00 66.86
ATOM   2860  O   LYS A 656     160.863 165.836 117.097  1.00 66.86
ATOM   2861  CB  LYS A 656     161.946 165.705 113.964  1.00 66.86
ATOM   2862  CG  LYS A 656     161.896 164.228 114.265  1.00 66.86
ATOM   2863  CD  LYS A 656     162.921 163.550 113.358  1.00 66.86
ATOM   2864  CE  LYS A 656     163.057 162.055 113.584  1.00 66.86
ATOM   2865  NZ  LYS A 656     164.091 161.473 112.681  1.00 66.86
ATOM   2866  N   ALA A 657     162.682 167.075 116.696  1.00 63.23
ATOM   2867  CA  ALA A 657     163.130 166.954 118.074  1.00 63.23
ATOM   2868  C   ALA A 657     162.118 167.552 119.033  1.00 63.23
ATOM   2869  O   ALA A 657     161.856 166.990 120.096  1.00 63.23
ATOM   2870  CB  ALA A 657     164.484 167.623 118.240  1.00 63.23
ATOM   2871  N   VAL A 658     161.505 168.667 118.662  1.00 64.12
ATOM   2872  CA  VAL A 658     160.534 169.291 119.550  1.00 64.12
ATOM   2873  C   VAL A 658     159.299 168.431 119.659  1.00 64.12
ATOM   2874  O   VAL A 658     158.770 168.214 120.750  1.00 64.12
ATOM   2875  CB  VAL A 658     160.155 170.686 119.051  1.00 64.12
ATOM   2876  CG1 VAL A 658     159.163 171.304 119.980  1.00 64.12
ATOM   2877  CG2 VAL A 658     161.349 171.567 118.925  1.00 64.12
ATOM   2878  N   PHE A 659     158.792 167.977 118.523  1.00 61.50
ATOM   2879  CA  PHE A 659     157.587 167.168 118.501  1.00 61.50
ATOM   2880  C   PHE A 659     157.762 165.924 119.339  1.00 61.50
ATOM   2881  O   PHE A 659     156.911 165.587 120.167  1.00 61.50
ATOM   2882  CB  PHE A 659     157.302 166.825 117.060  1.00 61.50
ATOM   2883  CG  PHE A 659     156.163 165.933 116.846  1.00 61.50
ATOM   2884  CD1 PHE A 659     154.902 166.431 116.756  1.00 61.50
ATOM   2885  CD2 PHE A 659     156.361 164.602 116.632  1.00 61.50
ATOM   2886  CE1 PHE A 659     153.860 165.614 116.518  1.00 61.50
ATOM   2887  CE2 PHE A 659     155.322 163.785 116.391  1.00 61.50
ATOM   2888  CZ  PHE A 659     154.068 164.290 116.334  1.00 61.50
ATOM   2889  N   ILE A 660     158.891 165.252 119.173  1.00 59.63
ATOM   2890  CA  ILE A 660     159.123 164.031 119.920  1.00 59.63
ATOM   2891  C   ILE A 660     159.323 164.333 121.386  1.00 59.63
ATOM   2892  O   ILE A 660     158.891 163.567 122.241  1.00 59.63
ATOM   2893  CB  ILE A 660     160.316 163.265 119.348  1.00 59.63
ATOM   2894  CG1 ILE A 660     160.071 162.886 117.890  1.00 59.63
ATOM   2895  CG2 ILE A 660     160.568 162.054 120.180  1.00 59.63
ATOM   2896  CD1 ILE A 660     158.938 161.922 117.634  1.00 59.63
ATOM   2897  N   ILE A 661     160.010 165.418 121.716  1.00 59.52
ATOM   2898  CA  ILE A 661     160.188 165.727 123.124  1.00 59.52
ATOM   2899  C   ILE A 661     158.856 166.035 123.756  1.00 59.52
ATOM   2900  O   ILE A 661     158.605 165.676 124.905  1.00 59.52
ATOM   2901  CB  ILE A 661     161.165 166.886 123.309  1.00 59.52
ATOM   2902  CG1 ILE A 661     162.561 166.452 122.902  1.00 59.52
ATOM   2903  CG2 ILE A 661     161.216 167.271 124.749  1.00 59.52
ATOM   2904  CD1 ILE A 661     163.450 167.579 122.499  1.00 59.52
ATOM   2905  N   LEU A 662     157.988 166.722 123.029  1.00 59.84
ATOM   2906  CA  LEU A 662     156.669 167.008 123.561  1.00 59.84
ATOM   2907  C   LEU A 662     155.920 165.735 123.831  1.00 59.84
ATOM   2908  O   LEU A 662     155.382 165.554 124.917  1.00 59.84
ATOM   2909  CB  LEU A 662     155.870 167.845 122.586  1.00 59.84
ATOM   2910  CG  LEU A 662     156.071 169.339 122.669  1.00 59.84
ATOM   2911  CD1 LEU A 662     155.456 169.963 121.462  1.00 59.84
ATOM   2912  CD2 LEU A 662     155.473 169.888 123.921  1.00 59.84
ATOM   2913  N   LEU A 663     155.878 164.839 122.854  1.00 58.09
ATOM   2914  CA  LEU A 663     155.129 163.610 123.047  1.00 58.09
ATOM   2915  C   LEU A 663     155.722 162.775 124.153  1.00 58.09
ATOM   2916  O   LEU A 663     154.990 162.150 124.909  1.00 58.09
ATOM   2917  CB  LEU A 663     155.098 162.806 121.773  1.00 58.09
ATOM   2918  CG  LEU A 663     154.204 163.359 120.699  1.00 58.09
ATOM   2919  CD1 LEU A 663     154.517 162.643 119.433  1.00 58.09
ATOM   2920  CD2 LEU A 663     152.779 163.176 121.082  1.00 58.09
ATOM   2921  N   LEU A 664     157.040 162.715 124.247  1.00 59.01
ATOM   2922  CA  LEU A 664     157.640 161.939 125.316  1.00 59.01
ATOM   2923  C   LEU A 664     157.335 162.554 126.662  1.00 59.01
ATOM   2924  O   LEU A 664     157.072 161.840 127.629  1.00 59.01
ATOM   2925  CB  LEU A 664     159.137 161.824 125.096  1.00 59.01
ATOM   2926  CG  LEU A 664     159.522 160.994 123.878  1.00 59.01
ATOM   2927  CD1 LEU A 664     160.990 161.118 123.591  1.00 59.01
ATOM   2928  CD2 LEU A 664     159.155 159.572 124.082  1.00 59.01
ATOM   2929  N   ALA A 665     157.358 163.876 126.748  1.00 58.59
ATOM   2930  CA  ALA A 665     156.983 164.519 127.990  1.00 58.59
ATOM   2931  C   ALA A 665     155.533 164.242 128.304  1.00 58.59
ATOM   2932  O   ALA A 665     155.178 164.000 129.456  1.00 58.59
ATOM   2933  CB  ALA A 665     157.248 166.014 127.902  1.00 58.59
ATOM   2934  N   TYR A 666     154.683 164.249 127.288  1.00 57.65
ATOM   2935  CA  TYR A 666     153.275 163.973 127.504  1.00 57.65
ATOM   2936  C   TYR A 666     153.076 162.556 127.987  1.00 57.65
ATOM   2937  O   TYR A 666     152.336 162.311 128.941  1.00 57.65
ATOM   2938  CB  TYR A 666     152.487 164.190 126.227  1.00 57.65
ATOM   2939  CG  TYR A 666     151.117 163.659 126.359  1.00 57.65
ATOM   2940  CD1 TYR A 666     150.245 164.188 127.263  1.00 57.65
ATOM   2941  CD2 TYR A 666     150.700 162.606 125.607  1.00 57.65
ATOM   2942  CE1 TYR A 666     148.997 163.702 127.398  1.00 57.65
ATOM   2943  CE2 TYR A 666     149.452 162.104 125.740  1.00 57.65
ATOM   2944  CZ  TYR A 666     148.606 162.652 126.641  1.00 57.65
ATOM   2945  OH  TYR A 666     147.347 162.137 126.776  1.00 57.65
ATOM   2946  N   VAL A 667     153.738 161.605 127.335  1.00 58.87
ATOM   2947  CA  VAL A 667     153.594 160.200 127.678  1.00 58.87
ATOM   2948  C   VAL A 667     154.079 159.957 129.088  1.00 58.87
ATOM   2949  O   VAL A 667     153.418 159.285 129.877  1.00 58.87
ATOM   2950  CB  VAL A 667     154.349 159.338 126.661  1.00 58.87
ATOM   2951  CG1 VAL A 667     154.692 157.992 127.211  1.00 58.87
ATOM   2952  CG2 VAL A 667     153.533 159.186 125.467  1.00 58.87
ATOM   2953  N   ILE A 668     155.246 160.482 129.428  1.00 62.75
ATOM   2954  CA  ILE A 668     155.749 160.289 130.777  1.00 62.75
ATOM   2955  C   ILE A 668     154.811 160.933 131.776  1.00 62.75
ATOM   2956  O   ILE A 668     154.567 160.388 132.853  1.00 62.75
ATOM   2957  CB  ILE A 668     157.172 160.845 130.916  1.00 62.75
ATOM   2958  CG1 ILE A 668     158.133 160.089 130.011  1.00 62.75
ATOM   2959  CG2 ILE A 668     157.635 160.734 132.359  1.00 62.75
ATOM   2960  CD1 ILE A 668     159.388 160.851 129.724  1.00 62.75
ATOM   2961  N   LEU A 669     154.282 162.106 131.451  1.00 62.03
ATOM   2962  CA  LEU A 669     153.491 162.820 132.435  1.00 62.03
ATOM   2963  C   LEU A 669     152.157 162.148 132.674  1.00 62.03
ATOM   2964  O   LEU A 669     151.719 162.026 133.818  1.00 62.03
ATOM   2965  CB  LEU A 669     153.293 164.252 131.992  1.00 62.03
ATOM   2966  CG  LEU A 669     154.502 165.135 132.209  1.00 62.03
ATOM   2967  CD1 LEU A 669     154.234 166.422 131.500  1.00 62.03
ATOM   2968  CD2 LEU A 669     154.782 165.383 133.672  1.00 62.03
ATOM   2969  N   THR A 670     151.491 161.712 131.620  1.00 62.39
ATOM   2970  CA  THR A 670     150.214 161.046 131.804  1.00 62.39
ATOM   2971  C   THR A 670     150.384 159.544 131.899  1.00 62.39
ATOM   2972  O   THR A 670     150.142 158.957 132.954  1.00 62.39
ATOM   2973  CB  THR A 670     149.288 161.386 130.654  1.00 62.39
ATOM   2974  OG1 THR A 670     149.853 160.891 129.442  1.00 62.39
ATOM   2975  CG2 THR A 670     149.128 162.865 130.561  1.00 62.39
ATOM   2976  N   TYR A 671     150.876 158.931 130.825  1.00 63.90
ATOM   2977  CA  TYR A 671     150.800 157.482 130.686  1.00 63.90
ATOM   2978  C   TYR A 671     151.549 156.779 131.792  1.00 63.90
ATOM   2979  O   TYR A 671     151.162 155.682 132.207  1.00 63.90
ATOM   2980  CB  TYR A 671     151.354 157.027 129.343  1.00 63.90
ATOM   2981  CG  TYR A 671     151.135 155.568 129.105  1.00 63.90
ATOM   2982  CD1 TYR A 671     149.896 155.106 128.750  1.00 63.90
ATOM   2983  CD2 TYR A 671     152.147 154.655 129.258  1.00 63.90
ATOM   2984  CE1 TYR A 671     149.658 153.786 128.522  1.00 63.90
ATOM   2985  CE2 TYR A 671     151.917 153.318 129.040  1.00 63.90
ATOM   2986  CZ  TYR A 671     150.661 152.892 128.669  1.00 63.90
ATOM   2987  OH  TYR A 671     150.387 151.565 128.448  1.00 63.90
ATOM   2988  N   ILE A 672     152.642 157.365 132.250  1.00 65.77
ATOM   2989  CA  ILE A 672     153.339 156.798 133.386  1.00 65.77
ATOM   2990  C   ILE A 672     152.994 157.540 134.667  1.00 65.77
ATOM   2991  O   ILE A 672     152.603 156.917 135.649  1.00 65.77
ATOM   2992  CB  ILE A 672     154.853 156.749 133.101  1.00 65.77
ATOM   2993  CG1 ILE A 672     155.103 155.774 131.939  1.00 65.77
ATOM   2994  CG2 ILE A 672     155.616 156.282 134.327  1.00 65.77
ATOM   2995  CD1 ILE A 672     156.519 155.699 131.425  1.00 65.77
ATOM   2996  N   LEU A 673     153.074 158.863 134.716  1.00 67.67
ATOM   2997  CA  LEU A 673     153.010 159.499 136.026  1.00 67.67
ATOM   2998  C   LEU A 673     151.580 159.665 136.499  1.00 67.67
ATOM   2999  O   LEU A 673     151.243 159.268 137.615  1.00 67.67
ATOM   3000  CB  LEU A 673     153.742 160.839 136.021  1.00 67.67
ATOM   3001  CG  LEU A 673     155.262 160.769 135.967  1.00 67.67
ATOM   3002  CD1 LEU A 673     155.798 162.156 135.863  1.00 67.67
ATOM   3003  CD2 LEU A 673     155.826 160.137 137.185  1.00 67.67
ATOM   3004  N   LEU A 674     150.722 160.235 135.677  1.00 68.30
ATOM   3005  CA  LEU A 674     149.397 160.554 136.179  1.00 68.30
ATOM   3006  C   LEU A 674     148.610 159.297 136.525  1.00 68.30
ATOM   3007  O   LEU A 674     148.072 159.182 137.632  1.00 68.30
ATOM   3008  CB  LEU A 674     148.665 161.395 135.152  1.00 68.30
ATOM   3009  CG  LEU A 674     147.400 162.112 135.561  1.00 68.30
ATOM   3010  CD1 LEU A 674     147.568 162.939 136.793  1.00 68.30
ATOM   3011  CD2 LEU A 674     147.000 162.976 134.426  1.00 68.30
ATOM   3012  N   LEU A 675     148.579 158.323 135.622  1.00 67.15
ATOM   3013  CA  LEU A 675     147.750 157.149 135.854  1.00 67.15
ATOM   3014  C   LEU A 675     148.244 156.367 137.056  1.00 67.15
ATOM   3015  O   LEU A 675     147.448 155.910 137.888  1.00 67.15
ATOM   3016  CB  LEU A 675     147.739 156.263 134.616  1.00 67.15
ATOM   3017  CG  LEU A 675     147.378 156.917 133.276  1.00 67.15
ATOM   3018  CD1 LEU A 675     147.603 155.949 132.125  1.00 67.15
ATOM   3019  CD2 LEU A 675     145.955 157.405 133.268  1.00 67.15
ATOM   3020  N   ASN A 676     149.551 156.225 137.192  1.00 73.74
ATOM   3021  CA  ASN A 676     150.049 155.512 138.352  1.00 73.74
ATOM   3022  C   ASN A 676     149.754 156.274 139.624  1.00 73.74
ATOM   3023  O   ASN A 676     149.541 155.662 140.672  1.00 73.74
ATOM   3024  CB  ASN A 676     151.540 155.248 138.201  1.00 73.74
ATOM   3025  CG  ASN A 676     151.858 154.437 136.959  1.00 73.74
ATOM   3026  OD1 ASN A 676     150.959 153.984 136.241  1.00 73.74
ATOM   3027  ND2 ASN A 676     153.146 154.268 136.688  1.00 73.74
ATOM   3028  N   MET A 677     149.701 157.597 139.557  1.00 78.09
ATOM   3029  CA  MET A 677     149.406 158.333 140.772  1.00 78.09
ATOM   3030  C   MET A 677     147.953 158.165 141.167  1.00 78.09
ATOM   3031  O   MET A 677     147.631 158.108 142.359  1.00 78.09
ATOM   3032  CB  MET A 677     149.739 159.806 140.597  1.00 78.09
ATOM   3033  CG  MET A 677     149.574 160.610 141.856  1.00 78.09
ATOM   3034  SD  MET A 677     150.366 159.871 143.309  1.00 78.09
ATOM   3035  CE  MET A 677     152.077 159.858 142.781  1.00 78.09
ATOM   3036  N   LEU A 678     147.069 158.094 140.179  1.00 75.12
ATOM   3037  CA  LEU A 678     145.687 157.723 140.439  1.00 75.12
ATOM   3038  C   LEU A 678     145.626 156.405 141.184  1.00 75.12
ATOM   3039  O   LEU A 678     144.912 156.268 142.186  1.00 75.12
ATOM   3040  CB  LEU A 678     144.943 157.638 139.108  1.00 75.12
ATOM   3041  CG  LEU A 678     143.632 156.887 138.957  1.00 75.12
ATOM   3042  CD1 LEU A 678     142.522 157.717 139.559  1.00 75.12
ATOM   3043  CD2 LEU A 678     143.396 156.608 137.489  1.00 75.12
ATOM   3044  N   ILE A 679     146.376 155.418 140.696  1.00 74.29
ATOM   3045  CA  ILE A 679     146.370 154.112 141.346  1.00 74.29
ATOM   3046  C   ILE A 679     146.897 154.225 142.769  1.00 74.29
ATOM   3047  O   ILE A 679     146.398 153.562 143.675  1.00 74.29
ATOM   3048  CB  ILE A 679     147.164 153.082 140.523  1.00 74.29
ATOM   3049  CG1 ILE A 679     146.479 152.824 139.181  1.00 74.29
ATOM   3050  CG2 ILE A 679     147.292 151.783 141.290  1.00 74.29
ATOM   3051  CD1 ILE A 679     147.359 152.167 138.148  1.00 74.29
ATOM   3052  N   ALA A 680     147.919 155.048 142.988  1.00 79.97
ATOM   3053  CA  ALA A 680     148.463 155.220 144.337  1.00 79.97
ATOM   3054  C   ALA A 680     147.420 155.787 145.292  1.00 79.97
ATOM   3055  O   ALA A 680     147.235 155.291 146.423  1.00 79.97
ATOM   3056  CB  ALA A 680     149.684 156.137 144.276  1.00 79.97
ATOM   3057  N   LEU A 681     146.715 156.817 144.846  1.00 81.65
ATOM   3058  CA  LEU A 681     145.687 157.415 145.680  1.00 81.65
ATOM   3059  C   LEU A 681     144.599 156.418 146.003  1.00 81.65
ATOM   3060  O   LEU A 681     144.239 156.234 147.175  1.00 81.65
ATOM   3061  CB  LEU A 681     145.073 158.594 144.965  1.00 81.65
ATOM   3062  CG  LEU A 681     145.997 159.763 144.752  1.00 81.65
ATOM   3063  CD1 LEU A 681     145.308 160.700 143.810  1.00 81.65
ATOM   3064  CD2 LEU A 681     146.287 160.433 146.068  1.00 81.65
ATOM   3065  N   MET A 682     144.076 155.761 144.976  1.00 81.58
ATOM   3066  CA  MET A 682     143.076 154.742 145.213  1.00 81.58
ATOM   3067  C   MET A 682     143.609 153.669 146.142  1.00 81.58
ATOM   3068  O   MET A 682     142.851 153.089 146.916  1.00 81.58
ATOM   3069  CB  MET A 682     142.644 154.115 143.901  1.00 81.58
ATOM   3070  CG  MET A 682     141.871 155.018 142.989  1.00 81.58
ATOM   3071  SD  MET A 682     141.664 154.207 141.396  1.00 81.58
ATOM   3072  CE  MET A 682     140.571 152.856 141.824  1.00 81.58
ATOM   3073  N   GLY A 683     144.904 153.378 146.070  1.00 86.91
ATOM   3074  CA  GLY A 683     145.461 152.356 146.931  1.00 86.91
ATOM   3075  C   GLY A 683     145.265 152.696 148.388  1.00 86.91
ATOM   3076  O   GLY A 683     144.648 151.929 149.142  1.00 86.91
ATOM   3077  N   GLU A 684     145.709 153.890 148.784  1.00 90.18
ATOM   3078  CA  GLU A 684     145.502 154.278 150.180  1.00 90.18
ATOM   3079  C   GLU A 684     144.018 154.304 150.521  1.00 90.18
ATOM   3080  O   GLU A 684     143.587 153.786 151.567  1.00 90.18
ATOM   3081  CB  GLU A 684     146.117 155.640 150.472  1.00 90.18
ATOM   3082  CG  GLU A 684     146.119 155.999 151.969  1.00 90.18
ATOM   3083  CD  GLU A 684     144.822 156.655 152.467  1.00 90.18
ATOM   3084  OE1 GLU A 684     143.952 157.009 151.639  1.00 90.18
ATOM   3085  OE2 GLU A 684     144.672 156.811 153.698  1.00 90.18
ATOM   3086  N   THR A 685     143.216 154.875 149.628  1.00 89.62
ATOM   3087  CA  THR A 685     141.814 155.079 149.941  1.00 89.62
ATOM   3088  C   THR A 685     141.101 153.757 150.162  1.00 89.62
ATOM   3089  O   THR A 685     140.448 153.565 151.193  1.00 89.62
ATOM   3090  CB  THR A 685     141.149 155.855 148.820  1.00 89.62
ATOM   3091  OG1 THR A 685     141.837 157.097 148.639  1.00 89.62
ATOM   3092  CG2 THR A 685     139.708 156.125 149.158  1.00 89.62
ATOM   3093  N   VAL A 686     141.250 152.819 149.225  1.00 89.24
ATOM   3094  CA  VAL A 686     140.536 151.553 149.326  1.00 89.24
ATOM   3095  C   VAL A 686     141.010 150.784 150.537  1.00 89.24
ATOM   3096  O   VAL A 686     140.191 150.151 151.225  1.00 89.24
ATOM   3097  CB  VAL A 686     140.681 150.717 148.043  1.00 89.24
ATOM   3098  CG1 VAL A 686     142.058 150.120 147.944  1.00 89.24
ATOM   3099  CG2 VAL A 686     139.643 149.620 148.016  1.00 89.24
ATOM   3100  N   ASN A 687     142.291 150.931 150.894  1.00 92.05
ATOM   3101  CA  ASN A 687     142.787 150.299 152.143  1.00 92.05
ATOM   3102  C   ASN A 687     141.972 150.884 153.299  1.00 92.05
ATOM   3103  O   ASN A 687     141.725 150.156 154.281  1.00 92.05
ATOM   3104  CB  ASN A 687     144.294 150.505 152.318  1.00 92.05
ATOM   3105  CG  ASN A 687     144.831 149.946 153.618  1.00 92.05
ATOM   3106  OD1 ASN A 687     144.876 148.732 153.807  1.00 92.05
ATOM   3107  ND2 ASN A 687     145.235 150.824 154.521  1.00 92.05
ATOM   3108  N   LYS A 688     141.538 152.142 153.160  1.00 92.62
ATOM   3109  CA  LYS A 688     140.767 152.765 154.230  1.00 92.62
ATOM   3110  C   LYS A 688     139.247 152.607 154.131  1.00 92.62
ATOM   3111  O   LYS A 688     138.567 152.921 155.112  1.00 92.62
ATOM   3112  CB  LYS A 688     141.093 154.259 154.312  1.00 92.62
ATOM   3113  CG  LYS A 688     142.550 154.565 154.644  1.00 92.62
ATOM   3114  CD  LYS A 688     142.967 154.114 156.039  1.00 92.62
ATOM   3115  CE  LYS A 688     144.459 154.220 156.212  1.00 92.62
ATOM   3116  NZ  LYS A 688     144.926 155.623 156.138  1.00 92.62
ATOM   3117  N   ILE A 689     138.674 152.214 152.989  1.00 91.66
ATOM   3118  CA  ILE A 689     137.214 152.290 152.813  1.00 91.66
ATOM   3119  C   ILE A 689     136.576 151.004 152.295  1.00 91.66
ATOM   3120  O   ILE A 689     135.365 151.017 151.951  1.00 91.66
ATOM   3121  CB  ILE A 689     136.817 153.483 151.931  1.00 91.66
ATOM   3122  CG1 ILE A 689     137.226 153.291 150.468  1.00 91.66
ATOM   3123  CG2 ILE A 689     137.424 154.749 152.512  1.00 91.66
ATOM   3124  CD1 ILE A 689     136.537 154.256 149.569  1.00 91.66
ATOM   3125  N   ALA A 690     137.329 149.906 152.200  1.00 93.45
ATOM   3126  CA  ALA A 690     136.679 148.629 151.925  1.00 93.45
ATOM   3127  C   ALA A 690     135.592 148.332 152.952  1.00 93.45
ATOM   3128  O   ALA A 690     134.501 147.864 152.600  1.00 93.45
ATOM   3129  CB  ALA A 690     137.705 147.503 151.909  1.00 93.45
ATOM   3130  N   GLN A 691     135.860 148.624 154.226  1.00 97.61
ATOM   3131  CA  GLN A 691     134.858 148.400 155.260  1.00 97.61
ATOM   3132  C   GLN A 691     133.607 149.233 155.055  1.00 97.61
ATOM   3133  O   GLN A 691     132.517 148.777 155.407  1.00 97.61
ATOM   3134  CB  GLN A 691     135.439 148.696 156.649  1.00 97.61
ATOM   3135  CG  GLN A 691     135.688 150.181 157.008  1.00 97.61
ATOM   3136  CD  GLN A 691     136.845 150.794 156.244  1.00 97.61
ATOM   3137  OE1 GLN A 691     137.095 150.443 155.097  1.00 97.61
ATOM   3138  NE2 GLN A 691     137.575 151.692 156.893  1.00 97.61
ATOM   3139  N   GLU A 692     133.728 150.438 154.508  1.00 96.70
ATOM   3140  CA  GLU A 692     132.539 151.263 154.362  1.00 96.70
ATOM   3141  C   GLU A 692     131.686 150.786 153.197  1.00 96.70
ATOM   3142  O   GLU A 692     130.456 150.754 153.308  1.00 96.70
ATOM   3143  CB  GLU A 692     132.936 152.730 154.223  1.00 96.70
ATOM   3144  CG  GLU A 692     133.526 153.291 155.519  1.00 96.70
ATOM   3145  CD  GLU A 692     134.039 154.704 155.376  1.00 96.70
ATOM   3146  OE1 GLU A 692     133.482 155.460 154.560  1.00 96.70
ATOM   3147  OE2 GLU A 692     135.007 155.055 156.080  1.00 96.70
ATOM   3148  N   SER A 693     132.305 150.368 152.091  1.00 90.55
ATOM   3149  CA  SER A 693     131.490 149.746 151.048  1.00 90.55
ATOM   3150  C   SER A 693     130.820 148.482 151.560  1.00 90.55
ATOM   3151  O   SER A 693     129.633 148.235 151.277  1.00 90.55
ATOM   3152  CB  SER A 693     132.334 149.417 149.825  1.00 90.55
ATOM   3153  OG  SER A 693     132.594 150.586 149.087  1.00 90.55
ATOM   3154  N   LYS A 694     131.554 147.691 152.351  1.00 95.92
ATOM   3155  CA  LYS A 694     131.047 146.403 152.812  1.00 95.92
ATOM   3156  C   LYS A 694     129.777 146.552 153.626  1.00 95.92
ATOM   3157  O   LYS A 694     129.027 145.585 153.788  1.00 95.92
ATOM   3158  CB  LYS A 694     132.109 145.693 153.649  1.00 95.92
ATOM   3159  CG  LYS A 694     133.190 144.981 152.854  1.00 95.92
ATOM   3160  CD  LYS A 694     134.206 144.395 153.809  1.00 95.92
ATOM   3161  CE  LYS A 694     135.315 143.679 153.086  1.00 95.92
ATOM   3162  NZ  LYS A 694     136.241 143.061 154.066  1.00 95.92
ATOM   3163  N   ASN A 695     129.540 147.731 154.178  1.00103.04
ATOM   3164  CA  ASN A 695     128.291 148.019 154.849  1.00103.04
ATOM   3165  C   ASN A 695     127.294 148.737 153.961  1.00103.04
ATOM   3166  O   ASN A 695     126.090 148.471 154.067  1.00103.04
ATOM   3167  CB  ASN A 695     128.572 148.868 156.077  1.00103.04
ATOM   3168  CG  ASN A 695     129.326 148.120 157.135  1.00103.04
ATOM   3169  OD1 ASN A 695     128.965 147.004 157.492  1.00103.04
ATOM   3170  ND2 ASN A 695     130.414 148.709 157.616  1.00103.04
ATOM   3171  N   ILE A 696     127.754 149.636 153.084  1.00 96.26
ATOM   3172  CA  ILE A 696     126.807 150.402 152.284  1.00 96.26
ATOM   3173  C   ILE A 696     125.998 149.458 151.405  1.00 96.26
ATOM   3174  O   ILE A 696     124.901 149.801 150.959  1.00 96.26
ATOM   3175  CB  ILE A 696     127.526 151.490 151.460  1.00 96.26
ATOM   3176  CG1 ILE A 696     126.622 152.709 151.289  1.00 96.26
ATOM   3177  CG2 ILE A 696     127.940 150.986 150.108  1.00 96.26
ATOM   3178  CD1 ILE A 696     127.312 153.876 150.727  1.00 96.26
ATOM   3179  N   TRP A 697     126.558 148.282 151.096  1.00 96.15
ATOM   3180  CA  TRP A 697     125.744 147.154 150.686  1.00 96.15
ATOM   3181  C   TRP A 697     124.469 147.039 151.514  1.00 96.15
ATOM   3182  O   TRP A 697     123.364 147.005 150.942  1.00 96.15
ATOM   3183  CB  TRP A 697     126.542 145.854 150.787  1.00 96.15
ATOM   3184  CG  TRP A 697     125.668 144.692 150.888  1.00 96.15
ATOM   3185  CD1 TRP A 697     124.824 144.217 149.938  1.00 96.15
ATOM   3186  CD2 TRP A 697     125.566 143.813 151.991  1.00 96.15
ATOM   3187  NE1 TRP A 697     124.189 143.106 150.389  1.00 96.15
ATOM   3188  CE2 TRP A 697     124.631 142.829 151.651  1.00 96.15
ATOM   3189  CE3 TRP A 697     126.178 143.764 153.230  1.00 96.15
ATOM   3190  CZ2 TRP A 697     124.288 141.808 152.500  1.00 96.15
ATOM   3191  CZ3 TRP A 697     125.829 142.766 154.092  1.00 96.15
ATOM   3192  CH2 TRP A 697     124.891 141.787 153.728  1.00 96.15
ATOM   3193  N   LYS A 698     124.582 147.061 152.853  1.00104.93
ATOM   3194  CA  LYS A 698     123.397 146.852 153.694  1.00104.93
ATOM   3195  C   LYS A 698     122.409 147.972 153.519  1.00104.93
ATOM   3196  O   LYS A 698     121.192 147.757 153.562  1.00104.93
ATOM   3197  CB  LYS A 698     123.732 146.775 155.181  1.00104.93
ATOM   3198  CG  LYS A 698     124.213 145.438 155.670  1.00104.93
ATOM   3199  CD  LYS A 698     124.257 145.357 157.208  1.00104.93
ATOM   3200  CE  LYS A 698     125.451 146.094 157.778  1.00104.93
ATOM   3201  NZ  LYS A 698     126.668 145.276 157.633  1.00104.93
ATOM   3202  N   LEU A 699     122.920 149.194 153.394  1.00104.70
ATOM   3203  CA  LEU A 699     122.037 150.332 153.230  1.00104.70
ATOM   3204  C   LEU A 699     121.249 150.222 151.946  1.00104.70
ATOM   3205  O   LEU A 699     120.062 150.513 151.921  1.00104.70
ATOM   3206  CB  LEU A 699     122.832 151.618 153.241  1.00104.70
ATOM   3207  CG  LEU A 699     123.310 152.025 154.625  1.00104.70
ATOM   3208  CD1 LEU A 699     124.441 153.018 154.502  1.00104.70
ATOM   3209  CD2 LEU A 699     122.175 152.602 155.389  1.00104.70
ATOM   3210  N   GLN A 700     121.890 149.836 150.856  1.00 91.98
ATOM   3211  CA  GLN A 700     121.110 149.673 149.644  1.00 91.98
ATOM   3212  C   GLN A 700     120.093 148.562 149.810  1.00 91.98
ATOM   3213  O   GLN A 700     119.006 148.627 149.223  1.00 91.98
ATOM   3214  CB  GLN A 700     122.015 149.429 148.441  1.00 91.98
ATOM   3215  CG  GLN A 700     121.363 149.815 147.138  1.00 91.98
ATOM   3216  CD  GLN A 700     120.358 148.823 146.624  1.00 91.98
ATOM   3217  OE1 GLN A 700     120.255 147.703 147.113  1.00 91.98
ATOM   3218  NE2 GLN A 700     119.606 149.226 145.625  1.00 91.98
ATOM   3219  N   ARG A 701     120.397 147.546 150.615  1.00100.03
ATOM   3220  CA  ARG A 701     119.376 146.523 150.830  1.00100.03
ATOM   3221  C   ARG A 701     118.194 147.077 151.602  1.00100.03
ATOM   3222  O   ARG A 701     117.037 146.718 151.345  1.00100.03
ATOM   3223  CB  ARG A 701     119.956 145.327 151.573  1.00100.03
ATOM   3224  CG  ARG A 701     120.355 144.208 150.650  1.00100.03
ATOM   3225  CD  ARG A 701     120.926 143.050 151.403  1.00100.03
ATOM   3226  NE  ARG A 701     119.898 142.218 152.014  1.00100.03
ATOM   3227  CZ  ARG A 701     120.092 141.440 153.079  1.00100.03
ATOM   3228  NH1 ARG A 701     121.259 141.385 153.689  1.00100.03
ATOM   3229  NH2 ARG A 701     119.104 140.714 153.560  1.00100.03
ATOM   3230  N   ALA A 702     118.472 147.944 152.563  1.00105.66
ATOM   3231  CA  ALA A 702     117.403 148.585 153.307  1.00105.66
ATOM   3232  C   ALA A 702     116.574 149.479 152.408  1.00105.66
ATOM   3233  O   ALA A 702     115.351 149.541 152.535  1.00105.66
ATOM   3234  CB  ALA A 702     118.009 149.379 154.451  1.00105.66
ATOM   3235  N   ILE A 703     117.229 150.200 151.512  1.00103.05
ATOM   3236  CA  ILE A 703     116.500 151.058 150.599  1.00103.05
ATOM   3237  C   ILE A 703     115.578 150.225 149.742  1.00103.05
ATOM   3238  O   ILE A 703     114.412 150.577 149.527  1.00103.05
ATOM   3239  CB  ILE A 703     117.477 151.862 149.735  1.00103.05
ATOM   3240  CG1 ILE A 703     118.223 152.885 150.587  1.00103.05
ATOM   3241  CG2 ILE A 703     116.753 152.498 148.579  1.00103.05
ATOM   3242  CD1 ILE A 703     117.418 154.078 151.017  1.00103.05
ATOM   3243  N   THR A 704     116.094 149.115 149.228  1.00101.69
ATOM   3244  CA  THR A 704     115.273 148.221 148.434  1.00101.69
ATOM   3245  C   THR A 704     114.054 147.771 149.215  1.00101.69
ATOM   3246  O   THR A 704     112.936 147.754 148.689  1.00101.69
ATOM   3247  CB  THR A 704     116.110 147.022 148.027  1.00101.69
ATOM   3248  OG1 THR A 704     117.370 147.469 147.519  1.00101.69
ATOM   3249  CG2 THR A 704     115.401 146.204 146.978  1.00101.69
ATOM   3250  N   ILE A 705     114.247 147.437 150.486  1.00106.74
ATOM   3251  CA  ILE A 705     113.145 146.917 151.284  1.00106.74
ATOM   3252  C   ILE A 705     112.119 148.005 151.555  1.00106.74
ATOM   3253  O   ILE A 705     110.909 147.769 151.499  1.00106.74
ATOM   3254  CB  ILE A 705     113.688 146.300 152.576  1.00106.74
ATOM   3255  CG1 ILE A 705     114.482 145.048 152.234  1.00106.74
ATOM   3256  CG2 ILE A 705     112.573 145.964 153.515  1.00106.74
ATOM   3257  CD1 ILE A 705     115.544 144.727 153.216  1.00106.74
ATOM   3258  N   LEU A 706     112.579 149.205 151.868  1.00109.73
ATOM   3259  CA  LEU A 706     111.643 150.282 152.143  1.00109.73
ATOM   3260  C   LEU A 706     110.861 150.656 150.902  1.00109.73
ATOM   3261  O   LEU A 706     109.651 150.888 150.972  1.00109.73
ATOM   3262  CB  LEU A 706     112.387 151.481 152.704  1.00109.73
ATOM   3263  CG  LEU A 706     113.070 151.176 154.032  1.00109.73
ATOM   3264  CD1 LEU A 706     113.949 152.315 154.390  1.00109.73
ATOM   3265  CD2 LEU A 706     112.058 150.936 155.117  1.00109.73
ATOM   3266  N   ASP A 707     111.523 150.691 149.754  1.00109.18
ATOM   3267  CA  ASP A 707     110.804 150.922 148.513  1.00109.18
ATOM   3268  C   ASP A 707     109.765 149.841 148.289  1.00109.18
ATOM   3269  O   ASP A 707     108.622 150.130 147.909  1.00109.18
ATOM   3270  CB  ASP A 707     111.789 150.955 147.347  1.00109.18
ATOM   3271  CG  ASP A 707     111.139 150.619 146.011  1.00109.18
ATOM   3272  OD1 ASP A 707     110.050 151.149 145.711  1.00109.18
ATOM   3273  OD2 ASP A 707     111.728 149.833 145.244  1.00109.18
ATOM   3274  N   THR A 708     110.147 148.587 148.521  1.00108.00
ATOM   3275  CA  THR A 708     109.239 147.482 148.269  1.00108.00
ATOM   3276  C   THR A 708     108.007 147.592 149.140  1.00108.00
ATOM   3277  O   THR A 708     106.883 147.392 148.673  1.00108.00
ATOM   3278  CB  THR A 708     109.953 146.163 148.529  1.00108.00
ATOM   3279  OG1 THR A 708     111.092 146.058 147.670  1.00108.00
ATOM   3280  CG2 THR A 708     109.017 145.005 148.288  1.00108.00
ATOM   3281  N   GLU A 709     108.196 147.931 150.406  1.00112.00
ATOM   3282  CA  GLU A 709     107.047 148.100 151.279  1.00112.00
ATOM   3283  C   GLU A 709     106.200 149.288 150.848  1.00112.00
ATOM   3284  O   GLU A 709     104.968 149.237 150.930  1.00112.00
ATOM   3285  CB  GLU A 709     107.503 148.249 152.723  1.00112.00
ATOM   3286  CG  GLU A 709     108.071 146.973 153.302  1.00112.00
ATOM   3287  CD  GLU A 709     108.068 146.973 154.805  1.00112.00
ATOM   3288  OE1 GLU A 709     107.817 148.036 155.398  1.00112.00
ATOM   3289  OE2 GLU A 709     108.315 145.911 155.412  1.00112.00
ATOM   3290  N   LYS A 710     106.833 150.368 150.384  1.00112.47
ATOM   3291  CA  LYS A 710     106.051 151.522 149.957  1.00112.47
ATOM   3292  C   LYS A 710     105.165 151.176 148.776  1.00112.47
ATOM   3293  O   LYS A 710     103.991 151.557 148.754  1.00112.47
ATOM   3294  CB  LYS A 710     106.946 152.695 149.582  1.00112.47
ATOM   3295  CG  LYS A 710     107.538 153.440 150.749  1.00112.47
ATOM   3296  CD  LYS A 710     106.550 154.382 151.386  1.00112.47
ATOM   3297  CE  LYS A 710     107.222 155.213 152.453  1.00112.47
ATOM   3298  NZ  LYS A 710     106.220 155.786 153.398  1.00112.47
ATOM   3299  N   SER A 711     105.683 150.435 147.795  1.00114.57
ATOM   3300  CA  SER A 711     104.872 150.270 146.600  1.00114.57
ATOM   3301  C   SER A 711     103.802 149.204 146.783  1.00114.57
ATOM   3302  O   SER A 711     102.628 149.528 146.990  1.00114.57
ATOM   3303  CB  SER A 711     105.753 149.894 145.418  1.00114.57
ATOM   3304  OG  SER A 711     106.298 148.608 145.628  1.00114.57
ATOM   3305  N   PHE A 712     104.189 147.933 146.724  1.00119.94
ATOM   3306  CA  PHE A 712     103.385 146.778 147.126  1.00119.94
ATOM   3307  C   PHE A 712     102.107 146.517 146.318  1.00119.94
ATOM   3308  O   PHE A 712     101.667 145.368 146.251  1.00119.94
ATOM   3309  CB  PHE A 712     103.011 146.922 148.604  1.00119.94
ATOM   3310  CG  PHE A 712     102.319 145.726 149.161  1.00119.94
ATOM   3311  CD1 PHE A 712     102.977 144.522 149.247  1.00119.94
ATOM   3312  CD2 PHE A 712     101.010 145.808 149.603  1.00119.94
ATOM   3313  CE1 PHE A 712     102.347 143.415 149.751  1.00119.94
ATOM   3314  CE2 PHE A 712     100.372 144.703 150.114  1.00119.94
ATOM   3315  CZ  PHE A 712     101.040 143.504 150.186  1.00119.94
ATOM   3316  N   LEU A 713     101.540 147.538 145.662  1.00125.00
ATOM   3317  CA  LEU A 713     100.634 147.409 144.515  1.00125.00
ATOM   3318  C   LEU A 713      99.468 146.439 144.731  1.00125.00
ATOM   3319  O   LEU A 713      99.125 145.694 143.812  1.00125.00
ATOM   3320  CB  LEU A 713     101.410 147.015 143.252  1.00125.00
ATOM   3321  CG  LEU A 713     102.564 147.953 142.860  1.00125.00
ATOM   3322  CD1 LEU A 713     103.197 147.516 141.566  1.00125.00
ATOM   3323  CD2 LEU A 713     102.120 149.409 142.737  1.00125.00
ATOM   3324  N   LYS A 714      98.859 146.403 145.924  1.00127.29
ATOM   3325  CA  LYS A 714      97.650 145.610 146.161  1.00127.29
ATOM   3326  C   LYS A 714      96.484 146.405 146.732  1.00127.29
ATOM   3327  O   LYS A 714      95.395 145.844 146.871  1.00127.29
ATOM   3328  CB  LYS A 714      97.944 144.432 147.109  1.00127.29
ATOM   3329  CG  LYS A 714      98.895 143.347 146.582  1.00127.29
ATOM   3330  CD  LYS A 714      98.465 142.706 145.248  1.00127.29
ATOM   3331  CE  LYS A 714      99.504 141.696 144.767  1.00127.29
ATOM   3332  NZ  LYS A 714      99.101 141.000 143.519  1.00127.29
ATOM   3333  N   CYS A 715      96.671 147.679 147.071  1.00129.12
ATOM   3334  CA  CYS A 715      95.655 148.479 147.764  1.00129.12
ATOM   3335  C   CYS A 715      95.310 147.907 149.140  1.00129.12
ATOM   3336  O   CYS A 715      94.208 148.122 149.648  1.00129.12
ATOM   3337  CB  CYS A 715      94.380 148.623 146.926  1.00129.12
ATOM   3338  SG  CYS A 715      94.659 149.180 145.239  1.00129.12
ATOM   3339  N   MET A 716      96.256 147.204 149.762  1.00127.78
ATOM   3340  CA  MET A 716      96.089 146.633 151.094  1.00127.78
ATOM   3341  C   MET A 716      97.409 146.772 151.837  1.00127.78
ATOM   3342  O   MET A 716      98.455 147.025 151.236  1.00127.78
ATOM   3343  CB  MET A 716      95.667 145.156 151.042  1.00127.78
ATOM   3344  CG  MET A 716      94.290 144.911 150.443  1.00127.78
ATOM   3345  SD  MET A 716      93.888 143.159 150.259  1.00127.78
ATOM   3346  CE  MET A 716      95.045 142.614 148.995  1.00127.78
ATOM   3347  N   ARG A 717      97.348 146.598 153.159  1.00126.43
ATOM   3348  CA  ARG A 717      98.513 146.755 154.024  1.00126.43
ATOM   3349  C   ARG A 717      98.941 145.444 154.679  1.00126.43
ATOM   3350  O   ARG A 717      99.718 145.469 155.634  1.00126.43
ATOM   3351  CB  ARG A 717      98.233 147.817 155.095  1.00126.43
ATOM   3352  CG  ARG A 717      97.994 149.244 154.547  1.00126.43
ATOM   3353  CD  ARG A 717      97.855 150.271 155.679  1.00126.43
ATOM   3354  NE  ARG A 717      97.411 151.584 155.214  1.00126.43
ATOM   3355  CZ  ARG A 717      97.059 152.591 156.016  1.00126.43
ATOM   3356  NH1 ARG A 717      97.096 152.462 157.335  1.00126.43
ATOM   3357  NH2 ARG A 717      96.663 153.742 155.497  1.00126.43
ATOM   3358  N   LYS A 718      98.490 144.293 154.172  1.00122.97
ATOM   3359  CA  LYS A 718      98.813 143.001 154.785  1.00122.97
ATOM   3360  C   LYS A 718     100.187 142.505 154.329  1.00122.97
ATOM   3361  O   LYS A 718     100.330 141.438 153.735  1.00122.97
ATOM   3362  CB  LYS A 718      97.746 141.966 154.458  1.00122.97
ATOM   3363  CG  LYS A 718      96.391 142.193 155.095  1.00122.97
ATOM   3364  CD  LYS A 718      95.411 141.126 154.616  1.00122.97
ATOM   3365  CE  LYS A 718      93.968 141.481 154.918  1.00122.97
ATOM   3366  NZ  LYS A 718      93.014 140.602 154.197  1.00122.97
ATOM   3367  N   ALA A 719     101.213 143.296 154.648  1.00119.62
ATOM   3368  CA  ALA A 719     102.600 142.937 154.370  1.00119.62
ATOM   3369  C   ALA A 719     103.450 143.088 155.619  1.00119.62
ATOM   3370  O   ALA A 719     104.653 143.354 155.534  1.00119.62
ATOM   3371  CB  ALA A 719     103.181 143.795 153.251  1.00119.62
ATOM   3372  N   PHE A 720     102.843 142.923 156.783  1.00123.76
ATOM   3373  CA  PHE A 720     103.579 143.136 158.004  1.00123.76
ATOM   3374  C   PHE A 720     104.555 141.996 158.225  1.00123.76
ATOM   3375  O   PHE A 720     104.414 140.903 157.673  1.00123.76
ATOM   3376  CB  PHE A 720     102.625 143.260 159.185  1.00123.76
ATOM   3377  CG  PHE A 720     101.878 144.555 159.214  1.00123.76
ATOM   3378  CD1 PHE A 720     100.679 144.695 158.546  1.00123.76
ATOM   3379  CD2 PHE A 720     102.381 145.638 159.905  1.00123.76
ATOM   3380  CE1 PHE A 720      99.992 145.889 158.572  1.00123.76
ATOM   3381  CE2 PHE A 720     101.696 146.830 159.931  1.00123.76
ATOM   3382  CZ  PHE A 720     100.502 146.956 159.261  1.00123.76
ATOM   3383  N   ARG A 721     105.566 142.271 159.042  1.00121.66
ATOM   3384  CA  ARG A 721     106.551 141.247 159.351  1.00121.66
ATOM   3385  C   ARG A 721     105.987 140.231 160.332  1.00121.66
ATOM   3386  O   ARG A 721     105.942 139.034 160.033  1.00121.66
ATOM   3387  CB  ARG A 721     107.821 141.894 159.904  1.00121.66
ATOM   3388  CG  ARG A 721     108.557 142.723 158.863  1.00121.66
ATOM   3389  CD  ARG A 721     109.581 143.667 159.476  1.00121.66
ATOM   3390  NE  ARG A 721     110.532 144.182 158.487  1.00121.66
ATOM   3391  CZ  ARG A 721     110.291 145.179 157.636  1.00121.66
ATOM   3392  NH1 ARG A 721     109.133 145.814 157.644  1.00121.66
ATOM   3393  NH2 ARG A 721     111.222 145.550 156.778  1.00121.66
ATOM   3394  N   SER A 722     105.510 140.681 161.487  1.00129.92
ATOM   3395  CA  SER A 722     105.196 139.741 162.551  1.00129.92
ATOM   3396  C   SER A 722     104.382 140.445 163.624  1.00129.92
ATOM   3397  O   SER A 722     104.043 141.624 163.506  1.00129.92
ATOM   3398  CB  SER A 722     106.477 139.165 163.140  1.00129.92
ATOM   3399  OG  SER A 722     107.239 140.220 163.684  1.00129.92
ATOM   3400  N   GLY A 723     104.060 139.687 164.668  1.00133.85
ATOM   3401  CA  GLY A 723     103.391 140.218 165.833  1.00133.85
ATOM   3402  C   GLY A 723     101.906 139.989 165.780  1.00133.85
ATOM   3403  O   GLY A 723     101.201 140.652 165.015  1.00133.85
ATOM   3404  N   LYS A 724     101.427 139.048 166.602  1.00136.78
ATOM   3405  CA  LYS A 724     100.016 138.682 166.636  1.00136.78
ATOM   3406  C   LYS A 724      99.488 138.496 168.052  1.00136.78
ATOM   3407  O   LYS A 724      98.295 138.206 168.213  1.00136.78
ATOM   3408  CB  LYS A 724      99.783 137.385 165.838  1.00136.78
ATOM   3409  CG  LYS A 724     100.043 137.503 164.338  1.00136.78
ATOM   3410  CD  LYS A 724      99.606 136.244 163.601  1.00136.78
ATOM   3411  CE  LYS A 724      99.910 136.327 162.114  1.00136.78
ATOM   3412  NZ  LYS A 724      99.601 135.043 161.423  1.00136.78
ATOM   3413  N   LEU A 725     100.320 138.669 169.078  1.00135.75
ATOM   3414  CA  LEU A 725      99.964 138.316 170.444  1.00135.75
ATOM   3415  C   LEU A 725     100.357 139.448 171.373  1.00135.75
ATOM   3416  O   LEU A 725     101.249 140.246 171.065  1.00135.75
ATOM   3417  CB  LEU A 725     100.647 137.002 170.898  1.00135.75
ATOM   3418  CG  LEU A 725     100.448 135.757 170.018  1.00135.75
ATOM   3419  CD1 LEU A 725     101.464 134.690 170.368  1.00135.75
ATOM   3420  CD2 LEU A 725      99.044 135.198 170.148  1.00135.75
ATOM   3421  N   LEU A 726      99.685 139.501 172.517  1.00135.46
ATOM   3422  CA  LEU A 726      99.880 140.598 173.452  1.00135.46
ATOM   3423  C   LEU A 726     101.288 140.631 174.054  1.00135.46
ATOM   3424  O   LEU A 726     102.192 139.919 173.615  1.00135.46
ATOM   3425  CB  LEU A 726      98.839 140.546 174.573  1.00135.46
ATOM   3426  CG  LEU A 726      97.400 140.942 174.209  1.00135.46
ATOM   3427  CD1 LEU A 726      96.432 140.416 175.233  1.00135.46
ATOM   3428  CD2 LEU A 726      97.235 142.445 174.096  1.00135.46
ATOM   3429  N   TYR A 738     100.208 143.844 172.928  1.00132.80
ATOM   3430  CA  TYR A 738     100.284 143.672 171.482  1.00132.80
ATOM   3431  C   TYR A 738     100.706 144.987 170.882  1.00132.80
ATOM   3432  O   TYR A 738      99.956 145.957 170.908  1.00132.80
ATOM   3433  CB  TYR A 738      98.938 143.229 170.891  1.00132.80
ATOM   3434  CG  TYR A 738      98.908 143.176 169.377  1.00132.80
ATOM   3435  CD1 TYR A 738      99.715 142.289 168.676  1.00132.80
ATOM   3436  CD2 TYR A 738      98.054 144.000 168.648  1.00132.80
ATOM   3437  CE1 TYR A 738      99.685 142.239 167.295  1.00132.80
ATOM   3438  CE2 TYR A 738      98.022 143.956 167.256  1.00132.80
ATOM   3439  CZ  TYR A 738      98.836 143.073 166.589  1.00132.80
ATOM   3440  OH  TYR A 738      98.799 143.032 165.218  1.00132.80
ATOM   3441  N   ARG A 739     101.947 145.051 170.425  1.00135.74
ATOM   3442  CA  ARG A 739     102.397 146.164 169.607  1.00135.74
ATOM   3443  C   ARG A 739     103.310 145.644 168.504  1.00135.74
ATOM   3444  O   ARG A 739     104.429 146.118 168.314  1.00135.74
ATOM   3445  CB  ARG A 739     103.058 147.244 170.458  1.00135.74
ATOM   3446  CG  ARG A 739     102.063 148.225 171.101  1.00135.74
ATOM   3447  CD  ARG A 739     102.789 149.460 171.625  1.00135.74
ATOM   3448  NE  ARG A 739     103.864 149.060 172.528  1.00135.74
ATOM   3449  CZ  ARG A 739     103.683 148.660 173.785  1.00135.74
ATOM   3450  NH1 ARG A 739     102.468 148.619 174.322  1.00135.74
ATOM   3451  NH2 ARG A 739     104.727 148.299 174.519  1.00135.74
ATOM   3452  N   TRP A 740     102.849 144.623 167.786  1.00129.76
ATOM   3453  CA  TRP A 740     103.613 144.007 166.707  1.00129.76
ATOM   3454  C   TRP A 740     104.919 143.411 167.241  1.00129.76
ATOM   3455  O   TRP A 740     106.017 143.829 166.891  1.00129.76
ATOM   3456  CB  TRP A 740     103.918 145.011 165.588  1.00129.76
ATOM   3457  CG  TRP A 740     102.736 145.690 164.957  1.00129.76
ATOM   3458  CD1 TRP A 740     102.310 146.956 165.189  1.00129.76
ATOM   3459  CD2 TRP A 740     101.864 145.150 163.957  1.00129.76
ATOM   3460  NE1 TRP A 740     101.220 147.239 164.413  1.00129.76
ATOM   3461  CE2 TRP A 740     100.927 146.144 163.645  1.00129.76
ATOM   3462  CE3 TRP A 740     101.782 143.919 163.303  1.00129.76
ATOM   3463  CZ2 TRP A 740      99.914 145.947 162.713  1.00129.76
ATOM   3464  CZ3 TRP A 740     100.780 143.729 162.375  1.00129.76
ATOM   3465  CH2 TRP A 740      99.859 144.737 162.089  1.00129.76
ATOM   3466  N   CYS A 741     104.766 142.425 168.115  1.00132.52
ATOM   3467  CA  CYS A 741     105.922 141.731 168.669  1.00132.52
ATOM   3468  C   CYS A 741     106.707 141.020 167.573  1.00132.52
ATOM   3469  O   CYS A 741     106.132 140.342 166.722  1.00132.52
ATOM   3470  CB  CYS A 741     105.468 140.716 169.717  1.00132.52
ATOM   3471  SG  CYS A 741     106.723 139.496 170.145  1.00132.52
ATOM   3472  N   PHE A 742     108.029 141.163 167.609  1.00128.92
ATOM   3473  CA  PHE A 742     108.935 140.478 166.696  1.00128.92
ATOM   3474  C   PHE A 742     109.934 139.672 167.511  1.00128.92
ATOM   3475  O   PHE A 742     110.561 140.208 168.423  1.00128.92
ATOM   3476  CB  PHE A 742     109.658 141.482 165.804  1.00128.92
ATOM   3477  CG  PHE A 742     110.693 140.870 164.915  1.00128.92
ATOM   3478  CD1 PHE A 742     110.334 140.224 163.751  1.00128.92
ATOM   3479  CD2 PHE A 742     112.027 140.957 165.230  1.00128.92
ATOM   3480  CE1 PHE A 742     111.273 139.667 162.934  1.00128.92
ATOM   3481  CE2 PHE A 742     112.969 140.400 164.407  1.00128.92
ATOM   3482  CZ  PHE A 742     112.592 139.753 163.261  1.00128.92
ATOM   3483  N   ARG A 743     110.085 138.395 167.186  1.00133.62
ATOM   3484  CA  ARG A 743     110.946 137.502 167.947  1.00133.62
ATOM   3485  C   ARG A 743     112.290 137.353 167.256  1.00133.62
ATOM   3486  O   ARG A 743     112.360 137.115 166.050  1.00133.62
ATOM   3487  CB  ARG A 743     110.299 136.124 168.117  1.00133.62
ATOM   3488  CG  ARG A 743     111.101 135.171 169.010  1.00133.62
ATOM   3489  CD  ARG A 743     110.428 133.816 169.206  1.00133.62
ATOM   3490  NE  ARG A 743     109.197 133.868 169.998  1.00133.62
ATOM   3491  CZ  ARG A 743     107.965 134.010 169.509  1.00133.62
ATOM   3492  NH1 ARG A 743     107.749 134.140 168.215  1.00133.62
ATOM   3493  NH2 ARG A 743     106.926 134.028 170.329  1.00133.62
ATOM   3494  N   VAL A 744     113.353 137.479 168.040  1.00132.64
ATOM   3495  CA  VAL A 744     114.717 137.249 167.594  1.00132.64
ATOM   3496  C   VAL A 744     115.291 136.182 168.496  1.00132.64
ATOM   3497  O   VAL A 744     115.356 136.368 169.715  1.00132.64
ATOM   3498  CB  VAL A 744     115.588 138.506 167.668  1.00132.64
ATOM   3499  CG1 VAL A 744     117.039 138.150 167.354  1.00132.64
ATOM   3500  CG2 VAL A 744     115.091 139.543 166.715  1.00132.64
ATOM   3501  N   ASP A 745     115.726 135.087 167.908  1.00134.85
ATOM   3502  CA  ASP A 745     116.312 133.980 168.646  1.00134.85
ATOM   3503  C   ASP A 745     117.811 134.017 168.375  1.00134.85
ATOM   3504  O   ASP A 745     118.278 133.584 167.320  1.00134.85
ATOM   3505  CB  ASP A 745     115.626 132.691 168.224  1.00134.85
ATOM   3506  CG  ASP A 745     114.101 132.846 168.192  1.00134.85
ATOM   3507  OD1 ASP A 745     113.450 132.616 169.237  1.00134.85
ATOM   3508  OD2 ASP A 745     113.567 133.247 167.136  1.00134.85
ATOM   3509  N   GLU A 746     118.557 134.551 169.334  1.00134.22
ATOM   3510  CA  GLU A 746     119.947 134.913 169.129  1.00134.22
ATOM   3511  C   GLU A 746     120.738 134.818 170.430  1.00134.22
ATOM   3512  O   GLU A 746     120.357 135.373 171.458  1.00134.22
ATOM   3513  CB  GLU A 746     120.024 136.326 168.546  1.00134.22
ATOM   3514  CG  GLU A 746     121.439 136.823 168.264  1.00134.22
ATOM   3515  CD  GLU A 746     121.459 138.169 167.548  1.00134.22
ATOM   3516  OE1 GLU A 746     120.613 138.389 166.659  1.00134.22
ATOM   3517  OE2 GLU A 746     122.312 139.017 167.876  1.00134.22
HETATM 3518  CBT 6EU A 901     122.156 153.028 138.029  1.00 64.41
HETATM 3519  OAH 6EU A 901     122.544 153.022 139.367  1.00 64.41
HETATM 3520  CBQ 6EU A 901     123.890 152.736 139.536  1.00 64.41
HETATM 3521  CBO 6EU A 901     124.677 152.736 138.507  1.00 64.41
HETATM 3522  CBS 6EU A 901     124.423 152.422 140.904  1.00 64.41
HETATM 3523  OAI 6EU A 901     123.528 152.432 141.966  1.00 64.41
HETATM 3524  CBR 6EU A 901     125.683 152.146 141.099  1.00 64.41
HETATM 3525  CBP 6EU A 901     126.613 152.153 139.901  1.00 64.41
HETATM 3526  CBN 6EU A 901     126.148 152.433 138.716  1.00 64.41
HETATM 3527  CBM 6EU A 901     127.120 152.412 137.526  1.00 64.41
HETATM 3528  CBK 6EU A 901     126.974 153.708 136.702  1.00 64.41
HETATM 3529  OAG 6EU A 901     125.975 153.957 136.139  1.00 64.41
HETATM 3530  OAF 6EU A 901     128.052 154.609 136.505  1.00 64.41
HETATM 3531  CBC 6EU A 901     128.499 154.519 135.165  1.00 64.41
HETATM 3532  CAX 6EU A 901     127.723 155.482 134.262  1.00 64.41
HETATM 3533  CAS 6EU A 901     128.043 156.716 134.422  1.00 64.41
HETATM 3534  CAK 6EU A 901     127.013 157.765 134.424  1.00 64.41
HETATM 3535  CAU 6EU A 901     127.452 155.055 132.839  1.00 64.41
HETATM 3536  CAR 6EU A 901     126.823 156.225 132.006  1.00 64.41
HETATM 3537  OAD 6EU A 901     125.533 156.429 132.418  1.00 64.41
HETATM 3538  CAZ 6EU A 901     126.790 155.767 130.659  1.00 64.41
HETATM 3539  OAE 6EU A 901     126.672 154.663 130.331  1.00 64.41
HETATM 3540  CBA 6EU A 901     126.940 157.010 129.717  1.00 64.41
HETATM 3541  CBF 6EU A 901     127.003 156.946 128.205  1.00 64.41
HETATM 3542  CAW 6EU A 901     127.466 158.054 130.552  1.00 64.41
HETATM 3543  CAO 6EU A 901     127.607 157.474 131.976  1.00 64.41
HETATM 3544  CAJ 6EU A 901     127.067 158.495 132.964  1.00 64.41
HETATM 3545  OAA 6EU A 901     128.075 159.561 133.033  1.00 64.41
HETATM 3546  CAN 6EU A 901     125.874 159.409 132.856  1.00 64.41
HETATM 3547  CAT 6EU A 901     126.193 160.623 132.038  1.00 64.41
HETATM 3548  CAP 6EU A 901     125.424 159.910 134.281  1.00 64.41
HETATM 3549  CAM 6EU A 901     126.593 160.018 135.235  1.00 64.41
HETATM 3550  CAV 6EU A 901     126.124 160.495 136.583  1.00 64.41
HETATM 3551  CBB 6EU A 901     125.016 161.520 136.477  1.00 64.41
HETATM 3552  CBD 6EU A 901     127.327 161.050 137.309  1.00 64.41
HETATM 3553  OAC 6EU A 901     127.372 160.799 134.855  1.00 64.41
HETATM 3554  CAL 6EU A 901     127.383 158.718 135.426  1.00 64.41
HETATM 3555  OAB 6EU A 901     128.564 158.983 135.161  1.00 64.41
HETATM 3556  CAQ 6EU A 901     128.447 159.977 134.325  1.00 64.41
HETATM 3557  CAY 6EU A 901     129.760 160.760 134.284  1.00 64.41
HETATM 3558  CBE 6EU A 901     130.671 159.998 133.348  1.00 64.41
HETATM 3559  CBG 6EU A 901     131.400 159.037 133.826  1.00 64.41
HETATM 3560  CBI 6EU A 901     132.317 158.265 132.904  1.00 64.41
HETATM 3561  CBL 6EU A 901     132.365 158.573 131.639  1.00 64.41
HETATM 3562  CBJ 6EU A 901     131.512 159.700 131.090  1.00 64.41
HETATM 3563  CBH 6EU A 901     130.721 160.365 131.882  1.00 64.41
CONECT 3518 3519                             
CONECT 3519 3520                             
CONECT 3520 3521 3522                        
CONECT 3521 3526                             
CONECT 3522 3523 3524                        
CONECT 3524 3525                             
CONECT 3525 3526                             
CONECT 3526 3527                             
CONECT 3527 3528                             
CONECT 3528 3529 3530                        
CONECT 3530 3531                             
CONECT 3531 3532                             
CONECT 3532 3533 3535                        
CONECT 3533 3534                             
CONECT 3534 3544 3554                        
CONECT 3535 3536                             
CONECT 3536 3537 3538 3543                   
CONECT 3538 3539 3540                        
CONECT 3540 3541 3542                        
CONECT 3542 3543                             
CONECT 3543 3544                             
CONECT 3544 3545 3546                        
CONECT 3545 3556                             
CONECT 3546 3547 3548                        
CONECT 3548 3549                             
CONECT 3549 3550 3553 3554                   
CONECT 3550 3551 3552                        
CONECT 3553 3556                             
CONECT 3554 3555                             
CONECT 3555 3556                             
CONECT 3556 3557                             
CONECT 3557 3558                             
CONECT 3558 3559 3563                        
CONECT 3559 3560                             
CONECT 3560 3561                             
CONECT 3561 3562                             
CONECT 3562 3563                             
SPDBVT        1.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         1.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         1.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVT        0.0000000000         0.0000000000         0.0000000000 
SPDBVV default;
SPDBVV      3.489880453777    1701.384545885313      20.000000000000
SPDBVV       -0.9519321961         0.2873377265         0.1061231591 
SPDBVV        0.2960502214         0.9519805894         0.0780206631 
SPDBVV       -0.0786089076         0.1056881660        -0.9912873707 
SPDBVV      148.4584960938       148.6060028076       147.4165039063 
SPDBVV        0.0000000000         0.0000000000         0.0000000000 
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16 16
SPDBVf 16 16 16 16 16 16 16 16 16 18
SPDBVo 3518d 6EU
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVR 1.00 1.00 0.00 1.00 1.00 0.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVl 1.00 1.00 1.00 1.00 1.00 1.00 
SPDBVb 0.00 0.00 0.00
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVg    64    64    64    64    64    64    64    64    64    64
SPDBVi        1 1 1 0 1 0 1 1 0 1 0 1 1 0  0
SPDBVp    10116
END



If you find results from this site helpful for your research, please cite one of our papers:

elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Between 2015 and 2025, it was hosted by US2B (Nantes).
Last modification: december 26th, 2025.