HEADER    VIRAL PROTEIN/IMMUNE SYSTEM             17-JAN-23   8I3S              
TITLE     LOCAL CRYOEM STRUCTURE OF THE SARS-COV-2 S6P IN COMPLEX WITH 7B3 FAB  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPIKE GLYCOPROTEIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RBD REGION;                                                
COMPND   5 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;                         
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES;                                                       
COMPND   8 MOL_ID: 2;                                                           
COMPND   9 MOLECULE: HEAVY CHAIN OD FAB 7B3;                                    
COMPND  10 CHAIN: H;                                                            
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 MOL_ID: 3;                                                           
COMPND  13 MOLECULE: LIGHT CHAIN OF FAB 7B3;                                    
COMPND  14 CHAIN: L;                                                            
COMPND  15 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_TAXID: 2697049;                                             
SOURCE   5 GENE: S, 2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_TAXID: 9606;                                                
SOURCE  11 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE  13 MOL_ID: 3;                                                           
SOURCE  14 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  15 ORGANISM_TAXID: 9606;                                                
SOURCE  16 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  17 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    SARS-COV-2, RECEPTOR BINDING DOMAIN, RBD, FAB, CORONAVIRUS, VIRAL     
KEYWDS   2 PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM COMPLEX                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    Z.LI,F.YU,S.CAO,H.ZHAO                                                
REVDAT   2   30-OCT-24 8I3S    1       REMARK                                   
REVDAT   1   04-OCT-23 8I3S    0                                                
JRNL        AUTH   Q.LIU,H.ZHAO,Z.LI,Z.ZHANG,R.HUANG,M.GU,K.ZHUANG,Q.XIONG,     
JRNL        AUTH 2 X.CHEN,W.YU,S.QIAN,Y.ZHANG,X.TAN,M.ZHANG,F.YU,M.GUO,Z.HUANG, 
JRNL        AUTH 3 X.WANG,W.XIANG,B.WU,F.MEI,K.CAI,L.ZHOU,L.ZHOU,Y.WU,H.YAN,    
JRNL        AUTH 4 S.CAO,K.LAN,Y.CHEN                                           
JRNL        TITL   BROADLY NEUTRALIZING ANTIBODIES DERIVED FROM THE EARLIEST    
JRNL        TITL 2 COVID-19 CONVALESCENTS PROTECT MICE FROM SARS-COV-2 VARIANTS 
JRNL        TITL 3 CHALLENGE.                                                   
JRNL        REF    SIGNAL TRANSDUCT TARGET THER  V.   8   347 2023              
JRNL        REFN                   ESSN 2059-3635                               
JRNL        PMID   37704615                                                     
JRNL        DOI    10.1038/S41392-023-01615-0                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.90 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)  : 3.900                          
REMARK   3   NUMBER OF PARTICLES               : 86212                          
REMARK   3   CTF CORRECTION METHOD             : PHASE FLIPPING AND AMPLITUDE   
REMARK   3                                       CORRECTION                     
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: NULL                                                  
REMARK   4                                                                      
REMARK   4 8I3S COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-FEB-23.                  
REMARK 100 THE DEPOSITION ID IS D_1300034386.                                   
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                 : SPIKE-FAB COMPLEX                 
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                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : JEOL CRYO ARM 300              
REMARK 245   DETECTOR TYPE                     : GATAN K3 (6K X 4K)             
REMARK 245   MINIMUM DEFOCUS (NM)              : 500.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2500.00                        
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)  : 4000.00                        
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L                               
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     GLN A    14                                                      
REMARK 465     CYS A    15                                                      
REMARK 465     VAL A    16                                                      
REMARK 465     ASN A    17                                                      
REMARK 465     LEU A    18                                                      
REMARK 465     THR A    19                                                      
REMARK 465     THR A    20                                                      
REMARK 465     ARG A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     GLN A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     TYR A    28                                                      
REMARK 465     THR A    29                                                      
REMARK 465     ASN A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     PHE A    32                                                      
REMARK 465     THR A    33                                                      
REMARK 465     ARG A    34                                                      
REMARK 465     GLY A    35                                                      
REMARK 465     VAL A    36                                                      
REMARK 465     TYR A    37                                                      
REMARK 465     TYR A    38                                                      
REMARK 465     PRO A    39                                                      
REMARK 465     ASP A    40                                                      
REMARK 465     LYS A    41                                                      
REMARK 465     VAL A    42                                                      
REMARK 465     PHE A    43                                                      
REMARK 465     ARG A    44                                                      
REMARK 465     SER A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     VAL A    47                                                      
REMARK 465     LEU A    48                                                      
REMARK 465     HIS A    49                                                      
REMARK 465     SER A    50                                                      
REMARK 465     THR A    51                                                      
REMARK 465     GLN A    52                                                      
REMARK 465     ASP A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     PHE A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     PRO A    57                                                      
REMARK 465     PHE A    58                                                      
REMARK 465     PHE A    59                                                      
REMARK 465     SER A    60                                                      
REMARK 465     ASN A    61                                                      
REMARK 465     VAL A    62                                                      
REMARK 465     THR A    63                                                      
REMARK 465     TRP A    64                                                      
REMARK 465     PHE A    65                                                      
REMARK 465     HIS A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     ILE A    68                                                      
REMARK 465     HIS A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     SER A    71                                                      
REMARK 465     GLY A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     ASN A    74                                                      
REMARK 465     GLY A    75                                                      
REMARK 465     THR A    76                                                      
REMARK 465     LYS A    77                                                      
REMARK 465     ARG A    78                                                      
REMARK 465     PHE A    79                                                      
REMARK 465     ASP A    80                                                      
REMARK 465     ASN A    81                                                      
REMARK 465     PRO A    82                                                      
REMARK 465     VAL A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     PRO A    85                                                      
REMARK 465     PHE A    86                                                      
REMARK 465     ASN A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     GLY A    89                                                      
REMARK 465     VAL A    90                                                      
REMARK 465     TYR A    91                                                      
REMARK 465     PHE A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     SER A    94                                                      
REMARK 465     THR A    95                                                      
REMARK 465     GLU A    96                                                      
REMARK 465     LYS A    97                                                      
REMARK 465     SER A    98                                                      
REMARK 465     ASN A    99                                                      
REMARK 465     ILE A   100                                                      
REMARK 465     ILE A   101                                                      
REMARK 465     ARG A   102                                                      
REMARK 465     GLY A   103                                                      
REMARK 465     TRP A   104                                                      
REMARK 465     ILE A   105                                                      
REMARK 465     PHE A   106                                                      
REMARK 465     GLY A   107                                                      
REMARK 465     THR A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     LEU A   110                                                      
REMARK 465     ASP A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     LYS A   113                                                      
REMARK 465     THR A   114                                                      
REMARK 465     GLN A   115                                                      
REMARK 465     SER A   116                                                      
REMARK 465     LEU A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     ILE A   119                                                      
REMARK 465     VAL A   120                                                      
REMARK 465     ASN A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     ALA A   123                                                      
REMARK 465     THR A   124                                                      
REMARK 465     ASN A   125                                                      
REMARK 465     VAL A   126                                                      
REMARK 465     VAL A   127                                                      
REMARK 465     ILE A   128                                                      
REMARK 465     LYS A   129                                                      
REMARK 465     VAL A   130                                                      
REMARK 465     CYS A   131                                                      
REMARK 465     GLU A   132                                                      
REMARK 465     PHE A   133                                                      
REMARK 465     GLN A   134                                                      
REMARK 465     PHE A   135                                                      
REMARK 465     CYS A   136                                                      
REMARK 465     ASN A   137                                                      
REMARK 465     ASP A   138                                                      
REMARK 465     PRO A   139                                                      
REMARK 465     PHE A   140                                                      
REMARK 465     LEU A   141                                                      
REMARK 465     GLY A   142                                                      
REMARK 465     VAL A   143                                                      
REMARK 465     TYR A   144                                                      
REMARK 465     TYR A   145                                                      
REMARK 465     HIS A   146                                                      
REMARK 465     LYS A   147                                                      
REMARK 465     ASN A   148                                                      
REMARK 465     ASN A   149                                                      
REMARK 465     LYS A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     TRP A   152                                                      
REMARK 465     MET A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     SER A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     PHE A   157                                                      
REMARK 465     ARG A   158                                                      
REMARK 465     VAL A   159                                                      
REMARK 465     TYR A   160                                                      
REMARK 465     SER A   161                                                      
REMARK 465     SER A   162                                                      
REMARK 465     ALA A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     ASN A   165                                                      
REMARK 465     CYS A   166                                                      
REMARK 465     THR A   167                                                      
REMARK 465     PHE A   168                                                      
REMARK 465     GLU A   169                                                      
REMARK 465     TYR A   170                                                      
REMARK 465     VAL A   171                                                      
REMARK 465     SER A   172                                                      
REMARK 465     GLN A   173                                                      
REMARK 465     PRO A   174                                                      
REMARK 465     PHE A   175                                                      
REMARK 465     LEU A   176                                                      
REMARK 465     MET A   177                                                      
REMARK 465     ASP A   178                                                      
REMARK 465     LEU A   179                                                      
REMARK 465     GLU A   180                                                      
REMARK 465     GLY A   181                                                      
REMARK 465     LYS A   182                                                      
REMARK 465     GLN A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     ASN A   185                                                      
REMARK 465     PHE A   186                                                      
REMARK 465     LYS A   187                                                      
REMARK 465     ASN A   188                                                      
REMARK 465     LEU A   189                                                      
REMARK 465     ARG A   190                                                      
REMARK 465     GLU A   191                                                      
REMARK 465     PHE A   192                                                      
REMARK 465     VAL A   193                                                      
REMARK 465     PHE A   194                                                      
REMARK 465     LYS A   195                                                      
REMARK 465     ASN A   196                                                      
REMARK 465     ILE A   197                                                      
REMARK 465     ASP A   198                                                      
REMARK 465     GLY A   199                                                      
REMARK 465     TYR A   200                                                      
REMARK 465     PHE A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     ILE A   203                                                      
REMARK 465     TYR A   204                                                      
REMARK 465     SER A   205                                                      
REMARK 465     LYS A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     THR A   208                                                      
REMARK 465     PRO A   209                                                      
REMARK 465     ILE A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     VAL A   213                                                      
REMARK 465     ARG A   214                                                      
REMARK 465     ASP A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     PRO A   217                                                      
REMARK 465     GLN A   218                                                      
REMARK 465     GLY A   219                                                      
REMARK 465     PHE A   220                                                      
REMARK 465     SER A   221                                                      
REMARK 465     ALA A   222                                                      
REMARK 465     LEU A   223                                                      
REMARK 465     GLU A   224                                                      
REMARK 465     PRO A   225                                                      
REMARK 465     LEU A   226                                                      
REMARK 465     VAL A   227                                                      
REMARK 465     ASP A   228                                                      
REMARK 465     LEU A   229                                                      
REMARK 465     PRO A   230                                                      
REMARK 465     ILE A   231                                                      
REMARK 465     GLY A   232                                                      
REMARK 465     ILE A   233                                                      
REMARK 465     ASN A   234                                                      
REMARK 465     ILE A   235                                                      
REMARK 465     THR A   236                                                      
REMARK 465     ARG A   237                                                      
REMARK 465     PHE A   238                                                      
REMARK 465     GLN A   239                                                      
REMARK 465     THR A   240                                                      
REMARK 465     LEU A   241                                                      
REMARK 465     LEU A   242                                                      
REMARK 465     ALA A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     HIS A   245                                                      
REMARK 465     ARG A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     TYR A   248                                                      
REMARK 465     LEU A   249                                                      
REMARK 465     THR A   250                                                      
REMARK 465     PRO A   251                                                      
REMARK 465     GLY A   252                                                      
REMARK 465     ASP A   253                                                      
REMARK 465     SER A   254                                                      
REMARK 465     SER A   255                                                      
REMARK 465     SER A   256                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     TRP A   258                                                      
REMARK 465     THR A   259                                                      
REMARK 465     ALA A   260                                                      
REMARK 465     GLY A   261                                                      
REMARK 465     ALA A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     ALA A   264                                                      
REMARK 465     TYR A   265                                                      
REMARK 465     TYR A   266                                                      
REMARK 465     VAL A   267                                                      
REMARK 465     GLY A   268                                                      
REMARK 465     TYR A   269                                                      
REMARK 465     LEU A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     PRO A   272                                                      
REMARK 465     ARG A   273                                                      
REMARK 465     THR A   274                                                      
REMARK 465     PHE A   275                                                      
REMARK 465     LEU A   276                                                      
REMARK 465     LEU A   277                                                      
REMARK 465     LYS A   278                                                      
REMARK 465     TYR A   279                                                      
REMARK 465     ASN A   280                                                      
REMARK 465     GLU A   281                                                      
REMARK 465     ASN A   282                                                      
REMARK 465     GLY A   283                                                      
REMARK 465     THR A   284                                                      
REMARK 465     ILE A   285                                                      
REMARK 465     THR A   286                                                      
REMARK 465     ASP A   287                                                      
REMARK 465     ALA A   288                                                      
REMARK 465     VAL A   289                                                      
REMARK 465     ASP A   290                                                      
REMARK 465     CYS A   291                                                      
REMARK 465     ALA A   292                                                      
REMARK 465     LEU A   293                                                      
REMARK 465     ASP A   294                                                      
REMARK 465     PRO A   295                                                      
REMARK 465     LEU A   296                                                      
REMARK 465     SER A   297                                                      
REMARK 465     GLU A   298                                                      
REMARK 465     THR A   299                                                      
REMARK 465     LYS A   300                                                      
REMARK 465     CYS A   301                                                      
REMARK 465     THR A   302                                                      
REMARK 465     LEU A   303                                                      
REMARK 465     LYS A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     PHE A   306                                                      
REMARK 465     THR A   307                                                      
REMARK 465     VAL A   308                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     LYS A   310                                                      
REMARK 465     GLY A   311                                                      
REMARK 465     ILE A   312                                                      
REMARK 465     TYR A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     THR A   315                                                      
REMARK 465     SER A   316                                                      
REMARK 465     ASN A   317                                                      
REMARK 465     PHE A   318                                                      
REMARK 465     ARG A   319                                                      
REMARK 465     VAL A   320                                                      
REMARK 465     GLN A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     THR A   323                                                      
REMARK 465     GLU A   324                                                      
REMARK 465     SER A   325                                                      
REMARK 465     ILE A   326                                                      
REMARK 465     VAL A   327                                                      
REMARK 465     ARG A   328                                                      
REMARK 465     PHE A   329                                                      
REMARK 465     PRO A   330                                                      
REMARK 465     ASN A   331                                                      
REMARK 465     ILE A   332                                                      
REMARK 465     LYS A   529                                                      
REMARK 465     SER A   530                                                      
REMARK 465     THR A   531                                                      
REMARK 465     ASN A   532                                                      
REMARK 465     LEU A   533                                                      
REMARK 465     VAL A   534                                                      
REMARK 465     LYS A   535                                                      
REMARK 465     ASN A   536                                                      
REMARK 465     LYS A   537                                                      
REMARK 465     CYS A   538                                                      
REMARK 465     VAL A   539                                                      
REMARK 465     ASN A   540                                                      
REMARK 465     PHE A   541                                                      
REMARK 465     ASN A   542                                                      
REMARK 465     PHE A   543                                                      
REMARK 465     ASN A   544                                                      
REMARK 465     GLY A   545                                                      
REMARK 465     LEU A   546                                                      
REMARK 465     THR A   547                                                      
REMARK 465     GLY A   548                                                      
REMARK 465     THR A   549                                                      
REMARK 465     GLY A   550                                                      
REMARK 465     VAL A   551                                                      
REMARK 465     LEU A   552                                                      
REMARK 465     THR A   553                                                      
REMARK 465     GLU A   554                                                      
REMARK 465     SER A   555                                                      
REMARK 465     ASN A   556                                                      
REMARK 465     LYS A   557                                                      
REMARK 465     LYS A   558                                                      
REMARK 465     PHE A   559                                                      
REMARK 465     LEU A   560                                                      
REMARK 465     PRO A   561                                                      
REMARK 465     PHE A   562                                                      
REMARK 465     GLN A   563                                                      
REMARK 465     GLN A   564                                                      
REMARK 465     PHE A   565                                                      
REMARK 465     GLY A   566                                                      
REMARK 465     ARG A   567                                                      
REMARK 465     ASP A   568                                                      
REMARK 465     ILE A   569                                                      
REMARK 465     ALA A   570                                                      
REMARK 465     ASP A   571                                                      
REMARK 465     THR A   572                                                      
REMARK 465     THR A   573                                                      
REMARK 465     ASP A   574                                                      
REMARK 465     ALA A   575                                                      
REMARK 465     VAL A   576                                                      
REMARK 465     ARG A   577                                                      
REMARK 465     ASP A   578                                                      
REMARK 465     PRO A   579                                                      
REMARK 465     GLN A   580                                                      
REMARK 465     THR A   581                                                      
REMARK 465     LEU A   582                                                      
REMARK 465     GLU A   583                                                      
REMARK 465     ILE A   584                                                      
REMARK 465     LEU A   585                                                      
REMARK 465     ASP A   586                                                      
REMARK 465     ILE A   587                                                      
REMARK 465     THR A   588                                                      
REMARK 465     PRO A   589                                                      
REMARK 465     CYS A   590                                                      
REMARK 465     SER A   591                                                      
REMARK 465     PHE A   592                                                      
REMARK 465     GLY A   593                                                      
REMARK 465     GLY A   594                                                      
REMARK 465     VAL A   595                                                      
REMARK 465     SER A   596                                                      
REMARK 465     VAL A   597                                                      
REMARK 465     ILE A   598                                                      
REMARK 465     THR A   599                                                      
REMARK 465     PRO A   600                                                      
REMARK 465     GLY A   601                                                      
REMARK 465     THR A   602                                                      
REMARK 465     ASN A   603                                                      
REMARK 465     THR A   604                                                      
REMARK 465     SER A   605                                                      
REMARK 465     ASN A   606                                                      
REMARK 465     GLN A   607                                                      
REMARK 465     VAL A   608                                                      
REMARK 465     ALA A   609                                                      
REMARK 465     VAL A   610                                                      
REMARK 465     LEU A   611                                                      
REMARK 465     TYR A   612                                                      
REMARK 465     GLN A   613                                                      
REMARK 465     ASP A   614                                                      
REMARK 465     VAL A   615                                                      
REMARK 465     ASN A   616                                                      
REMARK 465     CYS A   617                                                      
REMARK 465     THR A   618                                                      
REMARK 465     GLU A   619                                                      
REMARK 465     VAL A   620                                                      
REMARK 465     PRO A   621                                                      
REMARK 465     VAL A   622                                                      
REMARK 465     ALA A   623                                                      
REMARK 465     ILE A   624                                                      
REMARK 465     HIS A   625                                                      
REMARK 465     ALA A   626                                                      
REMARK 465     ASP A   627                                                      
REMARK 465     GLN A   628                                                      
REMARK 465     LEU A   629                                                      
REMARK 465     THR A   630                                                      
REMARK 465     PRO A   631                                                      
REMARK 465     THR A   632                                                      
REMARK 465     TRP A   633                                                      
REMARK 465     ARG A   634                                                      
REMARK 465     VAL A   635                                                      
REMARK 465     TYR A   636                                                      
REMARK 465     SER A   637                                                      
REMARK 465     THR A   638                                                      
REMARK 465     GLY A   639                                                      
REMARK 465     SER A   640                                                      
REMARK 465     ASN A   641                                                      
REMARK 465     VAL A   642                                                      
REMARK 465     PHE A   643                                                      
REMARK 465     GLN A   644                                                      
REMARK 465     THR A   645                                                      
REMARK 465     ARG A   646                                                      
REMARK 465     ALA A   647                                                      
REMARK 465     GLY A   648                                                      
REMARK 465     CYS A   649                                                      
REMARK 465     LEU A   650                                                      
REMARK 465     ILE A   651                                                      
REMARK 465     GLY A   652                                                      
REMARK 465     ALA A   653                                                      
REMARK 465     GLU A   654                                                      
REMARK 465     HIS A   655                                                      
REMARK 465     VAL A   656                                                      
REMARK 465     ASN A   657                                                      
REMARK 465     ASN A   658                                                      
REMARK 465     SER A   659                                                      
REMARK 465     TYR A   660                                                      
REMARK 465     GLU A   661                                                      
REMARK 465     CYS A   662                                                      
REMARK 465     ASP A   663                                                      
REMARK 465     ILE A   664                                                      
REMARK 465     PRO A   665                                                      
REMARK 465     ILE A   666                                                      
REMARK 465     GLY A   667                                                      
REMARK 465     ALA A   668                                                      
REMARK 465     GLY A   669                                                      
REMARK 465     ILE A   670                                                      
REMARK 465     CYS A   671                                                      
REMARK 465     ALA A   672                                                      
REMARK 465     SER A   673                                                      
REMARK 465     TYR A   674                                                      
REMARK 465     GLN A   675                                                      
REMARK 465     THR A   676                                                      
REMARK 465     GLN A   677                                                      
REMARK 465     THR A   678                                                      
REMARK 465     ASN A   679                                                      
REMARK 465     SER A   680                                                      
REMARK 465     PRO A   681                                                      
REMARK 465     ALA A   682                                                      
REMARK 465     SER A   683                                                      
REMARK 465     VAL A   684                                                      
REMARK 465     ALA A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     GLN A   687                                                      
REMARK 465     SER A   688                                                      
REMARK 465     ILE A   689                                                      
REMARK 465     ILE A   690                                                      
REMARK 465     ALA A   691                                                      
REMARK 465     TYR A   692                                                      
REMARK 465     THR A   693                                                      
REMARK 465     MET A   694                                                      
REMARK 465     SER A   695                                                      
REMARK 465     LEU A   696                                                      
REMARK 465     GLY A   697                                                      
REMARK 465     ALA A   698                                                      
REMARK 465     GLU A   699                                                      
REMARK 465     ASN A   700                                                      
REMARK 465     SER A   701                                                      
REMARK 465     VAL A   702                                                      
REMARK 465     ALA A   703                                                      
REMARK 465     TYR A   704                                                      
REMARK 465     SER A   705                                                      
REMARK 465     ASN A   706                                                      
REMARK 465     ASN A   707                                                      
REMARK 465     SER A   708                                                      
REMARK 465     ILE A   709                                                      
REMARK 465     ALA A   710                                                      
REMARK 465     ILE A   711                                                      
REMARK 465     PRO A   712                                                      
REMARK 465     THR A   713                                                      
REMARK 465     ASN A   714                                                      
REMARK 465     PHE A   715                                                      
REMARK 465     THR A   716                                                      
REMARK 465     ILE A   717                                                      
REMARK 465     SER A   718                                                      
REMARK 465     VAL A   719                                                      
REMARK 465     THR A   720                                                      
REMARK 465     THR A   721                                                      
REMARK 465     GLU A   722                                                      
REMARK 465     ILE A   723                                                      
REMARK 465     LEU A   724                                                      
REMARK 465     PRO A   725                                                      
REMARK 465     VAL A   726                                                      
REMARK 465     SER A   727                                                      
REMARK 465     MET A   728                                                      
REMARK 465     THR A   729                                                      
REMARK 465     LYS A   730                                                      
REMARK 465     THR A   731                                                      
REMARK 465     SER A   732                                                      
REMARK 465     VAL A   733                                                      
REMARK 465     ASP A   734                                                      
REMARK 465     CYS A   735                                                      
REMARK 465     THR A   736                                                      
REMARK 465     MET A   737                                                      
REMARK 465     TYR A   738                                                      
REMARK 465     ILE A   739                                                      
REMARK 465     CYS A   740                                                      
REMARK 465     GLY A   741                                                      
REMARK 465     ASP A   742                                                      
REMARK 465     SER A   743                                                      
REMARK 465     THR A   744                                                      
REMARK 465     GLU A   745                                                      
REMARK 465     CYS A   746                                                      
REMARK 465     SER A   747                                                      
REMARK 465     ASN A   748                                                      
REMARK 465     LEU A   749                                                      
REMARK 465     LEU A   750                                                      
REMARK 465     LEU A   751                                                      
REMARK 465     GLN A   752                                                      
REMARK 465     TYR A   753                                                      
REMARK 465     GLY A   754                                                      
REMARK 465     SER A   755                                                      
REMARK 465     PHE A   756                                                      
REMARK 465     CYS A   757                                                      
REMARK 465     THR A   758                                                      
REMARK 465     GLN A   759                                                      
REMARK 465     LEU A   760                                                      
REMARK 465     ASN A   761                                                      
REMARK 465     ARG A   762                                                      
REMARK 465     ALA A   763                                                      
REMARK 465     LEU A   764                                                      
REMARK 465     THR A   765                                                      
REMARK 465     GLY A   766                                                      
REMARK 465     ILE A   767                                                      
REMARK 465     ALA A   768                                                      
REMARK 465     VAL A   769                                                      
REMARK 465     GLU A   770                                                      
REMARK 465     GLN A   771                                                      
REMARK 465     ASP A   772                                                      
REMARK 465     LYS A   773                                                      
REMARK 465     ASN A   774                                                      
REMARK 465     THR A   775                                                      
REMARK 465     GLN A   776                                                      
REMARK 465     GLU A   777                                                      
REMARK 465     VAL A   778                                                      
REMARK 465     PHE A   779                                                      
REMARK 465     ALA A   780                                                      
REMARK 465     GLN A   781                                                      
REMARK 465     VAL A   782                                                      
REMARK 465     LYS A   783                                                      
REMARK 465     GLN A   784                                                      
REMARK 465     ILE A   785                                                      
REMARK 465     TYR A   786                                                      
REMARK 465     LYS A   787                                                      
REMARK 465     THR A   788                                                      
REMARK 465     PRO A   789                                                      
REMARK 465     PRO A   790                                                      
REMARK 465     ILE A   791                                                      
REMARK 465     LYS A   792                                                      
REMARK 465     ASP A   793                                                      
REMARK 465     PHE A   794                                                      
REMARK 465     GLY A   795                                                      
REMARK 465     GLY A   796                                                      
REMARK 465     PHE A   797                                                      
REMARK 465     ASN A   798                                                      
REMARK 465     PHE A   799                                                      
REMARK 465     SER A   800                                                      
REMARK 465     GLN A   801                                                      
REMARK 465     ILE A   802                                                      
REMARK 465     LEU A   803                                                      
REMARK 465     PRO A   804                                                      
REMARK 465     ASP A   805                                                      
REMARK 465     PRO A   806                                                      
REMARK 465     SER A   807                                                      
REMARK 465     LYS A   808                                                      
REMARK 465     PRO A   809                                                      
REMARK 465     SER A   810                                                      
REMARK 465     LYS A   811                                                      
REMARK 465     ARG A   812                                                      
REMARK 465     SER A   813                                                      
REMARK 465     PRO A   814                                                      
REMARK 465     ILE A   815                                                      
REMARK 465     GLU A   816                                                      
REMARK 465     ASP A   817                                                      
REMARK 465     LEU A   818                                                      
REMARK 465     LEU A   819                                                      
REMARK 465     PHE A   820                                                      
REMARK 465     ASN A   821                                                      
REMARK 465     LYS A   822                                                      
REMARK 465     VAL A   823                                                      
REMARK 465     THR A   824                                                      
REMARK 465     LEU A   825                                                      
REMARK 465     ALA A   826                                                      
REMARK 465     ASP A   827                                                      
REMARK 465     ALA A   828                                                      
REMARK 465     GLY A   829                                                      
REMARK 465     PHE A   830                                                      
REMARK 465     ILE A   831                                                      
REMARK 465     LYS A   832                                                      
REMARK 465     GLN A   833                                                      
REMARK 465     TYR A   834                                                      
REMARK 465     GLY A   835                                                      
REMARK 465     ASP A   836                                                      
REMARK 465     CYS A   837                                                      
REMARK 465     LEU A   838                                                      
REMARK 465     GLY A   839                                                      
REMARK 465     ASP A   840                                                      
REMARK 465     ILE A   841                                                      
REMARK 465     ALA A   842                                                      
REMARK 465     ALA A   843                                                      
REMARK 465     ARG A   844                                                      
REMARK 465     ASP A   845                                                      
REMARK 465     LEU A   846                                                      
REMARK 465     ILE A   847                                                      
REMARK 465     CYS A   848                                                      
REMARK 465     ALA A   849                                                      
REMARK 465     GLN A   850                                                      
REMARK 465     LYS A   851                                                      
REMARK 465     PHE A   852                                                      
REMARK 465     ASN A   853                                                      
REMARK 465     GLY A   854                                                      
REMARK 465     LEU A   855                                                      
REMARK 465     THR A   856                                                      
REMARK 465     VAL A   857                                                      
REMARK 465     LEU A   858                                                      
REMARK 465     PRO A   859                                                      
REMARK 465     PRO A   860                                                      
REMARK 465     LEU A   861                                                      
REMARK 465     LEU A   862                                                      
REMARK 465     THR A   863                                                      
REMARK 465     ASP A   864                                                      
REMARK 465     GLU A   865                                                      
REMARK 465     MET A   866                                                      
REMARK 465     ILE A   867                                                      
REMARK 465     ALA A   868                                                      
REMARK 465     GLN A   869                                                      
REMARK 465     TYR A   870                                                      
REMARK 465     THR A   871                                                      
REMARK 465     SER A   872                                                      
REMARK 465     ALA A   873                                                      
REMARK 465     LEU A   874                                                      
REMARK 465     LEU A   875                                                      
REMARK 465     ALA A   876                                                      
REMARK 465     GLY A   877                                                      
REMARK 465     THR A   878                                                      
REMARK 465     ILE A   879                                                      
REMARK 465     THR A   880                                                      
REMARK 465     SER A   881                                                      
REMARK 465     GLY A   882                                                      
REMARK 465     TRP A   883                                                      
REMARK 465     THR A   884                                                      
REMARK 465     PHE A   885                                                      
REMARK 465     GLY A   886                                                      
REMARK 465     ALA A   887                                                      
REMARK 465     GLY A   888                                                      
REMARK 465     PRO A   889                                                      
REMARK 465     ALA A   890                                                      
REMARK 465     LEU A   891                                                      
REMARK 465     GLN A   892                                                      
REMARK 465     ILE A   893                                                      
REMARK 465     PRO A   894                                                      
REMARK 465     PHE A   895                                                      
REMARK 465     PRO A   896                                                      
REMARK 465     MET A   897                                                      
REMARK 465     GLN A   898                                                      
REMARK 465     MET A   899                                                      
REMARK 465     ALA A   900                                                      
REMARK 465     TYR A   901                                                      
REMARK 465     ARG A   902                                                      
REMARK 465     PHE A   903                                                      
REMARK 465     ASN A   904                                                      
REMARK 465     GLY A   905                                                      
REMARK 465     ILE A   906                                                      
REMARK 465     GLY A   907                                                      
REMARK 465     VAL A   908                                                      
REMARK 465     THR A   909                                                      
REMARK 465     GLN A   910                                                      
REMARK 465     ASN A   911                                                      
REMARK 465     VAL A   912                                                      
REMARK 465     LEU A   913                                                      
REMARK 465     TYR A   914                                                      
REMARK 465     GLU A   915                                                      
REMARK 465     ASN A   916                                                      
REMARK 465     GLN A   917                                                      
REMARK 465     LYS A   918                                                      
REMARK 465     LEU A   919                                                      
REMARK 465     ILE A   920                                                      
REMARK 465     ALA A   921                                                      
REMARK 465     ASN A   922                                                      
REMARK 465     GLN A   923                                                      
REMARK 465     PHE A   924                                                      
REMARK 465     ASN A   925                                                      
REMARK 465     SER A   926                                                      
REMARK 465     ALA A   927                                                      
REMARK 465     ILE A   928                                                      
REMARK 465     GLY A   929                                                      
REMARK 465     LYS A   930                                                      
REMARK 465     ILE A   931                                                      
REMARK 465     GLN A   932                                                      
REMARK 465     ASP A   933                                                      
REMARK 465     SER A   934                                                      
REMARK 465     LEU A   935                                                      
REMARK 465     SER A   936                                                      
REMARK 465     SER A   937                                                      
REMARK 465     THR A   938                                                      
REMARK 465     PRO A   939                                                      
REMARK 465     SER A   940                                                      
REMARK 465     ALA A   941                                                      
REMARK 465     LEU A   942                                                      
REMARK 465     GLY A   943                                                      
REMARK 465     LYS A   944                                                      
REMARK 465     LEU A   945                                                      
REMARK 465     GLN A   946                                                      
REMARK 465     ASP A   947                                                      
REMARK 465     VAL A   948                                                      
REMARK 465     VAL A   949                                                      
REMARK 465     ASN A   950                                                      
REMARK 465     GLN A   951                                                      
REMARK 465     ASN A   952                                                      
REMARK 465     ALA A   953                                                      
REMARK 465     GLN A   954                                                      
REMARK 465     ALA A   955                                                      
REMARK 465     LEU A   956                                                      
REMARK 465     ASN A   957                                                      
REMARK 465     THR A   958                                                      
REMARK 465     LEU A   959                                                      
REMARK 465     VAL A   960                                                      
REMARK 465     LYS A   961                                                      
REMARK 465     GLN A   962                                                      
REMARK 465     LEU A   963                                                      
REMARK 465     SER A   964                                                      
REMARK 465     SER A   965                                                      
REMARK 465     ASN A   966                                                      
REMARK 465     PHE A   967                                                      
REMARK 465     GLY A   968                                                      
REMARK 465     ALA A   969                                                      
REMARK 465     ILE A   970                                                      
REMARK 465     SER A   971                                                      
REMARK 465     SER A   972                                                      
REMARK 465     VAL A   973                                                      
REMARK 465     LEU A   974                                                      
REMARK 465     ASN A   975                                                      
REMARK 465     ASP A   976                                                      
REMARK 465     ILE A   977                                                      
REMARK 465     LEU A   978                                                      
REMARK 465     SER A   979                                                      
REMARK 465     ARG A   980                                                      
REMARK 465     LEU A   981                                                      
REMARK 465     ASP A   982                                                      
REMARK 465     PRO A   983                                                      
REMARK 465     PRO A   984                                                      
REMARK 465     GLU A   985                                                      
REMARK 465     ALA A   986                                                      
REMARK 465     GLU A   987                                                      
REMARK 465     VAL A   988                                                      
REMARK 465     GLN A   989                                                      
REMARK 465     ILE A   990                                                      
REMARK 465     ASP A   991                                                      
REMARK 465     ARG A   992                                                      
REMARK 465     LEU A   993                                                      
REMARK 465     ILE A   994                                                      
REMARK 465     THR A   995                                                      
REMARK 465     GLY A   996                                                      
REMARK 465     ARG A   997                                                      
REMARK 465     LEU A   998                                                      
REMARK 465     GLN A   999                                                      
REMARK 465     SER A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     GLN A  1002                                                      
REMARK 465     THR A  1003                                                      
REMARK 465     TYR A  1004                                                      
REMARK 465     VAL A  1005                                                      
REMARK 465     THR A  1006                                                      
REMARK 465     GLN A  1007                                                      
REMARK 465     GLN A  1008                                                      
REMARK 465     LEU A  1009                                                      
REMARK 465     ILE A  1010                                                      
REMARK 465     ARG A  1011                                                      
REMARK 465     ALA A  1012                                                      
REMARK 465     ALA A  1013                                                      
REMARK 465     GLU A  1014                                                      
REMARK 465     ILE A  1015                                                      
REMARK 465     ARG A  1016                                                      
REMARK 465     ALA A  1017                                                      
REMARK 465     SER A  1018                                                      
REMARK 465     ALA A  1019                                                      
REMARK 465     ASN A  1020                                                      
REMARK 465     LEU A  1021                                                      
REMARK 465     ALA A  1022                                                      
REMARK 465     ALA A  1023                                                      
REMARK 465     THR A  1024                                                      
REMARK 465     LYS A  1025                                                      
REMARK 465     MET A  1026                                                      
REMARK 465     SER A  1027                                                      
REMARK 465     GLU A  1028                                                      
REMARK 465     CYS A  1029                                                      
REMARK 465     VAL A  1030                                                      
REMARK 465     LEU A  1031                                                      
REMARK 465     GLY A  1032                                                      
REMARK 465     GLN A  1033                                                      
REMARK 465     SER A  1034                                                      
REMARK 465     LYS A  1035                                                      
REMARK 465     ARG A  1036                                                      
REMARK 465     VAL A  1037                                                      
REMARK 465     ASP A  1038                                                      
REMARK 465     PHE A  1039                                                      
REMARK 465     CYS A  1040                                                      
REMARK 465     GLY A  1041                                                      
REMARK 465     LYS A  1042                                                      
REMARK 465     GLY A  1043                                                      
REMARK 465     TYR A  1044                                                      
REMARK 465     HIS A  1045                                                      
REMARK 465     LEU A  1046                                                      
REMARK 465     MET A  1047                                                      
REMARK 465     SER A  1048                                                      
REMARK 465     PHE A  1049                                                      
REMARK 465     PRO A  1050                                                      
REMARK 465     GLN A  1051                                                      
REMARK 465     SER A  1052                                                      
REMARK 465     ALA A  1053                                                      
REMARK 465     PRO A  1054                                                      
REMARK 465     HIS A  1055                                                      
REMARK 465     GLY A  1056                                                      
REMARK 465     VAL A  1057                                                      
REMARK 465     VAL A  1058                                                      
REMARK 465     PHE A  1059                                                      
REMARK 465     LEU A  1060                                                      
REMARK 465     HIS A  1061                                                      
REMARK 465     VAL A  1062                                                      
REMARK 465     THR A  1063                                                      
REMARK 465     TYR A  1064                                                      
REMARK 465     VAL A  1065                                                      
REMARK 465     PRO A  1066                                                      
REMARK 465     ALA A  1067                                                      
REMARK 465     GLN A  1068                                                      
REMARK 465     GLU A  1069                                                      
REMARK 465     LYS A  1070                                                      
REMARK 465     ASN A  1071                                                      
REMARK 465     PHE A  1072                                                      
REMARK 465     THR A  1073                                                      
REMARK 465     THR A  1074                                                      
REMARK 465     ALA A  1075                                                      
REMARK 465     PRO A  1076                                                      
REMARK 465     ALA A  1077                                                      
REMARK 465     ILE A  1078                                                      
REMARK 465     CYS A  1079                                                      
REMARK 465     HIS A  1080                                                      
REMARK 465     ASP A  1081                                                      
REMARK 465     GLY A  1082                                                      
REMARK 465     LYS A  1083                                                      
REMARK 465     ALA A  1084                                                      
REMARK 465     HIS A  1085                                                      
REMARK 465     PHE A  1086                                                      
REMARK 465     PRO A  1087                                                      
REMARK 465     ARG A  1088                                                      
REMARK 465     GLU A  1089                                                      
REMARK 465     GLY A  1090                                                      
REMARK 465     VAL A  1091                                                      
REMARK 465     PHE A  1092                                                      
REMARK 465     VAL A  1093                                                      
REMARK 465     SER A  1094                                                      
REMARK 465     ASN A  1095                                                      
REMARK 465     GLY A  1096                                                      
REMARK 465     THR A  1097                                                      
REMARK 465     HIS A  1098                                                      
REMARK 465     TRP A  1099                                                      
REMARK 465     PHE A  1100                                                      
REMARK 465     VAL A  1101                                                      
REMARK 465     THR A  1102                                                      
REMARK 465     GLN A  1103                                                      
REMARK 465     ARG A  1104                                                      
REMARK 465     ASN A  1105                                                      
REMARK 465     PHE A  1106                                                      
REMARK 465     TYR A  1107                                                      
REMARK 465     GLU A  1108                                                      
REMARK 465     PRO A  1109                                                      
REMARK 465     GLN A  1110                                                      
REMARK 465     ILE A  1111                                                      
REMARK 465     ILE A  1112                                                      
REMARK 465     THR A  1113                                                      
REMARK 465     THR A  1114                                                      
REMARK 465     ASP A  1115                                                      
REMARK 465     ASN A  1116                                                      
REMARK 465     THR A  1117                                                      
REMARK 465     PHE A  1118                                                      
REMARK 465     VAL A  1119                                                      
REMARK 465     SER A  1120                                                      
REMARK 465     GLY A  1121                                                      
REMARK 465     ASN A  1122                                                      
REMARK 465     CYS A  1123                                                      
REMARK 465     ASP A  1124                                                      
REMARK 465     VAL A  1125                                                      
REMARK 465     VAL A  1126                                                      
REMARK 465     ILE A  1127                                                      
REMARK 465     GLY A  1128                                                      
REMARK 465     ILE A  1129                                                      
REMARK 465     VAL A  1130                                                      
REMARK 465     ASN A  1131                                                      
REMARK 465     ASN A  1132                                                      
REMARK 465     THR A  1133                                                      
REMARK 465     VAL A  1134                                                      
REMARK 465     TYR A  1135                                                      
REMARK 465     ASP A  1136                                                      
REMARK 465     PRO A  1137                                                      
REMARK 465     LEU A  1138                                                      
REMARK 465     GLN A  1139                                                      
REMARK 465     PRO A  1140                                                      
REMARK 465     GLU A  1141                                                      
REMARK 465     LEU A  1142                                                      
REMARK 465     ASP A  1143                                                      
REMARK 465     SER A  1144                                                      
REMARK 465     PHE A  1145                                                      
REMARK 465     LYS A  1146                                                      
REMARK 465     GLU A  1147                                                      
REMARK 465     GLU A  1148                                                      
REMARK 465     LEU A  1149                                                      
REMARK 465     ASP A  1150                                                      
REMARK 465     LYS A  1151                                                      
REMARK 465     TYR A  1152                                                      
REMARK 465     PHE A  1153                                                      
REMARK 465     LYS A  1154                                                      
REMARK 465     ASN A  1155                                                      
REMARK 465     HIS A  1156                                                      
REMARK 465     THR A  1157                                                      
REMARK 465     SER A  1158                                                      
REMARK 465     PRO A  1159                                                      
REMARK 465     ASP A  1160                                                      
REMARK 465     VAL A  1161                                                      
REMARK 465     ASP A  1162                                                      
REMARK 465     LEU A  1163                                                      
REMARK 465     GLY A  1164                                                      
REMARK 465     ASP A  1165                                                      
REMARK 465     ILE A  1166                                                      
REMARK 465     SER A  1167                                                      
REMARK 465     GLY A  1168                                                      
REMARK 465     ILE A  1169                                                      
REMARK 465     ASN A  1170                                                      
REMARK 465     ALA A  1171                                                      
REMARK 465     SER A  1172                                                      
REMARK 465     VAL A  1173                                                      
REMARK 465     VAL A  1174                                                      
REMARK 465     ASN A  1175                                                      
REMARK 465     ILE A  1176                                                      
REMARK 465     GLN A  1177                                                      
REMARK 465     LYS A  1178                                                      
REMARK 465     GLU A  1179                                                      
REMARK 465     ILE A  1180                                                      
REMARK 465     ASP A  1181                                                      
REMARK 465     ARG A  1182                                                      
REMARK 465     LEU A  1183                                                      
REMARK 465     ASN A  1184                                                      
REMARK 465     GLU A  1185                                                      
REMARK 465     VAL A  1186                                                      
REMARK 465     ALA A  1187                                                      
REMARK 465     LYS A  1188                                                      
REMARK 465     ASN A  1189                                                      
REMARK 465     LEU A  1190                                                      
REMARK 465     ASN A  1191                                                      
REMARK 465     GLU A  1192                                                      
REMARK 465     SER A  1193                                                      
REMARK 465     LEU A  1194                                                      
REMARK 465     ILE A  1195                                                      
REMARK 465     ASP A  1196                                                      
REMARK 465     LEU A  1197                                                      
REMARK 465     GLN A  1198                                                      
REMARK 465     GLU A  1199                                                      
REMARK 465     LEU A  1200                                                      
REMARK 465     GLY A  1201                                                      
REMARK 465     LYS A  1202                                                      
REMARK 465     TYR A  1203                                                      
REMARK 465     GLU A  1204                                                      
REMARK 465     GLN A  1205                                                      
REMARK 465     TYR A  1206                                                      
REMARK 465     ILE A  1207                                                      
REMARK 465     LYS A  1208                                                      
REMARK 465     TRP A  1209                                                      
REMARK 465     PRO A  1210                                                      
REMARK 465     SER A  1211                                                      
REMARK 465     GLY A  1212                                                      
REMARK 465     ARG A  1213                                                      
REMARK 465     LEU A  1214                                                      
REMARK 465     VAL A  1215                                                      
REMARK 465     PRO A  1216                                                      
REMARK 465     ARG A  1217                                                      
REMARK 465     GLY A  1218                                                      
REMARK 465     SER A  1219                                                      
REMARK 465     PRO A  1220                                                      
REMARK 465     GLY A  1221                                                      
REMARK 465     SER A  1222                                                      
REMARK 465     GLY A  1223                                                      
REMARK 465     TYR A  1224                                                      
REMARK 465     ILE A  1225                                                      
REMARK 465     PRO A  1226                                                      
REMARK 465     GLU A  1227                                                      
REMARK 465     ALA A  1228                                                      
REMARK 465     PRO A  1229                                                      
REMARK 465     ARG A  1230                                                      
REMARK 465     ASP A  1231                                                      
REMARK 465     GLY A  1232                                                      
REMARK 465     GLN A  1233                                                      
REMARK 465     ALA A  1234                                                      
REMARK 465     TYR A  1235                                                      
REMARK 465     VAL A  1236                                                      
REMARK 465     ARG A  1237                                                      
REMARK 465     LYS A  1238                                                      
REMARK 465     ASP A  1239                                                      
REMARK 465     GLY A  1240                                                      
REMARK 465     GLU A  1241                                                      
REMARK 465     TRP A  1242                                                      
REMARK 465     VAL A  1243                                                      
REMARK 465     LEU A  1244                                                      
REMARK 465     LEU A  1245                                                      
REMARK 465     SER A  1246                                                      
REMARK 465     THR A  1247                                                      
REMARK 465     PHE A  1248                                                      
REMARK 465     LEU A  1249                                                      
REMARK 465     GLY A  1250                                                      
REMARK 465     HIS A  1251                                                      
REMARK 465     HIS A  1252                                                      
REMARK 465     HIS A  1253                                                      
REMARK 465     HIS A  1254                                                      
REMARK 465     HIS A  1255                                                      
REMARK 465     HIS A  1256                                                      
REMARK 465     ALA H   114                                                      
REMARK 465     SER H   115                                                      
REMARK 465     THR H   116                                                      
REMARK 465     LYS H   117                                                      
REMARK 465     GLY H   118                                                      
REMARK 465     PRO H   119                                                      
REMARK 465     SER H   120                                                      
REMARK 465     VAL H   121                                                      
REMARK 465     PHE H   122                                                      
REMARK 465     PRO H   123                                                      
REMARK 465     LEU H   124                                                      
REMARK 465     ALA H   125                                                      
REMARK 465     PRO H   126                                                      
REMARK 465     SER H   127                                                      
REMARK 465     SER H   128                                                      
REMARK 465     LYS H   129                                                      
REMARK 465     SER H   130                                                      
REMARK 465     THR H   131                                                      
REMARK 465     SER H   132                                                      
REMARK 465     GLY H   133                                                      
REMARK 465     GLY H   134                                                      
REMARK 465     THR H   135                                                      
REMARK 465     ALA H   136                                                      
REMARK 465     ALA H   137                                                      
REMARK 465     LEU H   138                                                      
REMARK 465     GLY H   139                                                      
REMARK 465     CYS H   140                                                      
REMARK 465     LEU H   141                                                      
REMARK 465     VAL H   142                                                      
REMARK 465     LYS H   143                                                      
REMARK 465     ASP H   144                                                      
REMARK 465     TYR H   145                                                      
REMARK 465     PHE H   146                                                      
REMARK 465     PRO H   147                                                      
REMARK 465     GLU H   148                                                      
REMARK 465     PRO H   149                                                      
REMARK 465     VAL H   150                                                      
REMARK 465     THR H   151                                                      
REMARK 465     VAL H   152                                                      
REMARK 465     SER H   153                                                      
REMARK 465     TRP H   154                                                      
REMARK 465     ASN H   155                                                      
REMARK 465     SER H   156                                                      
REMARK 465     GLY H   157                                                      
REMARK 465     ALA H   158                                                      
REMARK 465     LEU H   159                                                      
REMARK 465     THR H   160                                                      
REMARK 465     SER H   161                                                      
REMARK 465     GLY H   162                                                      
REMARK 465     VAL H   163                                                      
REMARK 465     HIS H   164                                                      
REMARK 465     THR H   165                                                      
REMARK 465     PHE H   166                                                      
REMARK 465     PRO H   167                                                      
REMARK 465     ALA H   168                                                      
REMARK 465     VAL H   169                                                      
REMARK 465     LEU H   170                                                      
REMARK 465     GLN H   171                                                      
REMARK 465     SER H   172                                                      
REMARK 465     SER H   173                                                      
REMARK 465     GLY H   174                                                      
REMARK 465     LEU H   175                                                      
REMARK 465     TYR H   176                                                      
REMARK 465     SER H   177                                                      
REMARK 465     LEU H   178                                                      
REMARK 465     SER H   179                                                      
REMARK 465     SER H   180                                                      
REMARK 465     VAL H   181                                                      
REMARK 465     VAL H   182                                                      
REMARK 465     THR H   183                                                      
REMARK 465     VAL H   184                                                      
REMARK 465     PRO H   185                                                      
REMARK 465     SER H   186                                                      
REMARK 465     SER H   187                                                      
REMARK 465     SER H   188                                                      
REMARK 465     LEU H   189                                                      
REMARK 465     GLY H   190                                                      
REMARK 465     THR H   191                                                      
REMARK 465     GLN H   192                                                      
REMARK 465     THR H   193                                                      
REMARK 465     TYR H   194                                                      
REMARK 465     ILE H   195                                                      
REMARK 465     CYS H   196                                                      
REMARK 465     ASN H   197                                                      
REMARK 465     VAL H   198                                                      
REMARK 465     ASN H   199                                                      
REMARK 465     HIS H   200                                                      
REMARK 465     LYS H   201                                                      
REMARK 465     PRO H   202                                                      
REMARK 465     SER H   203                                                      
REMARK 465     ASN H   204                                                      
REMARK 465     THR H   205                                                      
REMARK 465     LYS H   206                                                      
REMARK 465     VAL H   207                                                      
REMARK 465     ASP H   208                                                      
REMARK 465     LYS H   209                                                      
REMARK 465     LYS H   210                                                      
REMARK 465     VAL H   211                                                      
REMARK 465     GLU H   212                                                      
REMARK 465     PRO H   213                                                      
REMARK 465     LYS H   214                                                      
REMARK 465     SER H   215                                                      
REMARK 465     CYS H   216                                                      
REMARK 465     ASP H   217                                                      
REMARK 465     LYS H   218                                                      
REMARK 465     THR H   219                                                      
REMARK 465     HIS H   220                                                      
REMARK 465     HIS H   221                                                      
REMARK 465     HIS H   222                                                      
REMARK 465     HIS H   223                                                      
REMARK 465     HIS H   224                                                      
REMARK 465     HIS H   225                                                      
REMARK 465     ARG L   108                                                      
REMARK 465     THR L   109                                                      
REMARK 465     VAL L   110                                                      
REMARK 465     ALA L   111                                                      
REMARK 465     ALA L   112                                                      
REMARK 465     PRO L   113                                                      
REMARK 465     SER L   114                                                      
REMARK 465     VAL L   115                                                      
REMARK 465     PHE L   116                                                      
REMARK 465     ILE L   117                                                      
REMARK 465     PHE L   118                                                      
REMARK 465     PRO L   119                                                      
REMARK 465     PRO L   120                                                      
REMARK 465     SER L   121                                                      
REMARK 465     ASP L   122                                                      
REMARK 465     GLU L   123                                                      
REMARK 465     GLN L   124                                                      
REMARK 465     LEU L   125                                                      
REMARK 465     LYS L   126                                                      
REMARK 465     SER L   127                                                      
REMARK 465     GLY L   128                                                      
REMARK 465     THR L   129                                                      
REMARK 465     ALA L   130                                                      
REMARK 465     SER L   131                                                      
REMARK 465     VAL L   132                                                      
REMARK 465     VAL L   133                                                      
REMARK 465     CYS L   134                                                      
REMARK 465     LEU L   135                                                      
REMARK 465     LEU L   136                                                      
REMARK 465     ASN L   137                                                      
REMARK 465     ASN L   138                                                      
REMARK 465     PHE L   139                                                      
REMARK 465     TYR L   140                                                      
REMARK 465     PRO L   141                                                      
REMARK 465     ARG L   142                                                      
REMARK 465     GLU L   143                                                      
REMARK 465     ALA L   144                                                      
REMARK 465     LYS L   145                                                      
REMARK 465     VAL L   146                                                      
REMARK 465     GLN L   147                                                      
REMARK 465     TRP L   148                                                      
REMARK 465     LYS L   149                                                      
REMARK 465     VAL L   150                                                      
REMARK 465     ASP L   151                                                      
REMARK 465     ASN L   152                                                      
REMARK 465     ALA L   153                                                      
REMARK 465     LEU L   154                                                      
REMARK 465     GLN L   155                                                      
REMARK 465     SER L   156                                                      
REMARK 465     GLY L   157                                                      
REMARK 465     ASN L   158                                                      
REMARK 465     SER L   159                                                      
REMARK 465     GLN L   160                                                      
REMARK 465     GLU L   161                                                      
REMARK 465     SER L   162                                                      
REMARK 465     VAL L   163                                                      
REMARK 465     THR L   164                                                      
REMARK 465     GLU L   165                                                      
REMARK 465     GLN L   166                                                      
REMARK 465     ASP L   167                                                      
REMARK 465     SER L   168                                                      
REMARK 465     LYS L   169                                                      
REMARK 465     ASP L   170                                                      
REMARK 465     SER L   171                                                      
REMARK 465     THR L   172                                                      
REMARK 465     TYR L   173                                                      
REMARK 465     SER L   174                                                      
REMARK 465     LEU L   175                                                      
REMARK 465     SER L   176                                                      
REMARK 465     SER L   177                                                      
REMARK 465     THR L   178                                                      
REMARK 465     LEU L   179                                                      
REMARK 465     THR L   180                                                      
REMARK 465     LEU L   181                                                      
REMARK 465     SER L   182                                                      
REMARK 465     LYS L   183                                                      
REMARK 465     ALA L   184                                                      
REMARK 465     ASP L   185                                                      
REMARK 465     TYR L   186                                                      
REMARK 465     GLU L   187                                                      
REMARK 465     LYS L   188                                                      
REMARK 465     HIS L   189                                                      
REMARK 465     LYS L   190                                                      
REMARK 465     VAL L   191                                                      
REMARK 465     TYR L   192                                                      
REMARK 465     ALA L   193                                                      
REMARK 465     CYS L   194                                                      
REMARK 465     GLU L   195                                                      
REMARK 465     VAL L   196                                                      
REMARK 465     THR L   197                                                      
REMARK 465     HIS L   198                                                      
REMARK 465     GLN L   199                                                      
REMARK 465     GLY L   200                                                      
REMARK 465     LEU L   201                                                      
REMARK 465     SER L   202                                                      
REMARK 465     SER L   203                                                      
REMARK 465     PRO L   204                                                      
REMARK 465     VAL L   205                                                      
REMARK 465     THR L   206                                                      
REMARK 465     LYS L   207                                                      
REMARK 465     SER L   208                                                      
REMARK 465     PHE L   209                                                      
REMARK 465     ASN L   210                                                      
REMARK 465     ARG L   211                                                      
REMARK 465     GLY L   212                                                      
REMARK 465     GLU L   213                                                      
REMARK 465     CYS L   214                                                      
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   SG   CYS A   336     SG   CYS A   361              1.56            
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    ASN H 100B    -168.20    -78.88                                   
REMARK 500    THR L  10       31.07    -97.71                                   
REMARK 500    ARG L  61        7.03     82.20                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-35155   RELATED DB: EMDB                             
REMARK 900 LOCAL CRYOEM STRUCTURE OF THE SARS-COV-2 S6P IN COMPLEX WITH 7B3 FAB 
DBREF  8I3S A   14  1210  UNP    P0DTC2   SPIKE_SARS2     14   1213             
DBREF  8I3S H    1   225  PDB    8I3S     8I3S             1    225             
DBREF  8I3S L    1   214  PDB    8I3S     8I3S             1    214             
SEQADV 8I3S     A       UNP  P0DTC2    ARG   682 DELETION                       
SEQADV 8I3S     A       UNP  P0DTC2    ARG   683 DELETION                       
SEQADV 8I3S     A       UNP  P0DTC2    ALA   684 DELETION                       
SEQADV 8I3S ALA A  682  UNP  P0DTC2    ARG   685 CONFLICT                       
SEQADV 8I3S PRO A  814  UNP  P0DTC2    PHE   817 ENGINEERED MUTATION            
SEQADV 8I3S PRO A  889  UNP  P0DTC2    ALA   892 ENGINEERED MUTATION            
SEQADV 8I3S PRO A  896  UNP  P0DTC2    ALA   899 ENGINEERED MUTATION            
SEQADV 8I3S PRO A  939  UNP  P0DTC2    ALA   942 ENGINEERED MUTATION            
SEQADV 8I3S PRO A  983  UNP  P0DTC2    LYS   986 ENGINEERED MUTATION            
SEQADV 8I3S PRO A  984  UNP  P0DTC2    VAL   987 ENGINEERED MUTATION            
SEQADV 8I3S SER A 1211  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1212  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ARG A 1213  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S LEU A 1214  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S VAL A 1215  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S PRO A 1216  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ARG A 1217  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1218  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S SER A 1219  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S PRO A 1220  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1221  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S SER A 1222  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1223  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S TYR A 1224  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ILE A 1225  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S PRO A 1226  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLU A 1227  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ALA A 1228  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S PRO A 1229  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ARG A 1230  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ASP A 1231  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1232  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLN A 1233  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ALA A 1234  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S TYR A 1235  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S VAL A 1236  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ARG A 1237  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S LYS A 1238  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S ASP A 1239  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1240  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLU A 1241  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S TRP A 1242  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S VAL A 1243  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S LEU A 1244  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S LEU A 1245  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S SER A 1246  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S THR A 1247  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S PHE A 1248  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S LEU A 1249  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S GLY A 1250  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1251  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1252  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1253  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1254  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1255  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 8I3S HIS A 1256  UNP  P0DTC2              EXPRESSION TAG                 
SEQRES   1 A 1243  GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO          
SEQRES   2 A 1243  ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO          
SEQRES   3 A 1243  ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN          
SEQRES   4 A 1243  ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE          
SEQRES   5 A 1243  HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG          
SEQRES   6 A 1243  PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR          
SEQRES   7 A 1243  PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP          
SEQRES   8 A 1243  ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU          
SEQRES   9 A 1243  LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL          
SEQRES  10 A 1243  CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL          
SEQRES  11 A 1243  TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU          
SEQRES  12 A 1243  PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU          
SEQRES  13 A 1243  TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS          
SEQRES  14 A 1243  GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS          
SEQRES  15 A 1243  ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR          
SEQRES  16 A 1243  PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER          
SEQRES  17 A 1243  ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN          
SEQRES  18 A 1243  ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER          
SEQRES  19 A 1243  TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA          
SEQRES  20 A 1243  GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG          
SEQRES  21 A 1243  THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR          
SEQRES  22 A 1243  ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR          
SEQRES  23 A 1243  LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE          
SEQRES  24 A 1243  TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER          
SEQRES  25 A 1243  ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE          
SEQRES  26 A 1243  GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR          
SEQRES  27 A 1243  ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP          
SEQRES  28 A 1243  TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE          
SEQRES  29 A 1243  LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU          
SEQRES  30 A 1243  CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG          
SEQRES  31 A 1243  GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY          
SEQRES  32 A 1243  LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE          
SEQRES  33 A 1243  THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP          
SEQRES  34 A 1243  SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU          
SEQRES  35 A 1243  PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE          
SEQRES  36 A 1243  SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN          
SEQRES  37 A 1243  GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER          
SEQRES  38 A 1243  TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO          
SEQRES  39 A 1243  TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA          
SEQRES  40 A 1243  PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU          
SEQRES  41 A 1243  VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU          
SEQRES  42 A 1243  THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE          
SEQRES  43 A 1243  LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR          
SEQRES  44 A 1243  THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU          
SEQRES  45 A 1243  ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE          
SEQRES  46 A 1243  THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU          
SEQRES  47 A 1243  TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE          
SEQRES  48 A 1243  HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER          
SEQRES  49 A 1243  THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU          
SEQRES  50 A 1243  ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP          
SEQRES  51 A 1243  ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR          
SEQRES  52 A 1243  GLN THR ASN SER PRO ALA SER VAL ALA SER GLN SER ILE          
SEQRES  53 A 1243  ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SER VAL          
SEQRES  54 A 1243  ALA TYR SER ASN ASN SER ILE ALA ILE PRO THR ASN PHE          
SEQRES  55 A 1243  THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SER MET          
SEQRES  56 A 1243  THR LYS THR SER VAL ASP CYS THR MET TYR ILE CYS GLY          
SEQRES  57 A 1243  ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN TYR GLY          
SEQRES  58 A 1243  SER PHE CYS THR GLN LEU ASN ARG ALA LEU THR GLY ILE          
SEQRES  59 A 1243  ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL PHE ALA          
SEQRES  60 A 1243  GLN VAL LYS GLN ILE TYR LYS THR PRO PRO ILE LYS ASP          
SEQRES  61 A 1243  PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO          
SEQRES  62 A 1243  SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP LEU LEU          
SEQRES  63 A 1243  PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE ILE LYS          
SEQRES  64 A 1243  GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA ARG ASP          
SEQRES  65 A 1243  LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU THR VAL LEU          
SEQRES  66 A 1243  PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN TYR THR          
SEQRES  67 A 1243  SER ALA LEU LEU ALA GLY THR ILE THR SER GLY TRP THR          
SEQRES  68 A 1243  PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE PRO MET          
SEQRES  69 A 1243  GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN          
SEQRES  70 A 1243  ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA ASN GLN          
SEQRES  71 A 1243  PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER LEU SER          
SEQRES  72 A 1243  SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP VAL VAL          
SEQRES  73 A 1243  ASN GLN ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN          
SEQRES  74 A 1243  LEU SER SER ASN PHE GLY ALA ILE SER SER VAL LEU ASN          
SEQRES  75 A 1243  ASP ILE LEU SER ARG LEU ASP PRO PRO GLU ALA GLU VAL          
SEQRES  76 A 1243  GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU          
SEQRES  77 A 1243  GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU          
SEQRES  78 A 1243  ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS MET SER          
SEQRES  79 A 1243  GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS          
SEQRES  80 A 1243  GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SER ALA          
SEQRES  81 A 1243  PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO          
SEQRES  82 A 1243  ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA ILE CYS          
SEQRES  83 A 1243  HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY VAL PHE          
SEQRES  84 A 1243  VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN ARG ASN          
SEQRES  85 A 1243  PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN THR PHE          
SEQRES  86 A 1243  VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE VAL ASN          
SEQRES  87 A 1243  ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER          
SEQRES  88 A 1243  PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR          
SEQRES  89 A 1243  SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN          
SEQRES  90 A 1243  ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU          
SEQRES  91 A 1243  ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP          
SEQRES  92 A 1243  LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR ILE LYS TRP          
SEQRES  93 A 1243  PRO SER GLY ARG LEU VAL PRO ARG GLY SER PRO GLY SER          
SEQRES  94 A 1243  GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR          
SEQRES  95 A 1243  VAL ARG LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE          
SEQRES  96 A 1243  LEU GLY HIS HIS HIS HIS HIS HIS                              
SEQRES   1 H  230  GLN VAL GLN LEU VAL GLN SER GLY ALA GLU MET LYS ASN          
SEQRES   2 H  230  PHE GLY SER SER VAL LYS VAL SER CYS LYS ALA SER GLY          
SEQRES   3 H  230  GLY THR PHE SER ILE ASN TRP VAL ARG GLN ALA PRO GLY          
SEQRES   4 H  230  LEU GLY LEU GLU TYR MET GLY ARG ILE ILE PRO ALA LEU          
SEQRES   5 H  230  ASP ARG ALA ILE TYR THR GLN LYS PHE GLN GLY ARG VAL          
SEQRES   6 H  230  THR ILE THR ALA ASP LYS SER THR SER THR VAL TYR MET          
SEQRES   7 H  230  GLU LEU SER GLY LEU ARG SER GLU ASP THR ALA VAL TYR          
SEQRES   8 H  230  TYR CYS ALA ARG SER VAL VAL GLY PRO THR PRO ASN TYR          
SEQRES   9 H  230  PHE ASP PRO TRP GLY GLN GLY THR LEU VAL THR VAL SER          
SEQRES  10 H  230  SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA          
SEQRES  11 H  230  PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU          
SEQRES  12 H  230  GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR          
SEQRES  13 H  230  VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS          
SEQRES  14 H  230  THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER          
SEQRES  15 H  230  LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY          
SEQRES  16 H  230  THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER          
SEQRES  17 H  230  ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SER CYS          
SEQRES  18 H  230  ASP LYS THR HIS HIS HIS HIS HIS HIS                          
SEQRES   1 L  213  GLU ILE VAL MET THR GLN SER PRO ALA THR LEU SER VAL          
SEQRES   2 L  213  SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER          
SEQRES   3 L  213  GLN SER VAL SER SER ASP LEU ALA TRP TYR GLN GLN LYS          
SEQRES   4 L  213  ARG GLY GLN ALA PRO ARG LEU LEU ILE TYR GLY ALA SER          
SEQRES   5 L  213  THR ARG ALA THR GLY ILE PRO ALA ARG PHE SER GLY SER          
SEQRES   6 L  213  GLY SER GLY THR GLU PHE THR LEU THR ILE SER SER LEU          
SEQRES   7 L  213  GLN SER GLU ASP PHE ALA VAL TYR TYR CYS GLN GLN TYR          
SEQRES   8 L  213  ASN ASN PHE ILE ALA PHE GLY GLN GLY THR ARG LEU GLU          
SEQRES   9 L  213  ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE PHE          
SEQRES  10 L  213  PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SER          
SEQRES  11 L  213  VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU ALA          
SEQRES  12 L  213  LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER GLY          
SEQRES  13 L  213  ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS ASP          
SEQRES  14 L  213  SER THR TYR SER LEU SER SER THR LEU THR LEU SER LYS          
SEQRES  15 L  213  ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU VAL          
SEQRES  16 L  213  THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER PHE          
SEQRES  17 L  213  ASN ARG GLY GLU CYS                                          
HET    NAG  A1301      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   4  NAG    C8 H15 N O6                                                  
HELIX    1 AA1 PRO A  337  ALA A  344  1                                   8    
HELIX    2 AA2 TYR A  365  SER A  371  1                                   7    
HELIX    3 AA3 SER A  383  ASN A  388  5                                   6    
HELIX    4 AA4 GLU A  406  ALA A  411  5                                   6    
HELIX    5 AA5 GLY A  416  ASN A  422  1                                   7    
HELIX    6 AA6 SER A  438  SER A  443  1                                   6    
HELIX    7 AA7 ARG H   83  THR H   87  5                                   5    
SHEET    1 AA1 5 ASN A 354  ILE A 358  0                                        
SHEET    2 AA1 5 VAL A 395  ILE A 402 -1  O  ALA A 397   N  LYS A 356           
SHEET    3 AA1 5 TYR A 508  SER A 514 -1  O  TYR A 508   N  ILE A 402           
SHEET    4 AA1 5 GLY A 431  ASN A 437 -1  N  CYS A 432   O  LEU A 513           
SHEET    5 AA1 5 CYS A 379  TYR A 380 -1  N  TYR A 380   O  GLY A 431           
SHEET    1 AA2 2 CYS A 361  VAL A 362  0                                        
SHEET    2 AA2 2 VAL A 524  CYS A 525  1  O  CYS A 525   N  CYS A 361           
SHEET    1 AA3 2 LEU A 452  ARG A 454  0                                        
SHEET    2 AA3 2 LEU A 492  SER A 494 -1  O  GLN A 493   N  TYR A 453           
SHEET    1 AA4 2 TYR A 473  GLN A 474  0                                        
SHEET    2 AA4 2 CYS A 488  TYR A 489 -1  O  TYR A 489   N  TYR A 473           
SHEET    1 AA5 4 GLN H   6  SER H   7  0                                        
SHEET    2 AA5 4 VAL H  18  LYS H  23 -1  O  SER H  21   N  SER H   7           
SHEET    3 AA5 4 THR H  77  LEU H  82 -1  O  MET H  80   N  VAL H  20           
SHEET    4 AA5 4 VAL H  67  ASP H  72 -1  N  ASP H  72   O  THR H  77           
SHEET    1 AA6 2 LYS H  12  ASN H  13  0                                        
SHEET    2 AA6 2 VAL H 111  SER H 112  1  O  SER H 112   N  LYS H  12           
SHEET    1 AA7 4 ARG H  56  TYR H  59  0                                        
SHEET    2 AA7 4 LEU H  45  ILE H  52 -1  N  ARG H  50   O  ILE H  58           
SHEET    3 AA7 4 SER H  30  GLN H  39 -1  N  TRP H  36   O  GLY H  49           
SHEET    4 AA7 4 VAL H  89  SER H  95 -1  O  ALA H  93   N  ASN H  32           
SHEET    1 AA8 3 THR L  20  ARG L  24  0                                        
SHEET    2 AA8 3 GLU L  70  ILE L  75 -1  O  PHE L  71   N  CYS L  23           
SHEET    3 AA8 3 PHE L  62  SER L  65 -1  N  SER L  65   O  THR L  72           
SHEET    1 AA9 4 ARG L  45  LEU L  46  0                                        
SHEET    2 AA9 4 LEU L  33  GLN L  38 -1  N  GLN L  37   O  ARG L  45           
SHEET    3 AA9 4 VAL L  85  GLN L  90 -1  O  VAL L  85   N  GLN L  38           
SHEET    4 AA9 4 ALA L  97  PHE L  98 -1  O  ALA L  97   N  GLN L  90           
SSBOND   1 CYS A  379    CYS A  432                          1555   1555  2.03  
SSBOND   2 CYS A  391    CYS A  525                          1555   1555  2.03  
SSBOND   3 CYS A  480    CYS A  488                          1555   1555  2.03  
SSBOND   4 CYS H   22    CYS H   92                          1555   1555  2.03  
SSBOND   5 CYS L   23    CYS L   88                          1555   1555  2.03  
LINK         ND2 ASN A 343                 C1  NAG A1301     1555   1555  1.44  
CISPEP   1 ASP H  101    PRO H  102          0        -5.43                     
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1                      
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      1.000000  0.000000  0.000000        0.00000                         
SCALE2      0.000000  1.000000  0.000000        0.00000                         
SCALE3      0.000000  0.000000  1.000000        0.00000                         
ATOM      1  N   THR A 333     172.712 135.086 176.272  1.00 98.29           N  
ATOM      2  CA  THR A 333     171.804 134.051 175.797  1.00 98.29           C  
ATOM      3  C   THR A 333     172.041 133.739 174.320  1.00 98.29           C  
ATOM      4  O   THR A 333     173.044 133.121 173.959  1.00 98.29           O  
ATOM      5  CB  THR A 333     170.335 134.458 176.003  1.00 98.29           C  
ATOM      6  OG1 THR A 333     170.107 135.745 175.417  1.00 98.29           O  
ATOM      7  CG2 THR A 333     170.004 134.518 177.484  1.00 98.29           C  
ATOM      8  N   ASN A 334     171.114 134.170 173.470  1.00106.83           N  
ATOM      9  CA  ASN A 334     171.202 133.867 172.052  1.00106.83           C  
ATOM     10  C   ASN A 334     172.266 134.726 171.374  1.00106.83           C  
ATOM     11  O   ASN A 334     172.739 135.727 171.917  1.00106.83           O  
ATOM     12  CB  ASN A 334     169.848 134.074 171.374  1.00106.83           C  
ATOM     13  CG  ASN A 334     169.804 133.502 169.970  1.00106.83           C  
ATOM     14  OD1 ASN A 334     170.469 132.512 169.666  1.00106.83           O  
ATOM     15  ND2 ASN A 334     169.015 134.126 169.106  1.00106.83           N  
ATOM     16  N   LEU A 335     172.639 134.315 170.165  1.00113.94           N  
ATOM     17  CA  LEU A 335     173.630 135.046 169.391  1.00113.94           C  
ATOM     18  C   LEU A 335     173.076 136.388 168.922  1.00113.94           C  
ATOM     19  O   LEU A 335     171.869 136.558 168.731  1.00113.94           O  
ATOM     20  CB  LEU A 335     174.090 134.216 168.192  1.00113.94           C  
ATOM     21  CG  LEU A 335     174.849 132.912 168.460  1.00113.94           C  
ATOM     22  CD1 LEU A 335     175.113 132.125 167.181  1.00113.94           C  
ATOM     23  CD2 LEU A 335     176.153 133.202 169.188  1.00113.94           C  
ATOM     24  N   CYS A 336     173.977 137.348 168.747  1.00112.17           N  
ATOM     25  CA  CYS A 336     173.576 138.687 168.354  1.00112.17           C  
ATOM     26  C   CYS A 336     173.364 138.771 166.843  1.00112.17           C  
ATOM     27  O   CYS A 336     174.087 138.139 166.069  1.00112.17           O  
ATOM     28  CB  CYS A 336     174.631 139.701 168.780  1.00112.17           C  
ATOM     29  SG  CYS A 336     174.211 141.414 168.424  1.00112.17           S  
ATOM     30  N   PRO A 337     172.379 139.549 166.398  1.00 99.36           N  
ATOM     31  CA  PRO A 337     172.232 139.850 164.967  1.00 99.36           C  
ATOM     32  C   PRO A 337     173.129 140.971 164.462  1.00 99.36           C  
ATOM     33  O   PRO A 337     172.846 141.522 163.394  1.00 99.36           O  
ATOM     34  CB  PRO A 337     170.759 140.268 164.872  1.00 99.36           C  
ATOM     35  CG  PRO A 337     170.482 140.891 166.185  1.00 99.36           C  
ATOM     36  CD  PRO A 337     171.250 140.072 167.186  1.00 99.36           C  
ATOM     37  N   PHE A 338     174.192 141.335 165.204  1.00 95.93           N  
ATOM     38  CA  PHE A 338     175.032 142.467 164.829  1.00 95.93           C  
ATOM     39  C   PHE A 338     175.696 142.249 163.477  1.00 95.93           C  
ATOM     40  O   PHE A 338     176.001 143.212 162.765  1.00 95.93           O  
ATOM     41  CB  PHE A 338     176.088 142.708 165.903  1.00 95.93           C  
ATOM     42  CG  PHE A 338     176.508 144.134 166.020  1.00 95.93           C  
ATOM     43  CD1 PHE A 338     175.568 145.126 166.226  1.00 95.93           C  
ATOM     44  CD2 PHE A 338     177.839 144.487 165.913  1.00 95.93           C  
ATOM     45  CE1 PHE A 338     175.947 146.443 166.330  1.00 95.93           C  
ATOM     46  CE2 PHE A 338     178.224 145.804 166.015  1.00 95.93           C  
ATOM     47  CZ  PHE A 338     177.276 146.783 166.226  1.00 95.93           C  
ATOM     48  N   GLY A 339     175.927 140.977 163.112  1.00 94.64           N  
ATOM     49  CA  GLY A 339     176.564 140.703 161.836  1.00 94.64           C  
ATOM     50  C   GLY A 339     175.741 141.180 160.656  1.00 94.64           C  
ATOM     51  O   GLY A 339     176.286 141.670 159.665  1.00 94.64           O  
ATOM     52  N   GLU A 340     174.415 141.053 160.749  1.00 93.51           N  
ATOM     53  CA  GLU A 340     173.557 141.427 159.630  1.00 93.51           C  
ATOM     54  C   GLU A 340     173.637 142.920 159.339  1.00 93.51           C  
ATOM     55  O   GLU A 340     173.525 143.339 158.182  1.00 93.51           O  
ATOM     56  CB  GLU A 340     172.113 141.014 159.913  1.00 93.51           C  
ATOM     57  CG  GLU A 340     171.889 139.513 159.920  1.00 93.51           C  
ATOM     58  CD  GLU A 340     170.448 139.142 160.212  1.00 93.51           C  
ATOM     59  OE1 GLU A 340     169.718 139.985 160.774  1.00 93.51           O  
ATOM     60  OE2 GLU A 340     170.045 138.008 159.876  1.00 93.51           O  
ATOM     61  N   VAL A 341     173.824 143.740 160.374  1.00 86.10           N  
ATOM     62  CA  VAL A 341     173.887 145.185 160.170  1.00 86.10           C  
ATOM     63  C   VAL A 341     175.145 145.561 159.399  1.00 86.10           C  
ATOM     64  O   VAL A 341     175.099 146.343 158.444  1.00 86.10           O  
ATOM     65  CB  VAL A 341     173.815 145.922 161.517  1.00 86.10           C  
ATOM     66  CG1 VAL A 341     173.848 147.421 161.293  1.00 86.10           C  
ATOM     67  CG2 VAL A 341     172.565 145.514 162.276  1.00 86.10           C  
ATOM     68  N   PHE A 342     176.291 145.013 159.806  1.00 83.50           N  
ATOM     69  CA  PHE A 342     177.546 145.358 159.147  1.00 83.50           C  
ATOM     70  C   PHE A 342     177.689 144.653 157.803  1.00 83.50           C  
ATOM     71  O   PHE A 342     178.234 145.224 156.852  1.00 83.50           O  
ATOM     72  CB  PHE A 342     178.725 145.019 160.055  1.00 83.50           C  
ATOM     73  CG  PHE A 342     178.885 145.956 161.209  1.00 83.50           C  
ATOM     74  CD1 PHE A 342     177.780 146.423 161.894  1.00 83.50           C  
ATOM     75  CD2 PHE A 342     180.141 146.374 161.609  1.00 83.50           C  
ATOM     76  CE1 PHE A 342     177.925 147.289 162.957  1.00 83.50           C  
ATOM     77  CE2 PHE A 342     180.291 147.239 162.672  1.00 83.50           C  
ATOM     78  CZ  PHE A 342     179.181 147.697 163.347  1.00 83.50           C  
ATOM     79  N   ASN A 343     177.215 143.415 157.705  1.00 90.88           N  
ATOM     80  CA  ASN A 343     177.393 142.611 156.505  1.00 90.88           C  
ATOM     81  C   ASN A 343     176.233 142.734 155.528  1.00 90.88           C  
ATOM     82  O   ASN A 343     176.207 142.015 154.525  1.00 90.88           O  
ATOM     83  CB  ASN A 343     177.609 141.146 156.880  1.00 90.88           C  
ATOM     84  CG  ASN A 343     178.929 140.916 157.580  1.00 90.88           C  
ATOM     85  OD1 ASN A 343     179.637 141.863 157.919  1.00 90.88           O  
ATOM     86  ND2 ASN A 343     179.267 139.651 157.801  1.00 90.88           N  
ATOM     87  N   ALA A 344     175.270 143.613 155.798  1.00 85.76           N  
ATOM     88  CA  ALA A 344     174.201 143.843 154.839  1.00 85.76           C  
ATOM     89  C   ALA A 344     174.781 144.363 153.531  1.00 85.76           C  
ATOM     90  O   ALA A 344     175.532 145.341 153.509  1.00 85.76           O  
ATOM     91  CB  ALA A 344     173.182 144.836 155.397  1.00 85.76           C  
ATOM     92  N   THR A 345     174.431 143.692 152.433  1.00 89.08           N  
ATOM     93  CA  THR A 345     174.994 144.055 151.137  1.00 89.08           C  
ATOM     94  C   THR A 345     174.517 145.431 150.690  1.00 89.08           C  
ATOM     95  O   THR A 345     175.211 146.121 149.934  1.00 89.08           O  
ATOM     96  CB  THR A 345     174.639 142.997 150.092  1.00 89.08           C  
ATOM     97  OG1 THR A 345     175.042 143.450 148.793  1.00 89.08           O  
ATOM     98  CG2 THR A 345     173.142 142.725 150.090  1.00 89.08           C  
ATOM     99  N   ARG A 346     173.339 145.846 151.143  1.00 84.20           N  
ATOM    100  CA  ARG A 346     172.732 147.099 150.722  1.00 84.20           C  
ATOM    101  C   ARG A 346     172.479 147.994 151.926  1.00 84.20           C  
ATOM    102  O   ARG A 346     171.902 147.553 152.925  1.00 84.20           O  
ATOM    103  CB  ARG A 346     171.422 146.839 149.976  1.00 84.20           C  
ATOM    104  CG  ARG A 346     170.585 148.081 149.733  1.00 84.20           C  
ATOM    105  CD  ARG A 346     169.284 147.723 149.042  1.00 84.20           C  
ATOM    106  NE  ARG A 346     168.570 146.670 149.754  1.00 84.20           N  
ATOM    107  CZ  ARG A 346     167.451 146.103 149.325  1.00 84.20           C  
ATOM    108  NH1 ARG A 346     166.883 146.468 148.187  1.00 84.20           N  
ATOM    109  NH2 ARG A 346     166.888 145.144 150.055  1.00 84.20           N  
ATOM    110  N   PHE A 347     172.914 149.247 151.826  1.00 71.29           N  
ATOM    111  CA  PHE A 347     172.554 150.294 152.768  1.00 71.29           C  
ATOM    112  C   PHE A 347     171.791 151.379 152.027  1.00 71.29           C  
ATOM    113  O   PHE A 347     172.211 151.835 150.961  1.00 71.29           O  
ATOM    114  CB  PHE A 347     173.783 150.912 153.439  1.00 71.29           C  
ATOM    115  CG  PHE A 347     174.483 149.997 154.393  1.00 71.29           C  
ATOM    116  CD1 PHE A 347     173.798 148.977 155.023  1.00 71.29           C  
ATOM    117  CD2 PHE A 347     175.829 150.162 154.662  1.00 71.29           C  
ATOM    118  CE1 PHE A 347     174.444 148.137 155.902  1.00 71.29           C  
ATOM    119  CE2 PHE A 347     176.478 149.327 155.539  1.00 71.29           C  
ATOM    120  CZ  PHE A 347     175.787 148.313 156.160  1.00 71.29           C  
ATOM    121  N   ALA A 348     170.667 151.794 152.599  1.00 71.68           N  
ATOM    122  CA  ALA A 348     169.875 152.831 151.962  1.00 71.68           C  
ATOM    123  C   ALA A 348     170.608 154.167 152.024  1.00 71.68           C  
ATOM    124  O   ALA A 348     171.548 154.355 152.800  1.00 71.68           O  
ATOM    125  CB  ALA A 348     168.503 152.940 152.622  1.00 71.68           C  
ATOM    126  N   SER A 349     170.171 155.101 151.185  1.00 70.01           N  
ATOM    127  CA  SER A 349     170.821 156.399 151.127  1.00 70.01           C  
ATOM    128  C   SER A 349     170.610 157.165 152.429  1.00 70.01           C  
ATOM    129  O   SER A 349     169.798 156.793 153.280  1.00 70.01           O  
ATOM    130  CB  SER A 349     170.297 157.213 149.948  1.00 70.01           C  
ATOM    131  OG  SER A 349     171.076 158.380 149.766  1.00 70.01           O  
ATOM    132  N   VAL A 350     171.366 158.252 152.579  1.00 69.43           N  
ATOM    133  CA  VAL A 350     171.395 158.968 153.852  1.00 69.43           C  
ATOM    134  C   VAL A 350     170.055 159.642 154.132  1.00 69.43           C  
ATOM    135  O   VAL A 350     169.614 159.716 155.285  1.00 69.43           O  
ATOM    136  CB  VAL A 350     172.562 159.973 153.871  1.00 69.43           C  
ATOM    137  CG1 VAL A 350     172.464 160.937 152.703  1.00 69.43           C  
ATOM    138  CG2 VAL A 350     172.608 160.715 155.195  1.00 69.43           C  
ATOM    139  N   TYR A 351     169.385 160.140 153.089  1.00 72.80           N  
ATOM    140  CA  TYR A 351     168.119 160.841 153.294  1.00 72.80           C  
ATOM    141  C   TYR A 351     167.069 159.918 153.900  1.00 72.80           C  
ATOM    142  O   TYR A 351     166.274 160.342 154.747  1.00 72.80           O  
ATOM    143  CB  TYR A 351     167.624 161.436 151.975  1.00 72.80           C  
ATOM    144  CG  TYR A 351     166.925 160.447 151.073  1.00 72.80           C  
ATOM    145  CD1 TYR A 351     167.619 159.398 150.492  1.00 72.80           C  
ATOM    146  CD2 TYR A 351     165.572 160.567 150.799  1.00 72.80           C  
ATOM    147  CE1 TYR A 351     166.984 158.489 149.676  1.00 72.80           C  
ATOM    148  CE2 TYR A 351     164.929 159.666 149.977  1.00 72.80           C  
ATOM    149  CZ  TYR A 351     165.641 158.630 149.416  1.00 72.80           C  
ATOM    150  OH  TYR A 351     165.008 157.727 148.596  1.00 72.80           O  
ATOM    151  N   ALA A 352     167.050 158.658 153.481  1.00 76.76           N  
ATOM    152  CA  ALA A 352     166.174 157.638 154.048  1.00 76.76           C  
ATOM    153  C   ALA A 352     167.048 156.536 154.635  1.00 76.76           C  
ATOM    154  O   ALA A 352     167.318 155.524 153.985  1.00 76.76           O  
ATOM    155  CB  ALA A 352     165.213 157.090 152.992  1.00 76.76           C  
ATOM    156  N   TRP A 353     167.476 156.732 155.876  1.00 71.96           N  
ATOM    157  CA  TRP A 353     168.390 155.794 156.511  1.00 71.96           C  
ATOM    158  C   TRP A 353     167.620 154.654 157.162  1.00 71.96           C  
ATOM    159  O   TRP A 353     166.657 154.879 157.901  1.00 71.96           O  
ATOM    160  CB  TRP A 353     169.239 156.527 157.546  1.00 71.96           C  
ATOM    161  CG  TRP A 353     168.473 157.561 158.295  1.00 71.96           C  
ATOM    162  CD1 TRP A 353     168.266 158.853 157.922  1.00 71.96           C  
ATOM    163  CD2 TRP A 353     167.804 157.392 159.547  1.00 71.96           C  
ATOM    164  NE1 TRP A 353     167.509 159.503 158.863  1.00 71.96           N  
ATOM    165  CE2 TRP A 353     167.213 158.627 159.873  1.00 71.96           C  
ATOM    166  CE3 TRP A 353     167.648 156.318 160.426  1.00 71.96           C  
ATOM    167  CZ2 TRP A 353     166.478 158.818 161.039  1.00 71.96           C  
ATOM    168  CZ3 TRP A 353     166.917 156.508 161.582  1.00 71.96           C  
ATOM    169  CH2 TRP A 353     166.342 157.748 161.879  1.00 71.96           C  
ATOM    170  N   ASN A 354     168.043 153.424 156.883  1.00 73.36           N  
ATOM    171  CA  ASN A 354     167.402 152.267 157.489  1.00 73.36           C  
ATOM    172  C   ASN A 354     167.790 152.153 158.957  1.00 73.36           C  
ATOM    173  O   ASN A 354     168.973 152.153 159.306  1.00 73.36           O  
ATOM    174  CB  ASN A 354     167.789 150.993 156.741  1.00 73.36           C  
ATOM    175  CG  ASN A 354     167.126 150.893 155.384  1.00 73.36           C  
ATOM    176  OD1 ASN A 354     166.514 151.849 154.909  1.00 73.36           O  
ATOM    177  ND2 ASN A 354     167.245 149.733 154.751  1.00 73.36           N  
ATOM    178  N   ARG A 355     166.784 152.049 159.818  1.00 73.23           N  
ATOM    179  CA  ARG A 355     166.982 151.950 161.257  1.00 73.23           C  
ATOM    180  C   ARG A 355     166.548 150.569 161.721  1.00 73.23           C  
ATOM    181  O   ARG A 355     165.363 150.231 161.650  1.00 73.23           O  
ATOM    182  CB  ARG A 355     166.196 153.032 162.000  1.00 73.23           C  
ATOM    183  CG  ARG A 355     165.835 152.669 163.429  1.00 73.23           C  
ATOM    184  CD  ARG A 355     165.123 153.816 164.120  1.00 73.23           C  
ATOM    185  NE  ARG A 355     163.834 154.096 163.501  1.00 73.23           N  
ATOM    186  CZ  ARG A 355     162.713 153.440 163.769  1.00 73.23           C  
ATOM    187  NH1 ARG A 355     162.683 152.454 164.650  1.00 73.23           N  
ATOM    188  NH2 ARG A 355     161.593 153.785 163.139  1.00 73.23           N  
ATOM    189  N   LYS A 356     167.504 149.782 162.203  1.00 71.44           N  
ATOM    190  CA  LYS A 356     167.265 148.405 162.613  1.00 71.44           C  
ATOM    191  C   LYS A 356     167.164 148.341 164.129  1.00 71.44           C  
ATOM    192  O   LYS A 356     168.156 148.569 164.830  1.00 71.44           O  
ATOM    193  CB  LYS A 356     168.381 147.490 162.111  1.00 71.44           C  
ATOM    194  CG  LYS A 356     168.385 146.108 162.740  1.00 71.44           C  
ATOM    195  CD  LYS A 356     167.112 145.347 162.417  1.00 71.44           C  
ATOM    196  CE  LYS A 356     167.152 143.939 162.985  1.00 71.44           C  
ATOM    197  NZ  LYS A 356     165.901 143.185 162.700  1.00 71.44           N  
ATOM    198  N   ARG A 357     165.972 148.032 164.632  1.00 76.74           N  
ATOM    199  CA  ARG A 357     165.811 147.797 166.059  1.00 76.74           C  
ATOM    200  C   ARG A 357     166.550 146.524 166.454  1.00 76.74           C  
ATOM    201  O   ARG A 357     166.561 145.540 165.711  1.00 76.74           O  
ATOM    202  CB  ARG A 357     164.330 147.686 166.421  1.00 76.74           C  
ATOM    203  CG  ARG A 357     164.064 147.629 167.918  1.00 76.74           C  
ATOM    204  CD  ARG A 357     162.596 147.363 168.226  1.00 76.74           C  
ATOM    205  NE  ARG A 357     161.722 148.424 167.739  1.00 76.74           N  
ATOM    206  CZ  ARG A 357     160.416 148.482 167.965  1.00 76.74           C  
ATOM    207  NH1 ARG A 357     159.797 147.557 168.681  1.00 76.74           N  
ATOM    208  NH2 ARG A 357     159.714 149.493 167.462  1.00 76.74           N  
ATOM    209  N   ILE A 358     167.177 146.547 167.627  1.00 83.11           N  
ATOM    210  CA  ILE A 358     167.999 145.440 168.103  1.00 83.11           C  
ATOM    211  C   ILE A 358     167.391 144.905 169.389  1.00 83.11           C  
ATOM    212  O   ILE A 358     167.109 145.671 170.319  1.00 83.11           O  
ATOM    213  CB  ILE A 358     169.457 145.868 168.323  1.00 83.11           C  
ATOM    214  CG1 ILE A 358     170.085 146.306 167.001  1.00 83.11           C  
ATOM    215  CG2 ILE A 358     170.255 144.735 168.942  1.00 83.11           C  
ATOM    216  CD1 ILE A 358     170.065 145.235 165.936  1.00 83.11           C  
ATOM    217  N   SER A 359     167.192 143.591 169.441  1.00100.25           N  
ATOM    218  CA  SER A 359     166.657 142.935 170.623  1.00100.25           C  
ATOM    219  C   SER A 359     167.125 141.489 170.633  1.00100.25           C  
ATOM    220  O   SER A 359     167.357 140.885 169.582  1.00100.25           O  
ATOM    221  CB  SER A 359     165.127 143.008 170.662  1.00100.25           C  
ATOM    222  OG  SER A 359     164.563 142.435 169.495  1.00100.25           O  
ATOM    223  N   ASN A 360     167.260 140.940 171.841  1.00109.57           N  
ATOM    224  CA  ASN A 360     167.690 139.556 172.042  1.00109.57           C  
ATOM    225  C   ASN A 360     169.046 139.303 171.386  1.00109.57           C  
ATOM    226  O   ASN A 360     169.185 138.498 170.463  1.00109.57           O  
ATOM    227  CB  ASN A 360     166.634 138.577 171.527  1.00109.57           C  
ATOM    228  CG  ASN A 360     165.301 138.739 172.229  1.00109.57           C  
ATOM    229  OD1 ASN A 360     164.291 139.057 171.601  1.00109.57           O  
ATOM    230  ND2 ASN A 360     165.292 138.524 173.539  1.00109.57           N  
ATOM    231  N   CYS A 361     170.058 140.011 171.881  1.00109.94           N  
ATOM    232  CA  CYS A 361     171.398 139.985 171.318  1.00109.94           C  
ATOM    233  C   CYS A 361     172.423 139.875 172.436  1.00109.94           C  
ATOM    234  O   CYS A 361     172.153 140.231 173.586  1.00109.94           O  
ATOM    235  CB  CYS A 361     171.670 141.246 170.486  1.00109.94           C  
ATOM    236  SG  CYS A 361     173.279 141.286 169.664  1.00109.94           S  
ATOM    237  N   VAL A 362     173.603 139.375 172.089  1.00110.81           N  
ATOM    238  CA  VAL A 362     174.739 139.366 173.002  1.00110.81           C  
ATOM    239  C   VAL A 362     175.751 140.398 172.521  1.00110.81           C  
ATOM    240  O   VAL A 362     176.221 140.341 171.379  1.00110.81           O  
ATOM    241  CB  VAL A 362     175.363 137.962 173.098  1.00110.81           C  
ATOM    242  CG1 VAL A 362     175.533 137.346 171.716  1.00110.81           C  
ATOM    243  CG2 VAL A 362     176.693 138.021 173.831  1.00110.81           C  
ATOM    244  N   ALA A 363     176.083 141.352 173.390  1.00104.73           N  
ATOM    245  CA  ALA A 363     176.905 142.499 173.005  1.00104.73           C  
ATOM    246  C   ALA A 363     178.353 142.048 172.840  1.00104.73           C  
ATOM    247  O   ALA A 363     179.204 142.225 173.714  1.00104.73           O  
ATOM    248  CB  ALA A 363     176.779 143.616 174.032  1.00104.73           C  
ATOM    249  N   ASP A 364     178.633 141.452 171.682  1.00104.40           N  
ATOM    250  CA  ASP A 364     179.981 140.979 171.363  1.00104.40           C  
ATOM    251  C   ASP A 364     180.686 141.999 170.467  1.00104.40           C  
ATOM    252  O   ASP A 364     180.825 141.835 169.254  1.00104.40           O  
ATOM    253  CB  ASP A 364     179.921 139.605 170.710  1.00104.40           C  
ATOM    254  CG  ASP A 364     181.278 138.940 170.636  1.00104.40           C  
ATOM    255  OD1 ASP A 364     181.709 138.359 171.655  1.00104.40           O  
ATOM    256  OD2 ASP A 364     181.917 139.002 169.566  1.00104.40           O  
ATOM    257  N   TYR A 365     181.136 143.079 171.103  1.00 99.47           N  
ATOM    258  CA  TYR A 365     181.844 144.149 170.413  1.00 99.47           C  
ATOM    259  C   TYR A 365     183.347 143.923 170.339  1.00 99.47           C  
ATOM    260  O   TYR A 365     184.053 144.762 169.768  1.00 99.47           O  
ATOM    261  CB  TYR A 365     181.570 145.492 171.098  1.00 99.47           C  
ATOM    262  CG  TYR A 365     180.158 146.003 170.916  1.00 99.47           C  
ATOM    263  CD1 TYR A 365     179.143 145.626 171.785  1.00 99.47           C  
ATOM    264  CD2 TYR A 365     179.841 146.866 169.877  1.00 99.47           C  
ATOM    265  CE1 TYR A 365     177.854 146.093 171.621  1.00 99.47           C  
ATOM    266  CE2 TYR A 365     178.556 147.337 169.706  1.00 99.47           C  
ATOM    267  CZ  TYR A 365     177.567 146.947 170.579  1.00 99.47           C  
ATOM    268  OH  TYR A 365     176.287 147.417 170.408  1.00 99.47           O  
ATOM    269  N   SER A 366     183.853 142.830 170.915  1.00102.51           N  
ATOM    270  CA  SER A 366     185.292 142.585 170.906  1.00102.51           C  
ATOM    271  C   SER A 366     185.816 142.422 169.486  1.00102.51           C  
ATOM    272  O   SER A 366     186.859 142.986 169.131  1.00102.51           O  
ATOM    273  CB  SER A 366     185.616 141.347 171.741  1.00102.51           C  
ATOM    274  OG  SER A 366     185.107 141.469 173.057  1.00102.51           O  
ATOM    275  N   VAL A 367     185.104 141.655 168.659  1.00102.45           N  
ATOM    276  CA  VAL A 367     185.525 141.457 167.275  1.00102.45           C  
ATOM    277  C   VAL A 367     185.493 142.777 166.517  1.00102.45           C  
ATOM    278  O   VAL A 367     186.390 143.075 165.718  1.00102.45           O  
ATOM    279  CB  VAL A 367     184.643 140.393 166.597  1.00102.45           C  
ATOM    280  CG1 VAL A 367     185.159 140.087 165.200  1.00102.45           C  
ATOM    281  CG2 VAL A 367     184.592 139.132 167.446  1.00102.45           C  
ATOM    282  N   LEU A 368     184.459 143.585 166.753  1.00 92.45           N  
ATOM    283  CA  LEU A 368     184.360 144.877 166.082  1.00 92.45           C  
ATOM    284  C   LEU A 368     185.519 145.788 166.463  1.00 92.45           C  
ATOM    285  O   LEU A 368     186.138 146.413 165.595  1.00 92.45           O  
ATOM    286  CB  LEU A 368     183.027 145.538 166.425  1.00 92.45           C  
ATOM    287  CG  LEU A 368     181.790 144.803 165.912  1.00 92.45           C  
ATOM    288  CD1 LEU A 368     181.789 144.758 164.398  1.00 92.45           C  
ATOM    289  CD2 LEU A 368     181.723 143.402 166.500  1.00 92.45           C  
ATOM    290  N   TYR A 369     185.833 145.872 167.758  1.00 96.34           N  
ATOM    291  CA  TYR A 369     186.910 146.756 168.192  1.00 96.34           C  
ATOM    292  C   TYR A 369     188.266 146.263 167.704  1.00 96.34           C  
ATOM    293  O   TYR A 369     189.113 147.067 167.298  1.00 96.34           O  
ATOM    294  CB  TYR A 369     186.910 146.895 169.712  1.00 96.34           C  
ATOM    295  CG  TYR A 369     188.178 147.523 170.237  1.00 96.34           C  
ATOM    296  CD1 TYR A 369     188.476 148.853 169.974  1.00 96.34           C  
ATOM    297  CD2 TYR A 369     189.084 146.783 170.986  1.00 96.34           C  
ATOM    298  CE1 TYR A 369     189.639 149.430 170.446  1.00 96.34           C  
ATOM    299  CE2 TYR A 369     190.249 147.352 171.463  1.00 96.34           C  
ATOM    300  CZ  TYR A 369     190.521 148.676 171.190  1.00 96.34           C  
ATOM    301  OH  TYR A 369     191.680 149.247 171.663  1.00 96.34           O  
ATOM    302  N   ASN A 370     188.492 144.950 167.731  1.00 99.50           N  
ATOM    303  CA  ASN A 370     189.745 144.404 167.228  1.00 99.50           C  
ATOM    304  C   ASN A 370     189.817 144.397 165.709  1.00 99.50           C  
ATOM    305  O   ASN A 370     190.876 144.076 165.156  1.00 99.50           O  
ATOM    306  CB  ASN A 370     189.955 142.985 167.758  1.00 99.50           C  
ATOM    307  CG  ASN A 370     190.264 142.960 169.237  1.00 99.50           C  
ATOM    308  OD1 ASN A 370     189.920 143.887 169.969  1.00 99.50           O  
ATOM    309  ND2 ASN A 370     190.925 141.900 169.687  1.00 99.50           N  
ATOM    310  N   SER A 371     188.728 144.737 165.026  1.00 94.76           N  
ATOM    311  CA  SER A 371     188.736 144.757 163.572  1.00 94.76           C  
ATOM    312  C   SER A 371     189.581 145.916 163.061  1.00 94.76           C  
ATOM    313  O   SER A 371     189.453 147.050 163.530  1.00 94.76           O  
ATOM    314  CB  SER A 371     187.308 144.871 163.044  1.00 94.76           C  
ATOM    315  OG  SER A 371     186.469 143.900 163.642  1.00 94.76           O  
ATOM    316  N   ALA A 372     190.450 145.624 162.095  1.00 87.49           N  
ATOM    317  CA  ALA A 372     191.269 146.642 161.453  1.00 87.49           C  
ATOM    318  C   ALA A 372     190.616 147.226 160.209  1.00 87.49           C  
ATOM    319  O   ALA A 372     191.230 148.067 159.543  1.00 87.49           O  
ATOM    320  CB  ALA A 372     192.641 146.067 161.085  1.00 87.49           C  
ATOM    321  N   SER A 373     189.399 146.794 159.876  1.00 81.54           N  
ATOM    322  CA  SER A 373     188.725 147.315 158.693  1.00 81.54           C  
ATOM    323  C   SER A 373     188.090 148.673 158.965  1.00 81.54           C  
ATOM    324  O   SER A 373     187.891 149.469 158.041  1.00 81.54           O  
ATOM    325  CB  SER A 373     187.672 146.317 158.214  1.00 81.54           C  
ATOM    326  OG  SER A 373     188.234 145.028 158.049  1.00 81.54           O  
ATOM    327  N   PHE A 374     187.767 148.956 160.224  1.00 74.15           N  
ATOM    328  CA  PHE A 374     187.038 150.171 160.586  1.00 74.15           C  
ATOM    329  C   PHE A 374     188.016 151.336 160.654  1.00 74.15           C  
ATOM    330  O   PHE A 374     188.840 151.421 161.566  1.00 74.15           O  
ATOM    331  CB  PHE A 374     186.309 149.982 161.910  1.00 74.15           C  
ATOM    332  CG  PHE A 374     185.399 148.789 161.933  1.00 74.15           C  
ATOM    333  CD1 PHE A 374     184.766 148.363 160.779  1.00 74.15           C  
ATOM    334  CD2 PHE A 374     185.186 148.088 163.106  1.00 74.15           C  
ATOM    335  CE1 PHE A 374     183.933 147.265 160.796  1.00 74.15           C  
ATOM    336  CE2 PHE A 374     184.352 146.988 163.129  1.00 74.15           C  
ATOM    337  CZ  PHE A 374     183.725 146.576 161.972  1.00 74.15           C  
ATOM    338  N   SER A 375     187.921 152.245 159.681  1.00 67.99           N  
ATOM    339  CA  SER A 375     188.815 153.398 159.652  1.00 67.99           C  
ATOM    340  C   SER A 375     188.527 154.356 160.801  1.00 67.99           C  
ATOM    341  O   SER A 375     189.446 154.787 161.506  1.00 67.99           O  
ATOM    342  CB  SER A 375     188.694 154.118 158.310  1.00 67.99           C  
ATOM    343  OG  SER A 375     189.514 155.271 158.275  1.00 67.99           O  
ATOM    344  N   THR A 376     187.261 154.700 161.006  1.00 58.14           N  
ATOM    345  CA  THR A 376     186.854 155.608 162.067  1.00 58.14           C  
ATOM    346  C   THR A 376     185.934 154.868 163.024  1.00 58.14           C  
ATOM    347  O   THR A 376     184.992 154.199 162.588  1.00 58.14           O  
ATOM    348  CB  THR A 376     186.152 156.840 161.496  1.00 58.14           C  
ATOM    349  OG1 THR A 376     187.024 157.497 160.569  1.00 58.14           O  
ATOM    350  CG2 THR A 376     185.783 157.806 162.609  1.00 58.14           C  
ATOM    351  N   PHE A 377     186.214 154.977 164.321  1.00 65.41           N  
ATOM    352  CA  PHE A 377     185.467 154.262 165.352  1.00 65.41           C  
ATOM    353  C   PHE A 377     185.229 155.189 166.546  1.00 65.41           C  
ATOM    354  O   PHE A 377     185.222 154.768 167.702  1.00 65.41           O  
ATOM    355  CB  PHE A 377     186.221 152.999 165.764  1.00 65.41           C  
ATOM    356  CG  PHE A 377     185.335 151.878 166.225  1.00 65.41           C  
ATOM    357  CD1 PHE A 377     185.109 150.784 165.408  1.00 65.41           C  
ATOM    358  CD2 PHE A 377     184.723 151.918 167.464  1.00 65.41           C  
ATOM    359  CE1 PHE A 377     184.298 149.748 165.821  1.00 65.41           C  
ATOM    360  CE2 PHE A 377     183.909 150.883 167.883  1.00 65.41           C  
ATOM    361  CZ  PHE A 377     183.697 149.797 167.060  1.00 65.41           C  
ATOM    362  N   LYS A 378     185.022 156.471 166.259  1.00 61.72           N  
ATOM    363  CA  LYS A 378     184.946 157.494 167.295  1.00 61.72           C  
ATOM    364  C   LYS A 378     183.605 157.410 168.014  1.00 61.72           C  
ATOM    365  O   LYS A 378     182.584 157.860 167.485  1.00 61.72           O  
ATOM    366  CB  LYS A 378     185.146 158.884 166.693  1.00 61.72           C  
ATOM    367  CG  LYS A 378     186.555 159.143 166.191  1.00 61.72           C  
ATOM    368  CD  LYS A 378     187.559 159.116 167.332  1.00 61.72           C  
ATOM    369  CE  LYS A 378     188.982 159.226 166.816  1.00 61.72           C  
ATOM    370  NZ  LYS A 378     189.336 158.078 165.939  1.00 61.72           N  
ATOM    371  N   CYS A 379     183.613 156.855 169.222  1.00 67.60           N  
ATOM    372  CA  CYS A 379     182.413 156.728 170.037  1.00 67.60           C  
ATOM    373  C   CYS A 379     182.204 158.015 170.822  1.00 67.60           C  
ATOM    374  O   CYS A 379     183.166 158.595 171.335  1.00 67.60           O  
ATOM    375  CB  CYS A 379     182.517 155.542 170.993  1.00 67.60           C  
ATOM    376  SG  CYS A 379     182.899 153.952 170.232  1.00 67.60           S  
ATOM    377  N   TYR A 380     180.954 158.458 170.915  1.00 70.82           N  
ATOM    378  CA  TYR A 380     180.598 159.645 171.681  1.00 70.82           C  
ATOM    379  C   TYR A 380     179.718 159.237 172.854  1.00 70.82           C  
ATOM    380  O   TYR A 380     178.666 158.620 172.661  1.00 70.82           O  
ATOM    381  CB  TYR A 380     179.884 160.667 170.800  1.00 70.82           C  
ATOM    382  CG  TYR A 380     180.721 161.144 169.640  1.00 70.82           C  
ATOM    383  CD1 TYR A 380     181.535 162.260 169.761  1.00 70.82           C  
ATOM    384  CD2 TYR A 380     180.705 160.474 168.427  1.00 70.82           C  
ATOM    385  CE1 TYR A 380     182.305 162.697 168.705  1.00 70.82           C  
ATOM    386  CE2 TYR A 380     181.470 160.904 167.368  1.00 70.82           C  
ATOM    387  CZ  TYR A 380     182.268 162.014 167.510  1.00 70.82           C  
ATOM    388  OH  TYR A 380     183.032 162.442 166.450  1.00 70.82           O  
ATOM    389  N   GLY A 381     180.143 159.591 174.064  1.00 81.64           N  
ATOM    390  CA  GLY A 381     179.416 159.240 175.264  1.00 81.64           C  
ATOM    391  C   GLY A 381     179.779 157.903 175.873  1.00 81.64           C  
ATOM    392  O   GLY A 381     179.249 157.564 176.939  1.00 81.64           O  
ATOM    393  N   VAL A 382     180.658 157.130 175.233  1.00 78.43           N  
ATOM    394  CA  VAL A 382     181.075 155.830 175.742  1.00 78.43           C  
ATOM    395  C   VAL A 382     182.468 155.528 175.206  1.00 78.43           C  
ATOM    396  O   VAL A 382     182.841 155.954 174.111  1.00 78.43           O  
ATOM    397  CB  VAL A 382     180.071 154.716 175.353  1.00 78.43           C  
ATOM    398  CG1 VAL A 382     180.077 154.488 173.852  1.00 78.43           C  
ATOM    399  CG2 VAL A 382     180.371 153.428 176.102  1.00 78.43           C  
ATOM    400  N   SER A 383     183.250 154.800 175.999  1.00 83.32           N  
ATOM    401  CA  SER A 383     184.590 154.439 175.559  1.00 83.32           C  
ATOM    402  C   SER A 383     184.546 153.200 174.675  1.00 83.32           C  
ATOM    403  O   SER A 383     183.754 152.288 174.929  1.00 83.32           O  
ATOM    404  CB  SER A 383     185.500 154.176 176.758  1.00 83.32           C  
ATOM    405  OG  SER A 383     186.807 153.826 176.340  1.00 83.32           O  
ATOM    406  N   PRO A 384     185.380 153.148 173.632  1.00 85.63           N  
ATOM    407  CA  PRO A 384     185.322 152.000 172.709  1.00 85.63           C  
ATOM    408  C   PRO A 384     185.575 150.659 173.375  1.00 85.63           C  
ATOM    409  O   PRO A 384     184.977 149.653 172.976  1.00 85.63           O  
ATOM    410  CB  PRO A 384     186.408 152.331 171.676  1.00 85.63           C  
ATOM    411  CG  PRO A 384     186.563 153.810 171.746  1.00 85.63           C  
ATOM    412  CD  PRO A 384     186.335 154.173 173.182  1.00 85.63           C  
ATOM    413  N   THR A 385     186.450 150.613 174.380  1.00 89.38           N  
ATOM    414  CA  THR A 385     186.778 149.336 175.007  1.00 89.38           C  
ATOM    415  C   THR A 385     185.657 148.859 175.925  1.00 89.38           C  
ATOM    416  O   THR A 385     185.512 147.653 176.157  1.00 89.38           O  
ATOM    417  CB  THR A 385     188.092 149.450 175.778  1.00 89.38           C  
ATOM    418  OG1 THR A 385     188.345 148.225 176.477  1.00 89.38           O  
ATOM    419  CG2 THR A 385     188.031 150.599 176.775  1.00 89.38           C  
ATOM    420  N   LYS A 386     184.858 149.784 176.458  1.00 92.87           N  
ATOM    421  CA  LYS A 386     183.779 149.418 177.368  1.00 92.87           C  
ATOM    422  C   LYS A 386     182.599 148.764 176.662  1.00 92.87           C  
ATOM    423  O   LYS A 386     181.695 148.265 177.342  1.00 92.87           O  
ATOM    424  CB  LYS A 386     183.300 150.654 178.135  1.00 92.87           C  
ATOM    425  CG  LYS A 386     184.310 151.206 179.132  1.00 92.87           C  
ATOM    426  CD  LYS A 386     183.901 152.584 179.633  1.00 92.87           C  
ATOM    427  CE  LYS A 386     182.511 152.569 180.244  1.00 92.87           C  
ATOM    428  NZ  LYS A 386     182.437 151.670 181.426  1.00 92.87           N  
ATOM    429  N   LEU A 387     182.581 148.758 175.327  1.00 95.18           N  
ATOM    430  CA  LEU A 387     181.444 148.204 174.597  1.00 95.18           C  
ATOM    431  C   LEU A 387     181.307 146.703 174.821  1.00 95.18           C  
ATOM    432  O   LEU A 387     180.201 146.156 174.743  1.00 95.18           O  
ATOM    433  CB  LEU A 387     181.582 148.505 173.105  1.00 95.18           C  
ATOM    434  CG  LEU A 387     180.877 149.748 172.559  1.00 95.18           C  
ATOM    435  CD1 LEU A 387     181.253 150.983 173.354  1.00 95.18           C  
ATOM    436  CD2 LEU A 387     181.207 149.941 171.088  1.00 95.18           C  
ATOM    437  N   ASN A 388     182.421 146.017 175.085  1.00103.20           N  
ATOM    438  CA  ASN A 388     182.380 144.563 175.210  1.00103.20           C  
ATOM    439  C   ASN A 388     181.549 144.124 176.409  1.00103.20           C  
ATOM    440  O   ASN A 388     180.755 143.183 176.309  1.00103.20           O  
ATOM    441  CB  ASN A 388     183.799 144.003 175.309  1.00103.20           C  
ATOM    442  CG  ASN A 388     184.641 144.332 174.093  1.00103.20           C  
ATOM    443  OD1 ASN A 388     184.123 144.772 173.068  1.00103.20           O  
ATOM    444  ND2 ASN A 388     185.946 144.111 174.198  1.00103.20           N  
ATOM    445  N   ASP A 389     181.713 144.789 177.549  1.00107.39           N  
ATOM    446  CA  ASP A 389     181.044 144.404 178.791  1.00107.39           C  
ATOM    447  C   ASP A 389     180.198 145.584 179.262  1.00107.39           C  
ATOM    448  O   ASP A 389     180.662 146.426 180.034  1.00107.39           O  
ATOM    449  CB  ASP A 389     182.062 143.976 179.853  1.00107.39           C  
ATOM    450  CG  ASP A 389     181.498 142.960 180.830  1.00107.39           C  
ATOM    451  OD1 ASP A 389     181.380 141.774 180.457  1.00107.39           O  
ATOM    452  OD2 ASP A 389     181.175 143.345 181.972  1.00107.39           O  
ATOM    453  N   LEU A 390     178.953 145.636 178.795  1.00105.83           N  
ATOM    454  CA  LEU A 390     178.033 146.702 179.167  1.00105.83           C  
ATOM    455  C   LEU A 390     176.623 146.279 178.784  1.00105.83           C  
ATOM    456  O   LEU A 390     176.416 145.571 177.795  1.00105.83           O  
ATOM    457  CB  LEU A 390     178.411 148.024 178.492  1.00105.83           C  
ATOM    458  CG  LEU A 390     177.767 149.294 179.046  1.00105.83           C  
ATOM    459  CD1 LEU A 390     178.072 149.438 180.527  1.00105.83           C  
ATOM    460  CD2 LEU A 390     178.252 150.509 178.274  1.00105.83           C  
ATOM    461  N   CYS A 391     175.652 146.726 179.578  1.00104.94           N  
ATOM    462  CA  CYS A 391     174.246 146.397 179.371  1.00104.94           C  
ATOM    463  C   CYS A 391     173.554 147.563 178.680  1.00104.94           C  
ATOM    464  O   CYS A 391     173.551 148.684 179.200  1.00104.94           O  
ATOM    465  CB  CYS A 391     173.555 146.074 180.695  1.00104.94           C  
ATOM    466  SG  CYS A 391     173.676 144.347 181.218  1.00104.94           S  
ATOM    467  N   PHE A 392     172.958 147.293 177.520  1.00103.42           N  
ATOM    468  CA  PHE A 392     172.328 148.309 176.685  1.00103.42           C  
ATOM    469  C   PHE A 392     170.815 148.157 176.762  1.00103.42           C  
ATOM    470  O   PHE A 392     170.285 147.068 176.520  1.00103.42           O  
ATOM    471  CB  PHE A 392     172.800 148.192 175.235  1.00103.42           C  
ATOM    472  CG  PHE A 392     174.281 148.360 175.062  1.00103.42           C  
ATOM    473  CD1 PHE A 392     175.068 147.304 174.637  1.00103.42           C  
ATOM    474  CD2 PHE A 392     174.885 149.577 175.317  1.00103.42           C  
ATOM    475  CE1 PHE A 392     176.428 147.456 174.477  1.00103.42           C  
ATOM    476  CE2 PHE A 392     176.244 149.735 175.158  1.00103.42           C  
ATOM    477  CZ  PHE A 392     177.018 148.673 174.737  1.00103.42           C  
ATOM    478  N   THR A 393     170.125 149.255 177.084  1.00107.25           N  
ATOM    479  CA  THR A 393     168.668 149.219 177.177  1.00107.25           C  
ATOM    480  C   THR A 393     168.031 148.875 175.836  1.00107.25           C  
ATOM    481  O   THR A 393     167.215 147.951 175.749  1.00107.25           O  
ATOM    482  CB  THR A 393     168.144 150.563 177.682  1.00107.25           C  
ATOM    483  OG1 THR A 393     168.753 150.877 178.941  1.00107.25           O  
ATOM    484  CG2 THR A 393     166.631 150.525 177.843  1.00107.25           C  
ATOM    485  N   ASN A 394     168.394 149.603 174.783  1.00 96.84           N  
ATOM    486  CA  ASN A 394     167.893 149.350 173.441  1.00 96.84           C  
ATOM    487  C   ASN A 394     168.878 149.931 172.440  1.00 96.84           C  
ATOM    488  O   ASN A 394     169.444 151.002 172.669  1.00 96.84           O  
ATOM    489  CB  ASN A 394     166.502 149.960 173.233  1.00 96.84           C  
ATOM    490  CG  ASN A 394     165.780 149.371 172.036  1.00 96.84           C  
ATOM    491  OD1 ASN A 394     166.405 148.856 171.109  1.00 96.84           O  
ATOM    492  ND2 ASN A 394     164.454 149.443 172.053  1.00 96.84           N  
ATOM    493  N   VAL A 395     169.077 149.225 171.332  1.00 83.51           N  
ATOM    494  CA  VAL A 395     170.069 149.591 170.329  1.00 83.51           C  
ATOM    495  C   VAL A 395     169.363 149.822 169.003  1.00 83.51           C  
ATOM    496  O   VAL A 395     168.570 148.983 168.559  1.00 83.51           O  
ATOM    497  CB  VAL A 395     171.152 148.509 170.188  1.00 83.51           C  
ATOM    498  CG1 VAL A 395     172.264 148.993 169.278  1.00 83.51           C  
ATOM    499  CG2 VAL A 395     171.695 148.118 171.551  1.00 83.51           C  
ATOM    500  N   TYR A 396     169.651 150.958 168.373  1.00 75.65           N  
ATOM    501  CA  TYR A 396     169.172 151.267 167.033  1.00 75.65           C  
ATOM    502  C   TYR A 396     170.379 151.418 166.122  1.00 75.65           C  
ATOM    503  O   TYR A 396     171.250 152.255 166.377  1.00 75.65           O  
ATOM    504  CB  TYR A 396     168.330 152.544 167.023  1.00 75.65           C  
ATOM    505  CG  TYR A 396     167.012 152.423 167.748  1.00 75.65           C  
ATOM    506  CD1 TYR A 396     166.402 151.189 167.919  1.00 75.65           C  
ATOM    507  CD2 TYR A 396     166.375 153.545 168.260  1.00 75.65           C  
ATOM    508  CE1 TYR A 396     165.195 151.075 168.581  1.00 75.65           C  
ATOM    509  CE2 TYR A 396     165.170 153.441 168.923  1.00 75.65           C  
ATOM    510  CZ  TYR A 396     164.585 152.205 169.080  1.00 75.65           C  
ATOM    511  OH  TYR A 396     163.383 152.096 169.740  1.00 75.65           O  
ATOM    512  N   ALA A 397     170.428 150.617 165.063  1.00 67.31           N  
ATOM    513  CA  ALA A 397     171.550 150.615 164.133  1.00 67.31           C  
ATOM    514  C   ALA A 397     171.112 151.286 162.838  1.00 67.31           C  
ATOM    515  O   ALA A 397     170.522 150.642 161.966  1.00 67.31           O  
ATOM    516  CB  ALA A 397     172.036 149.192 163.875  1.00 67.31           C  
ATOM    517  N   ASP A 398     171.411 152.575 162.709  1.00 64.61           N  
ATOM    518  CA  ASP A 398     171.046 153.352 161.533  1.00 64.61           C  
ATOM    519  C   ASP A 398     172.253 153.423 160.609  1.00 64.61           C  
ATOM    520  O   ASP A 398     173.300 153.950 160.994  1.00 64.61           O  
ATOM    521  CB  ASP A 398     170.587 154.753 161.927  1.00 64.61           C  
ATOM    522  CG  ASP A 398     169.705 154.751 163.159  1.00 64.61           C  
ATOM    523  OD1 ASP A 398     169.217 153.668 163.542  1.00 64.61           O  
ATOM    524  OD2 ASP A 398     169.503 155.832 163.750  1.00 64.61           O  
ATOM    525  N   SER A 399     172.106 152.900 159.397  1.00 60.69           N  
ATOM    526  CA  SER A 399     173.213 152.776 158.460  1.00 60.69           C  
ATOM    527  C   SER A 399     172.910 153.541 157.180  1.00 60.69           C  
ATOM    528  O   SER A 399     171.762 153.573 156.728  1.00 60.69           O  
ATOM    529  CB  SER A 399     173.492 151.309 158.139  1.00 60.69           C  
ATOM    530  OG  SER A 399     174.566 151.191 157.227  1.00 60.69           O  
ATOM    531  N   PHE A 400     173.942 154.148 156.600  1.00 57.21           N  
ATOM    532  CA  PHE A 400     173.814 154.880 155.350  1.00 57.21           C  
ATOM    533  C   PHE A 400     175.181 154.995 154.691  1.00 57.21           C  
ATOM    534  O   PHE A 400     176.170 154.434 155.166  1.00 57.21           O  
ATOM    535  CB  PHE A 400     173.199 156.267 155.568  1.00 57.21           C  
ATOM    536  CG  PHE A 400     173.698 156.967 156.794  1.00 57.21           C  
ATOM    537  CD1 PHE A 400     173.019 156.858 157.993  1.00 57.21           C  
ATOM    538  CD2 PHE A 400     174.837 157.744 156.745  1.00 57.21           C  
ATOM    539  CE1 PHE A 400     173.472 157.504 159.120  1.00 57.21           C  
ATOM    540  CE2 PHE A 400     175.293 158.392 157.869  1.00 57.21           C  
ATOM    541  CZ  PHE A 400     174.610 158.272 159.058  1.00 57.21           C  
ATOM    542  N   VAL A 401     175.226 155.723 153.578  1.00 58.32           N  
ATOM    543  CA  VAL A 401     176.437 155.884 152.780  1.00 58.32           C  
ATOM    544  C   VAL A 401     176.753 157.369 152.662  1.00 58.32           C  
ATOM    545  O   VAL A 401     175.846 158.191 152.486  1.00 58.32           O  
ATOM    546  CB  VAL A 401     176.285 155.247 151.389  1.00 58.32           C  
ATOM    547  CG1 VAL A 401     177.616 155.261 150.658  1.00 58.32           C  
ATOM    548  CG2 VAL A 401     175.752 153.834 151.508  1.00 58.32           C  
ATOM    549  N   ILE A 402     178.037 157.710 152.765  1.00 66.76           N  
ATOM    550  CA  ILE A 402     178.511 159.082 152.655  1.00 66.76           C  
ATOM    551  C   ILE A 402     179.712 159.112 151.713  1.00 66.76           C  
ATOM    552  O   ILE A 402     180.396 158.108 151.502  1.00 66.76           O  
ATOM    553  CB  ILE A 402     178.874 159.676 154.034  1.00 66.76           C  
ATOM    554  CG1 ILE A 402     177.712 159.502 155.004  1.00 66.76           C  
ATOM    555  CG2 ILE A 402     179.213 161.156 153.938  1.00 66.76           C  
ATOM    556  CD1 ILE A 402     177.902 160.238 156.283  1.00 66.76           C  
ATOM    557  N   ARG A 403     179.957 160.288 151.140  1.00 76.61           N  
ATOM    558  CA  ARG A 403     181.077 160.493 150.236  1.00 76.61           C  
ATOM    559  C   ARG A 403     182.403 160.406 150.990  1.00 76.61           C  
ATOM    560  O   ARG A 403     182.461 160.534 152.217  1.00 76.61           O  
ATOM    561  CB  ARG A 403     180.946 161.849 149.544  1.00 76.61           C  
ATOM    562  CG  ARG A 403     181.648 161.954 148.206  1.00 76.61           C  
ATOM    563  CD  ARG A 403     181.334 163.285 147.554  1.00 76.61           C  
ATOM    564  NE  ARG A 403     181.663 164.402 148.430  1.00 76.61           N  
ATOM    565  CZ  ARG A 403     181.426 165.673 148.142  1.00 76.61           C  
ATOM    566  NH1 ARG A 403     180.849 166.029 147.006  1.00 76.61           N  
ATOM    567  NH2 ARG A 403     181.778 166.612 149.015  1.00 76.61           N  
ATOM    568  N   GLY A 404     183.480 160.175 150.233  1.00 78.39           N  
ATOM    569  CA  GLY A 404     184.789 160.015 150.849  1.00 78.39           C  
ATOM    570  C   GLY A 404     185.229 161.233 151.634  1.00 78.39           C  
ATOM    571  O   GLY A 404     185.662 161.119 152.783  1.00 78.39           O  
ATOM    572  N   ASP A 405     185.125 162.411 151.033  1.00 79.24           N  
ATOM    573  CA  ASP A 405     185.394 163.632 151.773  1.00 79.24           C  
ATOM    574  C   ASP A 405     184.256 163.913 152.747  1.00 79.24           C  
ATOM    575  O   ASP A 405     183.094 163.585 152.492  1.00 79.24           O  
ATOM    576  CB  ASP A 405     185.581 164.811 150.818  1.00 79.24           C  
ATOM    577  CG  ASP A 405     184.401 165.004 149.892  1.00 79.24           C  
ATOM    578  OD1 ASP A 405     183.666 164.024 149.657  1.00 79.24           O  
ATOM    579  OD2 ASP A 405     184.209 166.134 149.397  1.00 79.24           O  
ATOM    580  N   GLU A 406     184.609 164.514 153.882  1.00 81.52           N  
ATOM    581  CA  GLU A 406     183.634 164.928 154.889  1.00 81.52           C  
ATOM    582  C   GLU A 406     182.792 163.752 155.378  1.00 81.52           C  
ATOM    583  O   GLU A 406     181.566 163.837 155.469  1.00 81.52           O  
ATOM    584  CB  GLU A 406     182.742 166.051 154.357  1.00 81.52           C  
ATOM    585  CG  GLU A 406     183.510 167.281 153.908  1.00 81.52           C  
ATOM    586  CD  GLU A 406     182.609 168.349 153.324  1.00 81.52           C  
ATOM    587  OE1 GLU A 406     181.381 168.130 153.270  1.00 81.52           O  
ATOM    588  OE2 GLU A 406     183.130 169.409 152.918  1.00 81.52           O  
ATOM    589  N   VAL A 407     183.456 162.635 155.684  1.00 74.94           N  
ATOM    590  CA  VAL A 407     182.774 161.539 156.359  1.00 74.94           C  
ATOM    591  C   VAL A 407     182.384 161.932 157.778  1.00 74.94           C  
ATOM    592  O   VAL A 407     181.377 161.443 158.302  1.00 74.94           O  
ATOM    593  CB  VAL A 407     183.652 160.272 156.353  1.00 74.94           C  
ATOM    594  CG1 VAL A 407     184.968 160.525 157.070  1.00 74.94           C  
ATOM    595  CG2 VAL A 407     182.913 159.096 156.977  1.00 74.94           C  
ATOM    596  N   ARG A 408     183.144 162.827 158.407  1.00 75.78           N  
ATOM    597  CA  ARG A 408     182.912 163.228 159.788  1.00 75.78           C  
ATOM    598  C   ARG A 408     181.739 164.183 159.948  1.00 75.78           C  
ATOM    599  O   ARG A 408     181.585 164.766 161.027  1.00 75.78           O  
ATOM    600  CB  ARG A 408     184.178 163.865 160.366  1.00 75.78           C  
ATOM    601  CG  ARG A 408     184.582 165.168 159.701  1.00 75.78           C  
ATOM    602  CD  ARG A 408     185.868 165.718 160.288  1.00 75.78           C  
ATOM    603  NE  ARG A 408     186.246 166.981 159.667  1.00 75.78           N  
ATOM    604  CZ  ARG A 408     185.831 168.169 160.083  1.00 75.78           C  
ATOM    605  NH1 ARG A 408     185.029 168.295 161.126  1.00 75.78           N  
ATOM    606  NH2 ARG A 408     186.232 169.259 159.435  1.00 75.78           N  
ATOM    607  N   GLN A 409     180.920 164.369 158.911  1.00 77.18           N  
ATOM    608  CA  GLN A 409     179.746 165.225 159.042  1.00 77.18           C  
ATOM    609  C   GLN A 409     178.787 164.696 160.103  1.00 77.18           C  
ATOM    610  O   GLN A 409     178.042 165.468 160.718  1.00 77.18           O  
ATOM    611  CB  GLN A 409     179.036 165.348 157.693  1.00 77.18           C  
ATOM    612  CG  GLN A 409     179.830 166.073 156.620  1.00 77.18           C  
ATOM    613  CD  GLN A 409     180.177 167.498 157.010  1.00 77.18           C  
ATOM    614  OE1 GLN A 409     181.285 167.969 156.759  1.00 77.18           O  
ATOM    615  NE2 GLN A 409     179.228 168.192 157.628  1.00 77.18           N  
ATOM    616  N   ILE A 410     178.799 163.381 160.335  1.00 67.15           N  
ATOM    617  CA  ILE A 410     177.858 162.764 161.266  1.00 67.15           C  
ATOM    618  C   ILE A 410     178.116 163.213 162.696  1.00 67.15           C  
ATOM    619  O   ILE A 410     177.198 163.223 163.525  1.00 67.15           O  
ATOM    620  CB  ILE A 410     177.927 161.232 161.135  1.00 67.15           C  
ATOM    621  CG1 ILE A 410     177.592 160.830 159.706  1.00 67.15           C  
ATOM    622  CG2 ILE A 410     176.963 160.559 162.091  1.00 67.15           C  
ATOM    623  CD1 ILE A 410     176.308 161.449 159.209  1.00 67.15           C  
ATOM    624  N   ALA A 411     179.348 163.599 163.006  1.00 70.83           N  
ATOM    625  CA  ALA A 411     179.693 163.954 164.373  1.00 70.83           C  
ATOM    626  C   ALA A 411     178.780 165.072 164.870  1.00 70.83           C  
ATOM    627  O   ALA A 411     178.514 166.028 164.132  1.00 70.83           O  
ATOM    628  CB  ALA A 411     181.158 164.390 164.457  1.00 70.83           C  
ATOM    629  N   PRO A 412     178.262 164.972 166.091  1.00 71.45           N  
ATOM    630  CA  PRO A 412     177.322 165.986 166.580  1.00 71.45           C  
ATOM    631  C   PRO A 412     177.960 167.365 166.611  1.00 71.45           C  
ATOM    632  O   PRO A 412     179.151 167.514 166.887  1.00 71.45           O  
ATOM    633  CB  PRO A 412     176.973 165.494 167.989  1.00 71.45           C  
ATOM    634  CG  PRO A 412     177.275 164.034 167.967  1.00 71.45           C  
ATOM    635  CD  PRO A 412     178.453 163.881 167.058  1.00 71.45           C  
ATOM    636  N   GLY A 413     177.150 168.378 166.310  1.00 81.81           N  
ATOM    637  CA  GLY A 413     177.621 169.741 166.238  1.00 81.81           C  
ATOM    638  C   GLY A 413     178.292 170.108 164.934  1.00 81.81           C  
ATOM    639  O   GLY A 413     178.678 171.270 164.760  1.00 81.81           O  
ATOM    640  N   GLN A 414     178.441 169.161 164.014  1.00 82.78           N  
ATOM    641  CA  GLN A 414     179.044 169.413 162.715  1.00 82.78           C  
ATOM    642  C   GLN A 414     177.940 169.779 161.733  1.00 82.78           C  
ATOM    643  O   GLN A 414     177.002 169.000 161.531  1.00 82.78           O  
ATOM    644  CB  GLN A 414     179.822 168.193 162.225  1.00 82.78           C  
ATOM    645  CG  GLN A 414     180.594 168.435 160.949  1.00 82.78           C  
ATOM    646  CD  GLN A 414     181.649 169.507 161.111  1.00 82.78           C  
ATOM    647  OE1 GLN A 414     182.207 169.687 162.194  1.00 82.78           O  
ATOM    648  NE2 GLN A 414     181.925 170.234 160.035  1.00 82.78           N  
ATOM    649  N   THR A 415     178.052 170.957 161.129  1.00 83.16           N  
ATOM    650  CA  THR A 415     177.031 171.485 160.237  1.00 83.16           C  
ATOM    651  C   THR A 415     177.503 171.388 158.793  1.00 83.16           C  
ATOM    652  O   THR A 415     178.620 171.803 158.467  1.00 83.16           O  
ATOM    653  CB  THR A 415     176.691 172.934 160.592  1.00 83.16           C  
ATOM    654  OG1 THR A 415     177.871 173.741 160.498  1.00 83.16           O  
ATOM    655  CG2 THR A 415     176.117 173.026 161.999  1.00 83.16           C  
ATOM    656  N   GLY A 416     176.651 170.830 157.939  1.00 77.83           N  
ATOM    657  CA  GLY A 416     176.928 170.706 156.523  1.00 77.83           C  
ATOM    658  C   GLY A 416     175.640 170.367 155.808  1.00 77.83           C  
ATOM    659  O   GLY A 416     174.583 170.228 156.425  1.00 77.83           O  
ATOM    660  N   LYS A 417     175.737 170.234 154.484  1.00 76.78           N  
ATOM    661  CA  LYS A 417     174.550 169.918 153.697  1.00 76.78           C  
ATOM    662  C   LYS A 417     173.960 168.575 154.112  1.00 76.78           C  
ATOM    663  O   LYS A 417     172.773 168.482 154.447  1.00 76.78           O  
ATOM    664  CB  LYS A 417     174.886 169.927 152.205  1.00 76.78           C  
ATOM    665  CG  LYS A 417     176.191 169.237 151.848  1.00 76.78           C  
ATOM    666  CD  LYS A 417     176.386 169.171 150.344  1.00 76.78           C  
ATOM    667  CE  LYS A 417     177.770 168.650 149.992  1.00 76.78           C  
ATOM    668  NZ  LYS A 417     178.039 167.319 150.602  1.00 76.78           N  
ATOM    669  N   ILE A 418     174.787 167.529 154.132  1.00 73.74           N  
ATOM    670  CA  ILE A 418     174.300 166.201 154.490  1.00 73.74           C  
ATOM    671  C   ILE A 418     173.910 166.159 155.963  1.00 73.74           C  
ATOM    672  O   ILE A 418     172.923 165.519 156.343  1.00 73.74           O  
ATOM    673  CB  ILE A 418     175.352 165.132 154.139  1.00 73.74           C  
ATOM    674  CG1 ILE A 418     176.187 165.558 152.925  1.00 73.74           C  
ATOM    675  CG2 ILE A 418     174.695 163.773 153.930  1.00 73.74           C  
ATOM    676  CD1 ILE A 418     177.410 164.700 152.667  1.00 73.74           C  
ATOM    677  N   ALA A 419     174.676 166.840 156.813  1.00 74.07           N  
ATOM    678  CA  ALA A 419     174.362 166.850 158.236  1.00 74.07           C  
ATOM    679  C   ALA A 419     173.054 167.582 158.508  1.00 74.07           C  
ATOM    680  O   ALA A 419     172.191 167.079 159.233  1.00 74.07           O  
ATOM    681  CB  ALA A 419     175.508 167.484 159.023  1.00 74.07           C  
ATOM    682  N   ASP A 420     172.884 168.770 157.926  1.00 80.01           N  
ATOM    683  CA  ASP A 420     171.708 169.575 158.244  1.00 80.01           C  
ATOM    684  C   ASP A 420     170.454 169.032 157.572  1.00 80.01           C  
ATOM    685  O   ASP A 420     169.354 169.140 158.124  1.00 80.01           O  
ATOM    686  CB  ASP A 420     171.938 171.031 157.842  1.00 80.01           C  
ATOM    687  CG  ASP A 420     172.938 171.731 158.737  1.00 80.01           C  
ATOM    688  OD1 ASP A 420     173.239 171.197 159.824  1.00 80.01           O  
ATOM    689  OD2 ASP A 420     173.422 172.815 158.353  1.00 80.01           O  
ATOM    690  N   TYR A 421     170.591 168.448 156.381  1.00 78.55           N  
ATOM    691  CA  TYR A 421     169.430 168.073 155.591  1.00 78.55           C  
ATOM    692  C   TYR A 421     169.095 166.590 155.627  1.00 78.55           C  
ATOM    693  O   TYR A 421     167.922 166.247 155.795  1.00 78.55           O  
ATOM    694  CB  TYR A 421     169.633 168.492 154.129  1.00 78.55           C  
ATOM    695  CG  TYR A 421     169.748 169.986 153.936  1.00 78.55           C  
ATOM    696  CD1 TYR A 421     168.947 170.862 154.656  1.00 78.55           C  
ATOM    697  CD2 TYR A 421     170.663 170.520 153.041  1.00 78.55           C  
ATOM    698  CE1 TYR A 421     169.050 172.227 154.480  1.00 78.55           C  
ATOM    699  CE2 TYR A 421     170.775 171.884 152.862  1.00 78.55           C  
ATOM    700  CZ  TYR A 421     169.967 172.732 153.582  1.00 78.55           C  
ATOM    701  OH  TYR A 421     170.080 174.091 153.400  1.00 78.55           O  
ATOM    702  N   ASN A 422     170.082 165.708 155.485  1.00 71.97           N  
ATOM    703  CA  ASN A 422     169.828 164.288 155.271  1.00 71.97           C  
ATOM    704  C   ASN A 422     169.745 163.523 156.587  1.00 71.97           C  
ATOM    705  O   ASN A 422     168.723 162.895 156.867  1.00 71.97           O  
ATOM    706  CB  ASN A 422     170.905 163.707 154.357  1.00 71.97           C  
ATOM    707  CG  ASN A 422     170.824 164.257 152.954  1.00 71.97           C  
ATOM    708  OD1 ASN A 422     170.755 163.502 151.990  1.00 71.97           O  
ATOM    709  ND2 ASN A 422     170.822 165.577 152.832  1.00 71.97           N  
ATOM    710  N   TYR A 423     170.799 163.539 157.397  1.00 66.20           N  
ATOM    711  CA  TYR A 423     170.798 162.888 158.700  1.00 66.20           C  
ATOM    712  C   TYR A 423     171.578 163.754 159.673  1.00 66.20           C  
ATOM    713  O   TYR A 423     172.769 164.006 159.466  1.00 66.20           O  
ATOM    714  CB  TYR A 423     171.403 161.487 158.625  1.00 66.20           C  
ATOM    715  CG  TYR A 423     171.329 160.734 159.931  1.00 66.20           C  
ATOM    716  CD1 TYR A 423     170.105 160.374 160.474  1.00 66.20           C  
ATOM    717  CD2 TYR A 423     172.479 160.382 160.620  1.00 66.20           C  
ATOM    718  CE1 TYR A 423     170.026 159.686 161.668  1.00 66.20           C  
ATOM    719  CE2 TYR A 423     172.411 159.690 161.815  1.00 66.20           C  
ATOM    720  CZ  TYR A 423     171.180 159.346 162.335  1.00 66.20           C  
ATOM    721  OH  TYR A 423     171.097 158.661 163.523  1.00 66.20           O  
ATOM    722  N   LYS A 424     170.911 164.206 160.728  1.00 71.53           N  
ATOM    723  CA  LYS A 424     171.527 165.053 161.738  1.00 71.53           C  
ATOM    724  C   LYS A 424     171.573 164.292 163.052  1.00 71.53           C  
ATOM    725  O   LYS A 424     170.537 164.089 163.691  1.00 71.53           O  
ATOM    726  CB  LYS A 424     170.760 166.362 161.910  1.00 71.53           C  
ATOM    727  CG  LYS A 424     171.498 167.384 162.750  1.00 71.53           C  
ATOM    728  CD  LYS A 424     170.717 168.677 162.869  1.00 71.53           C  
ATOM    729  CE  LYS A 424     171.533 169.739 163.583  1.00 71.53           C  
ATOM    730  NZ  LYS A 424     171.985 169.277 164.922  1.00 71.53           N  
ATOM    731  N   LEU A 425     172.763 163.875 163.445  1.00 67.97           N  
ATOM    732  CA  LEU A 425     172.930 163.259 164.748  1.00 67.97           C  
ATOM    733  C   LEU A 425     172.796 164.335 165.820  1.00 67.97           C  
ATOM    734  O   LEU A 425     173.466 165.370 165.734  1.00 67.97           O  
ATOM    735  CB  LEU A 425     174.286 162.566 164.838  1.00 67.97           C  
ATOM    736  CG  LEU A 425     174.344 161.306 165.700  1.00 67.97           C  
ATOM    737  CD1 LEU A 425     173.242 160.345 165.302  1.00 67.97           C  
ATOM    738  CD2 LEU A 425     175.699 160.639 165.569  1.00 67.97           C  
ATOM    739  N   PRO A 426     171.940 164.143 166.823  1.00 73.73           N  
ATOM    740  CA  PRO A 426     171.685 165.216 167.790  1.00 73.73           C  
ATOM    741  C   PRO A 426     172.950 165.611 168.534  1.00 73.73           C  
ATOM    742  O   PRO A 426     173.850 164.798 168.749  1.00 73.73           O  
ATOM    743  CB  PRO A 426     170.648 164.601 168.737  1.00 73.73           C  
ATOM    744  CG  PRO A 426     170.837 163.131 168.598  1.00 73.73           C  
ATOM    745  CD  PRO A 426     171.214 162.909 167.164  1.00 73.73           C  
ATOM    746  N   ASP A 427     173.008 166.889 168.922  1.00 77.82           N  
ATOM    747  CA  ASP A 427     174.212 167.419 169.554  1.00 77.82           C  
ATOM    748  C   ASP A 427     174.543 166.662 170.834  1.00 77.82           C  
ATOM    749  O   ASP A 427     175.712 166.358 171.100  1.00 77.82           O  
ATOM    750  CB  ASP A 427     174.041 168.911 169.834  1.00 77.82           C  
ATOM    751  CG  ASP A 427     175.355 169.664 169.800  1.00 77.82           C  
ATOM    752  OD1 ASP A 427     176.399 169.054 170.110  1.00 77.82           O  
ATOM    753  OD2 ASP A 427     175.345 170.865 169.457  1.00 77.82           O  
ATOM    754  N   ASP A 428     173.531 166.350 171.638  1.00 75.94           N  
ATOM    755  CA  ASP A 428     173.692 165.461 172.782  1.00 75.94           C  
ATOM    756  C   ASP A 428     173.416 164.036 172.314  1.00 75.94           C  
ATOM    757  O   ASP A 428     172.269 163.580 172.330  1.00 75.94           O  
ATOM    758  CB  ASP A 428     172.762 165.871 173.919  1.00 75.94           C  
ATOM    759  CG  ASP A 428     173.189 167.165 174.585  1.00 75.94           C  
ATOM    760  OD1 ASP A 428     174.339 167.600 174.371  1.00 75.94           O  
ATOM    761  OD2 ASP A 428     172.372 167.748 175.325  1.00 75.94           O  
ATOM    762  N   PHE A 429     174.466 163.334 171.898  1.00 73.30           N  
ATOM    763  CA  PHE A 429     174.343 162.012 171.301  1.00 73.30           C  
ATOM    764  C   PHE A 429     175.065 160.984 172.156  1.00 73.30           C  
ATOM    765  O   PHE A 429     176.163 161.242 172.658  1.00 73.30           O  
ATOM    766  CB  PHE A 429     174.908 161.997 169.882  1.00 73.30           C  
ATOM    767  CG  PHE A 429     175.010 160.627 169.286  1.00 73.30           C  
ATOM    768  CD1 PHE A 429     173.871 159.913 168.961  1.00 73.30           C  
ATOM    769  CD2 PHE A 429     176.244 160.057 169.039  1.00 73.30           C  
ATOM    770  CE1 PHE A 429     173.963 158.656 168.407  1.00 73.30           C  
ATOM    771  CE2 PHE A 429     176.341 158.800 168.484  1.00 73.30           C  
ATOM    772  CZ  PHE A 429     175.199 158.099 168.168  1.00 73.30           C  
ATOM    773  N   THR A 430     174.445 159.812 172.311  1.00 79.47           N  
ATOM    774  CA  THR A 430     174.985 158.729 173.131  1.00 79.47           C  
ATOM    775  C   THR A 430     175.081 157.466 172.271  1.00 79.47           C  
ATOM    776  O   THR A 430     174.159 156.650 172.225  1.00 79.47           O  
ATOM    777  CB  THR A 430     174.123 158.496 174.370  1.00 79.47           C  
ATOM    778  OG1 THR A 430     173.983 159.724 175.095  1.00 79.47           O  
ATOM    779  CG2 THR A 430     174.762 157.454 175.272  1.00 79.47           C  
ATOM    780  N   GLY A 431     176.210 157.310 171.586  1.00 68.11           N  
ATOM    781  CA  GLY A 431     176.429 156.146 170.747  1.00 68.11           C  
ATOM    782  C   GLY A 431     177.766 156.249 170.052  1.00 68.11           C  
ATOM    783  O   GLY A 431     178.497 157.229 170.201  1.00 68.11           O  
ATOM    784  N   CYS A 432     178.079 155.217 169.279  1.00 64.98           N  
ATOM    785  CA  CYS A 432     179.346 155.137 168.565  1.00 64.98           C  
ATOM    786  C   CYS A 432     179.082 155.117 167.066  1.00 64.98           C  
ATOM    787  O   CYS A 432     178.366 154.242 166.570  1.00 64.98           O  
ATOM    788  CB  CYS A 432     180.134 153.896 168.982  1.00 64.98           C  
ATOM    789  SG  CYS A 432     181.866 153.964 168.487  1.00 64.98           S  
ATOM    790  N   VAL A 433     179.664 156.074 166.352  1.00 56.03           N  
ATOM    791  CA  VAL A 433     179.604 156.105 164.896  1.00 56.03           C  
ATOM    792  C   VAL A 433     180.857 155.437 164.350  1.00 56.03           C  
ATOM    793  O   VAL A 433     181.979 155.861 164.644  1.00 56.03           O  
ATOM    794  CB  VAL A 433     179.469 157.541 164.371  1.00 56.03           C  
ATOM    795  CG1 VAL A 433     178.163 158.146 164.823  1.00 56.03           C  
ATOM    796  CG2 VAL A 433     180.633 158.390 164.852  1.00 56.03           C  
ATOM    797  N   ILE A 434     180.669 154.389 163.557  1.00 55.86           N  
ATOM    798  CA  ILE A 434     181.765 153.634 162.968  1.00 55.86           C  
ATOM    799  C   ILE A 434     181.612 153.673 161.456  1.00 55.86           C  
ATOM    800  O   ILE A 434     180.543 153.351 160.927  1.00 55.86           O  
ATOM    801  CB  ILE A 434     181.796 152.187 163.491  1.00 55.86           C  
ATOM    802  CG1 ILE A 434     182.122 152.154 164.984  1.00 55.86           C  
ATOM    803  CG2 ILE A 434     182.781 151.357 162.694  1.00 55.86           C  
ATOM    804  CD1 ILE A 434     180.995 151.617 165.825  1.00 55.86           C  
ATOM    805  N   ALA A 435     182.676 154.070 160.765  1.00 55.82           N  
ATOM    806  CA  ALA A 435     182.647 154.224 159.321  1.00 55.82           C  
ATOM    807  C   ALA A 435     183.966 153.754 158.734  1.00 55.82           C  
ATOM    808  O   ALA A 435     185.027 153.974 159.322  1.00 55.82           O  
ATOM    809  CB  ALA A 435     182.390 155.677 158.921  1.00 55.82           C  
ATOM    810  N   TRP A 436     183.892 153.115 157.571  1.00 65.04           N  
ATOM    811  CA  TRP A 436     185.065 152.576 156.904  1.00 65.04           C  
ATOM    812  C   TRP A 436     184.916 152.744 155.400  1.00 65.04           C  
ATOM    813  O   TRP A 436     183.803 152.853 154.881  1.00 65.04           O  
ATOM    814  CB  TRP A 436     185.272 151.099 157.245  1.00 65.04           C  
ATOM    815  CG  TRP A 436     184.124 150.231 156.849  1.00 65.04           C  
ATOM    816  CD1 TRP A 436     184.032 149.459 155.731  1.00 65.04           C  
ATOM    817  CD2 TRP A 436     182.898 150.049 157.565  1.00 65.04           C  
ATOM    818  NE1 TRP A 436     182.826 148.802 155.708  1.00 65.04           N  
ATOM    819  CE2 TRP A 436     182.111 149.149 156.823  1.00 65.04           C  
ATOM    820  CE3 TRP A 436     182.391 150.558 158.762  1.00 65.04           C  
ATOM    821  CZ2 TRP A 436     180.846 148.748 157.238  1.00 65.04           C  
ATOM    822  CZ3 TRP A 436     181.136 150.159 159.171  1.00 65.04           C  
ATOM    823  CH2 TRP A 436     180.377 149.263 158.412  1.00 65.04           C  
ATOM    824  N   ASN A 437     186.050 152.765 154.706  1.00 72.43           N  
ATOM    825  CA  ASN A 437     186.029 152.903 153.257  1.00 72.43           C  
ATOM    826  C   ASN A 437     185.350 151.701 152.620  1.00 72.43           C  
ATOM    827  O   ASN A 437     185.735 150.553 152.858  1.00 72.43           O  
ATOM    828  CB  ASN A 437     187.449 153.052 152.717  1.00 72.43           C  
ATOM    829  CG  ASN A 437     187.499 153.031 151.204  1.00 72.43           C  
ATOM    830  OD1 ASN A 437     187.325 154.059 150.552  1.00 72.43           O  
ATOM    831  ND2 ASN A 437     187.738 151.856 150.635  1.00 72.43           N  
ATOM    832  N   SER A 438     184.335 151.970 151.802  1.00 80.74           N  
ATOM    833  CA  SER A 438     183.605 150.928 151.091  1.00 80.74           C  
ATOM    834  C   SER A 438     183.757 151.062 149.583  1.00 80.74           C  
ATOM    835  O   SER A 438     182.847 150.688 148.836  1.00 80.74           O  
ATOM    836  CB  SER A 438     182.128 150.955 151.481  1.00 80.74           C  
ATOM    837  OG  SER A 438     181.353 150.163 150.601  1.00 80.74           O  
ATOM    838  N   ASN A 439     184.889 151.598 149.123  1.00 88.56           N  
ATOM    839  CA  ASN A 439     185.085 151.809 147.693  1.00 88.56           C  
ATOM    840  C   ASN A 439     185.056 150.491 146.930  1.00 88.56           C  
ATOM    841  O   ASN A 439     184.497 150.412 145.831  1.00 88.56           O  
ATOM    842  CB  ASN A 439     186.400 152.547 147.449  1.00 88.56           C  
ATOM    843  CG  ASN A 439     186.614 152.887 145.990  1.00 88.56           C  
ATOM    844  OD1 ASN A 439     186.104 153.891 145.494  1.00 88.56           O  
ATOM    845  ND2 ASN A 439     187.375 152.053 145.294  1.00 88.56           N  
ATOM    846  N   ASN A 440     185.659 149.444 147.493  1.00 90.98           N  
ATOM    847  CA  ASN A 440     185.611 148.137 146.845  1.00 90.98           C  
ATOM    848  C   ASN A 440     184.225 147.514 146.965  1.00 90.98           C  
ATOM    849  O   ASN A 440     183.878 146.599 146.209  1.00 90.98           O  
ATOM    850  CB  ASN A 440     186.680 147.218 147.439  1.00 90.98           C  
ATOM    851  CG  ASN A 440     186.652 147.190 148.953  1.00 90.98           C  
ATOM    852  OD1 ASN A 440     187.282 148.017 149.612  1.00 90.98           O  
ATOM    853  ND2 ASN A 440     185.926 146.232 149.513  1.00 90.98           N  
ATOM    854  N   LEU A 441     183.415 147.995 147.913  1.00 87.42           N  
ATOM    855  CA  LEU A 441     182.097 147.401 148.118  1.00 87.42           C  
ATOM    856  C   LEU A 441     181.000 148.197 147.418  1.00 87.42           C  
ATOM    857  O   LEU A 441     180.220 147.633 146.642  1.00 87.42           O  
ATOM    858  CB  LEU A 441     181.800 147.281 149.611  1.00 87.42           C  
ATOM    859  CG  LEU A 441     182.735 146.397 150.435  1.00 87.42           C  
ATOM    860  CD1 LEU A 441     182.322 146.399 151.897  1.00 87.42           C  
ATOM    861  CD2 LEU A 441     182.758 144.981 149.885  1.00 87.42           C  
ATOM    862  N   ASP A 442     180.916 149.506 147.676  1.00 83.87           N  
ATOM    863  CA  ASP A 442     179.777 150.305 147.234  1.00 83.87           C  
ATOM    864  C   ASP A 442     180.122 151.279 146.114  1.00 83.87           C  
ATOM    865  O   ASP A 442     179.393 152.253 145.906  1.00 83.87           O  
ATOM    866  CB  ASP A 442     179.168 151.069 148.410  1.00 83.87           C  
ATOM    867  CG  ASP A 442     178.408 150.169 149.354  1.00 83.87           C  
ATOM    868  OD1 ASP A 442     178.476 148.935 149.182  1.00 83.87           O  
ATOM    869  OD2 ASP A 442     177.736 150.695 150.265  1.00 83.87           O  
ATOM    870  N   SER A 443     181.205 151.046 145.383  1.00 88.51           N  
ATOM    871  CA  SER A 443     181.553 151.870 144.234  1.00 88.51           C  
ATOM    872  C   SER A 443     181.737 150.977 143.017  1.00 88.51           C  
ATOM    873  O   SER A 443     182.411 149.945 143.095  1.00 88.51           O  
ATOM    874  CB  SER A 443     182.821 152.684 144.491  1.00 88.51           C  
ATOM    875  OG  SER A 443     183.132 153.500 143.375  1.00 88.51           O  
ATOM    876  N   LYS A 444     181.138 151.377 141.902  1.00 92.92           N  
ATOM    877  CA  LYS A 444     181.199 150.628 140.657  1.00 92.92           C  
ATOM    878  C   LYS A 444     181.923 151.455 139.604  1.00 92.92           C  
ATOM    879  O   LYS A 444     181.854 152.689 139.617  1.00 92.92           O  
ATOM    880  CB  LYS A 444     179.794 150.261 140.171  1.00 92.92           C  
ATOM    881  CG  LYS A 444     179.760 149.283 139.009  1.00 92.92           C  
ATOM    882  CD  LYS A 444     178.330 148.945 138.623  1.00 92.92           C  
ATOM    883  CE  LYS A 444     178.285 147.977 137.452  1.00 92.92           C  
ATOM    884  NZ  LYS A 444     176.887 147.652 137.055  1.00 92.92           N  
ATOM    885  N   VAL A 445     182.626 150.769 138.700  1.00 94.53           N  
ATOM    886  CA  VAL A 445     183.355 151.460 137.645  1.00 94.53           C  
ATOM    887  C   VAL A 445     182.386 152.274 136.801  1.00 94.53           C  
ATOM    888  O   VAL A 445     181.326 151.787 136.386  1.00 94.53           O  
ATOM    889  CB  VAL A 445     184.135 150.454 136.783  1.00 94.53           C  
ATOM    890  CG1 VAL A 445     184.981 151.184 135.753  1.00 94.53           C  
ATOM    891  CG2 VAL A 445     185.003 149.566 137.660  1.00 94.53           C  
ATOM    892  N   GLY A 446     182.748 153.528 136.547  1.00 92.31           N  
ATOM    893  CA  GLY A 446     181.890 154.442 135.827  1.00 92.31           C  
ATOM    894  C   GLY A 446     180.876 155.173 136.677  1.00 92.31           C  
ATOM    895  O   GLY A 446     180.112 155.984 136.139  1.00 92.31           O  
ATOM    896  N   GLY A 447     180.842 154.919 137.976  1.00 87.94           N  
ATOM    897  CA  GLY A 447     179.930 155.645 138.844  1.00 87.94           C  
ATOM    898  C   GLY A 447     178.759 154.801 139.303  1.00 87.94           C  
ATOM    899  O   GLY A 447     178.137 154.067 138.536  1.00 87.94           O  
ATOM    900  N   ASN A 448     178.456 154.912 140.594  1.00 90.57           N  
ATOM    901  CA  ASN A 448     177.300 154.266 141.202  1.00 90.57           C  
ATOM    902  C   ASN A 448     176.487 155.334 141.916  1.00 90.57           C  
ATOM    903  O   ASN A 448     176.863 155.781 143.004  1.00 90.57           O  
ATOM    904  CB  ASN A 448     177.726 153.166 142.175  1.00 90.57           C  
ATOM    905  CG  ASN A 448     176.551 152.371 142.704  1.00 90.57           C  
ATOM    906  OD1 ASN A 448     175.488 152.327 142.085  1.00 90.57           O  
ATOM    907  ND2 ASN A 448     176.736 151.736 143.855  1.00 90.57           N  
ATOM    908  N   TYR A 449     175.371 155.734 141.308  1.00 89.88           N  
ATOM    909  CA  TYR A 449     174.602 156.888 141.752  1.00 89.88           C  
ATOM    910  C   TYR A 449     173.368 156.509 142.562  1.00 89.88           C  
ATOM    911  O   TYR A 449     172.485 157.352 142.752  1.00 89.88           O  
ATOM    912  CB  TYR A 449     174.191 157.735 140.546  1.00 89.88           C  
ATOM    913  CG  TYR A 449     175.347 158.181 139.680  1.00 89.88           C  
ATOM    914  CD1 TYR A 449     176.017 159.368 139.939  1.00 89.88           C  
ATOM    915  CD2 TYR A 449     175.764 157.417 138.598  1.00 89.88           C  
ATOM    916  CE1 TYR A 449     177.071 159.779 139.149  1.00 89.88           C  
ATOM    917  CE2 TYR A 449     176.815 157.820 137.803  1.00 89.88           C  
ATOM    918  CZ  TYR A 449     177.465 159.002 138.082  1.00 89.88           C  
ATOM    919  OH  TYR A 449     178.515 159.406 137.291  1.00 89.88           O  
ATOM    920  N   ASN A 450     173.281 155.265 143.039  1.00 85.26           N  
ATOM    921  CA  ASN A 450     172.088 154.832 143.761  1.00 85.26           C  
ATOM    922  C   ASN A 450     171.905 155.609 145.059  1.00 85.26           C  
ATOM    923  O   ASN A 450     170.773 155.866 145.483  1.00 85.26           O  
ATOM    924  CB  ASN A 450     172.160 153.332 144.040  1.00 85.26           C  
ATOM    925  CG  ASN A 450     172.203 152.509 142.771  1.00 85.26           C  
ATOM    926  OD1 ASN A 450     172.510 153.023 141.696  1.00 85.26           O  
ATOM    927  ND2 ASN A 450     171.895 151.224 142.888  1.00 85.26           N  
ATOM    928  N   TYR A 451     173.003 155.985 145.707  1.00 74.94           N  
ATOM    929  CA  TYR A 451     172.928 156.776 146.926  1.00 74.94           C  
ATOM    930  C   TYR A 451     172.788 158.250 146.571  1.00 74.94           C  
ATOM    931  O   TYR A 451     173.511 158.759 145.710  1.00 74.94           O  
ATOM    932  CB  TYR A 451     174.173 156.544 147.777  1.00 74.94           C  
ATOM    933  CG  TYR A 451     174.490 155.084 147.987  1.00 74.94           C  
ATOM    934  CD1 TYR A 451     173.497 154.181 148.334  1.00 74.94           C  
ATOM    935  CD2 TYR A 451     175.780 154.604 147.816  1.00 74.94           C  
ATOM    936  CE1 TYR A 451     173.783 152.845 148.521  1.00 74.94           C  
ATOM    937  CE2 TYR A 451     176.075 153.268 148.002  1.00 74.94           C  
ATOM    938  CZ  TYR A 451     175.072 152.394 148.354  1.00 74.94           C  
ATOM    939  OH  TYR A 451     175.361 151.063 148.539  1.00 74.94           O  
ATOM    940  N   LEU A 452     171.858 158.936 147.234  1.00 72.12           N  
ATOM    941  CA  LEU A 452     171.567 160.326 146.919  1.00 72.12           C  
ATOM    942  C   LEU A 452     171.134 161.065 148.177  1.00 72.12           C  
ATOM    943  O   LEU A 452     170.602 160.474 149.119  1.00 72.12           O  
ATOM    944  CB  LEU A 452     170.492 160.434 145.832  1.00 72.12           C  
ATOM    945  CG  LEU A 452     169.117 159.858 146.161  1.00 72.12           C  
ATOM    946  CD1 LEU A 452     168.097 160.292 145.132  1.00 72.12           C  
ATOM    947  CD2 LEU A 452     169.182 158.345 146.250  1.00 72.12           C  
ATOM    948  N   TYR A 453     171.356 162.377 148.170  1.00 74.07           N  
ATOM    949  CA  TYR A 453     171.132 163.219 149.334  1.00 74.07           C  
ATOM    950  C   TYR A 453     170.253 164.404 148.961  1.00 74.07           C  
ATOM    951  O   TYR A 453     170.257 164.870 147.820  1.00 74.07           O  
ATOM    952  CB  TYR A 453     172.457 163.714 149.926  1.00 74.07           C  
ATOM    953  CG  TYR A 453     173.349 164.434 148.940  1.00 74.07           C  
ATOM    954  CD1 TYR A 453     174.176 163.728 148.078  1.00 74.07           C  
ATOM    955  CD2 TYR A 453     173.376 165.819 148.880  1.00 74.07           C  
ATOM    956  CE1 TYR A 453     174.995 164.378 147.180  1.00 74.07           C  
ATOM    957  CE2 TYR A 453     174.194 166.479 147.984  1.00 74.07           C  
ATOM    958  CZ  TYR A 453     175.001 165.753 147.137  1.00 74.07           C  
ATOM    959  OH  TYR A 453     175.818 166.403 146.242  1.00 74.07           O  
ATOM    960  N   ARG A 454     169.498 164.898 149.945  1.00 77.11           N  
ATOM    961  CA  ARG A 454     168.583 166.018 149.716  1.00 77.11           C  
ATOM    962  C   ARG A 454     169.367 167.320 149.831  1.00 77.11           C  
ATOM    963  O   ARG A 454     169.593 167.854 150.918  1.00 77.11           O  
ATOM    964  CB  ARG A 454     167.397 165.972 150.675  1.00 77.11           C  
ATOM    965  CG  ARG A 454     167.722 165.841 152.150  1.00 77.11           C  
ATOM    966  CD  ARG A 454     166.483 165.462 152.956  1.00 77.11           C  
ATOM    967  NE  ARG A 454     165.340 166.324 152.674  1.00 77.11           N  
ATOM    968  CZ  ARG A 454     164.307 165.976 151.920  1.00 77.11           C  
ATOM    969  NH1 ARG A 454     164.235 164.783 151.355  1.00 77.11           N  
ATOM    970  NH2 ARG A 454     163.322 166.849 151.726  1.00 77.11           N  
ATOM    971  N   LEU A 455     169.792 167.835 148.676  1.00 75.08           N  
ATOM    972  CA  LEU A 455     170.617 169.036 148.656  1.00 75.08           C  
ATOM    973  C   LEU A 455     169.853 170.251 149.167  1.00 75.08           C  
ATOM    974  O   LEU A 455     170.403 171.069 149.912  1.00 75.08           O  
ATOM    975  CB  LEU A 455     171.139 169.284 147.243  1.00 75.08           C  
ATOM    976  CG  LEU A 455     172.069 170.484 147.083  1.00 75.08           C  
ATOM    977  CD1 LEU A 455     173.245 170.380 148.040  1.00 75.08           C  
ATOM    978  CD2 LEU A 455     172.553 170.590 145.648  1.00 75.08           C  
ATOM    979  N   PHE A 456     168.589 170.390 148.780  1.00 79.36           N  
ATOM    980  CA  PHE A 456     167.788 171.556 149.127  1.00 79.36           C  
ATOM    981  C   PHE A 456     166.629 171.143 150.019  1.00 79.36           C  
ATOM    982  O   PHE A 456     166.045 170.071 149.830  1.00 79.36           O  
ATOM    983  CB  PHE A 456     167.257 172.256 147.873  1.00 79.36           C  
ATOM    984  CG  PHE A 456     168.330 172.834 147.000  1.00 79.36           C  
ATOM    985  CD1 PHE A 456     169.547 173.218 147.535  1.00 79.36           C  
ATOM    986  CD2 PHE A 456     168.122 172.992 145.643  1.00 79.36           C  
ATOM    987  CE1 PHE A 456     170.535 173.750 146.731  1.00 79.36           C  
ATOM    988  CE2 PHE A 456     169.105 173.522 144.834  1.00 79.36           C  
ATOM    989  CZ  PHE A 456     170.314 173.902 145.378  1.00 79.36           C  
ATOM    990  N   ARG A 457     166.302 171.995 150.986  1.00 81.62           N  
ATOM    991  CA  ARG A 457     165.140 171.795 151.835  1.00 81.62           C  
ATOM    992  C   ARG A 457     164.719 173.146 152.392  1.00 81.62           C  
ATOM    993  O   ARG A 457     165.534 174.066 152.501  1.00 81.62           O  
ATOM    994  CB  ARG A 457     165.432 170.802 152.966  1.00 81.62           C  
ATOM    995  CG  ARG A 457     164.193 170.271 153.668  1.00 81.62           C  
ATOM    996  CD  ARG A 457     164.541 169.174 154.659  1.00 81.62           C  
ATOM    997  NE  ARG A 457     163.366 168.715 155.390  1.00 81.62           N  
ATOM    998  CZ  ARG A 457     162.926 169.261 156.515  1.00 81.62           C  
ATOM    999  NH1 ARG A 457     163.547 170.285 157.076  1.00 81.62           N  
ATOM   1000  NH2 ARG A 457     161.834 168.767 157.092  1.00 81.62           N  
ATOM   1001  N   LYS A 458     163.433 173.263 152.732  1.00 82.41           N  
ATOM   1002  CA  LYS A 458     162.927 174.521 153.271  1.00 82.41           C  
ATOM   1003  C   LYS A 458     163.595 174.859 154.596  1.00 82.41           C  
ATOM   1004  O   LYS A 458     163.958 176.015 154.840  1.00 82.41           O  
ATOM   1005  CB  LYS A 458     161.409 174.447 153.435  1.00 82.41           C  
ATOM   1006  CG  LYS A 458     160.773 175.732 153.938  1.00 82.41           C  
ATOM   1007  CD  LYS A 458     159.256 175.625 153.957  1.00 82.41           C  
ATOM   1008  CE  LYS A 458     158.793 174.476 154.837  1.00 82.41           C  
ATOM   1009  NZ  LYS A 458     157.310 174.340 154.842  1.00 82.41           N  
ATOM   1010  N   SER A 459     163.774 173.864 155.457  1.00 79.55           N  
ATOM   1011  CA  SER A 459     164.400 174.054 156.754  1.00 79.55           C  
ATOM   1012  C   SER A 459     165.357 172.904 157.024  1.00 79.55           C  
ATOM   1013  O   SER A 459     165.258 171.832 156.421  1.00 79.55           O  
ATOM   1014  CB  SER A 459     163.356 174.145 157.875  1.00 79.55           C  
ATOM   1015  OG  SER A 459     162.585 172.959 157.945  1.00 79.55           O  
ATOM   1016  N   ASN A 460     166.297 173.142 157.933  1.00 81.04           N  
ATOM   1017  CA  ASN A 460     167.206 172.087 158.351  1.00 81.04           C  
ATOM   1018  C   ASN A 460     166.436 170.962 159.030  1.00 81.04           C  
ATOM   1019  O   ASN A 460     165.485 171.192 159.782  1.00 81.04           O  
ATOM   1020  CB  ASN A 460     168.275 172.638 159.295  1.00 81.04           C  
ATOM   1021  CG  ASN A 460     169.264 173.541 158.589  1.00 81.04           C  
ATOM   1022  OD1 ASN A 460     169.398 173.497 157.367  1.00 81.04           O  
ATOM   1023  ND2 ASN A 460     169.968 174.363 159.357  1.00 81.04           N  
ATOM   1024  N   LEU A 461     166.856 169.732 158.749  1.00 80.27           N  
ATOM   1025  CA  LEU A 461     166.150 168.564 159.252  1.00 80.27           C  
ATOM   1026  C   LEU A 461     166.219 168.494 160.772  1.00 80.27           C  
ATOM   1027  O   LEU A 461     167.258 168.767 161.378  1.00 80.27           O  
ATOM   1028  CB  LEU A 461     166.741 167.295 158.645  1.00 80.27           C  
ATOM   1029  CG  LEU A 461     166.205 165.979 159.200  1.00 80.27           C  
ATOM   1030  CD1 LEU A 461     164.712 165.858 158.952  1.00 80.27           C  
ATOM   1031  CD2 LEU A 461     166.947 164.820 158.581  1.00 80.27           C  
ATOM   1032  N   LYS A 462     165.098 168.124 161.386  1.00 83.82           N  
ATOM   1033  CA  LYS A 462     165.067 167.939 162.825  1.00 83.82           C  
ATOM   1034  C   LYS A 462     165.975 166.774 163.218  1.00 83.82           C  
ATOM   1035  O   LYS A 462     166.139 165.820 162.452  1.00 83.82           O  
ATOM   1036  CB  LYS A 462     163.641 167.680 163.301  1.00 83.82           C  
ATOM   1037  CG  LYS A 462     162.701 168.851 163.091  1.00 83.82           C  
ATOM   1038  CD  LYS A 462     161.360 168.599 163.755  1.00 83.82           C  
ATOM   1039  CE  LYS A 462     161.534 168.269 165.229  1.00 83.82           C  
ATOM   1040  NZ  LYS A 462     162.276 169.335 165.958  1.00 83.82           N  
ATOM   1041  N   PRO A 463     166.587 166.834 164.401  1.00 83.72           N  
ATOM   1042  CA  PRO A 463     167.567 165.808 164.779  1.00 83.72           C  
ATOM   1043  C   PRO A 463     166.962 164.413 164.807  1.00 83.72           C  
ATOM   1044  O   PRO A 463     165.835 164.211 165.264  1.00 83.72           O  
ATOM   1045  CB  PRO A 463     168.016 166.249 166.177  1.00 83.72           C  
ATOM   1046  CG  PRO A 463     167.724 167.710 166.227  1.00 83.72           C  
ATOM   1047  CD  PRO A 463     166.483 167.899 165.412  1.00 83.72           C  
ATOM   1048  N   PHE A 464     167.739 163.446 164.315  1.00 79.65           N  
ATOM   1049  CA  PHE A 464     167.387 162.027 164.381  1.00 79.65           C  
ATOM   1050  C   PHE A 464     166.028 161.753 163.740  1.00 79.65           C  
ATOM   1051  O   PHE A 464     165.172 161.082 164.319  1.00 79.65           O  
ATOM   1052  CB  PHE A 464     167.422 161.524 165.826  1.00 79.65           C  
ATOM   1053  CG  PHE A 464     167.599 160.038 165.948  1.00 79.65           C  
ATOM   1054  CD1 PHE A 464     168.813 159.446 165.642  1.00 79.65           C  
ATOM   1055  CD2 PHE A 464     166.556 159.234 166.380  1.00 79.65           C  
ATOM   1056  CE1 PHE A 464     168.983 158.079 165.756  1.00 79.65           C  
ATOM   1057  CE2 PHE A 464     166.719 157.865 166.495  1.00 79.65           C  
ATOM   1058  CZ  PHE A 464     167.935 157.287 166.183  1.00 79.65           C  
ATOM   1059  N   GLU A 465     165.822 162.283 162.536  1.00 82.30           N  
ATOM   1060  CA  GLU A 465     164.571 162.106 161.814  1.00 82.30           C  
ATOM   1061  C   GLU A 465     164.853 161.865 160.339  1.00 82.30           C  
ATOM   1062  O   GLU A 465     165.958 162.103 159.847  1.00 82.30           O  
ATOM   1063  CB  GLU A 465     163.642 163.316 161.977  1.00 82.30           C  
ATOM   1064  CG  GLU A 465     163.094 163.492 163.383  1.00 82.30           C  
ATOM   1065  CD  GLU A 465     162.091 164.621 163.477  1.00 82.30           C  
ATOM   1066  OE1 GLU A 465     161.711 165.170 162.423  1.00 82.30           O  
ATOM   1067  OE2 GLU A 465     161.683 164.961 164.607  1.00 82.30           O  
ATOM   1068  N   ARG A 466     163.833 161.374 159.640  1.00 76.66           N  
ATOM   1069  CA  ARG A 466     163.901 161.108 158.209  1.00 76.66           C  
ATOM   1070  C   ARG A 466     162.750 161.814 157.509  1.00 76.66           C  
ATOM   1071  O   ARG A 466     161.596 161.693 157.931  1.00 76.66           O  
ATOM   1072  CB  ARG A 466     163.851 159.603 157.927  1.00 76.66           C  
ATOM   1073  CG  ARG A 466     163.214 159.237 156.598  1.00 76.66           C  
ATOM   1074  CD  ARG A 466     163.416 157.769 156.277  1.00 76.66           C  
ATOM   1075  NE  ARG A 466     163.217 156.914 157.440  1.00 76.66           N  
ATOM   1076  CZ  ARG A 466     163.353 155.596 157.428  1.00 76.66           C  
ATOM   1077  NH1 ARG A 466     163.674 154.945 156.323  1.00 76.66           N  
ATOM   1078  NH2 ARG A 466     163.162 154.914 158.554  1.00 76.66           N  
ATOM   1079  N   ASP A 467     163.065 162.544 156.442  1.00 82.70           N  
ATOM   1080  CA  ASP A 467     162.071 163.244 155.635  1.00 82.70           C  
ATOM   1081  C   ASP A 467     162.238 162.807 154.186  1.00 82.70           C  
ATOM   1082  O   ASP A 467     163.080 163.348 153.462  1.00 82.70           O  
ATOM   1083  CB  ASP A 467     162.213 164.758 155.775  1.00 82.70           C  
ATOM   1084  CG  ASP A 467     161.694 165.273 157.104  1.00 82.70           C  
ATOM   1085  OD1 ASP A 467     161.139 164.468 157.880  1.00 82.70           O  
ATOM   1086  OD2 ASP A 467     161.840 166.483 157.372  1.00 82.70           O  
ATOM   1087  N   ILE A 468     161.431 161.834 153.765  1.00 76.00           N  
ATOM   1088  CA  ILE A 468     161.486 161.312 152.406  1.00 76.00           C  
ATOM   1089  C   ILE A 468     160.632 162.131 151.447  1.00 76.00           C  
ATOM   1090  O   ILE A 468     160.431 161.720 150.300  1.00 76.00           O  
ATOM   1091  CB  ILE A 468     161.077 159.832 152.366  1.00 76.00           C  
ATOM   1092  CG1 ILE A 468     159.701 159.641 153.006  1.00 76.00           C  
ATOM   1093  CG2 ILE A 468     162.110 158.980 153.069  1.00 76.00           C  
ATOM   1094  CD1 ILE A 468     159.233 158.204 153.022  1.00 76.00           C  
ATOM   1095  N   SER A 469     160.109 163.270 151.894  1.00 81.04           N  
ATOM   1096  CA  SER A 469     159.304 164.114 151.022  1.00 81.04           C  
ATOM   1097  C   SER A 469     160.131 164.572 149.828  1.00 81.04           C  
ATOM   1098  O   SER A 469     161.257 165.054 149.983  1.00 81.04           O  
ATOM   1099  CB  SER A 469     158.773 165.318 151.797  1.00 81.04           C  
ATOM   1100  OG  SER A 469     159.836 166.091 152.322  1.00 81.04           O  
ATOM   1101  N   THR A 470     159.564 164.420 148.630  1.00 76.94           N  
ATOM   1102  CA  THR A 470     160.267 164.718 147.388  1.00 76.94           C  
ATOM   1103  C   THR A 470     159.524 165.742 146.539  1.00 76.94           C  
ATOM   1104  O   THR A 470     159.569 165.674 145.308  1.00 76.94           O  
ATOM   1105  CB  THR A 470     160.499 163.436 146.587  1.00 76.94           C  
ATOM   1106  OG1 THR A 470     159.264 162.721 146.466  1.00 76.94           O  
ATOM   1107  CG2 THR A 470     161.515 162.551 147.285  1.00 76.94           C  
ATOM   1108  N   GLU A 471     158.836 166.687 147.172  1.00 80.52           N  
ATOM   1109  CA  GLU A 471     158.162 167.743 146.436  1.00 80.52           C  
ATOM   1110  C   GLU A 471     159.175 168.733 145.876  1.00 80.52           C  
ATOM   1111  O   GLU A 471     160.302 168.845 146.362  1.00 80.52           O  
ATOM   1112  CB  GLU A 471     157.162 168.463 147.337  1.00 80.52           C  
ATOM   1113  CG  GLU A 471     157.692 168.760 148.725  1.00 80.52           C  
ATOM   1114  CD  GLU A 471     156.600 169.189 149.679  1.00 80.52           C  
ATOM   1115  OE1 GLU A 471     155.653 169.869 149.232  1.00 80.52           O  
ATOM   1116  OE2 GLU A 471     156.683 168.837 150.874  1.00 80.52           O  
ATOM   1117  N   ILE A 472     158.760 169.455 144.834  1.00 85.45           N  
ATOM   1118  CA  ILE A 472     159.649 170.417 144.199  1.00 85.45           C  
ATOM   1119  C   ILE A 472     159.911 171.571 145.152  1.00 85.45           C  
ATOM   1120  O   ILE A 472     158.978 172.192 145.676  1.00 85.45           O  
ATOM   1121  CB  ILE A 472     159.045 170.910 142.877  1.00 85.45           C  
ATOM   1122  CG1 ILE A 472     158.951 169.762 141.874  1.00 85.45           C  
ATOM   1123  CG2 ILE A 472     159.877 172.041 142.305  1.00 85.45           C  
ATOM   1124  CD1 ILE A 472     160.290 169.171 141.518  1.00 85.45           C  
ATOM   1125  N   TYR A 473     161.188 171.863 145.384  1.00 90.22           N  
ATOM   1126  CA  TYR A 473     161.546 172.977 146.247  1.00 90.22           C  
ATOM   1127  C   TYR A 473     161.338 174.299 145.520  1.00 90.22           C  
ATOM   1128  O   TYR A 473     161.542 174.407 144.309  1.00 90.22           O  
ATOM   1129  CB  TYR A 473     162.995 172.859 146.710  1.00 90.22           C  
ATOM   1130  CG  TYR A 473     163.408 173.951 147.666  1.00 90.22           C  
ATOM   1131  CD1 TYR A 473     162.918 173.984 148.963  1.00 90.22           C  
ATOM   1132  CD2 TYR A 473     164.288 174.949 147.272  1.00 90.22           C  
ATOM   1133  CE1 TYR A 473     163.290 174.980 149.839  1.00 90.22           C  
ATOM   1134  CE2 TYR A 473     164.667 175.950 148.143  1.00 90.22           C  
ATOM   1135  CZ  TYR A 473     164.165 175.960 149.426  1.00 90.22           C  
ATOM   1136  OH  TYR A 473     164.540 176.955 150.299  1.00 90.22           O  
ATOM   1137  N   GLN A 474     160.928 175.313 146.275  1.00 95.42           N  
ATOM   1138  CA  GLN A 474     160.577 176.616 145.725  1.00 95.42           C  
ATOM   1139  C   GLN A 474     161.610 177.641 146.171  1.00 95.42           C  
ATOM   1140  O   GLN A 474     161.637 178.032 147.342  1.00 95.42           O  
ATOM   1141  CB  GLN A 474     159.174 177.024 146.171  1.00 95.42           C  
ATOM   1142  CG  GLN A 474     158.202 175.855 146.238  1.00 95.42           C  
ATOM   1143  CD  GLN A 474     156.849 176.179 145.642  1.00 95.42           C  
ATOM   1144  OE1 GLN A 474     156.537 177.338 145.372  1.00 95.42           O  
ATOM   1145  NE2 GLN A 474     156.037 175.150 145.426  1.00 95.42           N  
ATOM   1146  N   ALA A 475     162.453 178.074 145.237  1.00 95.79           N  
ATOM   1147  CA  ALA A 475     163.479 179.069 145.511  1.00 95.79           C  
ATOM   1148  C   ALA A 475     163.130 180.441 144.951  1.00 95.79           C  
ATOM   1149  O   ALA A 475     163.980 181.336 144.957  1.00 95.79           O  
ATOM   1150  CB  ALA A 475     164.825 178.605 144.954  1.00 95.79           C  
ATOM   1151  N   GLY A 476     161.901 180.627 144.466  1.00102.98           N  
ATOM   1152  CA  GLY A 476     161.495 181.891 143.900  1.00102.98           C  
ATOM   1153  C   GLY A 476     160.150 182.330 144.444  1.00102.98           C  
ATOM   1154  O   GLY A 476     159.463 181.591 145.149  1.00102.98           O  
ATOM   1155  N   SER A 477     159.787 183.570 144.106  1.00110.00           N  
ATOM   1156  CA  SER A 477     158.509 184.114 144.553  1.00110.00           C  
ATOM   1157  C   SER A 477     157.340 183.366 143.928  1.00110.00           C  
ATOM   1158  O   SER A 477     156.327 183.118 144.592  1.00110.00           O  
ATOM   1159  CB  SER A 477     158.429 185.604 144.223  1.00110.00           C  
ATOM   1160  OG  SER A 477     159.476 186.320 144.852  1.00110.00           O  
ATOM   1161  N   THR A 478     157.459 183.007 142.655  1.00110.21           N  
ATOM   1162  CA  THR A 478     156.373 182.320 141.973  1.00110.21           C  
ATOM   1163  C   THR A 478     156.156 180.940 142.588  1.00110.21           C  
ATOM   1164  O   THR A 478     157.116 180.176 142.755  1.00110.21           O  
ATOM   1165  CB  THR A 478     156.678 182.183 140.480  1.00110.21           C  
ATOM   1166  OG1 THR A 478     156.757 183.483 139.883  1.00110.21           O  
ATOM   1167  CG2 THR A 478     155.594 181.373 139.785  1.00110.21           C  
ATOM   1168  N   PRO A 479     154.920 180.588 142.943  1.00105.62           N  
ATOM   1169  CA  PRO A 479     154.658 179.238 143.459  1.00105.62           C  
ATOM   1170  C   PRO A 479     154.911 178.196 142.380  1.00105.62           C  
ATOM   1171  O   PRO A 479     154.401 178.302 141.263  1.00105.62           O  
ATOM   1172  CB  PRO A 479     153.179 179.288 143.861  1.00105.62           C  
ATOM   1173  CG  PRO A 479     152.854 180.744 143.976  1.00105.62           C  
ATOM   1174  CD  PRO A 479     153.713 181.429 142.962  1.00105.62           C  
ATOM   1175  N   CYS A 480     155.708 177.182 142.724  1.00 96.49           N  
ATOM   1176  CA  CYS A 480     156.042 176.155 141.745  1.00 96.49           C  
ATOM   1177  C   CYS A 480     154.845 175.270 141.428  1.00 96.49           C  
ATOM   1178  O   CYS A 480     154.848 174.576 140.406  1.00 96.49           O  
ATOM   1179  CB  CYS A 480     157.216 175.317 142.249  1.00 96.49           C  
ATOM   1180  SG  CYS A 480     158.677 176.287 142.692  1.00 96.49           S  
ATOM   1181  N   ASN A 481     153.818 175.286 142.283  1.00 92.35           N  
ATOM   1182  CA  ASN A 481     152.585 174.526 142.064  1.00 92.35           C  
ATOM   1183  C   ASN A 481     152.871 173.036 141.884  1.00 92.35           C  
ATOM   1184  O   ASN A 481     152.276 172.366 141.038  1.00 92.35           O  
ATOM   1185  CB  ASN A 481     151.802 175.082 140.872  1.00 92.35           C  
ATOM   1186  CG  ASN A 481     150.379 174.565 140.815  1.00 92.35           C  
ATOM   1187  OD1 ASN A 481     149.461 175.180 141.354  1.00 92.35           O  
ATOM   1188  ND2 ASN A 481     150.191 173.426 140.160  1.00 92.35           N  
ATOM   1189  N   GLY A 482     153.794 172.514 142.685  1.00 91.46           N  
ATOM   1190  CA  GLY A 482     154.185 171.118 142.560  1.00 91.46           C  
ATOM   1191  C   GLY A 482     154.824 170.799 141.226  1.00 91.46           C  
ATOM   1192  O   GLY A 482     154.819 169.640 140.795  1.00 91.46           O  
ATOM   1193  N   VAL A 483     155.379 171.819 140.578  1.00 87.28           N  
ATOM   1194  CA  VAL A 483     155.930 171.682 139.239  1.00 87.28           C  
ATOM   1195  C   VAL A 483     157.341 172.248 139.234  1.00 87.28           C  
ATOM   1196  O   VAL A 483     157.592 173.324 139.788  1.00 87.28           O  
ATOM   1197  CB  VAL A 483     155.041 172.391 138.194  1.00 87.28           C  
ATOM   1198  CG1 VAL A 483     155.880 172.988 137.076  1.00 87.28           C  
ATOM   1199  CG2 VAL A 483     154.009 171.425 137.641  1.00 87.28           C  
ATOM   1200  N   GLU A 484     158.266 171.499 138.611  1.00 93.91           N  
ATOM   1201  CA  GLU A 484     159.639 171.967 138.504  1.00 93.91           C  
ATOM   1202  C   GLU A 484     159.731 173.069 137.457  1.00 93.91           C  
ATOM   1203  O   GLU A 484     159.337 172.881 136.301  1.00 93.91           O  
ATOM   1204  CB  GLU A 484     160.564 170.808 138.143  1.00 93.91           C  
ATOM   1205  CG  GLU A 484     162.015 171.032 138.518  1.00 93.91           C  
ATOM   1206  CD  GLU A 484     162.859 169.789 138.330  1.00 93.91           C  
ATOM   1207  OE1 GLU A 484     162.680 169.098 137.306  1.00 93.91           O  
ATOM   1208  OE2 GLU A 484     163.693 169.497 139.212  1.00 93.91           O  
ATOM   1209  N   GLY A 485     160.254 174.221 137.864  1.00 91.07           N  
ATOM   1210  CA  GLY A 485     160.371 175.364 136.981  1.00 91.07           C  
ATOM   1211  C   GLY A 485     161.562 176.202 137.385  1.00 91.07           C  
ATOM   1212  O   GLY A 485     162.393 175.790 138.197  1.00 91.07           O  
ATOM   1213  N   PHE A 486     161.645 177.391 136.796  1.00 90.69           N  
ATOM   1214  CA  PHE A 486     162.731 178.297 137.135  1.00 90.69           C  
ATOM   1215  C   PHE A 486     162.610 178.737 138.587  1.00 90.69           C  
ATOM   1216  O   PHE A 486     161.519 179.048 139.070  1.00 90.69           O  
ATOM   1217  CB  PHE A 486     162.733 179.503 136.197  1.00 90.69           C  
ATOM   1218  CG  PHE A 486     163.262 179.194 134.825  1.00 90.69           C  
ATOM   1219  CD1 PHE A 486     164.593 179.411 134.517  1.00 90.69           C  
ATOM   1220  CD2 PHE A 486     162.431 178.672 133.849  1.00 90.69           C  
ATOM   1221  CE1 PHE A 486     165.083 179.122 133.260  1.00 90.69           C  
ATOM   1222  CE2 PHE A 486     162.916 178.383 132.589  1.00 90.69           C  
ATOM   1223  CZ  PHE A 486     164.243 178.608 132.295  1.00 90.69           C  
ATOM   1224  N   ASN A 487     163.748 178.738 139.286  1.00 92.71           N  
ATOM   1225  CA  ASN A 487     163.808 178.932 140.732  1.00 92.71           C  
ATOM   1226  C   ASN A 487     163.018 177.863 141.481  1.00 92.71           C  
ATOM   1227  O   ASN A 487     162.570 178.083 142.607  1.00 92.71           O  
ATOM   1228  CB  ASN A 487     163.334 180.332 141.132  1.00 92.71           C  
ATOM   1229  CG  ASN A 487     164.248 181.422 140.613  1.00 92.71           C  
ATOM   1230  OD1 ASN A 487     164.235 181.746 139.426  1.00 92.71           O  
ATOM   1231  ND2 ASN A 487     165.048 181.996 141.504  1.00 92.71           N  
ATOM   1232  N   CYS A 488     162.843 176.700 140.856  1.00 93.57           N  
ATOM   1233  CA  CYS A 488     162.250 175.532 141.491  1.00 93.57           C  
ATOM   1234  C   CYS A 488     163.203 174.362 141.306  1.00 93.57           C  
ATOM   1235  O   CYS A 488     163.692 174.130 140.196  1.00 93.57           O  
ATOM   1236  CB  CYS A 488     160.874 175.204 140.898  1.00 93.57           C  
ATOM   1237  SG  CYS A 488     159.679 176.558 140.947  1.00 93.57           S  
ATOM   1238  N   TYR A 489     163.469 173.631 142.385  1.00 82.48           N  
ATOM   1239  CA  TYR A 489     164.465 172.572 142.355  1.00 82.48           C  
ATOM   1240  C   TYR A 489     163.904 171.297 142.964  1.00 82.48           C  
ATOM   1241  O   TYR A 489     163.024 171.334 143.828  1.00 82.48           O  
ATOM   1242  CB  TYR A 489     165.734 172.962 143.120  1.00 82.48           C  
ATOM   1243  CG  TYR A 489     166.466 174.171 142.591  1.00 82.48           C  
ATOM   1244  CD1 TYR A 489     166.086 175.452 142.962  1.00 82.48           C  
ATOM   1245  CD2 TYR A 489     167.555 174.031 141.744  1.00 82.48           C  
ATOM   1246  CE1 TYR A 489     166.759 176.558 142.493  1.00 82.48           C  
ATOM   1247  CE2 TYR A 489     168.235 175.131 141.271  1.00 82.48           C  
ATOM   1248  CZ  TYR A 489     167.832 176.392 141.648  1.00 82.48           C  
ATOM   1249  OH  TYR A 489     168.501 177.498 141.183  1.00 82.48           O  
ATOM   1250  N   PHE A 490     164.426 170.168 142.497  1.00 71.64           N  
ATOM   1251  CA  PHE A 490     164.199 168.904 143.179  1.00 71.64           C  
ATOM   1252  C   PHE A 490     165.068 168.844 144.434  1.00 71.64           C  
ATOM   1253  O   PHE A 490     166.192 169.349 144.436  1.00 71.64           O  
ATOM   1254  CB  PHE A 490     164.526 167.734 142.251  1.00 71.64           C  
ATOM   1255  CG  PHE A 490     163.969 166.420 142.709  1.00 71.64           C  
ATOM   1256  CD1 PHE A 490     162.676 166.053 142.385  1.00 71.64           C  
ATOM   1257  CD2 PHE A 490     164.738 165.548 143.457  1.00 71.64           C  
ATOM   1258  CE1 PHE A 490     162.160 164.846 142.802  1.00 71.64           C  
ATOM   1259  CE2 PHE A 490     164.226 164.339 143.876  1.00 71.64           C  
ATOM   1260  CZ  PHE A 490     162.936 163.988 143.548  1.00 71.64           C  
ATOM   1261  N   PRO A 491     164.578 168.251 145.521  1.00 73.51           N  
ATOM   1262  CA  PRO A 491     165.375 168.269 146.758  1.00 73.51           C  
ATOM   1263  C   PRO A 491     166.582 167.345 146.726  1.00 73.51           C  
ATOM   1264  O   PRO A 491     167.650 167.722 147.223  1.00 73.51           O  
ATOM   1265  CB  PRO A 491     164.360 167.850 147.829  1.00 73.51           C  
ATOM   1266  CG  PRO A 491     163.338 167.072 147.092  1.00 73.51           C  
ATOM   1267  CD  PRO A 491     163.230 167.705 145.739  1.00 73.51           C  
ATOM   1268  N   LEU A 492     166.458 166.158 146.144  1.00 71.77           N  
ATOM   1269  CA  LEU A 492     167.488 165.132 146.237  1.00 71.77           C  
ATOM   1270  C   LEU A 492     168.519 165.282 145.125  1.00 71.77           C  
ATOM   1271  O   LEU A 492     168.166 165.466 143.957  1.00 71.77           O  
ATOM   1272  CB  LEU A 492     166.867 163.737 146.172  1.00 71.77           C  
ATOM   1273  CG  LEU A 492     165.684 163.453 147.099  1.00 71.77           C  
ATOM   1274  CD1 LEU A 492     165.107 162.092 146.797  1.00 71.77           C  
ATOM   1275  CD2 LEU A 492     166.095 163.529 148.551  1.00 71.77           C  
ATOM   1276  N   GLN A 493     169.794 165.194 145.495  1.00 73.26           N  
ATOM   1277  CA  GLN A 493     170.898 165.179 144.544  1.00 73.26           C  
ATOM   1278  C   GLN A 493     171.707 163.907 144.748  1.00 73.26           C  
ATOM   1279  O   GLN A 493     171.961 163.508 145.889  1.00 73.26           O  
ATOM   1280  CB  GLN A 493     171.795 166.409 144.708  1.00 73.26           C  
ATOM   1281  CG  GLN A 493     172.899 166.507 143.664  1.00 73.26           C  
ATOM   1282  CD  GLN A 493     173.815 167.695 143.885  1.00 73.26           C  
ATOM   1283  OE1 GLN A 493     174.443 167.822 144.935  1.00 73.26           O  
ATOM   1284  NE2 GLN A 493     173.894 168.574 142.894  1.00 73.26           N  
ATOM   1285  N   SER A 494     172.107 163.274 143.649  1.00 72.89           N  
ATOM   1286  CA  SER A 494     172.810 162.002 143.739  1.00 72.89           C  
ATOM   1287  C   SER A 494     174.293 162.211 144.011  1.00 72.89           C  
ATOM   1288  O   SER A 494     174.884 163.212 143.598  1.00 72.89           O  
ATOM   1289  CB  SER A 494     172.625 161.196 142.457  1.00 72.89           C  
ATOM   1290  OG  SER A 494     173.222 159.919 142.579  1.00 72.89           O  
ATOM   1291  N   TYR A 495     174.893 161.251 144.712  1.00 75.68           N  
ATOM   1292  CA  TYR A 495     176.319 161.302 144.997  1.00 75.68           C  
ATOM   1293  C   TYR A 495     177.133 160.973 143.754  1.00 75.68           C  
ATOM   1294  O   TYR A 495     176.684 160.253 142.859  1.00 75.68           O  
ATOM   1295  CB  TYR A 495     176.684 160.316 146.104  1.00 75.68           C  
ATOM   1296  CG  TYR A 495     176.339 160.770 147.499  1.00 75.68           C  
ATOM   1297  CD1 TYR A 495     177.143 161.677 148.170  1.00 75.68           C  
ATOM   1298  CD2 TYR A 495     175.222 160.274 148.155  1.00 75.68           C  
ATOM   1299  CE1 TYR A 495     176.840 162.088 149.448  1.00 75.68           C  
ATOM   1300  CE2 TYR A 495     174.910 160.678 149.435  1.00 75.68           C  
ATOM   1301  CZ  TYR A 495     175.723 161.585 150.076  1.00 75.68           C  
ATOM   1302  OH  TYR A 495     175.419 161.996 151.351  1.00 75.68           O  
ATOM   1303  N   GLY A 496     178.346 161.511 143.706  1.00 86.32           N  
ATOM   1304  CA  GLY A 496     179.303 161.106 142.698  1.00 86.32           C  
ATOM   1305  C   GLY A 496     180.346 160.175 143.278  1.00 86.32           C  
ATOM   1306  O   GLY A 496     181.281 160.623 143.948  1.00 86.32           O  
ATOM   1307  N   PHE A 497     180.199 158.875 143.031  1.00 86.29           N  
ATOM   1308  CA  PHE A 497     181.114 157.864 143.546  1.00 86.29           C  
ATOM   1309  C   PHE A 497     181.832 157.213 142.375  1.00 86.29           C  
ATOM   1310  O   PHE A 497     181.198 156.551 141.547  1.00 86.29           O  
ATOM   1311  CB  PHE A 497     180.372 156.809 144.368  1.00 86.29           C  
ATOM   1312  CG  PHE A 497     179.822 157.324 145.663  1.00 86.29           C  
ATOM   1313  CD1 PHE A 497     180.288 158.505 146.209  1.00 86.29           C  
ATOM   1314  CD2 PHE A 497     178.841 156.622 146.340  1.00 86.29           C  
ATOM   1315  CE1 PHE A 497     179.782 158.978 147.399  1.00 86.29           C  
ATOM   1316  CE2 PHE A 497     178.334 157.089 147.533  1.00 86.29           C  
ATOM   1317  CZ  PHE A 497     178.806 158.269 148.063  1.00 86.29           C  
ATOM   1318  N   GLN A 498     183.148 157.396 142.311  1.00100.63           N  
ATOM   1319  CA  GLN A 498     183.963 156.795 141.270  1.00100.63           C  
ATOM   1320  C   GLN A 498     185.126 156.059 141.924  1.00100.63           C  
ATOM   1321  O   GLN A 498     185.825 156.638 142.774  1.00100.63           O  
ATOM   1322  CB  GLN A 498     184.479 157.852 140.286  1.00100.63           C  
ATOM   1323  CG  GLN A 498     183.381 158.610 139.561  1.00100.63           C  
ATOM   1324  CD  GLN A 498     183.920 159.520 138.475  1.00100.63           C  
ATOM   1325  OE1 GLN A 498     185.076 159.404 138.069  1.00100.63           O  
ATOM   1326  NE2 GLN A 498     183.082 160.432 137.998  1.00100.63           N  
ATOM   1327  N   PRO A 499     185.360 154.792 141.572  1.00100.95           N  
ATOM   1328  CA  PRO A 499     186.503 154.076 142.163  1.00100.95           C  
ATOM   1329  C   PRO A 499     187.840 154.716 141.837  1.00100.95           C  
ATOM   1330  O   PRO A 499     188.798 154.573 142.607  1.00100.95           O  
ATOM   1331  CB  PRO A 499     186.378 152.669 141.564  1.00100.95           C  
ATOM   1332  CG  PRO A 499     185.620 152.867 140.295  1.00100.95           C  
ATOM   1333  CD  PRO A 499     184.654 153.980 140.567  1.00100.95           C  
ATOM   1334  N   THR A 500     187.928 155.420 140.707  1.00108.13           N  
ATOM   1335  CA  THR A 500     189.187 156.047 140.316  1.00108.13           C  
ATOM   1336  C   THR A 500     189.617 157.110 141.320  1.00108.13           C  
ATOM   1337  O   THR A 500     190.799 157.195 141.675  1.00108.13           O  
ATOM   1338  CB  THR A 500     189.057 156.650 138.918  1.00108.13           C  
ATOM   1339  OG1 THR A 500     188.005 157.622 138.912  1.00108.13           O  
ATOM   1340  CG2 THR A 500     188.738 155.563 137.903  1.00108.13           C  
ATOM   1341  N   ASN A 501     188.678 157.929 141.788  1.00101.20           N  
ATOM   1342  CA  ASN A 501     189.011 158.976 142.739  1.00101.20           C  
ATOM   1343  C   ASN A 501     189.442 158.377 144.074  1.00101.20           C  
ATOM   1344  O   ASN A 501     188.953 157.331 144.509  1.00101.20           O  
ATOM   1345  CB  ASN A 501     187.826 159.918 142.946  1.00101.20           C  
ATOM   1346  CG  ASN A 501     187.707 160.953 141.846  1.00101.20           C  
ATOM   1347  OD1 ASN A 501     188.707 161.380 141.268  1.00101.20           O  
ATOM   1348  ND2 ASN A 501     186.480 161.366 141.552  1.00101.20           N  
ATOM   1349  N   GLY A 502     190.375 159.065 144.726  1.00 96.01           N  
ATOM   1350  CA  GLY A 502     190.928 158.594 145.978  1.00 96.01           C  
ATOM   1351  C   GLY A 502     190.084 158.956 147.180  1.00 96.01           C  
ATOM   1352  O   GLY A 502     188.870 158.736 147.184  1.00 96.01           O  
ATOM   1353  N   VAL A 503     190.722 159.523 148.206  1.00 94.64           N  
ATOM   1354  CA  VAL A 503     190.020 159.841 149.446  1.00 94.64           C  
ATOM   1355  C   VAL A 503     188.936 160.884 149.204  1.00 94.64           C  
ATOM   1356  O   VAL A 503     188.014 161.041 150.014  1.00 94.64           O  
ATOM   1357  CB  VAL A 503     191.022 160.308 150.517  1.00 94.64           C  
ATOM   1358  CG1 VAL A 503     192.028 159.207 150.815  1.00 94.64           C  
ATOM   1359  CG2 VAL A 503     191.730 161.572 150.062  1.00 94.64           C  
ATOM   1360  N   GLY A 504     189.032 161.619 148.094  1.00 89.95           N  
ATOM   1361  CA  GLY A 504     188.039 162.641 147.810  1.00 89.95           C  
ATOM   1362  C   GLY A 504     186.655 162.073 147.560  1.00 89.95           C  
ATOM   1363  O   GLY A 504     185.660 162.588 148.077  1.00 89.95           O  
ATOM   1364  N   TYR A 505     186.569 161.001 146.768  1.00 95.03           N  
ATOM   1365  CA  TYR A 505     185.290 160.414 146.368  1.00 95.03           C  
ATOM   1366  C   TYR A 505     185.367 158.893 146.522  1.00 95.03           C  
ATOM   1367  O   TYR A 505     185.801 158.177 145.617  1.00 95.03           O  
ATOM   1368  CB  TYR A 505     184.925 160.815 144.939  1.00 95.03           C  
ATOM   1369  CG  TYR A 505     184.715 162.300 144.757  1.00 95.03           C  
ATOM   1370  CD1 TYR A 505     185.789 163.151 144.534  1.00 95.03           C  
ATOM   1371  CD2 TYR A 505     183.443 162.851 144.803  1.00 95.03           C  
ATOM   1372  CE1 TYR A 505     185.603 164.510 144.368  1.00 95.03           C  
ATOM   1373  CE2 TYR A 505     183.246 164.208 144.636  1.00 95.03           C  
ATOM   1374  CZ  TYR A 505     184.329 165.032 144.419  1.00 95.03           C  
ATOM   1375  OH  TYR A 505     184.138 166.384 144.252  1.00 95.03           O  
ATOM   1376  N   GLN A 506     184.932 158.405 147.683  1.00 86.62           N  
ATOM   1377  CA  GLN A 506     184.854 156.981 147.968  1.00 86.62           C  
ATOM   1378  C   GLN A 506     183.671 156.734 148.896  1.00 86.62           C  
ATOM   1379  O   GLN A 506     183.495 157.469 149.882  1.00 86.62           O  
ATOM   1380  CB  GLN A 506     186.152 156.465 148.603  1.00 86.62           C  
ATOM   1381  CG  GLN A 506     187.233 156.089 147.604  1.00 86.62           C  
ATOM   1382  CD  GLN A 506     188.559 155.775 148.268  1.00 86.62           C  
ATOM   1383  OE1 GLN A 506     189.025 156.517 149.132  1.00 86.62           O  
ATOM   1384  NE2 GLN A 506     189.171 154.667 147.870  1.00 86.62           N  
ATOM   1385  N   PRO A 507     182.841 155.732 148.624  1.00 80.57           N  
ATOM   1386  CA  PRO A 507     181.709 155.456 149.516  1.00 80.57           C  
ATOM   1387  C   PRO A 507     182.196 155.044 150.896  1.00 80.57           C  
ATOM   1388  O   PRO A 507     182.857 154.019 151.060  1.00 80.57           O  
ATOM   1389  CB  PRO A 507     180.971 154.312 148.812  1.00 80.57           C  
ATOM   1390  CG  PRO A 507     181.424 154.378 147.391  1.00 80.57           C  
ATOM   1391  CD  PRO A 507     182.837 154.862 147.439  1.00 80.57           C  
ATOM   1392  N   TYR A 508     181.873 155.862 151.890  1.00 70.90           N  
ATOM   1393  CA  TYR A 508     182.237 155.597 153.279  1.00 70.90           C  
ATOM   1394  C   TYR A 508     180.954 155.321 154.050  1.00 70.90           C  
ATOM   1395  O   TYR A 508     180.377 156.232 154.650  1.00 70.90           O  
ATOM   1396  CB  TYR A 508     183.002 156.770 153.880  1.00 70.90           C  
ATOM   1397  CG  TYR A 508     184.503 156.648 153.778  1.00 70.90           C  
ATOM   1398  CD1 TYR A 508     185.165 156.945 152.596  1.00 70.90           C  
ATOM   1399  CD2 TYR A 508     185.259 156.242 154.867  1.00 70.90           C  
ATOM   1400  CE1 TYR A 508     186.536 156.837 152.500  1.00 70.90           C  
ATOM   1401  CE2 TYR A 508     186.629 156.132 154.781  1.00 70.90           C  
ATOM   1402  CZ  TYR A 508     187.263 156.430 153.596  1.00 70.90           C  
ATOM   1403  OH  TYR A 508     188.630 156.321 153.506  1.00 70.90           O  
ATOM   1404  N   ARG A 509     180.512 154.067 154.041  1.00 65.24           N  
ATOM   1405  CA  ARG A 509     179.292 153.714 154.749  1.00 65.24           C  
ATOM   1406  C   ARG A 509     179.458 153.954 156.242  1.00 65.24           C  
ATOM   1407  O   ARG A 509     180.508 153.672 156.823  1.00 65.24           O  
ATOM   1408  CB  ARG A 509     178.920 152.257 154.478  1.00 65.24           C  
ATOM   1409  CG  ARG A 509     180.109 151.332 154.336  1.00 65.24           C  
ATOM   1410  CD  ARG A 509     179.666 149.910 154.045  1.00 65.24           C  
ATOM   1411  NE  ARG A 509     178.601 149.859 153.052  1.00 65.24           N  
ATOM   1412  CZ  ARG A 509     178.035 148.741 152.621  1.00 65.24           C  
ATOM   1413  NH1 ARG A 509     178.430 147.555 153.055  1.00 65.24           N  
ATOM   1414  NH2 ARG A 509     177.045 148.813 151.737  1.00 65.24           N  
ATOM   1415  N   VAL A 510     178.413 154.491 156.857  1.00 54.67           N  
ATOM   1416  CA  VAL A 510     178.408 154.838 158.271  1.00 54.67           C  
ATOM   1417  C   VAL A 510     177.335 154.009 158.952  1.00 54.67           C  
ATOM   1418  O   VAL A 510     176.219 153.890 158.436  1.00 54.67           O  
ATOM   1419  CB  VAL A 510     178.149 156.339 158.483  1.00 54.67           C  
ATOM   1420  CG1 VAL A 510     178.065 156.661 159.959  1.00 54.67           C  
ATOM   1421  CG2 VAL A 510     179.230 157.158 157.814  1.00 54.67           C  
ATOM   1422  N   VAL A 511     177.671 153.429 160.097  1.00 53.92           N  
ATOM   1423  CA  VAL A 511     176.719 152.684 160.909  1.00 53.92           C  
ATOM   1424  C   VAL A 511     176.692 153.320 162.287  1.00 53.92           C  
ATOM   1425  O   VAL A 511     177.569 153.056 163.118  1.00 53.92           O  
ATOM   1426  CB  VAL A 511     177.083 151.197 160.996  1.00 53.92           C  
ATOM   1427  CG1 VAL A 511     175.981 150.439 161.702  1.00 53.92           C  
ATOM   1428  CG2 VAL A 511     177.318 150.635 159.611  1.00 53.92           C  
ATOM   1429  N   VAL A 512     175.689 154.150 162.533  1.00 54.70           N  
ATOM   1430  CA  VAL A 512     175.565 154.890 163.781  1.00 54.70           C  
ATOM   1431  C   VAL A 512     174.889 153.981 164.795  1.00 54.70           C  
ATOM   1432  O   VAL A 512     173.671 153.784 164.750  1.00 54.70           O  
ATOM   1433  CB  VAL A 512     174.774 156.188 163.585  1.00 54.70           C  
ATOM   1434  CG1 VAL A 512     174.816 157.023 164.849  1.00 54.70           C  
ATOM   1435  CG2 VAL A 512     175.322 156.963 162.404  1.00 54.70           C  
ATOM   1436  N   LEU A 513     175.673 153.428 165.720  1.00 67.14           N  
ATOM   1437  CA  LEU A 513     175.138 152.541 166.753  1.00 67.14           C  
ATOM   1438  C   LEU A 513     174.662 153.383 167.932  1.00 67.14           C  
ATOM   1439  O   LEU A 513     175.284 153.443 168.994  1.00 67.14           O  
ATOM   1440  CB  LEU A 513     176.180 151.516 167.180  1.00 67.14           C  
ATOM   1441  CG  LEU A 513     176.333 150.274 166.301  1.00 67.14           C  
ATOM   1442  CD1 LEU A 513     174.974 149.766 165.860  1.00 67.14           C  
ATOM   1443  CD2 LEU A 513     177.223 150.540 165.107  1.00 67.14           C  
ATOM   1444  N   SER A 514     173.533 154.053 167.731  1.00 74.07           N  
ATOM   1445  CA  SER A 514     172.900 154.776 168.823  1.00 74.07           C  
ATOM   1446  C   SER A 514     172.196 153.794 169.747  1.00 74.07           C  
ATOM   1447  O   SER A 514     171.328 153.032 169.312  1.00 74.07           O  
ATOM   1448  CB  SER A 514     171.906 155.798 168.280  1.00 74.07           C  
ATOM   1449  OG  SER A 514     171.185 156.406 169.336  1.00 74.07           O  
ATOM   1450  N   PHE A 515     172.567 153.807 171.021  1.00 83.10           N  
ATOM   1451  CA  PHE A 515     171.992 152.868 171.976  1.00 83.10           C  
ATOM   1452  C   PHE A 515     171.939 153.531 173.349  1.00 83.10           C  
ATOM   1453  O   PHE A 515     172.059 154.755 173.467  1.00 83.10           O  
ATOM   1454  CB  PHE A 515     172.778 151.543 171.980  1.00 83.10           C  
ATOM   1455  CG  PHE A 515     174.273 151.710 172.020  1.00 83.10           C  
ATOM   1456  CD1 PHE A 515     174.902 152.260 173.123  1.00 83.10           C  
ATOM   1457  CD2 PHE A 515     175.053 151.282 170.958  1.00 83.10           C  
ATOM   1458  CE1 PHE A 515     176.274 152.403 173.156  1.00 83.10           C  
ATOM   1459  CE2 PHE A 515     176.426 151.418 170.988  1.00 83.10           C  
ATOM   1460  CZ  PHE A 515     177.037 151.982 172.087  1.00 83.10           C  
ATOM   1461  N   GLU A 516     171.748 152.713 174.386  1.00104.56           N  
ATOM   1462  CA  GLU A 516     171.602 153.174 175.767  1.00104.56           C  
ATOM   1463  C   GLU A 516     170.419 154.131 175.906  1.00104.56           C  
ATOM   1464  O   GLU A 516     170.567 155.294 176.286  1.00104.56           O  
ATOM   1465  CB  GLU A 516     172.893 153.813 176.284  1.00104.56           C  
ATOM   1466  CG  GLU A 516     172.810 154.242 177.741  1.00104.56           C  
ATOM   1467  CD  GLU A 516     174.107 154.829 178.258  1.00104.56           C  
ATOM   1468  OE1 GLU A 516     175.069 154.939 177.468  1.00104.56           O  
ATOM   1469  OE2 GLU A 516     174.166 155.184 179.453  1.00104.56           O  
ATOM   1470  N   LEU A 517     169.227 153.623 175.584  1.00111.39           N  
ATOM   1471  CA  LEU A 517     168.014 154.418 175.745  1.00111.39           C  
ATOM   1472  C   LEU A 517     167.751 154.738 177.210  1.00111.39           C  
ATOM   1473  O   LEU A 517     167.300 155.842 177.539  1.00111.39           O  
ATOM   1474  CB  LEU A 517     166.819 153.684 175.136  1.00111.39           C  
ATOM   1475  CG  LEU A 517     166.456 154.006 173.683  1.00111.39           C  
ATOM   1476  CD1 LEU A 517     166.100 155.478 173.537  1.00111.39           C  
ATOM   1477  CD2 LEU A 517     167.581 153.625 172.732  1.00111.39           C  
ATOM   1478  N   LEU A 518     168.027 153.784 178.102  1.00114.47           N  
ATOM   1479  CA  LEU A 518     167.727 153.913 179.530  1.00114.47           C  
ATOM   1480  C   LEU A 518     166.240 154.182 179.754  1.00114.47           C  
ATOM   1481  O   LEU A 518     165.853 155.125 180.447  1.00114.47           O  
ATOM   1482  CB  LEU A 518     168.591 154.994 180.188  1.00114.47           C  
ATOM   1483  CG  LEU A 518     168.752 154.920 181.708  1.00114.47           C  
ATOM   1484  CD1 LEU A 518     169.360 153.588 182.115  1.00114.47           C  
ATOM   1485  CD2 LEU A 518     169.598 156.074 182.218  1.00114.47           C  
ATOM   1486  N   HIS A 519     165.396 153.345 179.147  1.00119.12           N  
ATOM   1487  CA  HIS A 519     163.952 153.477 179.249  1.00119.12           C  
ATOM   1488  C   HIS A 519     163.242 152.170 179.575  1.00119.12           C  
ATOM   1489  O   HIS A 519     162.048 152.199 179.895  1.00119.12           O  
ATOM   1490  CB  HIS A 519     163.379 154.048 177.941  1.00119.12           C  
ATOM   1491  CG  HIS A 519     161.952 154.490 178.043  1.00119.12           C  
ATOM   1492  ND1 HIS A 519     161.573 155.632 178.714  1.00119.12           N  
ATOM   1493  CD2 HIS A 519     160.812 153.943 177.558  1.00119.12           C  
ATOM   1494  CE1 HIS A 519     160.261 155.770 178.639  1.00119.12           C  
ATOM   1495  NE2 HIS A 519     159.775 154.758 177.942  1.00119.12           N  
ATOM   1496  N   ALA A 520     163.934 151.038 179.521  1.00110.21           N  
ATOM   1497  CA  ALA A 520     163.311 149.735 179.708  1.00110.21           C  
ATOM   1498  C   ALA A 520     164.384 148.765 180.179  1.00110.21           C  
ATOM   1499  O   ALA A 520     165.578 149.091 180.154  1.00110.21           O  
ATOM   1500  CB  ALA A 520     162.650 149.243 178.408  1.00110.21           C  
ATOM   1501  N   PRO A 521     163.996 147.575 180.644  1.00104.77           N  
ATOM   1502  CA  PRO A 521     165.005 146.558 180.960  1.00104.77           C  
ATOM   1503  C   PRO A 521     165.872 146.254 179.747  1.00104.77           C  
ATOM   1504  O   PRO A 521     165.388 146.162 178.617  1.00104.77           O  
ATOM   1505  CB  PRO A 521     164.166 145.347 181.376  1.00104.77           C  
ATOM   1506  CG  PRO A 521     162.934 145.947 181.946  1.00104.77           C  
ATOM   1507  CD  PRO A 521     162.659 147.180 181.126  1.00104.77           C  
ATOM   1508  N   ALA A 522     167.170 146.102 179.996  1.00104.70           N  
ATOM   1509  CA  ALA A 522     168.126 145.944 178.911  1.00104.70           C  
ATOM   1510  C   ALA A 522     168.019 144.559 178.290  1.00104.70           C  
ATOM   1511  O   ALA A 522     168.067 143.544 178.991  1.00104.70           O  
ATOM   1512  CB  ALA A 522     169.544 146.182 179.427  1.00104.70           C  
ATOM   1513  N   THR A 523     167.874 144.520 176.967  1.00105.10           N  
ATOM   1514  CA  THR A 523     167.901 143.270 176.221  1.00105.10           C  
ATOM   1515  C   THR A 523     169.260 142.982 175.601  1.00105.10           C  
ATOM   1516  O   THR A 523     169.434 141.922 174.992  1.00105.10           O  
ATOM   1517  CB  THR A 523     166.836 143.279 175.117  1.00105.10           C  
ATOM   1518  OG1 THR A 523     166.874 142.036 174.405  1.00105.10           O  
ATOM   1519  CG2 THR A 523     167.088 144.419 174.145  1.00105.10           C  
ATOM   1520  N   VAL A 524     170.218 143.896 175.737  1.00105.04           N  
ATOM   1521  CA  VAL A 524     171.564 143.729 175.205  1.00105.04           C  
ATOM   1522  C   VAL A 524     172.543 143.911 176.355  1.00105.04           C  
ATOM   1523  O   VAL A 524     172.500 144.929 177.058  1.00105.04           O  
ATOM   1524  CB  VAL A 524     171.860 144.725 174.074  1.00105.04           C  
ATOM   1525  CG1 VAL A 524     173.191 144.399 173.420  1.00105.04           C  
ATOM   1526  CG2 VAL A 524     170.738 144.718 173.049  1.00105.04           C  
ATOM   1527  N   CYS A 525     173.421 142.930 176.547  1.00110.39           N  
ATOM   1528  CA  CYS A 525     174.427 142.981 177.597  1.00110.39           C  
ATOM   1529  C   CYS A 525     175.673 142.248 177.126  1.00110.39           C  
ATOM   1530  O   CYS A 525     175.631 141.445 176.190  1.00110.39           O  
ATOM   1531  CB  CYS A 525     173.921 142.365 178.909  1.00110.39           C  
ATOM   1532  SG  CYS A 525     172.652 143.310 179.800  1.00110.39           S  
ATOM   1533  N   GLY A 526     176.790 142.534 177.789  1.00105.23           N  
ATOM   1534  CA  GLY A 526     178.051 141.918 177.456  1.00105.23           C  
ATOM   1535  C   GLY A 526     178.092 140.448 177.821  1.00105.23           C  
ATOM   1536  O   GLY A 526     177.375 139.985 178.713  1.00105.23           O  
ATOM   1537  N   PRO A 527     178.935 139.684 177.129  1.00100.01           N  
ATOM   1538  CA  PRO A 527     179.033 138.250 177.421  1.00100.01           C  
ATOM   1539  C   PRO A 527     179.624 138.001 178.801  1.00100.01           C  
ATOM   1540  O   PRO A 527     180.390 138.810 179.327  1.00100.01           O  
ATOM   1541  CB  PRO A 527     179.951 137.726 176.311  1.00100.01           C  
ATOM   1542  CG  PRO A 527     180.761 138.910 175.911  1.00100.01           C  
ATOM   1543  CD  PRO A 527     179.846 140.093 176.048  1.00100.01           C  
ATOM   1544  N   LYS A 528     179.252 136.868 179.385  1.00 91.51           N  
ATOM   1545  CA  LYS A 528     179.747 136.481 180.698  1.00 91.51           C  
ATOM   1546  C   LYS A 528     180.454 135.133 180.620  1.00 91.51           C  
ATOM   1547  O   LYS A 528     179.813 134.085 180.544  1.00 91.51           O  
ATOM   1548  CB  LYS A 528     178.598 136.426 181.706  1.00 91.51           C  
ATOM   1549  CG  LYS A 528     179.009 136.024 183.113  1.00 91.51           C  
ATOM   1550  CD  LYS A 528     177.802 135.987 184.038  1.00 91.51           C  
ATOM   1551  CE  LYS A 528     178.187 135.565 185.445  1.00 91.51           C  
ATOM   1552  NZ  LYS A 528     177.001 135.527 186.345  1.00 91.51           N  
TER    1553      LYS A 528                                                      
ATOM   1554  N   GLN H   1     176.428 154.370 125.218  1.00152.06           N  
ATOM   1555  CA  GLN H   1     176.491 153.894 123.841  1.00152.06           C  
ATOM   1556  C   GLN H   1     175.099 153.562 123.317  1.00152.06           C  
ATOM   1557  O   GLN H   1     174.558 154.275 122.473  1.00152.06           O  
ATOM   1558  CB  GLN H   1     177.402 152.670 123.738  1.00152.06           C  
ATOM   1559  CG  GLN H   1     177.548 152.122 122.328  1.00152.06           C  
ATOM   1560  CD  GLN H   1     178.546 150.984 122.245  1.00152.06           C  
ATOM   1561  OE1 GLN H   1     179.223 150.664 123.223  1.00152.06           O  
ATOM   1562  NE2 GLN H   1     178.643 150.365 121.074  1.00152.06           N  
ATOM   1563  N   VAL H   2     174.522 152.472 123.823  1.00142.10           N  
ATOM   1564  CA  VAL H   2     173.181 152.078 123.405  1.00142.10           C  
ATOM   1565  C   VAL H   2     172.163 152.982 124.085  1.00142.10           C  
ATOM   1566  O   VAL H   2     172.132 153.096 125.317  1.00142.10           O  
ATOM   1567  CB  VAL H   2     172.928 150.599 123.715  1.00142.10           C  
ATOM   1568  CG1 VAL H   2     173.614 149.720 122.682  1.00142.10           C  
ATOM   1569  CG2 VAL H   2     173.422 150.252 125.112  1.00142.10           C  
ATOM   1570  N   GLN H   3     171.332 153.639 123.283  1.00122.46           N  
ATOM   1571  CA  GLN H   3     170.307 154.520 123.823  1.00122.46           C  
ATOM   1572  C   GLN H   3     169.232 153.713 124.541  1.00122.46           C  
ATOM   1573  O   GLN H   3     168.981 152.547 124.222  1.00122.46           O  
ATOM   1574  CB  GLN H   3     169.672 155.352 122.708  1.00122.46           C  
ATOM   1575  CG  GLN H   3     170.664 156.073 121.807  1.00122.46           C  
ATOM   1576  CD  GLN H   3     171.175 155.198 120.676  1.00122.46           C  
ATOM   1577  OE1 GLN H   3     170.886 154.002 120.621  1.00122.46           O  
ATOM   1578  NE2 GLN H   3     171.935 155.793 119.765  1.00122.46           N  
ATOM   1579  N   LEU H   4     168.599 154.344 125.527  1.00101.27           N  
ATOM   1580  CA  LEU H   4     167.488 153.705 126.218  1.00101.27           C  
ATOM   1581  C   LEU H   4     166.336 153.481 125.249  1.00101.27           C  
ATOM   1582  O   LEU H   4     165.796 154.431 124.677  1.00101.27           O  
ATOM   1583  CB  LEU H   4     167.029 154.559 127.400  1.00101.27           C  
ATOM   1584  CG  LEU H   4     168.005 154.752 128.562  1.00101.27           C  
ATOM   1585  CD1 LEU H   4     168.803 153.482 128.818  1.00101.27           C  
ATOM   1586  CD2 LEU H   4     168.924 155.940 128.324  1.00101.27           C  
ATOM   1587  N   VAL H   5     165.962 152.224 125.068  1.00100.81           N  
ATOM   1588  CA  VAL H   5     164.934 151.853 124.103  1.00100.81           C  
ATOM   1589  C   VAL H   5     163.579 152.313 124.618  1.00100.81           C  
ATOM   1590  O   VAL H   5     163.226 152.110 125.784  1.00100.81           O  
ATOM   1591  CB  VAL H   5     164.951 150.334 123.833  1.00100.81           C  
ATOM   1592  CG1 VAL H   5     163.900 149.964 122.797  1.00100.81           C  
ATOM   1593  CG2 VAL H   5     166.333 149.895 123.376  1.00100.81           C  
ATOM   1594  N   GLN H   6     162.814 152.950 123.735  1.00 92.25           N  
ATOM   1595  CA  GLN H   6     161.493 153.462 124.062  1.00 92.25           C  
ATOM   1596  C   GLN H   6     160.514 153.103 122.955  1.00 92.25           C  
ATOM   1597  O   GLN H   6     160.888 152.985 121.785  1.00 92.25           O  
ATOM   1598  CB  GLN H   6     161.519 154.978 124.264  1.00 92.25           C  
ATOM   1599  CG  GLN H   6     162.270 155.721 123.178  1.00 92.25           C  
ATOM   1600  CD  GLN H   6     162.386 157.202 123.460  1.00 92.25           C  
ATOM   1601  OE1 GLN H   6     163.344 157.851 123.041  1.00 92.25           O  
ATOM   1602  NE2 GLN H   6     161.407 157.748 124.171  1.00 92.25           N  
ATOM   1603  N   SER H   7     159.251 152.934 123.338  1.00 95.14           N  
ATOM   1604  CA  SER H   7     158.179 152.598 122.410  1.00 95.14           C  
ATOM   1605  C   SER H   7     157.042 153.589 122.600  1.00 95.14           C  
ATOM   1606  O   SER H   7     156.625 153.845 123.734  1.00 95.14           O  
ATOM   1607  CB  SER H   7     157.686 151.168 122.633  1.00 95.14           C  
ATOM   1608  OG  SER H   7     157.162 151.011 123.940  1.00 95.14           O  
ATOM   1609  N   GLY H   8     156.545 154.143 121.495  1.00103.90           N  
ATOM   1610  CA  GLY H   8     155.466 155.106 121.557  1.00103.90           C  
ATOM   1611  C   GLY H   8     154.623 155.066 120.298  1.00103.90           C  
ATOM   1612  O   GLY H   8     155.097 154.721 119.213  1.00103.90           O  
ATOM   1613  N   ALA H   9     153.356 155.435 120.464  1.00107.67           N  
ATOM   1614  CA  ALA H   9     152.420 155.436 119.349  1.00107.67           C  
ATOM   1615  C   ALA H   9     152.699 156.602 118.406  1.00107.67           C  
ATOM   1616  O   ALA H   9     153.216 157.647 118.807  1.00107.67           O  
ATOM   1617  CB  ALA H   9     150.982 155.509 119.859  1.00107.67           C  
ATOM   1618  N   GLU H  10     152.342 156.413 117.138  1.00107.52           N  
ATOM   1619  CA  GLU H  10     152.570 157.414 116.108  1.00107.52           C  
ATOM   1620  C   GLU H  10     151.302 157.627 115.293  1.00107.52           C  
ATOM   1621  O   GLU H  10     150.504 156.706 115.097  1.00107.52           O  
ATOM   1622  CB  GLU H  10     153.738 157.014 115.184  1.00107.52           C  
ATOM   1623  CG  GLU H  10     154.093 158.043 114.117  1.00107.52           C  
ATOM   1624  CD  GLU H  10     155.276 157.632 113.262  1.00107.52           C  
ATOM   1625  OE1 GLU H  10     155.809 156.521 113.469  1.00107.52           O  
ATOM   1626  OE2 GLU H  10     155.674 158.421 112.377  1.00107.52           O  
ATOM   1627  N   MET H  11     151.132 158.863 114.822  1.00 99.01           N  
ATOM   1628  CA  MET H  11     149.984 159.264 114.007  1.00 99.01           C  
ATOM   1629  C   MET H  11     148.664 158.958 114.709  1.00 99.01           C  
ATOM   1630  O   MET H  11     147.833 158.190 114.219  1.00 99.01           O  
ATOM   1631  CB  MET H  11     150.035 158.618 112.621  1.00 99.01           C  
ATOM   1632  CG  MET H  11     149.109 159.277 111.606  1.00 99.01           C  
ATOM   1633  SD  MET H  11     149.501 158.846 109.903  1.00 99.01           S  
ATOM   1634  CE  MET H  11     151.128 159.577 109.742  1.00 99.01           C  
ATOM   1635  N   LYS H  12     148.478 159.555 115.882  1.00 97.20           N  
ATOM   1636  CA  LYS H  12     147.193 159.488 116.561  1.00 97.20           C  
ATOM   1637  C   LYS H  12     146.318 160.666 116.149  1.00 97.20           C  
ATOM   1638  O   LYS H  12     146.816 161.745 115.817  1.00 97.20           O  
ATOM   1639  CB  LYS H  12     147.392 159.477 118.074  1.00 97.20           C  
ATOM   1640  CG  LYS H  12     147.927 158.166 118.624  1.00 97.20           C  
ATOM   1641  CD  LYS H  12     146.861 157.084 118.634  1.00 97.20           C  
ATOM   1642  CE  LYS H  12     147.372 155.818 119.305  1.00 97.20           C  
ATOM   1643  NZ  LYS H  12     146.335 154.752 119.354  1.00 97.20           N  
ATOM   1644  N   ASN H  13     145.005 160.454 116.168  1.00100.96           N  
ATOM   1645  CA  ASN H  13     144.068 161.494 115.775  1.00100.96           C  
ATOM   1646  C   ASN H  13     143.858 162.490 116.916  1.00100.96           C  
ATOM   1647  O   ASN H  13     144.345 162.312 118.036  1.00100.96           O  
ATOM   1648  CB  ASN H  13     142.736 160.882 115.343  1.00100.96           C  
ATOM   1649  CG  ASN H  13     142.804 160.247 113.968  1.00100.96           C  
ATOM   1650  OD1 ASN H  13     143.501 160.736 113.079  1.00100.96           O  
ATOM   1651  ND2 ASN H  13     142.077 159.152 113.785  1.00100.96           N  
ATOM   1652  N   PHE H  14     143.117 163.553 116.611  1.00 93.97           N  
ATOM   1653  CA  PHE H  14     142.914 164.632 117.569  1.00 93.97           C  
ATOM   1654  C   PHE H  14     142.187 164.135 118.811  1.00 93.97           C  
ATOM   1655  O   PHE H  14     141.300 163.282 118.735  1.00 93.97           O  
ATOM   1656  CB  PHE H  14     142.121 165.766 116.921  1.00 93.97           C  
ATOM   1657  CG  PHE H  14     141.358 166.608 117.899  1.00 93.97           C  
ATOM   1658  CD1 PHE H  14     141.993 167.599 118.626  1.00 93.97           C  
ATOM   1659  CD2 PHE H  14     140.003 166.407 118.095  1.00 93.97           C  
ATOM   1660  CE1 PHE H  14     141.292 168.373 119.527  1.00 93.97           C  
ATOM   1661  CE2 PHE H  14     139.295 167.179 118.996  1.00 93.97           C  
ATOM   1662  CZ  PHE H  14     139.940 168.163 119.712  1.00 93.97           C  
ATOM   1663  N   GLY H  15     142.579 164.675 119.963  1.00 98.20           N  
ATOM   1664  CA  GLY H  15     141.945 164.361 121.223  1.00 98.20           C  
ATOM   1665  C   GLY H  15     142.368 163.055 121.852  1.00 98.20           C  
ATOM   1666  O   GLY H  15     141.972 162.779 122.991  1.00 98.20           O  
ATOM   1667  N   SER H  16     143.161 162.247 121.158  1.00 98.92           N  
ATOM   1668  CA  SER H  16     143.585 160.964 121.691  1.00 98.92           C  
ATOM   1669  C   SER H  16     144.762 161.142 122.644  1.00 98.92           C  
ATOM   1670  O   SER H  16     145.310 162.235 122.803  1.00 98.92           O  
ATOM   1671  CB  SER H  16     143.961 160.013 120.557  1.00 98.92           C  
ATOM   1672  OG  SER H  16     144.920 160.605 119.702  1.00 98.92           O  
ATOM   1673  N   SER H  17     145.142 160.045 123.291  1.00 97.30           N  
ATOM   1674  CA  SER H  17     146.257 160.025 124.228  1.00 97.30           C  
ATOM   1675  C   SER H  17     147.301 159.033 123.736  1.00 97.30           C  
ATOM   1676  O   SER H  17     146.967 157.893 123.396  1.00 97.30           O  
ATOM   1677  CB  SER H  17     145.785 159.658 125.634  1.00 97.30           C  
ATOM   1678  OG  SER H  17     145.197 158.369 125.653  1.00 97.30           O  
ATOM   1679  N   VAL H  18     148.558 159.466 123.700  1.00 92.52           N  
ATOM   1680  CA  VAL H  18     149.678 158.620 123.307  1.00 92.52           C  
ATOM   1681  C   VAL H  18     150.364 158.115 124.566  1.00 92.52           C  
ATOM   1682  O   VAL H  18     150.630 158.891 125.492  1.00 92.52           O  
ATOM   1683  CB  VAL H  18     150.667 159.380 122.406  1.00 92.52           C  
ATOM   1684  CG1 VAL H  18     150.071 159.590 121.032  1.00 92.52           C  
ATOM   1685  CG2 VAL H  18     151.037 160.718 123.025  1.00 92.52           C  
ATOM   1686  N   LYS H  19     150.637 156.815 124.613  1.00 90.69           N  
ATOM   1687  CA  LYS H  19     151.338 156.200 125.732  1.00 90.69           C  
ATOM   1688  C   LYS H  19     152.710 155.746 125.254  1.00 90.69           C  
ATOM   1689  O   LYS H  19     152.816 154.800 124.467  1.00 90.69           O  
ATOM   1690  CB  LYS H  19     150.543 155.026 126.303  1.00 90.69           C  
ATOM   1691  CG  LYS H  19     151.000 154.583 127.685  1.00 90.69           C  
ATOM   1692  CD  LYS H  19     149.985 153.651 128.329  1.00 90.69           C  
ATOM   1693  CE  LYS H  19     150.308 153.396 129.793  1.00 90.69           C  
ATOM   1694  NZ  LYS H  19     150.347 154.657 130.584  1.00 90.69           N  
ATOM   1695  N   VAL H  20     153.753 156.424 125.728  1.00 89.97           N  
ATOM   1696  CA  VAL H  20     155.130 156.143 125.342  1.00 89.97           C  
ATOM   1697  C   VAL H  20     155.937 155.866 126.602  1.00 89.97           C  
ATOM   1698  O   VAL H  20     155.834 156.606 127.587  1.00 89.97           O  
ATOM   1699  CB  VAL H  20     155.741 157.304 124.536  1.00 89.97           C  
ATOM   1700  CG1 VAL H  20     155.438 158.633 125.202  1.00 89.97           C  
ATOM   1701  CG2 VAL H  20     157.240 157.114 124.380  1.00 89.97           C  
ATOM   1702  N   SER H  21     156.727 154.794 126.574  1.00 91.99           N  
ATOM   1703  CA  SER H  21     157.556 154.401 127.705  1.00 91.99           C  
ATOM   1704  C   SER H  21     158.933 153.995 127.209  1.00 91.99           C  
ATOM   1705  O   SER H  21     159.077 153.556 126.065  1.00 91.99           O  
ATOM   1706  CB  SER H  21     156.922 153.247 128.483  1.00 91.99           C  
ATOM   1707  OG  SER H  21     156.747 152.112 127.655  1.00 91.99           O  
ATOM   1708  N   CYS H  22     159.936 154.141 128.070  1.00 96.97           N  
ATOM   1709  CA  CYS H  22     161.299 153.710 127.788  1.00 96.97           C  
ATOM   1710  C   CYS H  22     161.747 152.718 128.851  1.00 96.97           C  
ATOM   1711  O   CYS H  22     161.314 152.802 130.005  1.00 96.97           O  
ATOM   1712  CB  CYS H  22     162.261 154.898 127.739  1.00 96.97           C  
ATOM   1713  SG  CYS H  22     161.913 156.222 128.914  1.00 96.97           S  
ATOM   1714  N   LYS H  23     162.608 151.782 128.460  1.00102.91           N  
ATOM   1715  CA  LYS H  23     163.126 150.769 129.374  1.00102.91           C  
ATOM   1716  C   LYS H  23     164.395 151.296 130.032  1.00102.91           C  
ATOM   1717  O   LYS H  23     165.395 151.552 129.354  1.00102.91           O  
ATOM   1718  CB  LYS H  23     163.394 149.459 128.638  1.00102.91           C  
ATOM   1719  CG  LYS H  23     164.315 148.514 129.395  1.00102.91           C  
ATOM   1720  CD  LYS H  23     164.293 147.115 128.804  1.00102.91           C  
ATOM   1721  CE  LYS H  23     163.012 146.386 129.172  1.00102.91           C  
ATOM   1722  NZ  LYS H  23     162.865 146.244 130.649  1.00102.91           N  
ATOM   1723  N   ALA H  24     164.353 151.456 131.351  1.00103.39           N  
ATOM   1724  CA  ALA H  24     165.521 151.912 132.087  1.00103.39           C  
ATOM   1725  C   ALA H  24     166.552 150.796 132.202  1.00103.39           C  
ATOM   1726  O   ALA H  24     166.214 149.617 132.334  1.00103.39           O  
ATOM   1727  CB  ALA H  24     165.122 152.400 133.479  1.00103.39           C  
ATOM   1728  N   SER H  25     167.828 151.183 132.142  1.00103.28           N  
ATOM   1729  CA  SER H  25     168.902 150.207 132.286  1.00103.28           C  
ATOM   1730  C   SER H  25     168.899 149.585 133.677  1.00103.28           C  
ATOM   1731  O   SER H  25     169.108 148.376 133.826  1.00103.28           O  
ATOM   1732  CB  SER H  25     170.251 150.864 131.993  1.00103.28           C  
ATOM   1733  OG  SER H  25     171.314 149.940 132.150  1.00103.28           O  
ATOM   1734  N   GLY H  26     168.662 150.395 134.706  1.00102.57           N  
ATOM   1735  CA  GLY H  26     168.640 149.900 136.068  1.00102.57           C  
ATOM   1736  C   GLY H  26     169.396 150.787 137.033  1.00102.57           C  
ATOM   1737  O   GLY H  26     170.553 151.141 136.788  1.00102.57           O  
ATOM   1738  N   GLY H  27     168.754 151.154 138.132  1.00 94.64           N  
ATOM   1739  CA  GLY H  27     169.352 151.999 139.136  1.00 94.64           C  
ATOM   1740  C   GLY H  27     168.400 153.104 139.529  1.00 94.64           C  
ATOM   1741  O   GLY H  27     167.212 153.072 139.214  1.00 94.64           O  
ATOM   1742  N   THR H  28     168.938 154.099 140.230  1.00 89.58           N  
ATOM   1743  CA  THR H  28     168.166 155.249 140.681  1.00 89.58           C  
ATOM   1744  C   THR H  28     168.290 156.444 139.744  1.00 89.58           C  
ATOM   1745  O   THR H  28     167.963 157.566 140.144  1.00 89.58           O  
ATOM   1746  CB  THR H  28     168.599 155.647 142.096  1.00 89.58           C  
ATOM   1747  OG1 THR H  28     169.997 155.962 142.091  1.00 89.58           O  
ATOM   1748  CG2 THR H  28     168.366 154.503 143.070  1.00 89.58           C  
ATOM   1749  N   PHE H  29     168.765 156.237 138.518  1.00 81.98           N  
ATOM   1750  CA  PHE H  29     168.875 157.333 137.566  1.00 81.98           C  
ATOM   1751  C   PHE H  29     167.494 157.848 137.190  1.00 81.98           C  
ATOM   1752  O   PHE H  29     166.620 157.075 136.789  1.00 81.98           O  
ATOM   1753  CB  PHE H  29     169.614 156.869 136.314  1.00 81.98           C  
ATOM   1754  CG  PHE H  29     170.868 156.109 136.599  1.00 81.98           C  
ATOM   1755  CD1 PHE H  29     171.194 154.990 135.855  1.00 81.98           C  
ATOM   1756  CD2 PHE H  29     171.726 156.513 137.605  1.00 81.98           C  
ATOM   1757  CE1 PHE H  29     172.349 154.284 136.113  1.00 81.98           C  
ATOM   1758  CE2 PHE H  29     172.881 155.811 137.869  1.00 81.98           C  
ATOM   1759  CZ  PHE H  29     173.195 154.695 137.121  1.00 81.98           C  
ATOM   1760  N   SER H  30     167.304 159.157 137.307  1.00 74.95           N  
ATOM   1761  CA  SER H  30     166.033 159.758 136.939  1.00 74.95           C  
ATOM   1762  C   SER H  30     165.823 159.675 135.433  1.00 74.95           C  
ATOM   1763  O   SER H  30     166.775 159.591 134.654  1.00 74.95           O  
ATOM   1764  CB  SER H  30     165.976 161.215 137.388  1.00 74.95           C  
ATOM   1765  OG  SER H  30     166.787 162.030 136.563  1.00 74.95           O  
ATOM   1766  N   ILE H  31     164.559 159.699 135.027  1.00 77.02           N  
ATOM   1767  CA  ILE H  31     164.179 159.630 133.622  1.00 77.02           C  
ATOM   1768  C   ILE H  31     163.517 160.944 133.241  1.00 77.02           C  
ATOM   1769  O   ILE H  31     162.507 161.336 133.839  1.00 77.02           O  
ATOM   1770  CB  ILE H  31     163.243 158.447 133.343  1.00 77.02           C  
ATOM   1771  CG1 ILE H  31     163.996 157.128 133.496  1.00 77.02           C  
ATOM   1772  CG2 ILE H  31     162.662 158.567 131.951  1.00 77.02           C  
ATOM   1773  CD1 ILE H  31     165.092 156.937 132.476  1.00 77.02           C  
ATOM   1774  N   ASN H  32     164.090 161.752 132.348  1.00 75.45           N  
ATOM   1775  CA  ASN H  32     163.448 163.076 132.101  1.00 75.45           C  
ATOM   1776  C   ASN H  32     162.844 163.154 130.706  1.00 75.45           C  
ATOM   1777  O   ASN H  32     163.347 162.484 129.786  1.00 75.45           O  
ATOM   1778  CB  ASN H  32     164.351 164.285 132.321  1.00 75.45           C  
ATOM   1779  CG  ASN H  32     164.658 164.521 133.777  1.00 75.45           C  
ATOM   1780  OD1 ASN H  32     164.725 163.569 134.546  1.00 75.45           O  
ATOM   1781  ND2 ASN H  32     164.835 165.777 134.154  1.00 75.45           N  
ATOM   1782  N   TRP H  36     161.805 163.981 130.597  1.00 80.35           N  
ATOM   1783  CA  TRP H  36     160.949 164.050 129.392  1.00 80.35           C  
ATOM   1784  C   TRP H  36     161.266 165.324 128.623  1.00 80.35           C  
ATOM   1785  O   TRP H  36     161.152 166.403 129.208  1.00 80.35           O  
ATOM   1786  CB  TRP H  36     159.476 163.880 129.766  1.00 80.35           C  
ATOM   1787  CG  TRP H  36     159.182 162.450 130.100  1.00 80.35           C  
ATOM   1788  CD1 TRP H  36     158.884 161.938 131.329  1.00 80.35           C  
ATOM   1789  CD2 TRP H  36     159.227 161.327 129.199  1.00 80.35           C  
ATOM   1790  NE1 TRP H  36     158.711 160.583 131.249  1.00 80.35           N  
ATOM   1791  CE2 TRP H  36     158.914 160.180 129.957  1.00 80.35           C  
ATOM   1792  CE3 TRP H  36     159.480 161.179 127.831  1.00 80.35           C  
ATOM   1793  CZ2 TRP H  36     158.852 158.909 129.390  1.00 80.35           C  
ATOM   1794  CZ3 TRP H  36     159.417 159.924 127.271  1.00 80.35           C  
ATOM   1795  CH2 TRP H  36     159.107 158.805 128.042  1.00 80.35           C  
ATOM   1796  N   VAL H  37     161.670 165.186 127.372  1.00 77.32           N  
ATOM   1797  CA  VAL H  37     162.087 166.302 126.534  1.00 77.32           C  
ATOM   1798  C   VAL H  37     161.237 166.291 125.274  1.00 77.32           C  
ATOM   1799  O   VAL H  37     161.179 165.281 124.563  1.00 77.32           O  
ATOM   1800  CB  VAL H  37     163.581 166.225 126.189  1.00 77.32           C  
ATOM   1801  CG1 VAL H  37     163.787 166.432 124.704  1.00 77.32           C  
ATOM   1802  CG2 VAL H  37     164.359 167.250 126.989  1.00 77.32           C  
ATOM   1803  N   ARG H  38     160.584 167.413 124.995  1.00 81.96           N  
ATOM   1804  CA  ARG H  38     159.757 167.566 123.808  1.00 81.96           C  
ATOM   1805  C   ARG H  38     160.473 168.440 122.790  1.00 81.96           C  
ATOM   1806  O   ARG H  38     160.939 169.534 123.117  1.00 81.96           O  
ATOM   1807  CB  ARG H  38     158.405 168.185 124.165  1.00 81.96           C  
ATOM   1808  CG  ARG H  38     157.613 168.670 122.969  1.00 81.96           C  
ATOM   1809  CD  ARG H  38     156.372 169.439 123.386  1.00 81.96           C  
ATOM   1810  NE  ARG H  38     155.715 170.052 122.238  1.00 81.96           N  
ATOM   1811  CZ  ARG H  38     154.638 170.821 122.308  1.00 81.96           C  
ATOM   1812  NH1 ARG H  38     154.059 171.097 123.465  1.00 81.96           N  
ATOM   1813  NH2 ARG H  38     154.127 171.327 121.189  1.00 81.96           N  
ATOM   1814  N   GLN H  39     160.560 167.955 121.555  1.00 79.45           N  
ATOM   1815  CA  GLN H  39     161.184 168.700 120.466  1.00 79.45           C  
ATOM   1816  C   GLN H  39     160.147 168.951 119.381  1.00 79.45           C  
ATOM   1817  O   GLN H  39     159.707 168.013 118.709  1.00 79.45           O  
ATOM   1818  CB  GLN H  39     162.387 167.951 119.899  1.00 79.45           C  
ATOM   1819  CG  GLN H  39     162.904 168.534 118.592  1.00 79.45           C  
ATOM   1820  CD  GLN H  39     164.091 167.776 118.037  1.00 79.45           C  
ATOM   1821  OE1 GLN H  39     164.694 166.953 118.725  1.00 79.45           O  
ATOM   1822  NE2 GLN H  39     164.432 168.048 116.784  1.00 79.45           N  
ATOM   1823  N   ALA H  40     159.764 170.211 119.207  1.00 82.12           N  
ATOM   1824  CA  ALA H  40     158.910 170.570 118.087  1.00 82.12           C  
ATOM   1825  C   ALA H  40     159.687 170.417 116.781  1.00 82.12           C  
ATOM   1826  O   ALA H  40     160.915 170.537 116.773  1.00 82.12           O  
ATOM   1827  CB  ALA H  40     158.403 172.003 118.236  1.00 82.12           C  
ATOM   1828  N   PRO H  41     159.010 170.136 115.668  1.00 81.62           N  
ATOM   1829  CA  PRO H  41     159.730 169.961 114.400  1.00 81.62           C  
ATOM   1830  C   PRO H  41     160.414 171.251 113.970  1.00 81.62           C  
ATOM   1831  O   PRO H  41     159.766 172.280 113.763  1.00 81.62           O  
ATOM   1832  CB  PRO H  41     158.626 169.553 113.418  1.00 81.62           C  
ATOM   1833  CG  PRO H  41     157.519 169.044 114.270  1.00 81.62           C  
ATOM   1834  CD  PRO H  41     157.573 169.857 115.525  1.00 81.62           C  
ATOM   1835  N   GLY H  42     161.733 171.183 113.833  1.00 85.68           N  
ATOM   1836  CA  GLY H  42     162.493 172.350 113.401  1.00 85.68           C  
ATOM   1837  C   GLY H  42     162.400 173.525 114.347  1.00 85.68           C  
ATOM   1838  O   GLY H  42     162.285 174.674 113.902  1.00 85.68           O  
ATOM   1839  N   LEU H  43     162.447 173.265 115.651  1.00 84.30           N  
ATOM   1840  CA  LEU H  43     162.391 174.321 116.650  1.00 84.30           C  
ATOM   1841  C   LEU H  43     163.290 173.940 117.817  1.00 84.30           C  
ATOM   1842  O   LEU H  43     163.986 172.922 117.787  1.00 84.30           O  
ATOM   1843  CB  LEU H  43     160.952 174.574 117.115  1.00 84.30           C  
ATOM   1844  CG  LEU H  43     160.052 175.375 116.173  1.00 84.30           C  
ATOM   1845  CD1 LEU H  43     158.656 175.523 116.755  1.00 84.30           C  
ATOM   1846  CD2 LEU H  43     160.659 176.739 115.891  1.00 84.30           C  
ATOM   1847  N   GLY H  44     163.273 174.776 118.854  1.00 81.70           N  
ATOM   1848  CA  GLY H  44     164.091 174.527 120.029  1.00 81.70           C  
ATOM   1849  C   GLY H  44     163.484 173.444 120.898  1.00 81.70           C  
ATOM   1850  O   GLY H  44     162.259 173.294 120.962  1.00 81.70           O  
ATOM   1851  N   LEU H  45     164.343 172.684 121.570  1.00 76.71           N  
ATOM   1852  CA  LEU H  45     163.870 171.618 122.441  1.00 76.71           C  
ATOM   1853  C   LEU H  45     163.157 172.195 123.655  1.00 76.71           C  
ATOM   1854  O   LEU H  45     163.413 173.329 124.068  1.00 76.71           O  
ATOM   1855  CB  LEU H  45     165.035 170.736 122.885  1.00 76.71           C  
ATOM   1856  CG  LEU H  45     165.305 169.484 122.048  1.00 76.71           C  
ATOM   1857  CD1 LEU H  45     165.616 169.845 120.608  1.00 76.71           C  
ATOM   1858  CD2 LEU H  45     166.439 168.683 122.658  1.00 76.71           C  
ATOM   1859  N   GLU H  46     162.250 171.407 124.221  1.00 81.97           N  
ATOM   1860  CA  GLU H  46     161.490 171.781 125.402  1.00 81.97           C  
ATOM   1861  C   GLU H  46     161.529 170.646 126.415  1.00 81.97           C  
ATOM   1862  O   GLU H  46     161.731 169.479 126.073  1.00 81.97           O  
ATOM   1863  CB  GLU H  46     160.040 172.120 125.043  1.00 81.97           C  
ATOM   1864  CG  GLU H  46     159.902 173.244 124.038  1.00 81.97           C  
ATOM   1865  CD  GLU H  46     158.458 173.618 123.787  1.00 81.97           C  
ATOM   1866  OE1 GLU H  46     157.582 173.129 124.530  1.00 81.97           O  
ATOM   1867  OE2 GLU H  46     158.200 174.398 122.848  1.00 81.97           O  
ATOM   1868  N   TYR H  47     161.323 171.002 127.677  1.00 73.25           N  
ATOM   1869  CA  TYR H  47     161.370 170.056 128.784  1.00 73.25           C  
ATOM   1870  C   TYR H  47     159.971 169.896 129.368  1.00 73.25           C  
ATOM   1871  O   TYR H  47     159.324 170.888 129.720  1.00 73.25           O  
ATOM   1872  CB  TYR H  47     162.357 170.526 129.850  1.00 73.25           C  
ATOM   1873  CG  TYR H  47     162.322 169.701 131.106  1.00 73.25           C  
ATOM   1874  CD1 TYR H  47     161.591 170.116 132.206  1.00 73.25           C  
ATOM   1875  CD2 TYR H  47     163.013 168.504 131.190  1.00 73.25           C  
ATOM   1876  CE1 TYR H  47     161.552 169.369 133.353  1.00 73.25           C  
ATOM   1877  CE2 TYR H  47     162.979 167.749 132.336  1.00 73.25           C  
ATOM   1878  CZ  TYR H  47     162.246 168.187 133.414  1.00 73.25           C  
ATOM   1879  OH  TYR H  47     162.202 167.444 134.566  1.00 73.25           O  
ATOM   1880  N   MET H  48     159.512 168.646 129.476  1.00 82.08           N  
ATOM   1881  CA  MET H  48     158.148 168.393 129.929  1.00 82.08           C  
ATOM   1882  C   MET H  48     158.103 168.023 131.407  1.00 82.08           C  
ATOM   1883  O   MET H  48     157.231 168.498 132.143  1.00 82.08           O  
ATOM   1884  CB  MET H  48     157.516 167.285 129.088  1.00 82.08           C  
ATOM   1885  CG  MET H  48     157.920 167.312 127.629  1.00 82.08           C  
ATOM   1886  SD  MET H  48     157.044 166.083 126.649  1.00 82.08           S  
ATOM   1887  CE  MET H  48     155.440 166.860 126.495  1.00 82.08           C  
ATOM   1888  N   GLY H  49     159.018 167.184 131.858  1.00 82.36           N  
ATOM   1889  CA  GLY H  49     159.025 166.753 133.243  1.00 82.36           C  
ATOM   1890  C   GLY H  49     159.993 165.605 133.443  1.00 82.36           C  
ATOM   1891  O   GLY H  49     160.870 165.347 132.625  1.00 82.36           O  
ATOM   1892  N   ARG H  50     159.822 164.927 134.576  1.00 77.79           N  
ATOM   1893  CA  ARG H  50     160.639 163.770 134.907  1.00 77.79           C  
ATOM   1894  C   ARG H  50     159.907 162.911 135.925  1.00 77.79           C  
ATOM   1895  O   ARG H  50     158.979 163.363 136.599  1.00 77.79           O  
ATOM   1896  CB  ARG H  50     162.013 164.184 135.456  1.00 77.79           C  
ATOM   1897  CG  ARG H  50     161.976 164.744 136.869  1.00 77.79           C  
ATOM   1898  CD  ARG H  50     163.020 165.830 137.077  1.00 77.79           C  
ATOM   1899  NE  ARG H  50     164.358 165.301 137.309  1.00 77.79           N  
ATOM   1900  CZ  ARG H  50     164.968 165.313 138.486  1.00 77.79           C  
ATOM   1901  NH1 ARG H  50     164.385 165.817 139.560  1.00 77.79           N  
ATOM   1902  NH2 ARG H  50     166.196 164.813 138.585  1.00 77.79           N  
ATOM   1903  N   ILE H  51     160.327 161.652 136.017  1.00 79.66           N  
ATOM   1904  CA  ILE H  51     159.885 160.744 137.067  1.00 79.66           C  
ATOM   1905  C   ILE H  51     161.073 159.886 137.471  1.00 79.66           C  
ATOM   1906  O   ILE H  51     161.706 159.256 136.616  1.00 79.66           O  
ATOM   1907  CB  ILE H  51     158.703 159.863 136.627  1.00 79.66           C  
ATOM   1908  CG1 ILE H  51     158.406 158.809 137.696  1.00 79.66           C  
ATOM   1909  CG2 ILE H  51     158.994 159.203 135.285  1.00 79.66           C  
ATOM   1910  CD1 ILE H  51     157.079 158.095 137.512  1.00 79.66           C  
ATOM   1911  N   ILE H  52     161.383 159.872 138.763  1.00 82.20           N  
ATOM   1912  CA  ILE H  52     162.432 159.001 139.284  1.00 82.20           C  
ATOM   1913  C   ILE H  52     161.864 157.588 139.340  1.00 82.20           C  
ATOM   1914  O   ILE H  52     160.845 157.360 140.006  1.00 82.20           O  
ATOM   1915  CB  ILE H  52     162.929 159.467 140.661  1.00 82.20           C  
ATOM   1916  CG1 ILE H  52     163.852 160.678 140.524  1.00 82.20           C  
ATOM   1917  CG2 ILE H  52     163.644 158.337 141.384  1.00 82.20           C  
ATOM   1918  CD1 ILE H  52     163.131 161.993 140.357  1.00 82.20           C  
ATOM   1919  N   PRO H  52A    162.470 156.621 138.654  1.00 84.52           N  
ATOM   1920  CA  PRO H  52A    161.906 155.265 138.631  1.00 84.52           C  
ATOM   1921  C   PRO H  52A    161.846 154.625 140.007  1.00 84.52           C  
ATOM   1922  O   PRO H  52A    160.834 154.019 140.371  1.00 84.52           O  
ATOM   1923  CB  PRO H  52A    162.863 154.503 137.706  1.00 84.52           C  
ATOM   1924  CG  PRO H  52A    163.514 155.555 136.879  1.00 84.52           C  
ATOM   1925  CD  PRO H  52A    163.641 156.747 137.774  1.00 84.52           C  
ATOM   1926  N   ALA H  53     162.928 154.752 140.777  1.00 86.83           N  
ATOM   1927  CA  ALA H  53     162.984 154.106 142.084  1.00 86.83           C  
ATOM   1928  C   ALA H  53     161.956 154.699 143.038  1.00 86.83           C  
ATOM   1929  O   ALA H  53     161.226 153.965 143.714  1.00 86.83           O  
ATOM   1930  CB  ALA H  53     164.390 154.225 142.667  1.00 86.83           C  
ATOM   1931  N   LEU H  54     161.881 156.028 143.105  1.00 87.74           N  
ATOM   1932  CA  LEU H  54     160.985 156.664 144.061  1.00 87.74           C  
ATOM   1933  C   LEU H  54     159.588 156.890 143.503  1.00 87.74           C  
ATOM   1934  O   LEU H  54     158.671 157.180 144.278  1.00 87.74           O  
ATOM   1935  CB  LEU H  54     161.582 157.989 144.526  1.00 87.74           C  
ATOM   1936  CG  LEU H  54     162.895 157.832 145.287  1.00 87.74           C  
ATOM   1937  CD1 LEU H  54     163.418 159.181 145.712  1.00 87.74           C  
ATOM   1938  CD2 LEU H  54     162.699 156.928 146.492  1.00 87.74           C  
ATOM   1939  N   ASP H  55     159.404 156.755 142.190  1.00 91.59           N  
ATOM   1940  CA  ASP H  55     158.105 156.963 141.548  1.00 91.59           C  
ATOM   1941  C   ASP H  55     157.522 158.330 141.902  1.00 91.59           C  
ATOM   1942  O   ASP H  55     156.356 158.450 142.281  1.00 91.59           O  
ATOM   1943  CB  ASP H  55     157.126 155.843 141.911  1.00 91.59           C  
ATOM   1944  CG  ASP H  55     155.927 155.797 140.987  1.00 91.59           C  
ATOM   1945  OD1 ASP H  55     155.934 156.518 139.967  1.00 91.59           O  
ATOM   1946  OD2 ASP H  55     154.976 155.042 141.280  1.00 91.59           O  
ATOM   1947  N   ARG H  56     158.342 159.370 141.784  1.00 89.81           N  
ATOM   1948  CA  ARG H  56     157.929 160.739 142.061  1.00 89.81           C  
ATOM   1949  C   ARG H  56     157.596 161.440 140.753  1.00 89.81           C  
ATOM   1950  O   ARG H  56     158.374 161.374 139.796  1.00 89.81           O  
ATOM   1951  CB  ARG H  56     159.021 161.505 142.806  1.00 89.81           C  
ATOM   1952  CG  ARG H  56     158.649 162.940 143.114  1.00 89.81           C  
ATOM   1953  CD  ARG H  56     157.383 163.001 143.948  1.00 89.81           C  
ATOM   1954  NE  ARG H  56     156.953 164.371 144.197  1.00 89.81           N  
ATOM   1955  CZ  ARG H  56     155.993 164.709 145.047  1.00 89.81           C  
ATOM   1956  NH1 ARG H  56     155.359 163.801 145.770  1.00 89.81           N  
ATOM   1957  NH2 ARG H  56     155.663 165.990 145.176  1.00 89.81           N  
ATOM   1958  N   ALA H  57     156.451 162.117 140.718  1.00 87.77           N  
ATOM   1959  CA  ALA H  57     155.958 162.745 139.500  1.00 87.77           C  
ATOM   1960  C   ALA H  57     156.380 164.208 139.447  1.00 87.77           C  
ATOM   1961  O   ALA H  57     156.177 164.956 140.408  1.00 87.77           O  
ATOM   1962  CB  ALA H  57     154.436 162.632 139.416  1.00 87.77           C  
ATOM   1963  N   ILE H  58     156.970 164.608 138.322  1.00 82.59           N  
ATOM   1964  CA  ILE H  58     157.395 165.981 138.082  1.00 82.59           C  
ATOM   1965  C   ILE H  58     156.819 166.438 136.749  1.00 82.59           C  
ATOM   1966  O   ILE H  58     156.879 165.706 135.755  1.00 82.59           O  
ATOM   1967  CB  ILE H  58     158.933 166.116 138.090  1.00 82.59           C  
ATOM   1968  CG1 ILE H  58     159.455 166.340 139.511  1.00 82.59           C  
ATOM   1969  CG2 ILE H  58     159.391 167.232 137.161  1.00 82.59           C  
ATOM   1970  CD1 ILE H  58     159.528 165.092 140.352  1.00 82.59           C  
ATOM   1971  N   TYR H  59     156.260 167.646 136.731  1.00 87.47           N  
ATOM   1972  CA  TYR H  59     155.653 168.209 135.535  1.00 87.47           C  
ATOM   1973  C   TYR H  59     156.140 169.639 135.333  1.00 87.47           C  
ATOM   1974  O   TYR H  59     156.849 170.204 136.169  1.00 87.47           O  
ATOM   1975  CB  TYR H  59     154.121 168.172 135.619  1.00 87.47           C  
ATOM   1976  CG  TYR H  59     153.554 166.793 135.867  1.00 87.47           C  
ATOM   1977  CD1 TYR H  59     153.318 165.918 134.817  1.00 87.47           C  
ATOM   1978  CD2 TYR H  59     153.252 166.367 137.152  1.00 87.47           C  
ATOM   1979  CE1 TYR H  59     152.798 164.659 135.040  1.00 87.47           C  
ATOM   1980  CE2 TYR H  59     152.733 165.111 137.384  1.00 87.47           C  
ATOM   1981  CZ  TYR H  59     152.508 164.261 136.325  1.00 87.47           C  
ATOM   1982  OH  TYR H  59     151.990 163.009 136.556  1.00 87.47           O  
ATOM   1983  N   THR H  60     155.753 170.218 134.200  1.00 89.72           N  
ATOM   1984  CA  THR H  60     156.080 171.590 133.843  1.00 89.72           C  
ATOM   1985  C   THR H  60     154.804 172.422 133.777  1.00 89.72           C  
ATOM   1986  O   THR H  60     153.735 171.918 133.420  1.00 89.72           O  
ATOM   1987  CB  THR H  60     156.814 171.649 132.497  1.00 89.72           C  
ATOM   1988  OG1 THR H  60     157.926 170.748 132.521  1.00 89.72           O  
ATOM   1989  CG2 THR H  60     157.327 173.052 132.212  1.00 89.72           C  
ATOM   1990  N   GLN H  61     154.926 173.705 134.131  1.00 93.18           N  
ATOM   1991  CA  GLN H  61     153.767 174.594 134.115  1.00 93.18           C  
ATOM   1992  C   GLN H  61     153.140 174.663 132.729  1.00 93.18           C  
ATOM   1993  O   GLN H  61     151.920 174.811 132.599  1.00 93.18           O  
ATOM   1994  CB  GLN H  61     154.169 175.989 134.594  1.00 93.18           C  
ATOM   1995  CG  GLN H  61     153.007 176.956 134.753  1.00 93.18           C  
ATOM   1996  CD  GLN H  61     153.424 178.271 135.389  1.00 93.18           C  
ATOM   1997  OE1 GLN H  61     154.571 178.440 135.802  1.00 93.18           O  
ATOM   1998  NE2 GLN H  61     152.489 179.210 135.473  1.00 93.18           N  
ATOM   1999  N   LYS H  62     153.958 174.563 131.680  1.00 88.01           N  
ATOM   2000  CA  LYS H  62     153.414 174.534 130.328  1.00 88.01           C  
ATOM   2001  C   LYS H  62     152.597 173.271 130.089  1.00 88.01           C  
ATOM   2002  O   LYS H  62     151.567 173.309 129.404  1.00 88.01           O  
ATOM   2003  CB  LYS H  62     154.542 174.641 129.302  1.00 88.01           C  
ATOM   2004  CG  LYS H  62     155.278 175.967 129.325  1.00 88.01           C  
ATOM   2005  CD  LYS H  62     156.249 176.073 128.160  1.00 88.01           C  
ATOM   2006  CE  LYS H  62     157.293 174.972 128.211  1.00 88.01           C  
ATOM   2007  NZ  LYS H  62     158.099 175.037 129.460  1.00 88.01           N  
ATOM   2008  N   PHE H  63     153.037 172.144 130.643  1.00 90.60           N  
ATOM   2009  CA  PHE H  63     152.427 170.851 130.372  1.00 90.60           C  
ATOM   2010  C   PHE H  63     151.734 170.251 131.587  1.00 90.60           C  
ATOM   2011  O   PHE H  63     151.508 169.038 131.618  1.00 90.60           O  
ATOM   2012  CB  PHE H  63     153.483 169.880 129.847  1.00 90.60           C  
ATOM   2013  CG  PHE H  63     154.363 170.469 128.789  1.00 90.60           C  
ATOM   2014  CD1 PHE H  63     153.935 170.541 127.478  1.00 90.60           C  
ATOM   2015  CD2 PHE H  63     155.615 170.961 129.109  1.00 90.60           C  
ATOM   2016  CE1 PHE H  63     154.739 171.088 126.505  1.00 90.60           C  
ATOM   2017  CE2 PHE H  63     156.425 171.509 128.140  1.00 90.60           C  
ATOM   2018  CZ  PHE H  63     155.986 171.573 126.835  1.00 90.60           C  
ATOM   2019  N   GLN H  64     151.399 171.063 132.586  1.00 91.98           N  
ATOM   2020  CA  GLN H  64     150.689 170.550 133.748  1.00 91.98           C  
ATOM   2021  C   GLN H  64     149.314 170.034 133.344  1.00 91.98           C  
ATOM   2022  O   GLN H  64     148.584 170.684 132.591  1.00 91.98           O  
ATOM   2023  CB  GLN H  64     150.554 171.639 134.814  1.00 91.98           C  
ATOM   2024  CG  GLN H  64     149.664 171.263 135.990  1.00 91.98           C  
ATOM   2025  CD  GLN H  64     150.214 170.107 136.805  1.00 91.98           C  
ATOM   2026  OE1 GLN H  64     151.396 169.775 136.720  1.00 91.98           O  
ATOM   2027  NE2 GLN H  64     149.352 169.487 137.603  1.00 91.98           N  
ATOM   2028  N   GLY H  65     148.969 168.855 133.841  1.00 88.68           N  
ATOM   2029  CA  GLY H  65     147.672 168.254 133.530  1.00 88.68           C  
ATOM   2030  C   GLY H  65     147.570 167.577 132.185  1.00 88.68           C  
ATOM   2031  O   GLY H  65     146.988 166.494 132.079  1.00 88.68           O  
ATOM   2032  N   ARG H  66     148.120 168.197 131.141  1.00 86.34           N  
ATOM   2033  CA  ARG H  66     148.054 167.598 129.813  1.00 86.34           C  
ATOM   2034  C   ARG H  66     148.872 166.314 129.743  1.00 86.34           C  
ATOM   2035  O   ARG H  66     148.458 165.341 129.103  1.00 86.34           O  
ATOM   2036  CB  ARG H  66     148.532 168.602 128.765  1.00 86.34           C  
ATOM   2037  CG  ARG H  66     148.006 170.011 128.982  1.00 86.34           C  
ATOM   2038  CD  ARG H  66     148.343 170.924 127.811  1.00 86.34           C  
ATOM   2039  NE  ARG H  66     147.515 170.655 126.641  1.00 86.34           N  
ATOM   2040  CZ  ARG H  66     147.895 169.930 125.597  1.00 86.34           C  
ATOM   2041  NH1 ARG H  66     149.098 169.382 125.535  1.00 86.34           N  
ATOM   2042  NH2 ARG H  66     147.048 169.754 124.588  1.00 86.34           N  
ATOM   2043  N   VAL H  67     150.026 166.289 130.400  1.00 85.62           N  
ATOM   2044  CA  VAL H  67     150.925 165.142 130.364  1.00 85.62           C  
ATOM   2045  C   VAL H  67     150.783 164.356 131.657  1.00 85.62           C  
ATOM   2046  O   VAL H  67     150.651 164.924 132.747  1.00 85.62           O  
ATOM   2047  CB  VAL H  67     152.386 165.587 130.148  1.00 85.62           C  
ATOM   2048  CG1 VAL H  67     153.289 164.381 129.952  1.00 85.62           C  
ATOM   2049  CG2 VAL H  67     152.481 166.528 128.965  1.00 85.62           C  
ATOM   2050  N   THR H  68     150.806 163.031 131.537  1.00 90.00           N  
ATOM   2051  CA  THR H  68     150.771 162.135 132.684  1.00 90.00           C  
ATOM   2052  C   THR H  68     151.858 161.082 132.529  1.00 90.00           C  
ATOM   2053  O   THR H  68     152.047 160.529 131.442  1.00 90.00           O  
ATOM   2054  CB  THR H  68     149.405 161.460 132.830  1.00 90.00           C  
ATOM   2055  OG1 THR H  68     148.984 160.957 131.559  1.00 90.00           O  
ATOM   2056  CG2 THR H  68     148.373 162.451 133.338  1.00 90.00           C  
ATOM   2057  N   ILE H  69     152.568 160.808 133.622  1.00 87.54           N  
ATOM   2058  CA  ILE H  69     153.705 159.896 133.619  1.00 87.54           C  
ATOM   2059  C   ILE H  69     153.472 158.816 134.665  1.00 87.54           C  
ATOM   2060  O   ILE H  69     153.160 159.118 135.822  1.00 87.54           O  
ATOM   2061  CB  ILE H  69     155.028 160.637 133.900  1.00 87.54           C  
ATOM   2062  CG1 ILE H  69     155.116 161.919 133.075  1.00 87.54           C  
ATOM   2063  CG2 ILE H  69     156.210 159.749 133.582  1.00 87.54           C  
ATOM   2064  CD1 ILE H  69     155.231 161.677 131.598  1.00 87.54           C  
ATOM   2065  N   THR H  70     153.629 157.558 134.259  1.00 88.52           N  
ATOM   2066  CA  THR H  70     153.465 156.418 135.149  1.00 88.52           C  
ATOM   2067  C   THR H  70     154.692 155.522 135.051  1.00 88.52           C  
ATOM   2068  O   THR H  70     155.404 155.521 134.045  1.00 88.52           O  
ATOM   2069  CB  THR H  70     152.203 155.606 134.821  1.00 88.52           C  
ATOM   2070  OG1 THR H  70     152.314 155.057 133.503  1.00 88.52           O  
ATOM   2071  CG2 THR H  70     150.964 156.483 134.894  1.00 88.52           C  
ATOM   2072  N   ALA H  71     154.928 154.751 136.111  1.00 95.21           N  
ATOM   2073  CA  ALA H  71     156.112 153.907 136.224  1.00 95.21           C  
ATOM   2074  C   ALA H  71     155.687 152.459 136.405  1.00 95.21           C  
ATOM   2075  O   ALA H  71     154.879 152.153 137.288  1.00 95.21           O  
ATOM   2076  CB  ALA H  71     156.994 154.353 137.394  1.00 95.21           C  
ATOM   2077  N   ASP H  72     156.237 151.570 135.579  1.00102.47           N  
ATOM   2078  CA  ASP H  72     155.990 150.133 135.683  1.00102.47           C  
ATOM   2079  C   ASP H  72     157.260 149.487 136.227  1.00102.47           C  
ATOM   2080  O   ASP H  72     158.265 149.374 135.521  1.00102.47           O  
ATOM   2081  CB  ASP H  72     155.592 149.550 134.332  1.00102.47           C  
ATOM   2082  CG  ASP H  72     154.842 148.239 134.461  1.00102.47           C  
ATOM   2083  OD1 ASP H  72     155.057 147.522 135.461  1.00102.47           O  
ATOM   2084  OD2 ASP H  72     154.036 147.925 133.561  1.00102.47           O  
ATOM   2085  N   LYS H  73     157.208 149.060 137.491  1.00107.99           N  
ATOM   2086  CA  LYS H  73     158.410 148.578 138.165  1.00107.99           C  
ATOM   2087  C   LYS H  73     158.853 147.218 137.640  1.00107.99           C  
ATOM   2088  O   LYS H  73     160.050 146.907 137.650  1.00107.99           O  
ATOM   2089  CB  LYS H  73     158.174 148.515 139.674  1.00107.99           C  
ATOM   2090  CG  LYS H  73     158.182 149.868 140.365  1.00107.99           C  
ATOM   2091  CD  LYS H  73     159.555 150.514 140.293  1.00107.99           C  
ATOM   2092  CE  LYS H  73     160.621 149.607 140.887  1.00107.99           C  
ATOM   2093  NZ  LYS H  73     160.281 149.193 142.275  1.00107.99           N  
ATOM   2094  N   SER H  74     157.904 146.390 137.191  1.00112.40           N  
ATOM   2095  CA  SER H  74     158.231 145.014 136.821  1.00112.40           C  
ATOM   2096  C   SER H  74     159.297 144.966 135.735  1.00112.40           C  
ATOM   2097  O   SER H  74     160.290 144.240 135.860  1.00112.40           O  
ATOM   2098  CB  SER H  74     156.970 144.279 136.368  1.00112.40           C  
ATOM   2099  OG  SER H  74     156.020 144.203 137.415  1.00112.40           O  
ATOM   2100  N   THR H  75     159.114 145.732 134.665  1.00111.03           N  
ATOM   2101  CA  THR H  75     160.130 145.870 133.633  1.00111.03           C  
ATOM   2102  C   THR H  75     160.926 147.162 133.765  1.00111.03           C  
ATOM   2103  O   THR H  75     161.710 147.482 132.864  1.00111.03           O  
ATOM   2104  CB  THR H  75     159.490 145.788 132.243  1.00111.03           C  
ATOM   2105  OG1 THR H  75     160.417 146.258 131.258  1.00111.03           O  
ATOM   2106  CG2 THR H  75     158.219 146.618 132.187  1.00111.03           C  
ATOM   2107  N   SER H  76     160.744 147.900 134.864  1.00103.97           N  
ATOM   2108  CA  SER H  76     161.466 149.149 135.121  1.00103.97           C  
ATOM   2109  C   SER H  76     161.283 150.146 133.980  1.00103.97           C  
ATOM   2110  O   SER H  76     162.242 150.758 133.505  1.00103.97           O  
ATOM   2111  CB  SER H  76     162.951 148.890 135.383  1.00103.97           C  
ATOM   2112  OG  SER H  76     163.628 150.094 135.696  1.00103.97           O  
ATOM   2113  N   THR H  77     160.042 150.311 133.535  1.00 98.72           N  
ATOM   2114  CA  THR H  77     159.704 151.229 132.458  1.00 98.72           C  
ATOM   2115  C   THR H  77     158.792 152.323 132.992  1.00 98.72           C  
ATOM   2116  O   THR H  77     157.932 152.062 133.839  1.00 98.72           O  
ATOM   2117  CB  THR H  77     159.022 150.498 131.301  1.00 98.72           C  
ATOM   2118  OG1 THR H  77     157.844 149.839 131.783  1.00 98.72           O  
ATOM   2119  CG2 THR H  77     159.960 149.471 130.695  1.00 98.72           C  
ATOM   2120  N   VAL H  78     158.986 153.543 132.498  1.00 92.94           N  
ATOM   2121  CA  VAL H  78     158.171 154.691 132.876  1.00 92.94           C  
ATOM   2122  C   VAL H  78     157.376 155.145 131.660  1.00 92.94           C  
ATOM   2123  O   VAL H  78     157.956 155.487 130.622  1.00 92.94           O  
ATOM   2124  CB  VAL H  78     159.042 155.833 133.423  1.00 92.94           C  
ATOM   2125  CG1 VAL H  78     159.729 155.403 134.702  1.00 92.94           C  
ATOM   2126  CG2 VAL H  78     160.073 156.240 132.387  1.00 92.94           C  
ATOM   2127  N   TYR H  79     156.053 155.163 131.791  1.00 93.25           N  
ATOM   2128  CA  TYR H  79     155.158 155.489 130.691  1.00 93.25           C  
ATOM   2129  C   TYR H  79     154.819 156.973 130.696  1.00 93.25           C  
ATOM   2130  O   TYR H  79     154.909 157.646 131.724  1.00 93.25           O  
ATOM   2131  CB  TYR H  79     153.867 154.670 130.773  1.00 93.25           C  
ATOM   2132  CG  TYR H  79     154.041 153.191 130.518  1.00 93.25           C  
ATOM   2133  CD1 TYR H  79     153.672 152.629 129.305  1.00 93.25           C  
ATOM   2134  CD2 TYR H  79     154.567 152.356 131.492  1.00 93.25           C  
ATOM   2135  CE1 TYR H  79     153.828 151.281 129.068  1.00 93.25           C  
ATOM   2136  CE2 TYR H  79     154.727 151.008 131.264  1.00 93.25           C  
ATOM   2137  CZ  TYR H  79     154.355 150.475 130.052  1.00 93.25           C  
ATOM   2138  OH  TYR H  79     154.513 149.129 129.823  1.00 93.25           O  
ATOM   2139  N   MET H  80     154.417 157.475 129.530  1.00 88.32           N  
ATOM   2140  CA  MET H  80     154.014 158.866 129.363  1.00 88.32           C  
ATOM   2141  C   MET H  80     152.717 158.908 128.574  1.00 88.32           C  
ATOM   2142  O   MET H  80     152.691 158.514 127.404  1.00 88.32           O  
ATOM   2143  CB  MET H  80     155.097 159.673 128.644  1.00 88.32           C  
ATOM   2144  CG  MET H  80     154.604 160.992 128.069  1.00 88.32           C  
ATOM   2145  SD  MET H  80     155.847 161.817 127.059  1.00 88.32           S  
ATOM   2146  CE  MET H  80     154.902 163.192 126.414  1.00 88.32           C  
ATOM   2147  N   GLU H  81     151.647 159.383 129.206  1.00 89.91           N  
ATOM   2148  CA  GLU H  81     150.361 159.557 128.547  1.00 89.91           C  
ATOM   2149  C   GLU H  81     150.062 161.042 128.415  1.00 89.91           C  
ATOM   2150  O   GLU H  81     150.124 161.783 129.403  1.00 89.91           O  
ATOM   2151  CB  GLU H  81     149.234 158.855 129.308  1.00 89.91           C  
ATOM   2152  CG  GLU H  81     149.142 157.364 129.055  1.00 89.91           C  
ATOM   2153  CD  GLU H  81     147.761 156.811 129.348  1.00 89.91           C  
ATOM   2154  OE1 GLU H  81     146.835 157.614 129.583  1.00 89.91           O  
ATOM   2155  OE2 GLU H  81     147.598 155.573 129.339  1.00 89.91           O  
ATOM   2156  N   LEU H  82     149.740 161.470 127.197  1.00 87.69           N  
ATOM   2157  CA  LEU H  82     149.435 162.864 126.896  1.00 87.69           C  
ATOM   2158  C   LEU H  82     147.975 162.953 126.470  1.00 87.69           C  
ATOM   2159  O   LEU H  82     147.635 162.634 125.327  1.00 87.69           O  
ATOM   2160  CB  LEU H  82     150.369 163.389 125.810  1.00 87.69           C  
ATOM   2161  CG  LEU H  82     150.142 164.800 125.275  1.00 87.69           C  
ATOM   2162  CD1 LEU H  82     150.043 165.804 126.404  1.00 87.69           C  
ATOM   2163  CD2 LEU H  82     151.276 165.166 124.339  1.00 87.69           C  
ATOM   2164  N   SER H  82A    147.115 163.400 127.387  1.00 92.71           N  
ATOM   2165  CA  SER H  82A    145.676 163.337 127.149  1.00 92.71           C  
ATOM   2166  C   SER H  82A    145.250 164.254 126.009  1.00 92.71           C  
ATOM   2167  O   SER H  82A    144.542 163.825 125.091  1.00 92.71           O  
ATOM   2168  CB  SER H  82A    144.920 163.696 128.426  1.00 92.71           C  
ATOM   2169  OG  SER H  82A    145.190 165.031 128.815  1.00 92.71           O  
ATOM   2170  N   GLY H  82B    145.669 165.515 126.047  1.00 94.00           N  
ATOM   2171  CA  GLY H  82B    145.237 166.512 125.084  1.00 94.00           C  
ATOM   2172  C   GLY H  82B    146.289 166.719 124.006  1.00 94.00           C  
ATOM   2173  O   GLY H  82B    147.455 166.981 124.307  1.00 94.00           O  
ATOM   2174  N   LEU H  82C    145.856 166.597 122.755  1.00 97.02           N  
ATOM   2175  CA  LEU H  82C    146.719 166.778 121.595  1.00 97.02           C  
ATOM   2176  C   LEU H  82C    146.263 167.993 120.800  1.00 97.02           C  
ATOM   2177  O   LEU H  82C    145.059 168.221 120.640  1.00 97.02           O  
ATOM   2178  CB  LEU H  82C    146.712 165.535 120.705  1.00 97.02           C  
ATOM   2179  CG  LEU H  82C    147.307 164.274 121.328  1.00 97.02           C  
ATOM   2180  CD1 LEU H  82C    147.318 163.135 120.326  1.00 97.02           C  
ATOM   2181  CD2 LEU H  82C    148.705 164.551 121.836  1.00 97.02           C  
ATOM   2182  N   ARG H  83     147.225 168.765 120.303  1.00 96.97           N  
ATOM   2183  CA  ARG H  83     146.958 169.953 119.510  1.00 96.97           C  
ATOM   2184  C   ARG H  83     147.615 169.804 118.145  1.00 96.97           C  
ATOM   2185  O   ARG H  83     148.425 168.902 117.914  1.00 96.97           O  
ATOM   2186  CB  ARG H  83     147.460 171.221 120.212  1.00 96.97           C  
ATOM   2187  CG  ARG H  83     146.728 171.543 121.503  1.00 96.97           C  
ATOM   2188  CD  ARG H  83     145.250 171.783 121.248  1.00 96.97           C  
ATOM   2189  NE  ARG H  83     144.520 172.053 122.481  1.00 96.97           N  
ATOM   2190  CZ  ARG H  83     143.220 172.308 122.541  1.00 96.97           C  
ATOM   2191  NH1 ARG H  83     142.471 172.338 121.452  1.00 96.97           N  
ATOM   2192  NH2 ARG H  83     142.658 172.537 123.725  1.00 96.97           N  
ATOM   2193  N   SER H  84     147.243 170.701 117.230  1.00 94.99           N  
ATOM   2194  CA  SER H  84     147.805 170.661 115.885  1.00 94.99           C  
ATOM   2195  C   SER H  84     149.309 170.901 115.909  1.00 94.99           C  
ATOM   2196  O   SER H  84     150.062 170.245 115.180  1.00 94.99           O  
ATOM   2197  CB  SER H  84     147.111 171.692 114.997  1.00 94.99           C  
ATOM   2198  OG  SER H  84     147.635 171.660 113.681  1.00 94.99           O  
ATOM   2199  N   GLU H  85     149.764 171.839 116.739  1.00 94.78           N  
ATOM   2200  CA  GLU H  85     151.188 172.122 116.862  1.00 94.78           C  
ATOM   2201  C   GLU H  85     151.907 171.140 117.775  1.00 94.78           C  
ATOM   2202  O   GLU H  85     153.139 171.191 117.864  1.00 94.78           O  
ATOM   2203  CB  GLU H  85     151.395 173.547 117.378  1.00 94.78           C  
ATOM   2204  CG  GLU H  85     150.828 173.787 118.770  1.00 94.78           C  
ATOM   2205  CD  GLU H  85     151.047 175.208 119.253  1.00 94.78           C  
ATOM   2206  OE1 GLU H  85     151.485 176.053 118.445  1.00 94.78           O  
ATOM   2207  OE2 GLU H  85     150.781 175.479 120.443  1.00 94.78           O  
ATOM   2208  N   ASP H  86     151.177 170.250 118.445  1.00 86.24           N  
ATOM   2209  CA  ASP H  86     151.742 169.343 119.433  1.00 86.24           C  
ATOM   2210  C   ASP H  86     152.427 168.134 118.803  1.00 86.24           C  
ATOM   2211  O   ASP H  86     152.868 167.236 119.528  1.00 86.24           O  
ATOM   2212  CB  ASP H  86     150.650 168.884 120.401  1.00 86.24           C  
ATOM   2213  CG  ASP H  86     151.192 168.545 121.771  1.00 86.24           C  
ATOM   2214  OD1 ASP H  86     151.316 169.466 122.606  1.00 86.24           O  
ATOM   2215  OD2 ASP H  86     151.500 167.361 122.012  1.00 86.24           O  
ATOM   2216  N   THR H  87     152.532 168.092 117.475  1.00 86.29           N  
ATOM   2217  CA  THR H  87     153.154 166.967 116.778  1.00 86.29           C  
ATOM   2218  C   THR H  87     154.666 167.061 116.953  1.00 86.29           C  
ATOM   2219  O   THR H  87     155.418 167.409 116.040  1.00 86.29           O  
ATOM   2220  CB  THR H  87     152.762 166.963 115.306  1.00 86.29           C  
ATOM   2221  OG1 THR H  87     153.452 165.906 114.629  1.00 86.29           O  
ATOM   2222  CG2 THR H  87     153.109 168.296 114.655  1.00 86.29           C  
ATOM   2223  N   ALA H  88     155.120 166.724 118.157  1.00 83.92           N  
ATOM   2224  CA  ALA H  88     156.512 166.900 118.538  1.00 83.92           C  
ATOM   2225  C   ALA H  88     157.096 165.591 119.042  1.00 83.92           C  
ATOM   2226  O   ALA H  88     156.438 164.847 119.774  1.00 83.92           O  
ATOM   2227  CB  ALA H  88     156.651 167.977 119.614  1.00 83.92           C  
ATOM   2228  N   VAL H  89     158.342 165.319 118.649  1.00 81.47           N  
ATOM   2229  CA  VAL H  89     159.037 164.134 119.134  1.00 81.47           C  
ATOM   2230  C   VAL H  89     159.299 164.280 120.625  1.00 81.47           C  
ATOM   2231  O   VAL H  89     159.771 165.325 121.091  1.00 81.47           O  
ATOM   2232  CB  VAL H  89     160.344 163.926 118.357  1.00 81.47           C  
ATOM   2233  CG1 VAL H  89     160.970 162.590 118.721  1.00 81.47           C  
ATOM   2234  CG2 VAL H  89     160.095 164.022 116.865  1.00 81.47           C  
ATOM   2235  N   TYR H  90     158.993 163.232 121.382  1.00 79.31           N  
ATOM   2236  CA  TYR H  90     159.178 163.224 122.827  1.00 79.31           C  
ATOM   2237  C   TYR H  90     160.332 162.292 123.168  1.00 79.31           C  
ATOM   2238  O   TYR H  90     160.239 161.080 122.951  1.00 79.31           O  
ATOM   2239  CB  TYR H  90     157.897 162.789 123.535  1.00 79.31           C  
ATOM   2240  CG  TYR H  90     156.673 163.547 123.076  1.00 79.31           C  
ATOM   2241  CD1 TYR H  90     156.468 164.866 123.455  1.00 79.31           C  
ATOM   2242  CD2 TYR H  90     155.724 162.947 122.261  1.00 79.31           C  
ATOM   2243  CE1 TYR H  90     155.355 165.565 123.038  1.00 79.31           C  
ATOM   2244  CE2 TYR H  90     154.603 163.639 121.841  1.00 79.31           C  
ATOM   2245  CZ  TYR H  90     154.427 164.949 122.231  1.00 79.31           C  
ATOM   2246  OH  TYR H  90     153.317 165.646 121.816  1.00 79.31           O  
ATOM   2247  N   TYR H  91     161.409 162.857 123.705  1.00 76.10           N  
ATOM   2248  CA  TYR H  91     162.634 162.120 123.987  1.00 76.10           C  
ATOM   2249  C   TYR H  91     162.642 161.641 125.430  1.00 76.10           C  
ATOM   2250  O   TYR H  91     162.301 162.398 126.345  1.00 76.10           O  
ATOM   2251  CB  TYR H  91     163.870 162.984 123.730  1.00 76.10           C  
ATOM   2252  CG  TYR H  91     164.339 162.990 122.297  1.00 76.10           C  
ATOM   2253  CD1 TYR H  91     164.960 161.881 121.749  1.00 76.10           C  
ATOM   2254  CD2 TYR H  91     164.176 164.110 121.499  1.00 76.10           C  
ATOM   2255  CE1 TYR H  91     165.395 161.881 120.441  1.00 76.10           C  
ATOM   2256  CE2 TYR H  91     164.609 164.120 120.190  1.00 76.10           C  
ATOM   2257  CZ  TYR H  91     165.218 163.004 119.667  1.00 76.10           C  
ATOM   2258  OH  TYR H  91     165.652 163.008 118.363  1.00 76.10           O  
ATOM   2259  N   CYS H  92     163.032 160.385 125.625  1.00 84.69           N  
ATOM   2260  CA  CYS H  92     163.316 159.882 126.959  1.00 84.69           C  
ATOM   2261  C   CYS H  92     164.803 160.023 127.259  1.00 84.69           C  
ATOM   2262  O   CYS H  92     165.657 159.484 126.551  1.00 84.69           O  
ATOM   2263  CB  CYS H  92     162.884 158.421 127.079  1.00 84.69           C  
ATOM   2264  SG  CYS H  92     163.401 157.567 128.585  1.00 84.69           S  
ATOM   2265  N   ALA H  93     165.112 160.761 128.321  1.00 74.86           N  
ATOM   2266  CA  ALA H  93     166.491 161.081 128.659  1.00 74.86           C  
ATOM   2267  C   ALA H  93     166.791 160.610 130.070  1.00 74.86           C  
ATOM   2268  O   ALA H  93     166.013 160.867 130.993  1.00 74.86           O  
ATOM   2269  CB  ALA H  93     166.755 162.582 128.538  1.00 74.86           C  
ATOM   2270  N   ARG H  94     167.914 159.916 130.228  1.00 73.30           N  
ATOM   2271  CA  ARG H  94     168.376 159.476 131.534  1.00 73.30           C  
ATOM   2272  C   ARG H  94     169.429 160.447 132.044  1.00 73.30           C  
ATOM   2273  O   ARG H  94     170.424 160.708 131.362  1.00 73.30           O  
ATOM   2274  CB  ARG H  94     168.959 158.066 131.460  1.00 73.30           C  
ATOM   2275  CG  ARG H  94     169.236 157.455 132.817  1.00 73.30           C  
ATOM   2276  CD  ARG H  94     170.351 156.427 132.753  1.00 73.30           C  
ATOM   2277  NE  ARG H  94     171.649 157.048 132.522  1.00 73.30           N  
ATOM   2278  CZ  ARG H  94     172.808 156.411 132.605  1.00 73.30           C  
ATOM   2279  NH1 ARG H  94     172.870 155.127 132.918  1.00 73.30           N  
ATOM   2280  NH2 ARG H  94     173.934 157.079 132.370  1.00 73.30           N  
ATOM   2281  N   SER H  95     169.210 160.977 133.240  1.00 73.37           N  
ATOM   2282  CA  SER H  95     170.118 161.948 133.821  1.00 73.37           C  
ATOM   2283  C   SER H  95     170.318 161.628 135.291  1.00 73.37           C  
ATOM   2284  O   SER H  95     169.442 161.051 135.939  1.00 73.37           O  
ATOM   2285  CB  SER H  95     169.587 163.376 133.668  1.00 73.37           C  
ATOM   2286  OG  SER H  95     168.358 163.530 134.356  1.00 73.37           O  
ATOM   2287  N   VAL H  96     171.487 162.004 135.811  1.00 70.87           N  
ATOM   2288  CA  VAL H  96     171.751 161.832 137.231  1.00 70.87           C  
ATOM   2289  C   VAL H  96     170.783 162.695 138.020  1.00 70.87           C  
ATOM   2290  O   VAL H  96     170.682 163.908 137.797  1.00 70.87           O  
ATOM   2291  CB  VAL H  96     173.210 162.181 137.550  1.00 70.87           C  
ATOM   2292  CG1 VAL H  96     173.456 162.094 139.044  1.00 70.87           C  
ATOM   2293  CG2 VAL H  96     174.146 161.254 136.791  1.00 70.87           C  
ATOM   2294  N   VAL H  97     170.053 162.066 138.943  1.00 70.72           N  
ATOM   2295  CA  VAL H  97     168.996 162.764 139.661  1.00 70.72           C  
ATOM   2296  C   VAL H  97     169.585 163.933 140.433  1.00 70.72           C  
ATOM   2297  O   VAL H  97     170.497 163.767 141.253  1.00 70.72           O  
ATOM   2298  CB  VAL H  97     168.251 161.792 140.585  1.00 70.72           C  
ATOM   2299  CG1 VAL H  97     169.192 161.247 141.640  1.00 70.72           C  
ATOM   2300  CG2 VAL H  97     167.064 162.482 141.233  1.00 70.72           C  
ATOM   2301  N   GLY H  98     169.068 165.127 140.165  1.00 69.88           N  
ATOM   2302  CA  GLY H  98     169.553 166.328 140.797  1.00 69.88           C  
ATOM   2303  C   GLY H  98     168.457 167.359 140.951  1.00 69.88           C  
ATOM   2304  O   GLY H  98     167.330 167.173 140.484  1.00 69.88           O  
ATOM   2305  N   PRO H  99     168.768 168.471 141.624  1.00 68.36           N  
ATOM   2306  CA  PRO H  99     167.759 169.531 141.775  1.00 68.36           C  
ATOM   2307  C   PRO H  99     167.242 170.046 140.448  1.00 68.36           C  
ATOM   2308  O   PRO H  99     166.075 170.441 140.345  1.00 68.36           O  
ATOM   2309  CB  PRO H  99     168.507 170.615 142.565  1.00 68.36           C  
ATOM   2310  CG  PRO H  99     169.951 170.314 142.368  1.00 68.36           C  
ATOM   2311  CD  PRO H  99     170.046 168.829 142.257  1.00 68.36           C  
ATOM   2312  N   THR H 100     168.086 170.054 139.431  1.00 72.11           N  
ATOM   2313  CA  THR H 100     167.709 170.337 138.061  1.00 72.11           C  
ATOM   2314  C   THR H 100     168.011 169.130 137.190  1.00 72.11           C  
ATOM   2315  O   THR H 100     168.890 168.325 137.515  1.00 72.11           O  
ATOM   2316  CB  THR H 100     168.471 171.554 137.525  1.00 72.11           C  
ATOM   2317  OG1 THR H 100     169.874 171.262 137.498  1.00 72.11           O  
ATOM   2318  CG2 THR H 100     168.230 172.761 138.411  1.00 72.11           C  
ATOM   2319  N   PRO H 100A    167.289 168.954 136.088  1.00 71.14           N  
ATOM   2320  CA  PRO H 100A    167.629 167.866 135.165  1.00 71.14           C  
ATOM   2321  C   PRO H 100A    169.036 168.050 134.618  1.00 71.14           C  
ATOM   2322  O   PRO H 100A    169.316 168.996 133.880  1.00 71.14           O  
ATOM   2323  CB  PRO H 100A    166.567 167.990 134.070  1.00 71.14           C  
ATOM   2324  CG  PRO H 100A    165.416 168.651 134.754  1.00 71.14           C  
ATOM   2325  CD  PRO H 100A    166.028 169.616 135.721  1.00 71.14           C  
ATOM   2326  N   ASN H 100B    169.919 167.131 134.984  1.00 71.66           N  
ATOM   2327  CA  ASN H 100B    171.333 167.251 134.663  1.00 71.66           C  
ATOM   2328  C   ASN H 100B    171.559 166.842 133.208  1.00 71.66           C  
ATOM   2329  O   ASN H 100B    170.611 166.705 132.431  1.00 71.66           O  
ATOM   2330  CB  ASN H 100B    172.165 166.419 135.643  1.00 71.66           C  
ATOM   2331  CG  ASN H 100B    172.338 167.100 136.988  1.00 71.66           C  
ATOM   2332  OD1 ASN H 100B    171.616 168.038 137.319  1.00 71.66           O  
ATOM   2333  ND2 ASN H 100B    173.301 166.629 137.769  1.00 71.66           N  
ATOM   2334  N   TYR H 100C    172.819 166.663 132.825  1.00 71.41           N  
ATOM   2335  CA  TYR H 100C    173.156 166.265 131.467  1.00 71.41           C  
ATOM   2336  C   TYR H 100C    172.463 164.960 131.100  1.00 71.41           C  
ATOM   2337  O   TYR H 100C    172.493 163.988 131.859  1.00 71.41           O  
ATOM   2338  CB  TYR H 100C    174.672 166.122 131.337  1.00 71.41           C  
ATOM   2339  CG  TYR H 100C    175.339 165.547 132.571  1.00 71.41           C  
ATOM   2340  CD1 TYR H 100C    175.792 166.376 133.592  1.00 71.41           C  
ATOM   2341  CD2 TYR H 100C    175.518 164.179 132.715  1.00 71.41           C  
ATOM   2342  CE1 TYR H 100C    176.398 165.859 134.718  1.00 71.41           C  
ATOM   2343  CE2 TYR H 100C    176.124 163.652 133.839  1.00 71.41           C  
ATOM   2344  CZ  TYR H 100C    176.562 164.496 134.836  1.00 71.41           C  
ATOM   2345  OH  TYR H 100C    177.167 163.973 135.955  1.00 71.41           O  
ATOM   2346  N   PHE H 100D    171.832 164.943 129.927  1.00 72.46           N  
ATOM   2347  CA  PHE H 100D    171.059 163.786 129.478  1.00 72.46           C  
ATOM   2348  C   PHE H 100D    172.013 162.711 128.955  1.00 72.46           C  
ATOM   2349  O   PHE H 100D    172.240 162.551 127.754  1.00 72.46           O  
ATOM   2350  CB  PHE H 100D    170.046 164.201 128.421  1.00 72.46           C  
ATOM   2351  CG  PHE H 100D    168.994 165.143 128.926  1.00 72.46           C  
ATOM   2352  CD1 PHE H 100D    168.798 165.324 130.284  1.00 72.46           C  
ATOM   2353  CD2 PHE H 100D    168.192 165.840 128.043  1.00 72.46           C  
ATOM   2354  CE1 PHE H 100D    167.829 166.191 130.750  1.00 72.46           C  
ATOM   2355  CE2 PHE H 100D    167.223 166.705 128.501  1.00 72.46           C  
ATOM   2356  CZ  PHE H 100D    167.040 166.882 129.857  1.00 72.46           C  
ATOM   2357  N   ASP H 101     172.574 161.956 129.895  1.00 76.68           N  
ATOM   2358  CA  ASP H 101     173.523 160.907 129.575  1.00 76.68           C  
ATOM   2359  C   ASP H 101     172.947 159.548 129.951  1.00 76.68           C  
ATOM   2360  O   ASP H 101     172.930 159.197 131.139  1.00 76.68           O  
ATOM   2361  CB  ASP H 101     174.851 161.129 130.315  1.00 76.68           C  
ATOM   2362  CG  ASP H 101     175.964 160.240 129.796  1.00 76.68           C  
ATOM   2363  OD1 ASP H 101     175.769 159.593 128.745  1.00 76.68           O  
ATOM   2364  OD2 ASP H 101     177.033 160.189 130.439  1.00 76.68           O  
ATOM   2365  N   PRO H 102     172.476 158.755 128.984  1.00 75.96           N  
ATOM   2366  CA  PRO H 102     172.337 159.071 127.563  1.00 75.96           C  
ATOM   2367  C   PRO H 102     170.885 159.323 127.167  1.00 75.96           C  
ATOM   2368  O   PRO H 102     169.972 159.182 127.975  1.00 75.96           O  
ATOM   2369  CB  PRO H 102     172.902 157.815 126.898  1.00 75.96           C  
ATOM   2370  CG  PRO H 102     172.434 156.704 127.813  1.00 75.96           C  
ATOM   2371  CD  PRO H 102     172.361 157.303 129.211  1.00 75.96           C  
ATOM   2372  N   TRP H 103     170.654 159.698 125.914  1.00 78.47           N  
ATOM   2373  CA  TRP H 103     169.312 159.929 125.406  1.00 78.47           C  
ATOM   2374  C   TRP H 103     168.641 158.609 125.035  1.00 78.47           C  
ATOM   2375  O   TRP H 103     169.260 157.543 125.022  1.00 78.47           O  
ATOM   2376  CB  TRP H 103     169.356 160.852 124.193  1.00 78.47           C  
ATOM   2377  CG  TRP H 103     169.746 162.250 124.522  1.00 78.47           C  
ATOM   2378  CD1 TRP H 103     170.965 162.683 124.949  1.00 78.47           C  
ATOM   2379  CD2 TRP H 103     168.915 163.409 124.438  1.00 78.47           C  
ATOM   2380  NE1 TRP H 103     170.943 164.040 125.143  1.00 78.47           N  
ATOM   2381  CE2 TRP H 103     169.693 164.509 124.837  1.00 78.47           C  
ATOM   2382  CE3 TRP H 103     167.585 163.621 124.069  1.00 78.47           C  
ATOM   2383  CZ2 TRP H 103     169.189 165.803 124.874  1.00 78.47           C  
ATOM   2384  CZ3 TRP H 103     167.084 164.906 124.109  1.00 78.47           C  
ATOM   2385  CH2 TRP H 103     167.883 165.981 124.509  1.00 78.47           C  
ATOM   2386  N   GLY H 104     167.350 158.693 124.728  1.00 90.15           N  
ATOM   2387  CA  GLY H 104     166.594 157.545 124.280  1.00 90.15           C  
ATOM   2388  C   GLY H 104     166.581 157.423 122.768  1.00 90.15           C  
ATOM   2389  O   GLY H 104     167.348 158.061 122.046  1.00 90.15           O  
ATOM   2390  N   GLN H 105     165.676 156.572 122.287  1.00 95.02           N  
ATOM   2391  CA  GLN H 105     165.560 156.347 120.851  1.00 95.02           C  
ATOM   2392  C   GLN H 105     164.914 157.539 120.155  1.00 95.02           C  
ATOM   2393  O   GLN H 105     165.394 157.994 119.112  1.00 95.02           O  
ATOM   2394  CB  GLN H 105     164.761 155.070 120.583  1.00 95.02           C  
ATOM   2395  CG  GLN H 105     165.250 154.262 119.389  1.00 95.02           C  
ATOM   2396  CD  GLN H 105     165.035 154.969 118.064  1.00 95.02           C  
ATOM   2397  OE1 GLN H 105     164.041 155.670 117.875  1.00 95.02           O  
ATOM   2398  NE2 GLN H 105     165.970 154.789 117.139  1.00 95.02           N  
ATOM   2399  N   GLY H 106     163.828 158.058 120.719  1.00 92.80           N  
ATOM   2400  CA  GLY H 106     163.100 159.141 120.091  1.00 92.80           C  
ATOM   2401  C   GLY H 106     161.928 158.637 119.278  1.00 92.80           C  
ATOM   2402  O   GLY H 106     162.111 157.884 118.316  1.00 92.80           O  
ATOM   2403  N   THR H 107     160.717 159.041 119.650  1.00 90.66           N  
ATOM   2404  CA  THR H 107     159.497 158.559 119.015  1.00 90.66           C  
ATOM   2405  C   THR H 107     158.800 159.717 118.318  1.00 90.66           C  
ATOM   2406  O   THR H 107     158.328 160.651 118.975  1.00 90.66           O  
ATOM   2407  CB  THR H 107     158.567 157.907 120.040  1.00 90.66           C  
ATOM   2408  OG1 THR H 107     157.483 157.261 119.362  1.00 90.66           O  
ATOM   2409  CG2 THR H 107     158.020 158.945 121.006  1.00 90.66           C  
ATOM   2410  N   LEU H 108     158.737 159.655 116.992  1.00 89.46           N  
ATOM   2411  CA  LEU H 108     158.041 160.670 116.218  1.00 89.46           C  
ATOM   2412  C   LEU H 108     156.537 160.472 116.336  1.00 89.46           C  
ATOM   2413  O   LEU H 108     156.028 159.358 116.186  1.00 89.46           O  
ATOM   2414  CB  LEU H 108     158.469 160.610 114.752  1.00 89.46           C  
ATOM   2415  CG  LEU H 108     158.598 161.935 113.997  1.00 89.46           C  
ATOM   2416  CD1 LEU H 108     159.252 161.705 112.645  1.00 89.46           C  
ATOM   2417  CD2 LEU H 108     157.250 162.620 113.829  1.00 89.46           C  
ATOM   2418  N   VAL H 109     155.825 161.561 116.609  1.00 88.12           N  
ATOM   2419  CA  VAL H 109     154.376 161.546 116.755  1.00 88.12           C  
ATOM   2420  C   VAL H 109     153.793 162.619 115.848  1.00 88.12           C  
ATOM   2421  O   VAL H 109     154.251 163.767 115.863  1.00 88.12           O  
ATOM   2422  CB  VAL H 109     153.951 161.771 118.217  1.00 88.12           C  
ATOM   2423  CG1 VAL H 109     152.439 161.772 118.335  1.00 88.12           C  
ATOM   2424  CG2 VAL H 109     154.558 160.708 119.117  1.00 88.12           C  
ATOM   2425  N   THR H 110     152.792 162.245 115.057  1.00 90.03           N  
ATOM   2426  CA  THR H 110     152.100 163.167 114.170  1.00 90.03           C  
ATOM   2427  C   THR H 110     150.623 163.207 114.531  1.00 90.03           C  
ATOM   2428  O   THR H 110     150.087 162.265 115.121  1.00 90.03           O  
ATOM   2429  CB  THR H 110     152.267 162.768 112.700  1.00 90.03           C  
ATOM   2430  OG1 THR H 110     151.866 161.404 112.524  1.00 90.03           O  
ATOM   2431  CG2 THR H 110     153.715 162.923 112.269  1.00 90.03           C  
ATOM   2432  N   VAL H 111     149.966 164.310 114.179  1.00 92.20           N  
ATOM   2433  CA  VAL H 111     148.559 164.526 114.496  1.00 92.20           C  
ATOM   2434  C   VAL H 111     147.779 164.667 113.197  1.00 92.20           C  
ATOM   2435  O   VAL H 111     148.161 165.446 112.316  1.00 92.20           O  
ATOM   2436  CB  VAL H 111     148.360 165.760 115.397  1.00 92.20           C  
ATOM   2437  CG1 VAL H 111     148.816 165.456 116.814  1.00 92.20           C  
ATOM   2438  CG2 VAL H 111     149.113 166.960 114.843  1.00 92.20           C  
ATOM   2439  N   SER H 112     146.698 163.904 113.077  1.00 94.49           N  
ATOM   2440  CA  SER H 112     145.798 163.973 111.934  1.00 94.49           C  
ATOM   2441  C   SER H 112     144.492 164.607 112.390  1.00 94.49           C  
ATOM   2442  O   SER H 112     143.721 163.986 113.129  1.00 94.49           O  
ATOM   2443  CB  SER H 112     145.549 162.586 111.343  1.00 94.49           C  
ATOM   2444  OG  SER H 112     146.761 161.984 110.921  1.00 94.49           O  
ATOM   2445  N   SER H 113     144.249 165.838 111.952  1.00 93.63           N  
ATOM   2446  CA  SER H 113     143.051 166.570 112.344  1.00 93.63           C  
ATOM   2447  C   SER H 113     141.795 165.889 111.816  1.00 93.63           C  
ATOM   2448  O   SER H 113     140.702 166.070 112.352  1.00 93.63           O  
ATOM   2449  CB  SER H 113     143.118 168.013 111.841  1.00 93.63           C  
ATOM   2450  OG  SER H 113     144.266 168.674 112.344  1.00 93.63           O  
TER    2451      SER H 113                                                      
ATOM   2452  N   GLU L   1     163.666 183.367 134.953  1.00 68.68           N  
ATOM   2453  CA  GLU L   1     163.435 183.113 133.536  1.00 68.68           C  
ATOM   2454  C   GLU L   1     164.730 183.266 132.750  1.00 68.68           C  
ATOM   2455  O   GLU L   1     164.960 184.289 132.108  1.00 68.68           O  
ATOM   2456  CB  GLU L   1     162.370 184.060 132.985  1.00 68.68           C  
ATOM   2457  CG  GLU L   1     161.757 183.604 131.674  1.00 68.68           C  
ATOM   2458  CD  GLU L   1     160.816 182.429 131.851  1.00 68.68           C  
ATOM   2459  OE1 GLU L   1     160.335 182.217 132.984  1.00 68.68           O  
ATOM   2460  OE2 GLU L   1     160.558 181.715 130.859  1.00 68.68           O  
ATOM   2461  N   ILE L   2     165.571 182.240 132.803  1.00 73.34           N  
ATOM   2462  CA  ILE L   2     166.882 182.269 132.165  1.00 73.34           C  
ATOM   2463  C   ILE L   2     166.764 181.669 130.771  1.00 73.34           C  
ATOM   2464  O   ILE L   2     166.385 180.503 130.617  1.00 73.34           O  
ATOM   2465  CB  ILE L   2     167.920 181.511 133.003  1.00 73.34           C  
ATOM   2466  CG1 ILE L   2     168.009 182.110 134.406  1.00 73.34           C  
ATOM   2467  CG2 ILE L   2     169.275 181.542 132.324  1.00 73.34           C  
ATOM   2468  CD1 ILE L   2     169.013 181.420 135.295  1.00 73.34           C  
ATOM   2469  N   VAL L   3     167.091 182.462 129.756  1.00 72.45           N  
ATOM   2470  CA  VAL L   3     167.080 182.015 128.369  1.00 72.45           C  
ATOM   2471  C   VAL L   3     168.516 181.937 127.876  1.00 72.45           C  
ATOM   2472  O   VAL L   3     169.263 182.920 127.949  1.00 72.45           O  
ATOM   2473  CB  VAL L   3     166.240 182.951 127.484  1.00 72.45           C  
ATOM   2474  CG1 VAL L   3     166.504 184.408 127.838  1.00 72.45           C  
ATOM   2475  CG2 VAL L   3     166.536 182.695 126.017  1.00 72.45           C  
ATOM   2476  N   MET L   4     168.907 180.767 127.373  1.00 72.71           N  
ATOM   2477  CA  MET L   4     170.274 180.551 126.905  1.00 72.71           C  
ATOM   2478  C   MET L   4     170.411 181.075 125.476  1.00 72.71           C  
ATOM   2479  O   MET L   4     170.490 180.328 124.498  1.00 72.71           O  
ATOM   2480  CB  MET L   4     170.647 179.081 127.008  1.00 72.71           C  
ATOM   2481  CG  MET L   4     170.598 178.569 128.426  1.00 72.71           C  
ATOM   2482  SD  MET L   4     171.448 179.697 129.542  1.00 72.71           S  
ATOM   2483  CE  MET L   4     173.135 179.508 128.977  1.00 72.71           C  
ATOM   2484  N   THR L   5     170.433 182.401 125.372  1.00 73.17           N  
ATOM   2485  CA  THR L   5     170.622 183.045 124.082  1.00 73.17           C  
ATOM   2486  C   THR L   5     171.968 182.654 123.485  1.00 73.17           C  
ATOM   2487  O   THR L   5     173.001 182.713 124.157  1.00 73.17           O  
ATOM   2488  CB  THR L   5     170.531 184.563 124.234  1.00 73.17           C  
ATOM   2489  OG1 THR L   5     171.498 185.007 125.194  1.00 73.17           O  
ATOM   2490  CG2 THR L   5     169.144 184.967 124.700  1.00 73.17           C  
ATOM   2491  N   GLN L   6     171.950 182.248 122.222  1.00 71.60           N  
ATOM   2492  CA  GLN L   6     173.159 181.924 121.475  1.00 71.60           C  
ATOM   2493  C   GLN L   6     173.290 182.946 120.355  1.00 71.60           C  
ATOM   2494  O   GLN L   6     172.403 183.053 119.501  1.00 71.60           O  
ATOM   2495  CB  GLN L   6     173.097 180.500 120.932  1.00 71.60           C  
ATOM   2496  CG  GLN L   6     172.684 179.473 121.974  1.00 71.60           C  
ATOM   2497  CD  GLN L   6     172.571 178.069 121.408  1.00 71.60           C  
ATOM   2498  OE1 GLN L   6     171.497 177.469 121.421  1.00 71.60           O  
ATOM   2499  NE2 GLN L   6     173.682 177.536 120.920  1.00 71.60           N  
ATOM   2500  N   SER L   7     174.394 183.699 120.359  1.00 75.17           N  
ATOM   2501  CA  SER L   7     174.528 184.789 119.392  1.00 75.17           C  
ATOM   2502  C   SER L   7     174.764 184.287 117.972  1.00 75.17           C  
ATOM   2503  O   SER L   7     174.029 184.713 117.064  1.00 75.17           O  
ATOM   2504  CB  SER L   7     175.617 185.763 119.852  1.00 75.17           C  
ATOM   2505  OG  SER L   7     175.805 186.808 118.915  1.00 75.17           O  
ATOM   2506  N   PRO L   8     175.744 183.411 117.693  1.00 76.07           N  
ATOM   2507  CA  PRO L   8     175.905 182.964 116.293  1.00 76.07           C  
ATOM   2508  C   PRO L   8     175.036 181.751 115.972  1.00 76.07           C  
ATOM   2509  O   PRO L   8     175.512 180.622 115.806  1.00 76.07           O  
ATOM   2510  CB  PRO L   8     177.400 182.652 116.225  1.00 76.07           C  
ATOM   2511  CG  PRO L   8     177.704 182.121 117.581  1.00 76.07           C  
ATOM   2512  CD  PRO L   8     176.802 182.850 118.554  1.00 76.07           C  
ATOM   2513  N   ALA L   9     173.725 181.984 115.877  1.00 78.80           N  
ATOM   2514  CA  ALA L   9     172.799 180.891 115.596  1.00 78.80           C  
ATOM   2515  C   ALA L   9     173.082 180.265 114.237  1.00 78.80           C  
ATOM   2516  O   ALA L   9     173.023 179.039 114.083  1.00 78.80           O  
ATOM   2517  CB  ALA L   9     171.357 181.389 115.670  1.00 78.80           C  
ATOM   2518  N   THR L  10     173.394 181.090 113.239  1.00 84.58           N  
ATOM   2519  CA  THR L  10     173.713 180.613 111.902  1.00 84.58           C  
ATOM   2520  C   THR L  10     175.216 180.518 111.667  1.00 84.58           C  
ATOM   2521  O   THR L  10     175.675 180.707 110.536  1.00 84.58           O  
ATOM   2522  CB  THR L  10     173.067 181.516 110.851  1.00 84.58           C  
ATOM   2523  OG1 THR L  10     173.516 181.131 109.546  1.00 84.58           O  
ATOM   2524  CG2 THR L  10     173.432 182.973 111.104  1.00 84.58           C  
ATOM   2525  N   LEU L  11     175.990 180.238 112.714  1.00 82.02           N  
ATOM   2526  CA  LEU L  11     177.437 180.124 112.579  1.00 82.02           C  
ATOM   2527  C   LEU L  11     177.788 179.035 111.575  1.00 82.02           C  
ATOM   2528  O   LEU L  11     177.263 177.921 111.637  1.00 82.02           O  
ATOM   2529  CB  LEU L  11     178.066 179.823 113.942  1.00 82.02           C  
ATOM   2530  CG  LEU L  11     179.548 180.137 114.173  1.00 82.02           C  
ATOM   2531  CD1 LEU L  11     180.462 179.101 113.532  1.00 82.02           C  
ATOM   2532  CD2 LEU L  11     179.882 181.533 113.670  1.00 82.02           C  
ATOM   2533  N   SER L  12     178.679 179.363 110.645  1.00 85.41           N  
ATOM   2534  CA  SER L  12     179.049 178.453 109.572  1.00 85.41           C  
ATOM   2535  C   SER L  12     180.523 178.628 109.249  1.00 85.41           C  
ATOM   2536  O   SER L  12     180.988 179.754 109.047  1.00 85.41           O  
ATOM   2537  CB  SER L  12     178.196 178.705 108.328  1.00 85.41           C  
ATOM   2538  OG  SER L  12     176.817 178.668 108.649  1.00 85.41           O  
ATOM   2539  N   VAL L  13     181.253 177.517 109.202  1.00 88.36           N  
ATOM   2540  CA  VAL L  13     182.681 177.519 108.915  1.00 88.36           C  
ATOM   2541  C   VAL L  13     182.999 176.353 107.991  1.00 88.36           C  
ATOM   2542  O   VAL L  13     182.494 175.242 108.185  1.00 88.36           O  
ATOM   2543  CB  VAL L  13     183.519 177.436 110.204  1.00 88.36           C  
ATOM   2544  CG1 VAL L  13     183.524 178.776 110.915  1.00 88.36           C  
ATOM   2545  CG2 VAL L  13     182.977 176.353 111.118  1.00 88.36           C  
ATOM   2546  N   SER L  14     183.828 176.612 106.985  1.00 87.76           N  
ATOM   2547  CA  SER L  14     184.379 175.535 106.185  1.00 87.76           C  
ATOM   2548  C   SER L  14     185.345 174.715 107.039  1.00 87.76           C  
ATOM   2549  O   SER L  14     185.829 175.195 108.067  1.00 87.76           O  
ATOM   2550  CB  SER L  14     185.096 176.096 104.960  1.00 87.76           C  
ATOM   2551  OG  SER L  14     184.194 176.797 104.121  1.00 87.76           O  
ATOM   2552  N   PRO L  15     185.618 173.468 106.655  1.00 91.31           N  
ATOM   2553  CA  PRO L  15     186.525 172.636 107.456  1.00 91.31           C  
ATOM   2554  C   PRO L  15     187.863 173.324 107.681  1.00 91.31           C  
ATOM   2555  O   PRO L  15     188.490 173.830 106.749  1.00 91.31           O  
ATOM   2556  CB  PRO L  15     186.676 171.369 106.611  1.00 91.31           C  
ATOM   2557  CG  PRO L  15     185.412 171.290 105.843  1.00 91.31           C  
ATOM   2558  CD  PRO L  15     185.027 172.711 105.538  1.00 91.31           C  
ATOM   2559  N   GLY L  16     188.295 173.342 108.937  1.00 91.63           N  
ATOM   2560  CA  GLY L  16     189.519 174.028 109.293  1.00 91.63           C  
ATOM   2561  C   GLY L  16     189.987 173.598 110.665  1.00 91.63           C  
ATOM   2562  O   GLY L  16     189.336 172.810 111.354  1.00 91.63           O  
ATOM   2563  N   GLU L  17     191.142 174.138 111.054  1.00 93.11           N  
ATOM   2564  CA  GLU L  17     191.741 173.766 112.330  1.00 93.11           C  
ATOM   2565  C   GLU L  17     190.923 174.288 113.505  1.00 93.11           C  
ATOM   2566  O   GLU L  17     190.874 173.654 114.564  1.00 93.11           O  
ATOM   2567  CB  GLU L  17     193.177 174.285 112.401  1.00 93.11           C  
ATOM   2568  CG  GLU L  17     194.034 173.614 113.460  1.00 93.11           C  
ATOM   2569  CD  GLU L  17     194.438 172.201 113.078  1.00 93.11           C  
ATOM   2570  OE1 GLU L  17     194.242 171.818 111.906  1.00 93.11           O  
ATOM   2571  OE2 GLU L  17     194.953 171.472 113.952  1.00 93.11           O  
ATOM   2572  N   ARG L  18     190.281 175.441 113.344  1.00 86.59           N  
ATOM   2573  CA  ARG L  18     189.598 176.119 114.437  1.00 86.59           C  
ATOM   2574  C   ARG L  18     188.120 176.273 114.119  1.00 86.59           C  
ATOM   2575  O   ARG L  18     187.756 176.629 112.994  1.00 86.59           O  
ATOM   2576  CB  ARG L  18     190.223 177.491 114.700  1.00 86.59           C  
ATOM   2577  CG  ARG L  18     189.523 178.305 115.773  1.00 86.59           C  
ATOM   2578  CD  ARG L  18     190.138 179.687 115.876  1.00 86.59           C  
ATOM   2579  NE  ARG L  18     190.092 180.387 114.598  1.00 86.59           N  
ATOM   2580  CZ  ARG L  18     190.738 181.514 114.337  1.00 86.59           C  
ATOM   2581  NH1 ARG L  18     191.505 182.097 115.244  1.00 86.59           N  
ATOM   2582  NH2 ARG L  18     190.616 182.069 113.135  1.00 86.59           N  
ATOM   2583  N   ALA L  19     187.277 176.001 115.111  1.00 87.00           N  
ATOM   2584  CA  ALA L  19     185.845 176.251 115.036  1.00 87.00           C  
ATOM   2585  C   ALA L  19     185.398 176.929 116.320  1.00 87.00           C  
ATOM   2586  O   ALA L  19     185.856 176.572 117.409  1.00 87.00           O  
ATOM   2587  CB  ALA L  19     185.057 174.958 114.824  1.00 87.00           C  
ATOM   2588  N   THR L  20     184.506 177.905 116.194  1.00 83.61           N  
ATOM   2589  CA  THR L  20     184.081 178.722 117.321  1.00 83.61           C  
ATOM   2590  C   THR L  20     182.567 178.677 117.462  1.00 83.61           C  
ATOM   2591  O   THR L  20     181.841 178.863 116.481  1.00 83.61           O  
ATOM   2592  CB  THR L  20     184.550 180.167 117.152  1.00 83.61           C  
ATOM   2593  OG1 THR L  20     184.202 180.630 115.841  1.00 83.61           O  
ATOM   2594  CG2 THR L  20     186.054 180.257 117.332  1.00 83.61           C  
ATOM   2595  N   LEU L  21     182.101 178.427 118.684  1.00 84.53           N  
ATOM   2596  CA  LEU L  21     180.688 178.480 119.033  1.00 84.53           C  
ATOM   2597  C   LEU L  21     180.546 179.254 120.334  1.00 84.53           C  
ATOM   2598  O   LEU L  21     181.479 179.296 121.139  1.00 84.53           O  
ATOM   2599  CB  LEU L  21     180.079 177.078 119.183  1.00 84.53           C  
ATOM   2600  CG  LEU L  21     179.841 176.248 117.918  1.00 84.53           C  
ATOM   2601  CD1 LEU L  21     181.120 175.585 117.431  1.00 84.53           C  
ATOM   2602  CD2 LEU L  21     178.760 175.210 118.160  1.00 84.53           C  
ATOM   2603  N   SER L  22     179.383 179.867 120.538  1.00 79.11           N  
ATOM   2604  CA  SER L  22     179.157 180.738 121.683  1.00 79.11           C  
ATOM   2605  C   SER L  22     177.836 180.400 122.355  1.00 79.11           C  
ATOM   2606  O   SER L  22     176.933 179.844 121.726  1.00 79.11           O  
ATOM   2607  CB  SER L  22     179.157 182.212 121.266  1.00 79.11           C  
ATOM   2608  OG  SER L  22     180.368 182.555 120.614  1.00 79.11           O  
ATOM   2609  N   CYS L  23     177.736 180.736 123.639  1.00 80.28           N  
ATOM   2610  CA  CYS L  23     176.501 180.607 124.398  1.00 80.28           C  
ATOM   2611  C   CYS L  23     176.489 181.637 125.517  1.00 80.28           C  
ATOM   2612  O   CYS L  23     177.515 181.881 126.158  1.00 80.28           O  
ATOM   2613  CB  CYS L  23     176.341 179.199 124.979  1.00 80.28           C  
ATOM   2614  SG  CYS L  23     174.775 178.939 125.845  1.00 80.28           S  
ATOM   2615  N   ARG L  24     175.325 182.236 125.750  1.00 78.67           N  
ATOM   2616  CA  ARG L  24     175.165 183.265 126.766  1.00 78.67           C  
ATOM   2617  C   ARG L  24     173.927 182.980 127.600  1.00 78.67           C  
ATOM   2618  O   ARG L  24     173.027 182.246 127.187  1.00 78.67           O  
ATOM   2619  CB  ARG L  24     175.059 184.666 126.148  1.00 78.67           C  
ATOM   2620  CG  ARG L  24     176.385 185.268 125.715  1.00 78.67           C  
ATOM   2621  CD  ARG L  24     176.204 186.705 125.253  1.00 78.67           C  
ATOM   2622  NE  ARG L  24     175.388 187.472 126.186  1.00 78.67           N  
ATOM   2623  CZ  ARG L  24     175.859 188.095 127.258  1.00 78.67           C  
ATOM   2624  NH1 ARG L  24     177.146 188.068 127.563  1.00 78.67           N  
ATOM   2625  NH2 ARG L  24     175.017 188.759 128.045  1.00 78.67           N  
ATOM   2626  N   ALA L  25     173.892 183.576 128.787  1.00 75.23           N  
ATOM   2627  CA  ALA L  25     172.779 183.417 129.708  1.00 75.23           C  
ATOM   2628  C   ALA L  25     172.275 184.783 130.140  1.00 75.23           C  
ATOM   2629  O   ALA L  25     173.028 185.762 130.139  1.00 75.23           O  
ATOM   2630  CB  ALA L  25     173.185 182.604 130.937  1.00 75.23           C  
ATOM   2631  N   SER L  26     170.994 184.844 130.503  1.00 77.43           N  
ATOM   2632  CA  SER L  26     170.424 186.098 130.984  1.00 77.43           C  
ATOM   2633  C   SER L  26     170.875 186.399 132.408  1.00 77.43           C  
ATOM   2634  O   SER L  26     170.952 187.567 132.806  1.00 77.43           O  
ATOM   2635  CB  SER L  26     168.901 186.047 130.903  1.00 77.43           C  
ATOM   2636  OG  SER L  26     168.382 185.072 131.788  1.00 77.43           O  
ATOM   2637  N   GLN L  27     171.163 185.366 133.193  1.00 75.90           N  
ATOM   2638  CA  GLN L  27     171.630 185.536 134.559  1.00 75.90           C  
ATOM   2639  C   GLN L  27     172.906 184.736 134.781  1.00 75.90           C  
ATOM   2640  O   GLN L  27     173.403 184.054 133.882  1.00 75.90           O  
ATOM   2641  CB  GLN L  27     170.563 185.114 135.574  1.00 75.90           C  
ATOM   2642  CG  GLN L  27     169.336 186.001 135.571  1.00 75.90           C  
ATOM   2643  CD  GLN L  27     168.410 185.704 136.726  1.00 75.90           C  
ATOM   2644  OE1 GLN L  27     168.737 184.914 137.610  1.00 75.90           O  
ATOM   2645  NE2 GLN L  27     167.245 186.339 136.728  1.00 75.90           N  
ATOM   2646  N   SER L  28     173.432 184.834 135.999  1.00 72.65           N  
ATOM   2647  CA  SER L  28     174.689 184.178 136.330  1.00 72.65           C  
ATOM   2648  C   SER L  28     174.537 182.663 136.302  1.00 72.65           C  
ATOM   2649  O   SER L  28     173.558 182.112 136.814  1.00 72.65           O  
ATOM   2650  CB  SER L  28     175.172 184.634 137.706  1.00 72.65           C  
ATOM   2651  OG  SER L  28     174.224 184.314 138.707  1.00 72.65           O  
ATOM   2652  N   VAL L  29     175.515 181.991 135.699  1.00 74.07           N  
ATOM   2653  CA  VAL L  29     175.570 180.534 135.634  1.00 74.07           C  
ATOM   2654  C   VAL L  29     176.839 180.087 136.343  1.00 74.07           C  
ATOM   2655  O   VAL L  29     177.935 180.562 136.022  1.00 74.07           O  
ATOM   2656  CB  VAL L  29     175.542 180.021 134.185  1.00 74.07           C  
ATOM   2657  CG1 VAL L  29     175.862 178.537 134.139  1.00 74.07           C  
ATOM   2658  CG2 VAL L  29     174.189 180.292 133.558  1.00 74.07           C  
ATOM   2659  N   SER L  30     176.694 179.176 137.305  1.00 75.41           N  
ATOM   2660  CA  SER L  30     177.833 178.697 138.090  1.00 75.41           C  
ATOM   2661  C   SER L  30     178.518 177.536 137.366  1.00 75.41           C  
ATOM   2662  O   SER L  30     178.752 176.460 137.918  1.00 75.41           O  
ATOM   2663  CB  SER L  30     177.380 178.298 139.489  1.00 75.41           C  
ATOM   2664  OG  SER L  30     178.448 177.735 140.230  1.00 75.41           O  
ATOM   2665  N   SER L  31     178.855 177.790 136.101  1.00 73.77           N  
ATOM   2666  CA  SER L  31     179.604 176.845 135.272  1.00 73.77           C  
ATOM   2667  C   SER L  31     178.917 175.483 135.205  1.00 73.77           C  
ATOM   2668  O   SER L  31     179.556 174.434 135.310  1.00 73.77           O  
ATOM   2669  CB  SER L  31     181.041 176.702 135.774  1.00 73.77           C  
ATOM   2670  OG  SER L  31     181.682 177.963 135.840  1.00 73.77           O  
ATOM   2671  N   ASP L  32     177.598 175.496 135.031  1.00 69.95           N  
ATOM   2672  CA  ASP L  32     176.817 174.274 134.908  1.00 69.95           C  
ATOM   2673  C   ASP L  32     176.330 174.026 133.487  1.00 69.95           C  
ATOM   2674  O   ASP L  32     175.227 173.503 133.302  1.00 69.95           O  
ATOM   2675  CB  ASP L  32     175.630 174.306 135.869  1.00 69.95           C  
ATOM   2676  CG  ASP L  32     175.901 173.540 137.143  1.00 69.95           C  
ATOM   2677  OD1 ASP L  32     176.731 172.609 137.106  1.00 69.95           O  
ATOM   2678  OD2 ASP L  32     175.284 173.864 138.179  1.00 69.95           O  
ATOM   2679  N   LEU L  33     177.122 174.386 132.485  1.00 69.55           N  
ATOM   2680  CA  LEU L  33     176.692 174.255 131.103  1.00 69.55           C  
ATOM   2681  C   LEU L  33     176.801 172.813 130.624  1.00 69.55           C  
ATOM   2682  O   LEU L  33     177.410 171.959 131.273  1.00 69.55           O  
ATOM   2683  CB  LEU L  33     177.530 175.152 130.200  1.00 69.55           C  
ATOM   2684  CG  LEU L  33     176.778 175.700 128.992  1.00 69.55           C  
ATOM   2685  CD1 LEU L  33     175.874 176.839 129.432  1.00 69.55           C  
ATOM   2686  CD2 LEU L  33     177.745 176.137 127.910  1.00 69.55           C  
ATOM   2687  N   ALA L  34     176.190 172.549 129.474  1.00 62.61           N  
ATOM   2688  CA  ALA L  34     176.340 171.290 128.765  1.00 62.61           C  
ATOM   2689  C   ALA L  34     176.088 171.526 127.285  1.00 62.61           C  
ATOM   2690  O   ALA L  34     175.296 172.391 126.905  1.00 62.61           O  
ATOM   2691  CB  ALA L  34     175.384 170.219 129.299  1.00 62.61           C  
ATOM   2692  N   TRP L  35     176.772 170.753 126.450  1.00 70.12           N  
ATOM   2693  CA  TRP L  35     176.623 170.833 125.002  1.00 70.12           C  
ATOM   2694  C   TRP L  35     176.125 169.490 124.488  1.00 70.12           C  
ATOM   2695  O   TRP L  35     176.715 168.449 124.796  1.00 70.12           O  
ATOM   2696  CB  TRP L  35     177.943 171.212 124.330  1.00 70.12           C  
ATOM   2697  CG  TRP L  35     178.469 172.555 124.736  1.00 70.12           C  
ATOM   2698  CD1 TRP L  35     179.299 172.826 125.779  1.00 70.12           C  
ATOM   2699  CD2 TRP L  35     178.202 173.810 124.101  1.00 70.12           C  
ATOM   2700  NE1 TRP L  35     179.564 174.170 125.839  1.00 70.12           N  
ATOM   2701  CE2 TRP L  35     178.902 174.797 124.818  1.00 70.12           C  
ATOM   2702  CE3 TRP L  35     177.437 174.195 122.998  1.00 70.12           C  
ATOM   2703  CZ2 TRP L  35     178.861 176.143 124.470  1.00 70.12           C  
ATOM   2704  CZ3 TRP L  35     177.397 175.533 122.653  1.00 70.12           C  
ATOM   2705  CH2 TRP L  35     178.104 176.490 123.386  1.00 70.12           C  
ATOM   2706  N   TYR L  36     175.042 169.512 123.719  1.00 64.04           N  
ATOM   2707  CA  TYR L  36     174.476 168.309 123.126  1.00 64.04           C  
ATOM   2708  C   TYR L  36     174.655 168.366 121.617  1.00 64.04           C  
ATOM   2709  O   TYR L  36     174.296 169.364 120.985  1.00 64.04           O  
ATOM   2710  CB  TYR L  36     172.993 168.163 123.471  1.00 64.04           C  
ATOM   2711  CG  TYR L  36     172.689 168.218 124.948  1.00 64.04           C  
ATOM   2712  CD1 TYR L  36     173.609 167.779 125.882  1.00 64.04           C  
ATOM   2713  CD2 TYR L  36     171.478 168.715 125.407  1.00 64.04           C  
ATOM   2714  CE1 TYR L  36     173.335 167.834 127.231  1.00 64.04           C  
ATOM   2715  CE2 TYR L  36     171.196 168.771 126.753  1.00 64.04           C  
ATOM   2716  CZ  TYR L  36     172.128 168.329 127.660  1.00 64.04           C  
ATOM   2717  OH  TYR L  36     171.857 168.381 129.006  1.00 64.04           O  
ATOM   2718  N   GLN L  37     175.208 167.301 121.046  1.00 71.13           N  
ATOM   2719  CA  GLN L  37     175.380 167.202 119.604  1.00 71.13           C  
ATOM   2720  C   GLN L  37     174.140 166.553 119.003  1.00 71.13           C  
ATOM   2721  O   GLN L  37     173.905 165.356 119.197  1.00 71.13           O  
ATOM   2722  CB  GLN L  37     176.630 166.397 119.258  1.00 71.13           C  
ATOM   2723  CG  GLN L  37     176.906 166.293 117.769  1.00 71.13           C  
ATOM   2724  CD  GLN L  37     178.105 165.420 117.458  1.00 71.13           C  
ATOM   2725  OE1 GLN L  37     178.638 164.744 118.338  1.00 71.13           O  
ATOM   2726  NE2 GLN L  37     178.537 165.430 116.202  1.00 71.13           N  
ATOM   2727  N   GLN L  38     173.354 167.338 118.278  1.00 69.84           N  
ATOM   2728  CA  GLN L  38     172.119 166.870 117.660  1.00 69.84           C  
ATOM   2729  C   GLN L  38     172.360 166.774 116.161  1.00 69.84           C  
ATOM   2730  O   GLN L  38     172.304 167.784 115.452  1.00 69.84           O  
ATOM   2731  CB  GLN L  38     170.958 167.810 117.981  1.00 69.84           C  
ATOM   2732  CG  GLN L  38     169.582 167.156 117.972  1.00 69.84           C  
ATOM   2733  CD  GLN L  38     168.981 167.043 116.583  1.00 69.84           C  
ATOM   2734  OE1 GLN L  38     169.527 167.562 115.611  1.00 69.84           O  
ATOM   2735  NE2 GLN L  38     167.844 166.366 116.487  1.00 69.84           N  
ATOM   2736  N   LYS L  39     172.642 165.568 115.685  1.00 77.05           N  
ATOM   2737  CA  LYS L  39     172.863 165.368 114.263  1.00 77.05           C  
ATOM   2738  C   LYS L  39     171.535 165.392 113.512  1.00 77.05           C  
ATOM   2739  O   LYS L  39     170.461 165.181 114.084  1.00 77.05           O  
ATOM   2740  CB  LYS L  39     173.602 164.054 114.018  1.00 77.05           C  
ATOM   2741  CG  LYS L  39     174.803 164.185 113.100  1.00 77.05           C  
ATOM   2742  CD  LYS L  39     175.839 163.117 113.403  1.00 77.05           C  
ATOM   2743  CE  LYS L  39     176.358 163.251 114.825  1.00 77.05           C  
ATOM   2744  NZ  LYS L  39     177.390 162.228 115.143  1.00 77.05           N  
ATOM   2745  N   ARG L  40     171.619 165.670 112.213  1.00 83.28           N  
ATOM   2746  CA  ARG L  40     170.422 165.764 111.387  1.00 83.28           C  
ATOM   2747  C   ARG L  40     169.680 164.435 111.371  1.00 83.28           C  
ATOM   2748  O   ARG L  40     170.232 163.405 110.975  1.00 83.28           O  
ATOM   2749  CB  ARG L  40     170.793 166.179 109.964  1.00 83.28           C  
ATOM   2750  CG  ARG L  40     171.406 167.564 109.856  1.00 83.28           C  
ATOM   2751  CD  ARG L  40     170.419 168.636 110.281  1.00 83.28           C  
ATOM   2752  NE  ARG L  40     169.202 168.608 109.479  1.00 83.28           N  
ATOM   2753  CZ  ARG L  40     169.028 169.293 108.357  1.00 83.28           C  
ATOM   2754  NH1 ARG L  40     169.981 170.067 107.865  1.00 83.28           N  
ATOM   2755  NH2 ARG L  40     167.868 169.199 107.713  1.00 83.28           N  
ATOM   2756  N   GLY L  41     168.423 164.465 111.799  1.00 81.18           N  
ATOM   2757  CA  GLY L  41     167.640 163.243 111.891  1.00 81.18           C  
ATOM   2758  C   GLY L  41     168.215 162.237 112.862  1.00 81.18           C  
ATOM   2759  O   GLY L  41     168.241 161.036 112.568  1.00 81.18           O  
ATOM   2760  N   GLN L  42     168.685 162.702 114.017  1.00 80.02           N  
ATOM   2761  CA  GLN L  42     169.311 161.838 115.004  1.00 80.02           C  
ATOM   2762  C   GLN L  42     168.916 162.299 116.398  1.00 80.02           C  
ATOM   2763  O   GLN L  42     168.514 163.446 116.606  1.00 80.02           O  
ATOM   2764  CB  GLN L  42     170.840 161.837 114.872  1.00 80.02           C  
ATOM   2765  CG  GLN L  42     171.373 161.187 113.606  1.00 80.02           C  
ATOM   2766  CD  GLN L  42     171.563 159.693 113.754  1.00 80.02           C  
ATOM   2767  OE1 GLN L  42     171.224 159.111 114.784  1.00 80.02           O  
ATOM   2768  NE2 GLN L  42     172.113 159.062 112.724  1.00 80.02           N  
ATOM   2769  N   ALA L  43     169.030 161.388 117.349  1.00 73.48           N  
ATOM   2770  CA  ALA L  43     168.819 161.762 118.737  1.00 73.48           C  
ATOM   2771  C   ALA L  43     170.037 162.521 119.259  1.00 73.48           C  
ATOM   2772  O   ALA L  43     171.163 162.257 118.831  1.00 73.48           O  
ATOM   2773  CB  ALA L  43     168.567 160.526 119.594  1.00 73.48           C  
ATOM   2774  N   PRO L  44     169.841 163.469 120.175  1.00 65.34           N  
ATOM   2775  CA  PRO L  44     170.983 164.208 120.720  1.00 65.34           C  
ATOM   2776  C   PRO L  44     171.880 163.305 121.550  1.00 65.34           C  
ATOM   2777  O   PRO L  44     171.455 162.264 122.055  1.00 65.34           O  
ATOM   2778  CB  PRO L  44     170.328 165.291 121.586  1.00 65.34           C  
ATOM   2779  CG  PRO L  44     168.929 165.380 121.104  1.00 65.34           C  
ATOM   2780  CD  PRO L  44     168.563 163.998 120.670  1.00 65.34           C  
ATOM   2781  N   ARG L  45     173.144 163.706 121.669  1.00 68.90           N  
ATOM   2782  CA  ARG L  45     174.112 163.024 122.514  1.00 68.90           C  
ATOM   2783  C   ARG L  45     174.866 164.052 123.340  1.00 68.90           C  
ATOM   2784  O   ARG L  45     175.183 165.140 122.852  1.00 68.90           O  
ATOM   2785  CB  ARG L  45     175.095 162.195 121.686  1.00 68.90           C  
ATOM   2786  CG  ARG L  45     176.114 161.442 122.517  1.00 68.90           C  
ATOM   2787  CD  ARG L  45     177.013 160.583 121.648  1.00 68.90           C  
ATOM   2788  NE  ARG L  45     177.843 161.377 120.753  1.00 68.90           N  
ATOM   2789  CZ  ARG L  45     178.991 161.938 121.106  1.00 68.90           C  
ATOM   2790  NH1 ARG L  45     179.470 161.818 122.333  1.00 68.90           N  
ATOM   2791  NH2 ARG L  45     179.674 162.640 120.205  1.00 68.90           N  
ATOM   2792  N   LEU L  46     175.148 163.706 124.591  1.00 64.74           N  
ATOM   2793  CA  LEU L  46     175.880 164.608 125.468  1.00 64.74           C  
ATOM   2794  C   LEU L  46     177.335 164.720 125.031  1.00 64.74           C  
ATOM   2795  O   LEU L  46     177.957 163.734 124.629  1.00 64.74           O  
ATOM   2796  CB  LEU L  46     175.799 164.119 126.911  1.00 64.74           C  
ATOM   2797  CG  LEU L  46     176.574 164.912 127.962  1.00 64.74           C  
ATOM   2798  CD1 LEU L  46     176.050 166.329 128.073  1.00 64.74           C  
ATOM   2799  CD2 LEU L  46     176.508 164.209 129.301  1.00 64.74           C  
ATOM   2800  N   LEU L  47     177.877 165.935 125.110  1.00 72.31           N  
ATOM   2801  CA  LEU L  47     179.264 166.207 124.752  1.00 72.31           C  
ATOM   2802  C   LEU L  47     180.102 166.673 125.932  1.00 72.31           C  
ATOM   2803  O   LEU L  47     181.194 166.145 126.160  1.00 72.31           O  
ATOM   2804  CB  LEU L  47     179.325 167.252 123.630  1.00 72.31           C  
ATOM   2805  CG  LEU L  47     180.722 167.693 123.196  1.00 72.31           C  
ATOM   2806  CD1 LEU L  47     181.483 166.519 122.621  1.00 72.31           C  
ATOM   2807  CD2 LEU L  47     180.627 168.807 122.175  1.00 72.31           C  
ATOM   2808  N   ILE L  48     179.626 167.660 126.689  1.00 68.71           N  
ATOM   2809  CA  ILE L  48     180.369 168.234 127.808  1.00 68.71           C  
ATOM   2810  C   ILE L  48     179.444 168.211 129.018  1.00 68.71           C  
ATOM   2811  O   ILE L  48     178.657 169.143 129.219  1.00 68.71           O  
ATOM   2812  CB  ILE L  48     180.851 169.659 127.517  1.00 68.71           C  
ATOM   2813  CG1 ILE L  48     181.382 169.775 126.088  1.00 68.71           C  
ATOM   2814  CG2 ILE L  48     181.925 170.063 128.501  1.00 68.71           C  
ATOM   2815  CD1 ILE L  48     182.663 169.022 125.848  1.00 68.71           C  
ATOM   2816  N   TYR L  49     179.534 167.159 129.836  1.00 76.88           N  
ATOM   2817  CA  TYR L  49     178.657 167.076 131.001  1.00 76.88           C  
ATOM   2818  C   TYR L  49     179.005 168.148 132.025  1.00 76.88           C  
ATOM   2819  O   TYR L  49     178.124 168.653 132.731  1.00 76.88           O  
ATOM   2820  CB  TYR L  49     178.712 165.682 131.628  1.00 76.88           C  
ATOM   2821  CG  TYR L  49     180.081 165.196 132.039  1.00 76.88           C  
ATOM   2822  CD1 TYR L  49     180.615 165.526 133.277  1.00 76.88           C  
ATOM   2823  CD2 TYR L  49     180.825 164.378 131.203  1.00 76.88           C  
ATOM   2824  CE1 TYR L  49     181.860 165.073 133.660  1.00 76.88           C  
ATOM   2825  CE2 TYR L  49     182.068 163.919 131.579  1.00 76.88           C  
ATOM   2826  CZ  TYR L  49     182.583 164.269 132.806  1.00 76.88           C  
ATOM   2827  OH  TYR L  49     183.824 163.811 133.181  1.00 76.88           O  
ATOM   2828  N   GLY L  50     180.280 168.501 132.130  1.00 68.14           N  
ATOM   2829  CA  GLY L  50     180.674 169.661 132.894  1.00 68.14           C  
ATOM   2830  C   GLY L  50     180.590 170.918 132.057  1.00 68.14           C  
ATOM   2831  O   GLY L  50     180.109 170.921 130.925  1.00 68.14           O  
ATOM   2832  N   ALA L  51     181.059 172.020 132.642  1.00 69.77           N  
ATOM   2833  CA  ALA L  51     181.195 173.248 131.868  1.00 69.77           C  
ATOM   2834  C   ALA L  51     182.223 173.079 130.756  1.00 69.77           C  
ATOM   2835  O   ALA L  51     182.011 173.536 129.627  1.00 69.77           O  
ATOM   2836  CB  ALA L  51     181.573 174.411 132.783  1.00 69.77           C  
ATOM   2837  N   SER L  52     183.341 172.417 131.056  1.00 72.41           N  
ATOM   2838  CA  SER L  52     184.397 172.185 130.084  1.00 72.41           C  
ATOM   2839  C   SER L  52     184.920 170.756 130.078  1.00 72.41           C  
ATOM   2840  O   SER L  52     185.768 170.433 129.238  1.00 72.41           O  
ATOM   2841  CB  SER L  52     185.572 173.141 130.334  1.00 72.41           C  
ATOM   2842  OG  SER L  52     186.081 172.985 131.646  1.00 72.41           O  
ATOM   2843  N   THR L  53     184.450 169.898 130.979  1.00 72.55           N  
ATOM   2844  CA  THR L  53     184.908 168.516 131.037  1.00 72.55           C  
ATOM   2845  C   THR L  53     184.153 167.684 130.008  1.00 72.55           C  
ATOM   2846  O   THR L  53     182.942 167.477 130.138  1.00 72.55           O  
ATOM   2847  CB  THR L  53     184.701 167.949 132.439  1.00 72.55           C  
ATOM   2848  OG1 THR L  53     185.285 168.833 133.403  1.00 72.55           O  
ATOM   2849  CG2 THR L  53     185.352 166.585 132.555  1.00 72.55           C  
ATOM   2850  N   ARG L  54     184.865 167.194 128.996  1.00 80.27           N  
ATOM   2851  CA  ARG L  54     184.217 166.476 127.909  1.00 80.27           C  
ATOM   2852  C   ARG L  54     183.733 165.103 128.377  1.00 80.27           C  
ATOM   2853  O   ARG L  54     184.109 164.605 129.440  1.00 80.27           O  
ATOM   2854  CB  ARG L  54     185.162 166.344 126.718  1.00 80.27           C  
ATOM   2855  CG  ARG L  54     186.552 165.854 127.060  1.00 80.27           C  
ATOM   2856  CD  ARG L  54     187.460 166.002 125.855  1.00 80.27           C  
ATOM   2857  NE  ARG L  54     188.806 165.505 126.102  1.00 80.27           N  
ATOM   2858  CZ  ARG L  54     189.807 165.609 125.239  1.00 80.27           C  
ATOM   2859  NH1 ARG L  54     189.648 166.197 124.065  1.00 80.27           N  
ATOM   2860  NH2 ARG L  54     190.998 165.113 125.563  1.00 80.27           N  
ATOM   2861  N   ALA L  55     182.890 164.488 127.551  1.00 81.32           N  
ATOM   2862  CA  ALA L  55     182.152 163.300 127.952  1.00 81.32           C  
ATOM   2863  C   ALA L  55     183.053 162.070 128.014  1.00 81.32           C  
ATOM   2864  O   ALA L  55     184.217 162.089 127.607  1.00 81.32           O  
ATOM   2865  CB  ALA L  55     180.994 163.038 126.991  1.00 81.32           C  
ATOM   2866  N   THR L  56     182.480 160.981 128.534  1.00 92.55           N  
ATOM   2867  CA  THR L  56     183.214 159.730 128.682  1.00 92.55           C  
ATOM   2868  C   THR L  56     183.348 158.974 127.367  1.00 92.55           C  
ATOM   2869  O   THR L  56     183.962 157.902 127.343  1.00 92.55           O  
ATOM   2870  CB  THR L  56     182.532 158.835 129.717  1.00 92.55           C  
ATOM   2871  OG1 THR L  56     181.170 158.611 129.332  1.00 92.55           O  
ATOM   2872  CG2 THR L  56     182.563 159.487 131.089  1.00 92.55           C  
ATOM   2873  N   GLY L  57     182.674 159.451 126.322  1.00 92.91           N  
ATOM   2874  CA  GLY L  57     182.676 158.700 125.052  1.00 92.91           C  
ATOM   2875  C   GLY L  57     183.956 158.936 124.287  1.00 92.91           C  
ATOM   2876  O   GLY L  57     185.042 158.635 124.815  1.00 92.91           O  
ATOM   2877  N   ILE L  58     183.845 159.460 123.070  1.00 94.99           N  
ATOM   2878  CA  ILE L  58     185.096 159.817 122.344  1.00 94.99           C  
ATOM   2879  C   ILE L  58     184.954 161.250 121.846  1.00 94.99           C  
ATOM   2880  O   ILE L  58     184.902 161.445 120.619  1.00 94.99           O  
ATOM   2881  CB  ILE L  58     185.385 158.837 121.188  1.00 94.99           C  
ATOM   2882  CG1 ILE L  58     184.272 158.834 120.135  1.00 94.99           C  
ATOM   2883  CG2 ILE L  58     185.663 157.440 121.722  1.00 94.99           C  
ATOM   2884  CD1 ILE L  58     184.611 158.054 118.887  1.00 94.99           C  
ATOM   2885  N   PRO L  59     184.909 162.272 122.723  1.00 89.13           N  
ATOM   2886  CA  PRO L  59     184.878 163.639 122.271  1.00 89.13           C  
ATOM   2887  C   PRO L  59     186.328 164.097 122.110  1.00 89.13           C  
ATOM   2888  O   PRO L  59     186.672 165.131 122.635  1.00 89.13           O  
ATOM   2889  CB  PRO L  59     184.214 164.367 123.441  1.00 89.13           C  
ATOM   2890  CG  PRO L  59     183.898 163.289 124.450  1.00 89.13           C  
ATOM   2891  CD  PRO L  59     184.921 162.214 124.178  1.00 89.13           C  
ATOM   2892  N   ALA L  60     187.137 163.328 121.383  1.00 89.67           N  
ATOM   2893  CA  ALA L  60     188.549 163.721 121.205  1.00 89.67           C  
ATOM   2894  C   ALA L  60     188.662 164.906 120.246  1.00 89.67           C  
ATOM   2895  O   ALA L  60     188.026 164.813 119.179  1.00 89.67           O  
ATOM   2896  CB  ALA L  60     189.314 162.590 120.573  1.00 89.67           C  
ATOM   2897  N   ARG L  61     189.397 165.960 120.630  1.00 93.82           N  
ATOM   2898  CA  ARG L  61     189.508 167.197 119.810  1.00 93.82           C  
ATOM   2899  C   ARG L  61     188.306 168.114 120.042  1.00 93.82           C  
ATOM   2900  O   ARG L  61     188.238 169.130 119.362  1.00 93.82           O  
ATOM   2901  CB  ARG L  61     189.778 166.876 118.337  1.00 93.82           C  
ATOM   2902  CG  ARG L  61     191.082 166.125 118.104  1.00 93.82           C  
ATOM   2903  CD  ARG L  61     190.906 164.805 117.379  1.00 93.82           C  
ATOM   2904  NE  ARG L  61     192.189 164.197 117.062  1.00 93.82           N  
ATOM   2905  CZ  ARG L  61     192.433 162.894 117.110  1.00 93.82           C  
ATOM   2906  NH1 ARG L  61     191.474 162.054 117.460  1.00 93.82           N  
ATOM   2907  NH2 ARG L  61     193.633 162.434 116.807  1.00 93.82           N  
ATOM   2908  N   PHE L  62     187.436 167.791 120.998  1.00 89.26           N  
ATOM   2909  CA  PHE L  62     186.293 168.677 121.345  1.00 89.26           C  
ATOM   2910  C   PHE L  62     186.605 169.249 122.720  1.00 89.26           C  
ATOM   2911  O   PHE L  62     186.917 168.457 123.619  1.00 89.26           O  
ATOM   2912  CB  PHE L  62     184.982 167.894 121.440  1.00 89.26           C  
ATOM   2913  CG  PHE L  62     184.392 167.422 120.134  1.00 89.26           C  
ATOM   2914  CD1 PHE L  62     185.028 166.462 119.367  1.00 89.26           C  
ATOM   2915  CD2 PHE L  62     183.181 167.919 119.685  1.00 89.26           C  
ATOM   2916  CE1 PHE L  62     184.482 166.028 118.171  1.00 89.26           C  
ATOM   2917  CE2 PHE L  62     182.632 167.484 118.491  1.00 89.26           C  
ATOM   2918  CZ  PHE L  62     183.284 166.539 117.738  1.00 89.26           C  
ATOM   2919  N   SER L  63     186.529 170.567 122.881  1.00 87.04           N  
ATOM   2920  CA  SER L  63     186.978 171.137 124.175  1.00 87.04           C  
ATOM   2921  C   SER L  63     186.091 172.281 124.639  1.00 87.04           C  
ATOM   2922  O   SER L  63     186.103 173.345 123.991  1.00 87.04           O  
ATOM   2923  CB  SER L  63     188.399 171.607 124.086  1.00 87.04           C  
ATOM   2924  OG  SER L  63     188.653 172.606 125.064  1.00 87.04           O  
ATOM   2925  N   GLY L  64     185.381 172.071 125.745  1.00 79.68           N  
ATOM   2926  CA  GLY L  64     184.611 173.168 126.294  1.00 79.68           C  
ATOM   2927  C   GLY L  64     185.492 174.187 126.989  1.00 79.68           C  
ATOM   2928  O   GLY L  64     186.625 173.906 127.380  1.00 79.68           O  
ATOM   2929  N   SER L  65     184.956 175.396 127.140  1.00 82.00           N  
ATOM   2930  CA  SER L  65     185.677 176.473 127.800  1.00 82.00           C  
ATOM   2931  C   SER L  65     184.702 177.580 128.168  1.00 82.00           C  
ATOM   2932  O   SER L  65     183.644 177.725 127.550  1.00 82.00           O  
ATOM   2933  CB  SER L  65     186.799 177.025 126.913  1.00 82.00           C  
ATOM   2934  OG  SER L  65     186.319 177.311 125.613  1.00 82.00           O  
ATOM   2935  N   GLY L  66     185.066 178.353 129.185  1.00 79.84           N  
ATOM   2936  CA  GLY L  66     184.292 179.503 129.596  1.00 79.84           C  
ATOM   2937  C   GLY L  66     183.547 179.270 130.901  1.00 79.84           C  
ATOM   2938  O   GLY L  66     183.237 178.141 131.289  1.00 79.84           O  
ATOM   2939  N   SER L  67     183.260 180.373 131.589  1.00 78.87           N  
ATOM   2940  CA  SER L  67     182.519 180.342 132.841  1.00 78.87           C  
ATOM   2941  C   SER L  67     181.764 181.653 132.995  1.00 78.87           C  
ATOM   2942  O   SER L  67     182.109 182.666 132.382  1.00 78.87           O  
ATOM   2943  CB  SER L  67     183.443 180.112 134.043  1.00 78.87           C  
ATOM   2944  OG  SER L  67     182.713 180.136 135.258  1.00 78.87           O  
ATOM   2945  N   GLY L  68     180.726 181.624 133.828  1.00 81.22           N  
ATOM   2946  CA  GLY L  68     179.925 182.814 134.045  1.00 81.22           C  
ATOM   2947  C   GLY L  68     178.826 182.969 133.005  1.00 81.22           C  
ATOM   2948  O   GLY L  68     178.122 182.021 132.660  1.00 81.22           O  
ATOM   2949  N   THR L  69     178.675 184.199 132.512  1.00 83.31           N  
ATOM   2950  CA  THR L  69     177.655 184.466 131.503  1.00 83.31           C  
ATOM   2951  C   THR L  69     178.075 183.953 130.131  1.00 83.31           C  
ATOM   2952  O   THR L  69     177.244 183.442 129.371  1.00 83.31           O  
ATOM   2953  CB  THR L  69     177.354 185.963 131.442  1.00 83.31           C  
ATOM   2954  OG1 THR L  69     176.623 186.256 130.245  1.00 83.31           O  
ATOM   2955  CG2 THR L  69     178.643 186.771 131.458  1.00 83.31           C  
ATOM   2956  N   GLU L  70     179.354 184.083 129.792  1.00 87.18           N  
ATOM   2957  CA  GLU L  70     179.839 183.750 128.460  1.00 87.18           C  
ATOM   2958  C   GLU L  70     180.407 182.338 128.438  1.00 87.18           C  
ATOM   2959  O   GLU L  70     181.184 181.958 129.319  1.00 87.18           O  
ATOM   2960  CB  GLU L  70     180.905 184.749 128.011  1.00 87.18           C  
ATOM   2961  CG  GLU L  70     181.482 184.475 126.629  1.00 87.18           C  
ATOM   2962  CD  GLU L  70     180.594 184.980 125.507  1.00 87.18           C  
ATOM   2963  OE1 GLU L  70     179.567 185.624 125.801  1.00 87.18           O  
ATOM   2964  OE2 GLU L  70     180.928 184.737 124.328  1.00 87.18           O  
ATOM   2965  N   PHE L  71     180.018 181.567 127.427  1.00 83.10           N  
ATOM   2966  CA  PHE L  71     180.546 180.230 127.213  1.00 83.10           C  
ATOM   2967  C   PHE L  71     180.903 180.058 125.747  1.00 83.10           C  
ATOM   2968  O   PHE L  71     180.294 180.671 124.867  1.00 83.10           O  
ATOM   2969  CB  PHE L  71     179.547 179.153 127.623  1.00 83.10           C  
ATOM   2970  CG  PHE L  71     179.246 179.130 129.089  1.00 83.10           C  
ATOM   2971  CD1 PHE L  71     180.160 178.615 129.988  1.00 83.10           C  
ATOM   2972  CD2 PHE L  71     178.041 179.609 129.566  1.00 83.10           C  
ATOM   2973  CE1 PHE L  71     179.881 178.587 131.337  1.00 83.10           C  
ATOM   2974  CE2 PHE L  71     177.754 179.580 130.912  1.00 83.10           C  
ATOM   2975  CZ  PHE L  71     178.675 179.071 131.800  1.00 83.10           C  
ATOM   2976  N   THR L  72     181.897 179.212 125.489  1.00 82.92           N  
ATOM   2977  CA  THR L  72     182.356 178.971 124.131  1.00 82.92           C  
ATOM   2978  C   THR L  72     182.812 177.529 123.985  1.00 82.92           C  
ATOM   2979  O   THR L  72     183.158 176.865 124.965  1.00 82.92           O  
ATOM   2980  CB  THR L  72     183.496 179.922 123.742  1.00 82.92           C  
ATOM   2981  OG1 THR L  72     184.048 179.518 122.484  1.00 82.92           O  
ATOM   2982  CG2 THR L  72     184.585 179.911 124.800  1.00 82.92           C  
ATOM   2983  N   LEU L  73     182.807 177.052 122.742  1.00 83.44           N  
ATOM   2984  CA  LEU L  73     183.251 175.708 122.405  1.00 83.44           C  
ATOM   2985  C   LEU L  73     184.177 175.792 121.203  1.00 83.44           C  
ATOM   2986  O   LEU L  73     183.914 176.553 120.268  1.00 83.44           O  
ATOM   2987  CB  LEU L  73     182.060 174.791 122.103  1.00 83.44           C  
ATOM   2988  CG  LEU L  73     182.322 173.349 121.659  1.00 83.44           C  
ATOM   2989  CD1 LEU L  73     183.031 172.600 122.772  1.00 83.44           C  
ATOM   2990  CD2 LEU L  73     181.035 172.627 121.279  1.00 83.44           C  
ATOM   2991  N   THR L  74     185.258 175.017 121.230  1.00 85.06           N  
ATOM   2992  CA  THR L  74     186.201 174.954 120.123  1.00 85.06           C  
ATOM   2993  C   THR L  74     186.580 173.505 119.858  1.00 85.06           C  
ATOM   2994  O   THR L  74     186.695 172.705 120.790  1.00 85.06           O  
ATOM   2995  CB  THR L  74     187.463 175.776 120.406  1.00 85.06           C  
ATOM   2996  OG1 THR L  74     187.962 175.455 121.710  1.00 85.06           O  
ATOM   2997  CG2 THR L  74     187.163 177.265 120.331  1.00 85.06           C  
ATOM   2998  N   ILE L  75     186.774 173.175 118.584  1.00 91.82           N  
ATOM   2999  CA  ILE L  75     187.114 171.824 118.156  1.00 91.82           C  
ATOM   3000  C   ILE L  75     188.260 171.909 117.157  1.00 91.82           C  
ATOM   3001  O   ILE L  75     188.174 172.644 116.167  1.00 91.82           O  
ATOM   3002  CB  ILE L  75     185.896 171.102 117.548  1.00 91.82           C  
ATOM   3003  CG1 ILE L  75     184.800 170.879 118.592  1.00 91.82           C  
ATOM   3004  CG2 ILE L  75     186.318 169.789 116.910  1.00 91.82           C  
ATOM   3005  CD1 ILE L  75     183.682 171.894 118.507  1.00 91.82           C  
ATOM   3006  N   SER L  76     189.338 171.171 117.426  1.00 92.83           N  
ATOM   3007  CA  SER L  76     190.502 171.227 116.549  1.00 92.83           C  
ATOM   3008  C   SER L  76     190.261 170.471 115.250  1.00 92.83           C  
ATOM   3009  O   SER L  76     190.614 170.956 114.169  1.00 92.83           O  
ATOM   3010  CB  SER L  76     191.726 170.665 117.269  1.00 92.83           C  
ATOM   3011  OG  SER L  76     191.563 169.284 117.538  1.00 92.83           O  
ATOM   3012  N   SER L  77     189.661 169.288 115.332  1.00 96.40           N  
ATOM   3013  CA  SER L  77     189.495 168.398 114.188  1.00 96.40           C  
ATOM   3014  C   SER L  77     188.045 168.456 113.724  1.00 96.40           C  
ATOM   3015  O   SER L  77     187.212 167.660 114.170  1.00 96.40           O  
ATOM   3016  CB  SER L  77     189.898 166.971 114.552  1.00 96.40           C  
ATOM   3017  OG  SER L  77     189.563 166.066 113.514  1.00 96.40           O  
ATOM   3018  N   LEU L  78     187.751 169.388 112.819  1.00 94.52           N  
ATOM   3019  CA  LEU L  78     186.403 169.541 112.275  1.00 94.52           C  
ATOM   3020  C   LEU L  78     186.215 168.578 111.102  1.00 94.52           C  
ATOM   3021  O   LEU L  78     186.423 168.905 109.932  1.00 94.52           O  
ATOM   3022  CB  LEU L  78     186.154 170.988 111.869  1.00 94.52           C  
ATOM   3023  CG  LEU L  78     185.360 171.862 112.845  1.00 94.52           C  
ATOM   3024  CD1 LEU L  78     184.737 173.035 112.114  1.00 94.52           C  
ATOM   3025  CD2 LEU L  78     184.279 171.068 113.561  1.00 94.52           C  
ATOM   3026  N   GLN L  79     185.834 167.351 111.445  1.00 96.71           N  
ATOM   3027  CA  GLN L  79     185.470 166.379 110.427  1.00 96.71           C  
ATOM   3028  C   GLN L  79     184.042 166.622 109.951  1.00 96.71           C  
ATOM   3029  O   GLN L  79     183.248 167.297 110.612  1.00 96.71           O  
ATOM   3030  CB  GLN L  79     185.612 164.955 110.964  1.00 96.71           C  
ATOM   3031  CG  GLN L  79     186.476 164.051 110.098  1.00 96.71           C  
ATOM   3032  CD  GLN L  79     185.894 163.830 108.715  1.00 96.71           C  
ATOM   3033  OE1 GLN L  79     184.679 163.868 108.526  1.00 96.71           O  
ATOM   3034  NE2 GLN L  79     186.763 163.601 107.738  1.00 96.71           N  
ATOM   3035  N   SER L  80     183.721 166.060 108.785  1.00 97.51           N  
ATOM   3036  CA  SER L  80     182.393 166.248 108.211  1.00 97.51           C  
ATOM   3037  C   SER L  80     181.310 165.665 109.110  1.00 97.51           C  
ATOM   3038  O   SER L  80     180.240 166.263 109.273  1.00 97.51           O  
ATOM   3039  CB  SER L  80     182.331 165.610 106.824  1.00 97.51           C  
ATOM   3040  OG  SER L  80     182.601 164.221 106.895  1.00 97.51           O  
ATOM   3041  N   GLU L  81     181.568 164.495 109.698  1.00 97.27           N  
ATOM   3042  CA  GLU L  81     180.533 163.803 110.459  1.00 97.27           C  
ATOM   3043  C   GLU L  81     180.112 164.593 111.693  1.00 97.27           C  
ATOM   3044  O   GLU L  81     178.923 164.644 112.027  1.00 97.27           O  
ATOM   3045  CB  GLU L  81     181.018 162.404 110.846  1.00 97.27           C  
ATOM   3046  CG  GLU L  81     181.206 161.449 109.676  1.00 97.27           C  
ATOM   3047  CD  GLU L  81     181.756 160.098 110.095  1.00 97.27           C  
ATOM   3048  OE1 GLU L  81     182.171 159.958 111.264  1.00 97.27           O  
ATOM   3049  OE2 GLU L  81     181.770 159.175 109.254  1.00 97.27           O  
ATOM   3050  N   ASP L  82     181.068 165.222 112.383  1.00 92.39           N  
ATOM   3051  CA  ASP L  82     180.738 165.888 113.640  1.00 92.39           C  
ATOM   3052  C   ASP L  82     179.940 167.165 113.405  1.00 92.39           C  
ATOM   3053  O   ASP L  82     179.420 167.761 114.354  1.00 92.39           O  
ATOM   3054  CB  ASP L  82     182.009 166.185 114.435  1.00 92.39           C  
ATOM   3055  CG  ASP L  82     182.946 167.130 113.714  1.00 92.39           C  
ATOM   3056  OD1 ASP L  82     182.632 168.334 113.622  1.00 92.39           O  
ATOM   3057  OD2 ASP L  82     184.007 166.668 113.248  1.00 92.39           O  
ATOM   3058  N   PHE L  83     179.842 167.606 112.153  1.00 91.53           N  
ATOM   3059  CA  PHE L  83     179.034 168.777 111.839  1.00 91.53           C  
ATOM   3060  C   PHE L  83     177.566 168.506 112.135  1.00 91.53           C  
ATOM   3061  O   PHE L  83     176.952 167.620 111.535  1.00 91.53           O  
ATOM   3062  CB  PHE L  83     179.215 169.166 110.373  1.00 91.53           C  
ATOM   3063  CG  PHE L  83     180.228 170.248 110.158  1.00 91.53           C  
ATOM   3064  CD1 PHE L  83     179.882 171.577 110.310  1.00 91.53           C  
ATOM   3065  CD2 PHE L  83     181.527 169.936 109.797  1.00 91.53           C  
ATOM   3066  CE1 PHE L  83     180.813 172.574 110.111  1.00 91.53           C  
ATOM   3067  CE2 PHE L  83     182.460 170.931 109.596  1.00 91.53           C  
ATOM   3068  CZ  PHE L  83     182.102 172.251 109.753  1.00 91.53           C  
ATOM   3069  N   ALA L  84     177.001 169.280 113.057  1.00 79.75           N  
ATOM   3070  CA  ALA L  84     175.624 169.083 113.491  1.00 79.75           C  
ATOM   3071  C   ALA L  84     175.179 170.314 114.265  1.00 79.75           C  
ATOM   3072  O   ALA L  84     175.920 171.291 114.397  1.00 79.75           O  
ATOM   3073  CB  ALA L  84     175.479 167.826 114.348  1.00 79.75           C  
ATOM   3074  N   VAL L  85     173.951 170.252 114.776  1.00 71.94           N  
ATOM   3075  CA  VAL L  85     173.419 171.338 115.588  1.00 71.94           C  
ATOM   3076  C   VAL L  85     173.748 171.076 117.049  1.00 71.94           C  
ATOM   3077  O   VAL L  85     173.417 170.016 117.595  1.00 71.94           O  
ATOM   3078  CB  VAL L  85     171.906 171.476 115.377  1.00 71.94           C  
ATOM   3079  CG1 VAL L  85     171.399 172.758 116.016  1.00 71.94           C  
ATOM   3080  CG2 VAL L  85     171.573 171.434 113.895  1.00 71.94           C  
ATOM   3081  N   TYR L  86     174.396 172.042 117.692  1.00 70.95           N  
ATOM   3082  CA  TYR L  86     174.840 171.909 119.074  1.00 70.95           C  
ATOM   3083  C   TYR L  86     173.965 172.783 119.959  1.00 70.95           C  
ATOM   3084  O   TYR L  86     173.983 174.012 119.837  1.00 70.95           O  
ATOM   3085  CB  TYR L  86     176.314 172.288 119.210  1.00 70.95           C  
ATOM   3086  CG  TYR L  86     177.235 171.337 118.485  1.00 70.95           C  
ATOM   3087  CD1 TYR L  86     177.906 170.333 119.166  1.00 70.95           C  
ATOM   3088  CD2 TYR L  86     177.418 171.429 117.114  1.00 70.95           C  
ATOM   3089  CE1 TYR L  86     178.740 169.456 118.502  1.00 70.95           C  
ATOM   3090  CE2 TYR L  86     178.248 170.556 116.443  1.00 70.95           C  
ATOM   3091  CZ  TYR L  86     178.907 169.573 117.140  1.00 70.95           C  
ATOM   3092  OH  TYR L  86     179.736 168.704 116.472  1.00 70.95           O  
ATOM   3093  N   TYR L  87     173.203 172.146 120.846  1.00 62.27           N  
ATOM   3094  CA  TYR L  87     172.246 172.832 121.707  1.00 62.27           C  
ATOM   3095  C   TYR L  87     172.899 173.121 123.051  1.00 62.27           C  
ATOM   3096  O   TYR L  87     173.103 172.210 123.858  1.00 62.27           O  
ATOM   3097  CB  TYR L  87     170.981 171.997 121.890  1.00 62.27           C  
ATOM   3098  CG  TYR L  87     170.020 172.081 120.732  1.00 62.27           C  
ATOM   3099  CD1 TYR L  87     170.187 171.287 119.608  1.00 62.27           C  
ATOM   3100  CD2 TYR L  87     168.944 172.954 120.764  1.00 62.27           C  
ATOM   3101  CE1 TYR L  87     169.311 171.361 118.547  1.00 62.27           C  
ATOM   3102  CE2 TYR L  87     168.062 173.035 119.707  1.00 62.27           C  
ATOM   3103  CZ  TYR L  87     168.250 172.237 118.602  1.00 62.27           C  
ATOM   3104  OH  TYR L  87     167.373 172.316 117.547  1.00 62.27           O  
ATOM   3105  N   CYS L  88     173.225 174.386 123.286  1.00 66.63           N  
ATOM   3106  CA  CYS L  88     173.679 174.805 124.601  1.00 66.63           C  
ATOM   3107  C   CYS L  88     172.597 174.515 125.631  1.00 66.63           C  
ATOM   3108  O   CYS L  88     171.406 174.686 125.364  1.00 66.63           O  
ATOM   3109  CB  CYS L  88     174.019 176.293 124.590  1.00 66.63           C  
ATOM   3110  SG  CYS L  88     174.685 176.932 126.137  1.00 66.63           S  
ATOM   3111  N   GLN L  89     173.010 174.041 126.822  1.00 60.34           N  
ATOM   3112  CA  GLN L  89     172.082 173.661 127.876  1.00 60.34           C  
ATOM   3113  C   GLN L  89     172.601 174.141 129.223  1.00 60.34           C  
ATOM   3114  O   GLN L  89     173.784 173.983 129.534  1.00 60.34           O  
ATOM   3115  CB  GLN L  89     171.881 172.147 127.889  1.00 60.34           C  
ATOM   3116  CG  GLN L  89     170.842 171.659 128.872  1.00 60.34           C  
ATOM   3117  CD  GLN L  89     171.394 171.500 130.265  1.00 60.34           C  
ATOM   3118  OE1 GLN L  89     172.475 170.958 130.457  1.00 60.34           O  
ATOM   3119  NE2 GLN L  89     170.654 171.985 131.254  1.00 60.34           N  
ATOM   3120  N   GLN L  90     171.715 174.743 130.002  1.00 60.58           N  
ATOM   3121  CA  GLN L  90     172.067 175.272 131.312  1.00 60.58           C  
ATOM   3122  C   GLN L  90     171.156 174.672 132.372  1.00 60.58           C  
ATOM   3123  O   GLN L  90     169.934 174.645 132.200  1.00 60.58           O  
ATOM   3124  CB  GLN L  90     171.963 176.797 131.333  1.00 60.58           C  
ATOM   3125  CG  GLN L  90     172.157 177.425 132.708  1.00 60.58           C  
ATOM   3126  CD  GLN L  90     170.860 177.554 133.487  1.00 60.58           C  
ATOM   3127  OE1 GLN L  90     170.729 177.026 134.592  1.00 60.58           O  
ATOM   3128  NE2 GLN L  90     169.895 178.258 132.912  1.00 60.58           N  
ATOM   3129  N   TYR L  91     171.751 174.197 133.465  1.00 63.82           N  
ATOM   3130  CA  TYR L  91     170.995 173.647 134.582  1.00 63.82           C  
ATOM   3131  C   TYR L  91     171.471 174.183 135.927  1.00 63.82           C  
ATOM   3132  O   TYR L  91     171.322 173.503 136.947  1.00 63.82           O  
ATOM   3133  CB  TYR L  91     171.056 172.120 134.562  1.00 63.82           C  
ATOM   3134  CG  TYR L  91     172.440 171.548 134.756  1.00 63.82           C  
ATOM   3135  CD1 TYR L  91     173.032 171.521 136.008  1.00 63.82           C  
ATOM   3136  CD2 TYR L  91     173.149 171.024 133.686  1.00 63.82           C  
ATOM   3137  CE1 TYR L  91     174.297 170.995 136.189  1.00 63.82           C  
ATOM   3138  CE2 TYR L  91     174.414 170.497 133.857  1.00 63.82           C  
ATOM   3139  CZ  TYR L  91     174.982 170.485 135.111  1.00 63.82           C  
ATOM   3140  OH  TYR L  91     176.239 169.962 135.287  1.00 63.82           O  
ATOM   3141  N   ASN L  92     172.049 175.386 135.951  1.00 63.36           N  
ATOM   3142  CA  ASN L  92     172.414 176.001 137.223  1.00 63.36           C  
ATOM   3143  C   ASN L  92     171.176 176.332 138.047  1.00 63.36           C  
ATOM   3144  O   ASN L  92     171.151 176.118 139.265  1.00 63.36           O  
ATOM   3145  CB  ASN L  92     173.252 177.255 136.983  1.00 63.36           C  
ATOM   3146  CG  ASN L  92     173.302 178.164 138.198  1.00 63.36           C  
ATOM   3147  OD1 ASN L  92     172.658 179.212 138.230  1.00 63.36           O  
ATOM   3148  ND2 ASN L  92     174.061 177.760 139.210  1.00 63.36           N  
ATOM   3149  N   ASN L  93     170.139 176.858 137.398  1.00 62.87           N  
ATOM   3150  CA  ASN L  93     168.883 177.211 138.049  1.00 62.87           C  
ATOM   3151  C   ASN L  93     167.741 176.292 137.648  1.00 62.87           C  
ATOM   3152  O   ASN L  93     167.035 175.761 138.509  1.00 62.87           O  
ATOM   3153  CB  ASN L  93     168.517 178.666 137.725  1.00 62.87           C  
ATOM   3154  CG  ASN L  93     167.091 179.007 138.105  1.00 62.87           C  
ATOM   3155  OD1 ASN L  93     166.178 178.911 137.285  1.00 62.87           O  
ATOM   3156  ND2 ASN L  93     166.892 179.412 139.353  1.00 62.87           N  
ATOM   3157  N   PHE L  94     167.540 176.099 136.350  1.00 57.20           N  
ATOM   3158  CA  PHE L  94     166.516 175.202 135.846  1.00 57.20           C  
ATOM   3159  C   PHE L  94     166.924 174.785 134.445  1.00 57.20           C  
ATOM   3160  O   PHE L  94     167.721 175.459 133.787  1.00 57.20           O  
ATOM   3161  CB  PHE L  94     165.133 175.867 135.853  1.00 57.20           C  
ATOM   3162  CG  PHE L  94     164.028 174.996 135.319  1.00 57.20           C  
ATOM   3163  CD1 PHE L  94     163.591 173.893 136.029  1.00 57.20           C  
ATOM   3164  CD2 PHE L  94     163.417 175.294 134.113  1.00 57.20           C  
ATOM   3165  CE1 PHE L  94     162.573 173.098 135.541  1.00 57.20           C  
ATOM   3166  CE2 PHE L  94     162.399 174.503 133.621  1.00 57.20           C  
ATOM   3167  CZ  PHE L  94     161.975 173.406 134.337  1.00 57.20           C  
ATOM   3168  N   ILE L  96     166.382 173.657 133.996  1.00 50.34           N  
ATOM   3169  CA  ILE L  96     166.713 173.159 132.668  1.00 50.34           C  
ATOM   3170  C   ILE L  96     166.225 174.166 131.636  1.00 50.34           C  
ATOM   3171  O   ILE L  96     165.019 174.384 131.477  1.00 50.34           O  
ATOM   3172  CB  ILE L  96     166.106 171.771 132.440  1.00 50.34           C  
ATOM   3173  CG1 ILE L  96     166.202 171.381 130.967  1.00 50.34           C  
ATOM   3174  CG2 ILE L  96     164.676 171.719 132.946  1.00 50.34           C  
ATOM   3175  CD1 ILE L  96     166.397 169.911 130.754  1.00 50.34           C  
ATOM   3176  N   ALA L  97     167.165 174.805 130.945  1.00 54.75           N  
ATOM   3177  CA  ALA L  97     166.861 175.851 129.975  1.00 54.75           C  
ATOM   3178  C   ALA L  97     167.670 175.591 128.714  1.00 54.75           C  
ATOM   3179  O   ALA L  97     168.900 175.700 128.726  1.00 54.75           O  
ATOM   3180  CB  ALA L  97     167.165 177.233 130.546  1.00 54.75           C  
ATOM   3181  N   PHE L  98     166.980 175.255 127.630  1.00 56.85           N  
ATOM   3182  CA  PHE L  98     167.623 174.958 126.361  1.00 56.85           C  
ATOM   3183  C   PHE L  98     167.798 176.231 125.547  1.00 56.85           C  
ATOM   3184  O   PHE L  98     166.861 177.023 125.413  1.00 56.85           O  
ATOM   3185  CB  PHE L  98     166.800 173.946 125.567  1.00 56.85           C  
ATOM   3186  CG  PHE L  98     167.202 172.523 125.796  1.00 56.85           C  
ATOM   3187  CD1 PHE L  98     168.002 171.865 124.879  1.00 56.85           C  
ATOM   3188  CD2 PHE L  98     166.781 171.841 126.922  1.00 56.85           C  
ATOM   3189  CE1 PHE L  98     168.375 170.556 125.080  1.00 56.85           C  
ATOM   3190  CE2 PHE L  98     167.152 170.530 127.127  1.00 56.85           C  
ATOM   3191  CZ  PHE L  98     167.950 169.887 126.205  1.00 56.85           C  
ATOM   3192  N   GLY L  99     168.998 176.423 125.008  1.00 60.81           N  
ATOM   3193  CA  GLY L  99     169.199 177.474 124.029  1.00 60.81           C  
ATOM   3194  C   GLY L  99     168.503 177.132 122.723  1.00 60.81           C  
ATOM   3195  O   GLY L  99     168.228 175.969 122.427  1.00 60.81           O  
ATOM   3196  N   GLN L 100     168.215 178.168 121.929  1.00 61.94           N  
ATOM   3197  CA  GLN L 100     167.475 177.964 120.686  1.00 61.94           C  
ATOM   3198  C   GLN L 100     168.217 177.033 119.736  1.00 61.94           C  
ATOM   3199  O   GLN L 100     167.603 176.396 118.874  1.00 61.94           O  
ATOM   3200  CB  GLN L 100     167.197 179.307 120.007  1.00 61.94           C  
ATOM   3201  CG  GLN L 100     166.344 180.262 120.826  1.00 61.94           C  
ATOM   3202  CD  GLN L 100     167.172 181.175 121.707  1.00 61.94           C  
ATOM   3203  OE1 GLN L 100     168.123 181.806 121.247  1.00 61.94           O  
ATOM   3204  NE2 GLN L 100     166.814 181.248 122.983  1.00 61.94           N  
ATOM   3205  N   GLY L 101     169.536 176.942 119.874  1.00 66.42           N  
ATOM   3206  CA  GLY L 101     170.308 176.039 119.047  1.00 66.42           C  
ATOM   3207  C   GLY L 101     171.229 176.751 118.081  1.00 66.42           C  
ATOM   3208  O   GLY L 101     170.879 177.805 117.543  1.00 66.42           O  
ATOM   3209  N   THR L 102     172.410 176.187 117.854  1.00 70.10           N  
ATOM   3210  CA  THR L 102     173.385 176.744 116.924  1.00 70.10           C  
ATOM   3211  C   THR L 102     173.670 175.722 115.832  1.00 70.10           C  
ATOM   3212  O   THR L 102     174.357 174.723 116.074  1.00 70.10           O  
ATOM   3213  CB  THR L 102     174.669 177.134 117.648  1.00 70.10           C  
ATOM   3214  OG1 THR L 102     174.393 178.195 118.570  1.00 70.10           O  
ATOM   3215  CG2 THR L 102     175.722 177.591 116.652  1.00 70.10           C  
ATOM   3216  N   ARG L 103     173.145 175.967 114.637  1.00 73.78           N  
ATOM   3217  CA  ARG L 103     173.509 175.155 113.488  1.00 73.78           C  
ATOM   3218  C   ARG L 103     174.936 175.467 113.061  1.00 73.78           C  
ATOM   3219  O   ARG L 103     175.423 176.588 113.225  1.00 73.78           O  
ATOM   3220  CB  ARG L 103     172.557 175.399 112.316  1.00 73.78           C  
ATOM   3221  CG  ARG L 103     171.203 174.728 112.451  1.00 73.78           C  
ATOM   3222  CD  ARG L 103     170.651 174.335 111.088  1.00 73.78           C  
ATOM   3223  NE  ARG L 103     169.381 173.626 111.190  1.00 73.78           N  
ATOM   3224  CZ  ARG L 103     168.196 174.171 110.949  1.00 73.78           C  
ATOM   3225  NH1 ARG L 103     168.080 175.435 110.577  1.00 73.78           N  
ATOM   3226  NH2 ARG L 103     167.101 173.429 111.082  1.00 73.78           N  
ATOM   3227  N   LEU L 104     175.609 174.458 112.519  1.00 77.81           N  
ATOM   3228  CA  LEU L 104     176.945 174.609 111.960  1.00 77.81           C  
ATOM   3229  C   LEU L 104     176.924 174.165 110.506  1.00 77.81           C  
ATOM   3230  O   LEU L 104     176.433 173.075 110.193  1.00 77.81           O  
ATOM   3231  CB  LEU L 104     177.971 173.802 112.755  1.00 77.81           C  
ATOM   3232  CG  LEU L 104     178.134 174.184 114.225  1.00 77.81           C  
ATOM   3233  CD1 LEU L 104     179.326 173.468 114.826  1.00 77.81           C  
ATOM   3234  CD2 LEU L 104     178.282 175.686 114.374  1.00 77.81           C  
ATOM   3235  N   GLU L 105     177.454 175.005 109.622  1.00 86.66           N  
ATOM   3236  CA  GLU L 105     177.420 174.752 108.191  1.00 86.66           C  
ATOM   3237  C   GLU L 105     178.815 174.902 107.597  1.00 86.66           C  
ATOM   3238  O   GLU L 105     179.726 175.451 108.222  1.00 86.66           O  
ATOM   3239  CB  GLU L 105     176.434 175.694 107.489  1.00 86.66           C  
ATOM   3240  CG  GLU L 105     174.993 175.530 107.956  1.00 86.66           C  
ATOM   3241  CD  GLU L 105     174.085 176.650 107.483  1.00 86.66           C  
ATOM   3242  OE1 GLU L 105     174.599 177.747 107.178  1.00 86.66           O  
ATOM   3243  OE2 GLU L 105     172.857 176.435 107.417  1.00 86.66           O  
ATOM   3244  N   ILE L 106     178.967 174.410 106.368  1.00 87.42           N  
ATOM   3245  CA  ILE L 106     180.271 174.282 105.727  1.00 87.42           C  
ATOM   3246  C   ILE L 106     180.676 175.546 104.976  1.00 87.42           C  
ATOM   3247  O   ILE L 106     181.688 175.539 104.269  1.00 87.42           O  
ATOM   3248  CB  ILE L 106     180.302 173.066 104.787  1.00 87.42           C  
ATOM   3249  CG1 ILE L 106     179.259 173.218 103.677  1.00 87.42           C  
ATOM   3250  CG2 ILE L 106     180.091 171.779 105.565  1.00 87.42           C  
ATOM   3251  CD1 ILE L 106     179.366 172.173 102.586  1.00 87.42           C  
ATOM   3252  N   LYS L 107     179.914 176.627 105.107  1.00 76.38           N  
ATOM   3253  CA  LYS L 107     180.190 177.850 104.358  1.00 76.38           C  
ATOM   3254  C   LYS L 107     181.593 178.385 104.628  1.00 76.38           C  
ATOM   3255  O   LYS L 107     182.178 179.076 103.794  1.00 76.38           O  
ATOM   3256  CB  LYS L 107     179.149 178.921 104.688  1.00 76.38           C  
ATOM   3257  CG  LYS L 107     177.903 178.864 103.819  1.00 76.38           C  
ATOM   3258  CD  LYS L 107     178.244 179.130 102.360  1.00 76.38           C  
ATOM   3259  CE  LYS L 107     177.001 179.129 101.484  1.00 76.38           C  
ATOM   3260  NZ  LYS L 107     176.047 180.206 101.865  1.00 76.38           N  
TER    3261      LYS L 107                                                      
HETATM 3262  C1  NAG A1301     180.494 139.273 158.456  1.00 98.37           C  
HETATM 3263  C2  NAG A1301     181.696 139.389 157.522  1.00 98.37           C  
HETATM 3264  C3  NAG A1301     182.959 138.912 158.231  1.00 98.37           C  
HETATM 3265  C4  NAG A1301     183.137 139.650 159.552  1.00 98.37           C  
HETATM 3266  C5  NAG A1301     181.869 139.546 160.397  1.00 98.37           C  
HETATM 3267  C6  NAG A1301     181.933 140.372 161.659  1.00 98.37           C  
HETATM 3268  C7  NAG A1301     181.093 139.198 155.151  1.00 98.37           C  
HETATM 3269  C8  NAG A1301     180.914 138.268 153.990  1.00 98.37           C  
HETATM 3270  N2  NAG A1301     181.480 138.633 156.299  1.00 98.37           N  
HETATM 3271  O3  NAG A1301     184.085 139.135 157.390  1.00 98.37           O  
HETATM 3272  O4  NAG A1301     184.225 139.090 160.277  1.00 98.37           O  
HETATM 3273  O5  NAG A1301     180.740 140.021 159.650  1.00 98.37           O  
HETATM 3274  O6  NAG A1301     180.694 140.350 162.354  1.00 98.37           O  
HETATM 3275  O7  NAG A1301     180.898 140.405 155.054  1.00 98.37           O  
CONECT   86 3262                                                                
CONECT  376  789                                                                
CONECT  466 1532                                                                
CONECT  789  376                                                                
CONECT 1180 1237                                                                
CONECT 1237 1180                                                                
CONECT 1532  466                                                                
CONECT 1713 2264                                                                
CONECT 2264 1713                                                                
CONECT 2614 3110                                                                
CONECT 3110 2614                                                                
CONECT 3262   86 3263 3273                                                      
CONECT 3263 3262 3264 3270                                                      
CONECT 3264 3263 3265 3271                                                      
CONECT 3265 3264 3266 3272                                                      
CONECT 3266 3265 3267 3273                                                      
CONECT 3267 3266 3274                                                           
CONECT 3268 3269 3270 3275                                                      
CONECT 3269 3268                                                                
CONECT 3270 3263 3268                                                           
CONECT 3271 3264                                                                
CONECT 3272 3265                                                                
CONECT 3273 3262 3266                                                           
CONECT 3274 3267                                                                
CONECT 3275 3268                                                                
MASTER     1400    0    1    7   28    0    0    6 3272    3   25  131          
END