HEADER    VIRAL PROTEIN                           11-JUL-20   6XRA              
TITLE     DISTINCT CONFORMATIONAL STATES OF SARS-COV-2 SPIKE PROTEIN            
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPIKE GLYCOPROTEIN;                                        
COMPND   3 CHAIN: C, A, B;                                                      
COMPND   4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_COMMON: 2019-NCOV;                                          
SOURCE   5 ORGANISM_TAXID: 2697049;                                             
SOURCE   6 GENE: S, 2;                                                          
SOURCE   7 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   8 EXPRESSION_SYSTEM_COMMON: HUMAN;                                     
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    VIRAL PROTEIN                                                         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    J.ZHANG,Y.F.CAI,T.S.XIAO,H.Q.PENG,S.M.STERLING,R.M.WALSH JR,S.RAWSON, 
AUTHOR   2 S.RITS-VOLLOCH,B.CHEN                                                
REVDAT   4   07-OCT-20 6XRA    1       JRNL   HETSYN                            
REVDAT   3   05-AUG-20 6XRA    1       JRNL                                     
REVDAT   2   29-JUL-20 6XRA    1       COMPND REMARK HETNAM LINK                
REVDAT   2 2                   1       SITE   ATOM                              
REVDAT   1   22-JUL-20 6XRA    0                                                
JRNL        AUTH   Y.CAI,J.ZHANG,T.XIAO,H.PENG,S.M.STERLING,R.M.WALSH JR.,      
JRNL        AUTH 2 S.RAWSON,S.RITS-VOLLOCH,B.CHEN                               
JRNL        TITL   DISTINCT CONFORMATIONAL STATES OF SARS-COV-2 SPIKE PROTEIN.  
JRNL        REF    SCIENCE                       V. 369  1586 2020              
JRNL        REFN                   ESSN 1095-9203                               
JRNL        PMID   32694201                                                     
JRNL        DOI    10.1126/SCIENCE.ABD4251                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : COOT, RELION, RELION, PHENIX              
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 6B3O                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : AB INITIO MODEL                     
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)  : 3.000                          
REMARK   3   NUMBER OF PARTICLES               : 196506                         
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 6XRA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 13-JUL-20.                  
REMARK 100 THE DEPOSITION ID IS D_1000250619.                                   
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                 : POST-FUSION SARS-COV-2 SPIKE      
REMARK 245                                    GLYCOPROTEIN                      
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : 0.30                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : OVERALL MAP OF POST-FUSION SARS   
REMARK 245  -COV-2 SPIKE GLYCOPROTEIN                                           
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 BIOQUANTUM (6K X      
REMARK 245                                       4K)                            
REMARK 245   MINIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MAXIMUM DEFOCUS (NM)              : NULL                           
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 54.30                          
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: C, A, B, D, E, F, G, H, I, J,         
REMARK 350                    AND CHAINS: K, L, M, N, O, P, Q, R                
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     MET C     1                                                      
REMARK 465     PHE C     2                                                      
REMARK 465     VAL C     3                                                      
REMARK 465     PHE C     4                                                      
REMARK 465     LEU C     5                                                      
REMARK 465     VAL C     6                                                      
REMARK 465     LEU C     7                                                      
REMARK 465     LEU C     8                                                      
REMARK 465     PRO C     9                                                      
REMARK 465     LEU C    10                                                      
REMARK 465     VAL C    11                                                      
REMARK 465     SER C    12                                                      
REMARK 465     SER C    13                                                      
REMARK 465     GLN C    14                                                      
REMARK 465     CYS C    15                                                      
REMARK 465     VAL C    16                                                      
REMARK 465     ASN C    17                                                      
REMARK 465     LEU C    18                                                      
REMARK 465     THR C    19                                                      
REMARK 465     THR C    20                                                      
REMARK 465     ARG C    21                                                      
REMARK 465     THR C    22                                                      
REMARK 465     GLN C    23                                                      
REMARK 465     LEU C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     PRO C    26                                                      
REMARK 465     ALA C    27                                                      
REMARK 465     TYR C    28                                                      
REMARK 465     THR C    29                                                      
REMARK 465     ASN C    30                                                      
REMARK 465     SER C    31                                                      
REMARK 465     PHE C    32                                                      
REMARK 465     THR C    33                                                      
REMARK 465     ARG C    34                                                      
REMARK 465     GLY C    35                                                      
REMARK 465     VAL C    36                                                      
REMARK 465     TYR C    37                                                      
REMARK 465     TYR C    38                                                      
REMARK 465     PRO C    39                                                      
REMARK 465     ASP C    40                                                      
REMARK 465     LYS C    41                                                      
REMARK 465     VAL C    42                                                      
REMARK 465     PHE C    43                                                      
REMARK 465     ARG C    44                                                      
REMARK 465     SER C    45                                                      
REMARK 465     SER C    46                                                      
REMARK 465     VAL C    47                                                      
REMARK 465     LEU C    48                                                      
REMARK 465     HIS C    49                                                      
REMARK 465     SER C    50                                                      
REMARK 465     THR C    51                                                      
REMARK 465     GLN C    52                                                      
REMARK 465     ASP C    53                                                      
REMARK 465     LEU C    54                                                      
REMARK 465     PHE C    55                                                      
REMARK 465     LEU C    56                                                      
REMARK 465     PRO C    57                                                      
REMARK 465     PHE C    58                                                      
REMARK 465     PHE C    59                                                      
REMARK 465     SER C    60                                                      
REMARK 465     ASN C    61                                                      
REMARK 465     VAL C    62                                                      
REMARK 465     THR C    63                                                      
REMARK 465     TRP C    64                                                      
REMARK 465     PHE C    65                                                      
REMARK 465     HIS C    66                                                      
REMARK 465     ALA C    67                                                      
REMARK 465     ILE C    68                                                      
REMARK 465     HIS C    69                                                      
REMARK 465     VAL C    70                                                      
REMARK 465     SER C    71                                                      
REMARK 465     GLY C    72                                                      
REMARK 465     THR C    73                                                      
REMARK 465     ASN C    74                                                      
REMARK 465     GLY C    75                                                      
REMARK 465     THR C    76                                                      
REMARK 465     LYS C    77                                                      
REMARK 465     ARG C    78                                                      
REMARK 465     PHE C    79                                                      
REMARK 465     ASP C    80                                                      
REMARK 465     ASN C    81                                                      
REMARK 465     PRO C    82                                                      
REMARK 465     VAL C    83                                                      
REMARK 465     LEU C    84                                                      
REMARK 465     PRO C    85                                                      
REMARK 465     PHE C    86                                                      
REMARK 465     ASN C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     GLY C    89                                                      
REMARK 465     VAL C    90                                                      
REMARK 465     TYR C    91                                                      
REMARK 465     PHE C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     SER C    94                                                      
REMARK 465     THR C    95                                                      
REMARK 465     GLU C    96                                                      
REMARK 465     LYS C    97                                                      
REMARK 465     SER C    98                                                      
REMARK 465     ASN C    99                                                      
REMARK 465     ILE C   100                                                      
REMARK 465     ILE C   101                                                      
REMARK 465     ARG C   102                                                      
REMARK 465     GLY C   103                                                      
REMARK 465     TRP C   104                                                      
REMARK 465     ILE C   105                                                      
REMARK 465     PHE C   106                                                      
REMARK 465     GLY C   107                                                      
REMARK 465     THR C   108                                                      
REMARK 465     THR C   109                                                      
REMARK 465     LEU C   110                                                      
REMARK 465     ASP C   111                                                      
REMARK 465     SER C   112                                                      
REMARK 465     LYS C   113                                                      
REMARK 465     THR C   114                                                      
REMARK 465     GLN C   115                                                      
REMARK 465     SER C   116                                                      
REMARK 465     LEU C   117                                                      
REMARK 465     LEU C   118                                                      
REMARK 465     ILE C   119                                                      
REMARK 465     VAL C   120                                                      
REMARK 465     ASN C   121                                                      
REMARK 465     ASN C   122                                                      
REMARK 465     ALA C   123                                                      
REMARK 465     THR C   124                                                      
REMARK 465     ASN C   125                                                      
REMARK 465     VAL C   126                                                      
REMARK 465     VAL C   127                                                      
REMARK 465     ILE C   128                                                      
REMARK 465     LYS C   129                                                      
REMARK 465     VAL C   130                                                      
REMARK 465     CYS C   131                                                      
REMARK 465     GLU C   132                                                      
REMARK 465     PHE C   133                                                      
REMARK 465     GLN C   134                                                      
REMARK 465     PHE C   135                                                      
REMARK 465     CYS C   136                                                      
REMARK 465     ASN C   137                                                      
REMARK 465     ASP C   138                                                      
REMARK 465     PRO C   139                                                      
REMARK 465     PHE C   140                                                      
REMARK 465     LEU C   141                                                      
REMARK 465     GLY C   142                                                      
REMARK 465     VAL C   143                                                      
REMARK 465     TYR C   144                                                      
REMARK 465     TYR C   145                                                      
REMARK 465     HIS C   146                                                      
REMARK 465     LYS C   147                                                      
REMARK 465     ASN C   148                                                      
REMARK 465     ASN C   149                                                      
REMARK 465     LYS C   150                                                      
REMARK 465     SER C   151                                                      
REMARK 465     TRP C   152                                                      
REMARK 465     MET C   153                                                      
REMARK 465     GLU C   154                                                      
REMARK 465     SER C   155                                                      
REMARK 465     GLU C   156                                                      
REMARK 465     PHE C   157                                                      
REMARK 465     ARG C   158                                                      
REMARK 465     VAL C   159                                                      
REMARK 465     TYR C   160                                                      
REMARK 465     SER C   161                                                      
REMARK 465     SER C   162                                                      
REMARK 465     ALA C   163                                                      
REMARK 465     ASN C   164                                                      
REMARK 465     ASN C   165                                                      
REMARK 465     CYS C   166                                                      
REMARK 465     THR C   167                                                      
REMARK 465     PHE C   168                                                      
REMARK 465     GLU C   169                                                      
REMARK 465     TYR C   170                                                      
REMARK 465     VAL C   171                                                      
REMARK 465     SER C   172                                                      
REMARK 465     GLN C   173                                                      
REMARK 465     PRO C   174                                                      
REMARK 465     PHE C   175                                                      
REMARK 465     LEU C   176                                                      
REMARK 465     MET C   177                                                      
REMARK 465     ASP C   178                                                      
REMARK 465     LEU C   179                                                      
REMARK 465     GLU C   180                                                      
REMARK 465     GLY C   181                                                      
REMARK 465     LYS C   182                                                      
REMARK 465     GLN C   183                                                      
REMARK 465     GLY C   184                                                      
REMARK 465     ASN C   185                                                      
REMARK 465     PHE C   186                                                      
REMARK 465     LYS C   187                                                      
REMARK 465     ASN C   188                                                      
REMARK 465     LEU C   189                                                      
REMARK 465     ARG C   190                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     PHE C   192                                                      
REMARK 465     VAL C   193                                                      
REMARK 465     PHE C   194                                                      
REMARK 465     LYS C   195                                                      
REMARK 465     ASN C   196                                                      
REMARK 465     ILE C   197                                                      
REMARK 465     ASP C   198                                                      
REMARK 465     GLY C   199                                                      
REMARK 465     TYR C   200                                                      
REMARK 465     PHE C   201                                                      
REMARK 465     LYS C   202                                                      
REMARK 465     ILE C   203                                                      
REMARK 465     TYR C   204                                                      
REMARK 465     SER C   205                                                      
REMARK 465     LYS C   206                                                      
REMARK 465     HIS C   207                                                      
REMARK 465     THR C   208                                                      
REMARK 465     PRO C   209                                                      
REMARK 465     ILE C   210                                                      
REMARK 465     ASN C   211                                                      
REMARK 465     LEU C   212                                                      
REMARK 465     VAL C   213                                                      
REMARK 465     ARG C   214                                                      
REMARK 465     ASP C   215                                                      
REMARK 465     LEU C   216                                                      
REMARK 465     PRO C   217                                                      
REMARK 465     GLN C   218                                                      
REMARK 465     GLY C   219                                                      
REMARK 465     PHE C   220                                                      
REMARK 465     SER C   221                                                      
REMARK 465     ALA C   222                                                      
REMARK 465     LEU C   223                                                      
REMARK 465     GLU C   224                                                      
REMARK 465     PRO C   225                                                      
REMARK 465     LEU C   226                                                      
REMARK 465     VAL C   227                                                      
REMARK 465     ASP C   228                                                      
REMARK 465     LEU C   229                                                      
REMARK 465     PRO C   230                                                      
REMARK 465     ILE C   231                                                      
REMARK 465     GLY C   232                                                      
REMARK 465     ILE C   233                                                      
REMARK 465     ASN C   234                                                      
REMARK 465     ILE C   235                                                      
REMARK 465     THR C   236                                                      
REMARK 465     ARG C   237                                                      
REMARK 465     PHE C   238                                                      
REMARK 465     GLN C   239                                                      
REMARK 465     THR C   240                                                      
REMARK 465     LEU C   241                                                      
REMARK 465     LEU C   242                                                      
REMARK 465     ALA C   243                                                      
REMARK 465     LEU C   244                                                      
REMARK 465     HIS C   245                                                      
REMARK 465     ARG C   246                                                      
REMARK 465     SER C   247                                                      
REMARK 465     TYR C   248                                                      
REMARK 465     LEU C   249                                                      
REMARK 465     THR C   250                                                      
REMARK 465     PRO C   251                                                      
REMARK 465     GLY C   252                                                      
REMARK 465     ASP C   253                                                      
REMARK 465     SER C   254                                                      
REMARK 465     SER C   255                                                      
REMARK 465     SER C   256                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     TRP C   258                                                      
REMARK 465     THR C   259                                                      
REMARK 465     ALA C   260                                                      
REMARK 465     GLY C   261                                                      
REMARK 465     ALA C   262                                                      
REMARK 465     ALA C   263                                                      
REMARK 465     ALA C   264                                                      
REMARK 465     TYR C   265                                                      
REMARK 465     TYR C   266                                                      
REMARK 465     VAL C   267                                                      
REMARK 465     GLY C   268                                                      
REMARK 465     TYR C   269                                                      
REMARK 465     LEU C   270                                                      
REMARK 465     GLN C   271                                                      
REMARK 465     PRO C   272                                                      
REMARK 465     ARG C   273                                                      
REMARK 465     THR C   274                                                      
REMARK 465     PHE C   275                                                      
REMARK 465     LEU C   276                                                      
REMARK 465     LEU C   277                                                      
REMARK 465     LYS C   278                                                      
REMARK 465     TYR C   279                                                      
REMARK 465     ASN C   280                                                      
REMARK 465     GLU C   281                                                      
REMARK 465     ASN C   282                                                      
REMARK 465     GLY C   283                                                      
REMARK 465     THR C   284                                                      
REMARK 465     ILE C   285                                                      
REMARK 465     THR C   286                                                      
REMARK 465     ASP C   287                                                      
REMARK 465     ALA C   288                                                      
REMARK 465     VAL C   289                                                      
REMARK 465     ASP C   290                                                      
REMARK 465     CYS C   291                                                      
REMARK 465     ALA C   292                                                      
REMARK 465     LEU C   293                                                      
REMARK 465     ASP C   294                                                      
REMARK 465     PRO C   295                                                      
REMARK 465     LEU C   296                                                      
REMARK 465     SER C   297                                                      
REMARK 465     GLU C   298                                                      
REMARK 465     THR C   299                                                      
REMARK 465     LYS C   300                                                      
REMARK 465     CYS C   301                                                      
REMARK 465     THR C   302                                                      
REMARK 465     LEU C   303                                                      
REMARK 465     LYS C   304                                                      
REMARK 465     SER C   305                                                      
REMARK 465     PHE C   306                                                      
REMARK 465     THR C   307                                                      
REMARK 465     VAL C   308                                                      
REMARK 465     GLU C   309                                                      
REMARK 465     LYS C   310                                                      
REMARK 465     GLY C   311                                                      
REMARK 465     ILE C   312                                                      
REMARK 465     TYR C   313                                                      
REMARK 465     GLN C   314                                                      
REMARK 465     THR C   315                                                      
REMARK 465     SER C   316                                                      
REMARK 465     ASN C   317                                                      
REMARK 465     PHE C   318                                                      
REMARK 465     ARG C   319                                                      
REMARK 465     VAL C   320                                                      
REMARK 465     GLN C   321                                                      
REMARK 465     PRO C   322                                                      
REMARK 465     THR C   323                                                      
REMARK 465     GLU C   324                                                      
REMARK 465     SER C   325                                                      
REMARK 465     ILE C   326                                                      
REMARK 465     VAL C   327                                                      
REMARK 465     ARG C   328                                                      
REMARK 465     PHE C   329                                                      
REMARK 465     PRO C   330                                                      
REMARK 465     ASN C   331                                                      
REMARK 465     ILE C   332                                                      
REMARK 465     THR C   333                                                      
REMARK 465     ASN C   334                                                      
REMARK 465     LEU C   335                                                      
REMARK 465     CYS C   336                                                      
REMARK 465     PRO C   337                                                      
REMARK 465     PHE C   338                                                      
REMARK 465     GLY C   339                                                      
REMARK 465     GLU C   340                                                      
REMARK 465     VAL C   341                                                      
REMARK 465     PHE C   342                                                      
REMARK 465     ASN C   343                                                      
REMARK 465     ALA C   344                                                      
REMARK 465     THR C   345                                                      
REMARK 465     ARG C   346                                                      
REMARK 465     PHE C   347                                                      
REMARK 465     ALA C   348                                                      
REMARK 465     SER C   349                                                      
REMARK 465     VAL C   350                                                      
REMARK 465     TYR C   351                                                      
REMARK 465     ALA C   352                                                      
REMARK 465     TRP C   353                                                      
REMARK 465     ASN C   354                                                      
REMARK 465     ARG C   355                                                      
REMARK 465     LYS C   356                                                      
REMARK 465     ARG C   357                                                      
REMARK 465     ILE C   358                                                      
REMARK 465     SER C   359                                                      
REMARK 465     ASN C   360                                                      
REMARK 465     CYS C   361                                                      
REMARK 465     VAL C   362                                                      
REMARK 465     ALA C   363                                                      
REMARK 465     ASP C   364                                                      
REMARK 465     TYR C   365                                                      
REMARK 465     SER C   366                                                      
REMARK 465     VAL C   367                                                      
REMARK 465     LEU C   368                                                      
REMARK 465     TYR C   369                                                      
REMARK 465     ASN C   370                                                      
REMARK 465     SER C   371                                                      
REMARK 465     ALA C   372                                                      
REMARK 465     SER C   373                                                      
REMARK 465     PHE C   374                                                      
REMARK 465     SER C   375                                                      
REMARK 465     THR C   376                                                      
REMARK 465     PHE C   377                                                      
REMARK 465     LYS C   378                                                      
REMARK 465     CYS C   379                                                      
REMARK 465     TYR C   380                                                      
REMARK 465     GLY C   381                                                      
REMARK 465     VAL C   382                                                      
REMARK 465     SER C   383                                                      
REMARK 465     PRO C   384                                                      
REMARK 465     THR C   385                                                      
REMARK 465     LYS C   386                                                      
REMARK 465     LEU C   387                                                      
REMARK 465     ASN C   388                                                      
REMARK 465     ASP C   389                                                      
REMARK 465     LEU C   390                                                      
REMARK 465     CYS C   391                                                      
REMARK 465     PHE C   392                                                      
REMARK 465     THR C   393                                                      
REMARK 465     ASN C   394                                                      
REMARK 465     VAL C   395                                                      
REMARK 465     TYR C   396                                                      
REMARK 465     ALA C   397                                                      
REMARK 465     ASP C   398                                                      
REMARK 465     SER C   399                                                      
REMARK 465     PHE C   400                                                      
REMARK 465     VAL C   401                                                      
REMARK 465     ILE C   402                                                      
REMARK 465     ARG C   403                                                      
REMARK 465     GLY C   404                                                      
REMARK 465     ASP C   405                                                      
REMARK 465     GLU C   406                                                      
REMARK 465     VAL C   407                                                      
REMARK 465     ARG C   408                                                      
REMARK 465     GLN C   409                                                      
REMARK 465     ILE C   410                                                      
REMARK 465     ALA C   411                                                      
REMARK 465     PRO C   412                                                      
REMARK 465     GLY C   413                                                      
REMARK 465     GLN C   414                                                      
REMARK 465     THR C   415                                                      
REMARK 465     GLY C   416                                                      
REMARK 465     LYS C   417                                                      
REMARK 465     ILE C   418                                                      
REMARK 465     ALA C   419                                                      
REMARK 465     ASP C   420                                                      
REMARK 465     TYR C   421                                                      
REMARK 465     ASN C   422                                                      
REMARK 465     TYR C   423                                                      
REMARK 465     LYS C   424                                                      
REMARK 465     LEU C   425                                                      
REMARK 465     PRO C   426                                                      
REMARK 465     ASP C   427                                                      
REMARK 465     ASP C   428                                                      
REMARK 465     PHE C   429                                                      
REMARK 465     THR C   430                                                      
REMARK 465     GLY C   431                                                      
REMARK 465     CYS C   432                                                      
REMARK 465     VAL C   433                                                      
REMARK 465     ILE C   434                                                      
REMARK 465     ALA C   435                                                      
REMARK 465     TRP C   436                                                      
REMARK 465     ASN C   437                                                      
REMARK 465     SER C   438                                                      
REMARK 465     ASN C   439                                                      
REMARK 465     ASN C   440                                                      
REMARK 465     LEU C   441                                                      
REMARK 465     ASP C   442                                                      
REMARK 465     SER C   443                                                      
REMARK 465     LYS C   444                                                      
REMARK 465     VAL C   445                                                      
REMARK 465     GLY C   446                                                      
REMARK 465     GLY C   447                                                      
REMARK 465     ASN C   448                                                      
REMARK 465     TYR C   449                                                      
REMARK 465     ASN C   450                                                      
REMARK 465     TYR C   451                                                      
REMARK 465     LEU C   452                                                      
REMARK 465     TYR C   453                                                      
REMARK 465     ARG C   454                                                      
REMARK 465     LEU C   455                                                      
REMARK 465     PHE C   456                                                      
REMARK 465     ARG C   457                                                      
REMARK 465     LYS C   458                                                      
REMARK 465     SER C   459                                                      
REMARK 465     ASN C   460                                                      
REMARK 465     LEU C   461                                                      
REMARK 465     LYS C   462                                                      
REMARK 465     PRO C   463                                                      
REMARK 465     PHE C   464                                                      
REMARK 465     GLU C   465                                                      
REMARK 465     ARG C   466                                                      
REMARK 465     ASP C   467                                                      
REMARK 465     ILE C   468                                                      
REMARK 465     SER C   469                                                      
REMARK 465     THR C   470                                                      
REMARK 465     GLU C   471                                                      
REMARK 465     ILE C   472                                                      
REMARK 465     TYR C   473                                                      
REMARK 465     GLN C   474                                                      
REMARK 465     ALA C   475                                                      
REMARK 465     GLY C   476                                                      
REMARK 465     SER C   477                                                      
REMARK 465     THR C   478                                                      
REMARK 465     PRO C   479                                                      
REMARK 465     CYS C   480                                                      
REMARK 465     ASN C   481                                                      
REMARK 465     GLY C   482                                                      
REMARK 465     VAL C   483                                                      
REMARK 465     GLU C   484                                                      
REMARK 465     GLY C   485                                                      
REMARK 465     PHE C   486                                                      
REMARK 465     ASN C   487                                                      
REMARK 465     CYS C   488                                                      
REMARK 465     TYR C   489                                                      
REMARK 465     PHE C   490                                                      
REMARK 465     PRO C   491                                                      
REMARK 465     LEU C   492                                                      
REMARK 465     GLN C   493                                                      
REMARK 465     SER C   494                                                      
REMARK 465     TYR C   495                                                      
REMARK 465     GLY C   496                                                      
REMARK 465     PHE C   497                                                      
REMARK 465     GLN C   498                                                      
REMARK 465     PRO C   499                                                      
REMARK 465     THR C   500                                                      
REMARK 465     ASN C   501                                                      
REMARK 465     GLY C   502                                                      
REMARK 465     VAL C   503                                                      
REMARK 465     GLY C   504                                                      
REMARK 465     TYR C   505                                                      
REMARK 465     GLN C   506                                                      
REMARK 465     PRO C   507                                                      
REMARK 465     TYR C   508                                                      
REMARK 465     ARG C   509                                                      
REMARK 465     VAL C   510                                                      
REMARK 465     VAL C   511                                                      
REMARK 465     VAL C   512                                                      
REMARK 465     LEU C   513                                                      
REMARK 465     SER C   514                                                      
REMARK 465     PHE C   515                                                      
REMARK 465     GLU C   516                                                      
REMARK 465     LEU C   517                                                      
REMARK 465     LEU C   518                                                      
REMARK 465     HIS C   519                                                      
REMARK 465     ALA C   520                                                      
REMARK 465     PRO C   521                                                      
REMARK 465     ALA C   522                                                      
REMARK 465     THR C   523                                                      
REMARK 465     VAL C   524                                                      
REMARK 465     CYS C   525                                                      
REMARK 465     GLY C   526                                                      
REMARK 465     PRO C   527                                                      
REMARK 465     LYS C   528                                                      
REMARK 465     LYS C   529                                                      
REMARK 465     SER C   530                                                      
REMARK 465     THR C   531                                                      
REMARK 465     ASN C   532                                                      
REMARK 465     LEU C   533                                                      
REMARK 465     VAL C   534                                                      
REMARK 465     LYS C   535                                                      
REMARK 465     ASN C   536                                                      
REMARK 465     LYS C   537                                                      
REMARK 465     CYS C   538                                                      
REMARK 465     VAL C   539                                                      
REMARK 465     ASN C   540                                                      
REMARK 465     PHE C   541                                                      
REMARK 465     ASN C   542                                                      
REMARK 465     PHE C   543                                                      
REMARK 465     ASN C   544                                                      
REMARK 465     GLY C   545                                                      
REMARK 465     LEU C   546                                                      
REMARK 465     THR C   547                                                      
REMARK 465     GLY C   548                                                      
REMARK 465     THR C   549                                                      
REMARK 465     GLY C   550                                                      
REMARK 465     VAL C   551                                                      
REMARK 465     LEU C   552                                                      
REMARK 465     THR C   553                                                      
REMARK 465     GLU C   554                                                      
REMARK 465     SER C   555                                                      
REMARK 465     ASN C   556                                                      
REMARK 465     LYS C   557                                                      
REMARK 465     LYS C   558                                                      
REMARK 465     PHE C   559                                                      
REMARK 465     LEU C   560                                                      
REMARK 465     PRO C   561                                                      
REMARK 465     PHE C   562                                                      
REMARK 465     GLN C   563                                                      
REMARK 465     GLN C   564                                                      
REMARK 465     PHE C   565                                                      
REMARK 465     GLY C   566                                                      
REMARK 465     ARG C   567                                                      
REMARK 465     ASP C   568                                                      
REMARK 465     ILE C   569                                                      
REMARK 465     ALA C   570                                                      
REMARK 465     ASP C   571                                                      
REMARK 465     THR C   572                                                      
REMARK 465     THR C   573                                                      
REMARK 465     ASP C   574                                                      
REMARK 465     ALA C   575                                                      
REMARK 465     VAL C   576                                                      
REMARK 465     ARG C   577                                                      
REMARK 465     ASP C   578                                                      
REMARK 465     PRO C   579                                                      
REMARK 465     GLN C   580                                                      
REMARK 465     THR C   581                                                      
REMARK 465     LEU C   582                                                      
REMARK 465     GLU C   583                                                      
REMARK 465     ILE C   584                                                      
REMARK 465     LEU C   585                                                      
REMARK 465     ASP C   586                                                      
REMARK 465     ILE C   587                                                      
REMARK 465     THR C   588                                                      
REMARK 465     PRO C   589                                                      
REMARK 465     CYS C   590                                                      
REMARK 465     SER C   591                                                      
REMARK 465     PHE C   592                                                      
REMARK 465     GLY C   593                                                      
REMARK 465     GLY C   594                                                      
REMARK 465     VAL C   595                                                      
REMARK 465     SER C   596                                                      
REMARK 465     VAL C   597                                                      
REMARK 465     ILE C   598                                                      
REMARK 465     THR C   599                                                      
REMARK 465     PRO C   600                                                      
REMARK 465     GLY C   601                                                      
REMARK 465     THR C   602                                                      
REMARK 465     ASN C   603                                                      
REMARK 465     THR C   604                                                      
REMARK 465     SER C   605                                                      
REMARK 465     ASN C   606                                                      
REMARK 465     GLN C   607                                                      
REMARK 465     VAL C   608                                                      
REMARK 465     ALA C   609                                                      
REMARK 465     VAL C   610                                                      
REMARK 465     LEU C   611                                                      
REMARK 465     TYR C   612                                                      
REMARK 465     GLN C   613                                                      
REMARK 465     ASP C   614                                                      
REMARK 465     VAL C   615                                                      
REMARK 465     ASN C   616                                                      
REMARK 465     CYS C   617                                                      
REMARK 465     THR C   618                                                      
REMARK 465     GLU C   619                                                      
REMARK 465     VAL C   620                                                      
REMARK 465     PRO C   621                                                      
REMARK 465     VAL C   622                                                      
REMARK 465     ALA C   623                                                      
REMARK 465     ILE C   624                                                      
REMARK 465     HIS C   625                                                      
REMARK 465     ALA C   626                                                      
REMARK 465     ASP C   627                                                      
REMARK 465     GLN C   628                                                      
REMARK 465     LEU C   629                                                      
REMARK 465     THR C   630                                                      
REMARK 465     PRO C   631                                                      
REMARK 465     THR C   632                                                      
REMARK 465     TRP C   633                                                      
REMARK 465     ARG C   634                                                      
REMARK 465     VAL C   635                                                      
REMARK 465     TYR C   636                                                      
REMARK 465     SER C   637                                                      
REMARK 465     THR C   638                                                      
REMARK 465     GLY C   639                                                      
REMARK 465     SER C   640                                                      
REMARK 465     ASN C   641                                                      
REMARK 465     VAL C   642                                                      
REMARK 465     PHE C   643                                                      
REMARK 465     GLN C   644                                                      
REMARK 465     THR C   645                                                      
REMARK 465     ARG C   646                                                      
REMARK 465     ALA C   647                                                      
REMARK 465     GLY C   648                                                      
REMARK 465     CYS C   649                                                      
REMARK 465     LEU C   650                                                      
REMARK 465     ILE C   651                                                      
REMARK 465     GLY C   652                                                      
REMARK 465     ALA C   653                                                      
REMARK 465     GLU C   654                                                      
REMARK 465     HIS C   655                                                      
REMARK 465     VAL C   656                                                      
REMARK 465     ASN C   657                                                      
REMARK 465     ASN C   658                                                      
REMARK 465     SER C   659                                                      
REMARK 465     TYR C   660                                                      
REMARK 465     GLU C   661                                                      
REMARK 465     CYS C   662                                                      
REMARK 465     ASP C   663                                                      
REMARK 465     ILE C   664                                                      
REMARK 465     PRO C   665                                                      
REMARK 465     ILE C   666                                                      
REMARK 465     GLY C   667                                                      
REMARK 465     ALA C   668                                                      
REMARK 465     GLY C   669                                                      
REMARK 465     ILE C   670                                                      
REMARK 465     CYS C   671                                                      
REMARK 465     ALA C   672                                                      
REMARK 465     SER C   673                                                      
REMARK 465     TYR C   674                                                      
REMARK 465     GLN C   675                                                      
REMARK 465     THR C   676                                                      
REMARK 465     GLN C   677                                                      
REMARK 465     THR C   678                                                      
REMARK 465     ASN C   679                                                      
REMARK 465     SER C   680                                                      
REMARK 465     PRO C   681                                                      
REMARK 465     ARG C   682                                                      
REMARK 465     ARG C   683                                                      
REMARK 465     ALA C   684                                                      
REMARK 465     ARG C   685                                                      
REMARK 465     SER C   686                                                      
REMARK 465     VAL C   687                                                      
REMARK 465     ALA C   688                                                      
REMARK 465     SER C   689                                                      
REMARK 465     GLN C   690                                                      
REMARK 465     SER C   691                                                      
REMARK 465     ILE C   692                                                      
REMARK 465     ILE C   693                                                      
REMARK 465     ALA C   694                                                      
REMARK 465     TYR C   695                                                      
REMARK 465     THR C   696                                                      
REMARK 465     MET C   697                                                      
REMARK 465     SER C   698                                                      
REMARK 465     LEU C   699                                                      
REMARK 465     GLY C   700                                                      
REMARK 465     ALA C   701                                                      
REMARK 465     GLU C   702                                                      
REMARK 465     ALA C   771                                                      
REMARK 465     VAL C   772                                                      
REMARK 465     GLU C   773                                                      
REMARK 465     GLN C   774                                                      
REMARK 465     ASP C   775                                                      
REMARK 465     LYS C   776                                                      
REMARK 465     ASN C   777                                                      
REMARK 465     THR C   778                                                      
REMARK 465     GLN C   779                                                      
REMARK 465     GLU C   780                                                      
REMARK 465     VAL C   781                                                      
REMARK 465     PHE C   782                                                      
REMARK 465     ALA C   783                                                      
REMARK 465     GLN C   784                                                      
REMARK 465     VAL C   785                                                      
REMARK 465     LYS C   786                                                      
REMARK 465     GLN C   787                                                      
REMARK 465     ILE C   788                                                      
REMARK 465     TYR C   789                                                      
REMARK 465     LYS C   790                                                      
REMARK 465     THR C   791                                                      
REMARK 465     PRO C   792                                                      
REMARK 465     PRO C   793                                                      
REMARK 465     ILE C   794                                                      
REMARK 465     LYS C   795                                                      
REMARK 465     ASP C   796                                                      
REMARK 465     PHE C   797                                                      
REMARK 465     GLY C   798                                                      
REMARK 465     GLY C   799                                                      
REMARK 465     PHE C   800                                                      
REMARK 465     ASN C   801                                                      
REMARK 465     PHE C   802                                                      
REMARK 465     SER C   803                                                      
REMARK 465     GLN C   804                                                      
REMARK 465     ILE C   805                                                      
REMARK 465     LEU C   806                                                      
REMARK 465     PRO C   807                                                      
REMARK 465     ASP C   808                                                      
REMARK 465     PRO C   809                                                      
REMARK 465     SER C   810                                                      
REMARK 465     LYS C   811                                                      
REMARK 465     PRO C   812                                                      
REMARK 465     SER C   813                                                      
REMARK 465     LYS C   814                                                      
REMARK 465     ARG C   815                                                      
REMARK 465     SER C   816                                                      
REMARK 465     PHE C   817                                                      
REMARK 465     ILE C   818                                                      
REMARK 465     GLU C   819                                                      
REMARK 465     ASP C   820                                                      
REMARK 465     LEU C   821                                                      
REMARK 465     LEU C   822                                                      
REMARK 465     PHE C   823                                                      
REMARK 465     ASN C   824                                                      
REMARK 465     LYS C   825                                                      
REMARK 465     VAL C   826                                                      
REMARK 465     THR C   827                                                      
REMARK 465     LEU C   828                                                      
REMARK 465     ALA C   829                                                      
REMARK 465     ASP C   830                                                      
REMARK 465     ALA C   831                                                      
REMARK 465     GLY C   832                                                      
REMARK 465     PHE C   833                                                      
REMARK 465     ILE C   834                                                      
REMARK 465     LYS C   835                                                      
REMARK 465     GLN C   836                                                      
REMARK 465     TYR C   837                                                      
REMARK 465     GLY C   838                                                      
REMARK 465     ASP C   839                                                      
REMARK 465     CYS C   840                                                      
REMARK 465     LEU C   841                                                      
REMARK 465     GLY C   842                                                      
REMARK 465     ASP C   843                                                      
REMARK 465     ILE C   844                                                      
REMARK 465     ALA C   845                                                      
REMARK 465     ALA C   846                                                      
REMARK 465     ARG C   847                                                      
REMARK 465     ASP C   848                                                      
REMARK 465     LEU C   849                                                      
REMARK 465     ILE C   850                                                      
REMARK 465     CYS C   851                                                      
REMARK 465     ALA C   852                                                      
REMARK 465     GLN C   853                                                      
REMARK 465     LYS C   854                                                      
REMARK 465     PHE C   855                                                      
REMARK 465     ASN C   856                                                      
REMARK 465     GLY C   857                                                      
REMARK 465     LEU C   858                                                      
REMARK 465     THR C   859                                                      
REMARK 465     VAL C   860                                                      
REMARK 465     LEU C   861                                                      
REMARK 465     PRO C   862                                                      
REMARK 465     PRO C   863                                                      
REMARK 465     LEU C   864                                                      
REMARK 465     LEU C   865                                                      
REMARK 465     THR C   866                                                      
REMARK 465     ASP C   867                                                      
REMARK 465     GLU C   868                                                      
REMARK 465     MET C   869                                                      
REMARK 465     ILE C   870                                                      
REMARK 465     ALA C   871                                                      
REMARK 465     GLN C   872                                                      
REMARK 465     TYR C   873                                                      
REMARK 465     THR C   874                                                      
REMARK 465     SER C   875                                                      
REMARK 465     ALA C   876                                                      
REMARK 465     LEU C   877                                                      
REMARK 465     LEU C   878                                                      
REMARK 465     ALA C   879                                                      
REMARK 465     GLY C   880                                                      
REMARK 465     THR C   881                                                      
REMARK 465     ILE C   882                                                      
REMARK 465     THR C   883                                                      
REMARK 465     SER C   884                                                      
REMARK 465     GLY C   885                                                      
REMARK 465     TRP C   886                                                      
REMARK 465     THR C   887                                                      
REMARK 465     PHE C   888                                                      
REMARK 465     GLY C   889                                                      
REMARK 465     ALA C   890                                                      
REMARK 465     GLY C   891                                                      
REMARK 465     ALA C   892                                                      
REMARK 465     ALA C   893                                                      
REMARK 465     LEU C   894                                                      
REMARK 465     GLN C   895                                                      
REMARK 465     ILE C   896                                                      
REMARK 465     PRO C   897                                                      
REMARK 465     PHE C   898                                                      
REMARK 465     ALA C   899                                                      
REMARK 465     MET C   900                                                      
REMARK 465     GLN C   901                                                      
REMARK 465     MET C   902                                                      
REMARK 465     ALA C   903                                                      
REMARK 465     TYR C   904                                                      
REMARK 465     ARG C   905                                                      
REMARK 465     PHE C   906                                                      
REMARK 465     ASN C   907                                                      
REMARK 465     GLY C   908                                                      
REMARK 465     ILE C   909                                                      
REMARK 465     GLY C   910                                                      
REMARK 465     VAL C   911                                                      
REMARK 465     ALA C  1174                                                      
REMARK 465     SER C  1175                                                      
REMARK 465     VAL C  1176                                                      
REMARK 465     VAL C  1177                                                      
REMARK 465     ASN C  1178                                                      
REMARK 465     ILE C  1179                                                      
REMARK 465     ILE C  1198                                                      
REMARK 465     ASP C  1199                                                      
REMARK 465     LEU C  1200                                                      
REMARK 465     GLN C  1201                                                      
REMARK 465     GLU C  1202                                                      
REMARK 465     LEU C  1203                                                      
REMARK 465     GLY C  1204                                                      
REMARK 465     LYS C  1205                                                      
REMARK 465     TYR C  1206                                                      
REMARK 465     GLU C  1207                                                      
REMARK 465     GLN C  1208                                                      
REMARK 465     TYR C  1209                                                      
REMARK 465     ILE C  1210                                                      
REMARK 465     LYS C  1211                                                      
REMARK 465     TRP C  1212                                                      
REMARK 465     PRO C  1213                                                      
REMARK 465     TRP C  1214                                                      
REMARK 465     TYR C  1215                                                      
REMARK 465     ILE C  1216                                                      
REMARK 465     TRP C  1217                                                      
REMARK 465     LEU C  1218                                                      
REMARK 465     GLY C  1219                                                      
REMARK 465     PHE C  1220                                                      
REMARK 465     ILE C  1221                                                      
REMARK 465     ALA C  1222                                                      
REMARK 465     GLY C  1223                                                      
REMARK 465     LEU C  1224                                                      
REMARK 465     ILE C  1225                                                      
REMARK 465     ALA C  1226                                                      
REMARK 465     ILE C  1227                                                      
REMARK 465     VAL C  1228                                                      
REMARK 465     MET C  1229                                                      
REMARK 465     VAL C  1230                                                      
REMARK 465     THR C  1231                                                      
REMARK 465     ILE C  1232                                                      
REMARK 465     MET C  1233                                                      
REMARK 465     LEU C  1234                                                      
REMARK 465     CYS C  1235                                                      
REMARK 465     CYS C  1236                                                      
REMARK 465     MET C  1237                                                      
REMARK 465     THR C  1238                                                      
REMARK 465     SER C  1239                                                      
REMARK 465     CYS C  1240                                                      
REMARK 465     CYS C  1241                                                      
REMARK 465     SER C  1242                                                      
REMARK 465     CYS C  1243                                                      
REMARK 465     LEU C  1244                                                      
REMARK 465     LYS C  1245                                                      
REMARK 465     GLY C  1246                                                      
REMARK 465     CYS C  1247                                                      
REMARK 465     CYS C  1248                                                      
REMARK 465     SER C  1249                                                      
REMARK 465     CYS C  1250                                                      
REMARK 465     GLY C  1251                                                      
REMARK 465     SER C  1252                                                      
REMARK 465     CYS C  1253                                                      
REMARK 465     CYS C  1254                                                      
REMARK 465     LYS C  1255                                                      
REMARK 465     PHE C  1256                                                      
REMARK 465     ASP C  1257                                                      
REMARK 465     GLU C  1258                                                      
REMARK 465     ASP C  1259                                                      
REMARK 465     ASP C  1260                                                      
REMARK 465     SER C  1261                                                      
REMARK 465     GLU C  1262                                                      
REMARK 465     PRO C  1263                                                      
REMARK 465     VAL C  1264                                                      
REMARK 465     LEU C  1265                                                      
REMARK 465     LYS C  1266                                                      
REMARK 465     GLY C  1267                                                      
REMARK 465     VAL C  1268                                                      
REMARK 465     LYS C  1269                                                      
REMARK 465     LEU C  1270                                                      
REMARK 465     HIS C  1271                                                      
REMARK 465     TYR C  1272                                                      
REMARK 465     THR C  1273                                                      
REMARK 465     LEU C  1274                                                      
REMARK 465     GLU C  1275                                                      
REMARK 465     SER C  1276                                                      
REMARK 465     GLY C  1277                                                      
REMARK 465     GLY C  1278                                                      
REMARK 465     GLY C  1279                                                      
REMARK 465     SER C  1280                                                      
REMARK 465     ALA C  1281                                                      
REMARK 465     TRP C  1282                                                      
REMARK 465     SER C  1283                                                      
REMARK 465     HIS C  1284                                                      
REMARK 465     PRO C  1285                                                      
REMARK 465     GLN C  1286                                                      
REMARK 465     PHE C  1287                                                      
REMARK 465     GLU C  1288                                                      
REMARK 465     LYS C  1289                                                      
REMARK 465     GLY C  1290                                                      
REMARK 465     GLY C  1291                                                      
REMARK 465     GLY C  1292                                                      
REMARK 465     SER C  1293                                                      
REMARK 465     GLY C  1294                                                      
REMARK 465     GLY C  1295                                                      
REMARK 465     GLY C  1296                                                      
REMARK 465     SER C  1297                                                      
REMARK 465     GLY C  1298                                                      
REMARK 465     GLY C  1299                                                      
REMARK 465     SER C  1300                                                      
REMARK 465     SER C  1301                                                      
REMARK 465     ALA C  1302                                                      
REMARK 465     TRP C  1303                                                      
REMARK 465     SER C  1304                                                      
REMARK 465     HIS C  1305                                                      
REMARK 465     PRO C  1306                                                      
REMARK 465     GLN C  1307                                                      
REMARK 465     PHE C  1308                                                      
REMARK 465     GLU C  1309                                                      
REMARK 465     LYS C  1310                                                      
REMARK 465     MET A     1                                                      
REMARK 465     PHE A     2                                                      
REMARK 465     VAL A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     LEU A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     VAL A    11                                                      
REMARK 465     SER A    12                                                      
REMARK 465     SER A    13                                                      
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     THR A   333                                                      
REMARK 465     ASN A   334                                                      
REMARK 465     LEU A   335                                                      
REMARK 465     CYS A   336                                                      
REMARK 465     PRO A   337                                                      
REMARK 465     PHE A   338                                                      
REMARK 465     GLY A   339                                                      
REMARK 465     GLU A   340                                                      
REMARK 465     VAL A   341                                                      
REMARK 465     PHE A   342                                                      
REMARK 465     ASN A   343                                                      
REMARK 465     ALA A   344                                                      
REMARK 465     THR A   345                                                      
REMARK 465     ARG A   346                                                      
REMARK 465     PHE A   347                                                      
REMARK 465     ALA A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     VAL A   350                                                      
REMARK 465     TYR A   351                                                      
REMARK 465     ALA A   352                                                      
REMARK 465     TRP A   353                                                      
REMARK 465     ASN A   354                                                      
REMARK 465     ARG A   355                                                      
REMARK 465     LYS A   356                                                      
REMARK 465     ARG A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     SER A   359                                                      
REMARK 465     ASN A   360                                                      
REMARK 465     CYS A   361                                                      
REMARK 465     VAL A   362                                                      
REMARK 465     ALA A   363                                                      
REMARK 465     ASP A   364                                                      
REMARK 465     TYR A   365                                                      
REMARK 465     SER A   366                                                      
REMARK 465     VAL A   367                                                      
REMARK 465     LEU A   368                                                      
REMARK 465     TYR A   369                                                      
REMARK 465     ASN A   370                                                      
REMARK 465     SER A   371                                                      
REMARK 465     ALA A   372                                                      
REMARK 465     SER A   373                                                      
REMARK 465     PHE A   374                                                      
REMARK 465     SER A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     PHE A   377                                                      
REMARK 465     LYS A   378                                                      
REMARK 465     CYS A   379                                                      
REMARK 465     TYR A   380                                                      
REMARK 465     GLY A   381                                                      
REMARK 465     VAL A   382                                                      
REMARK 465     SER A   383                                                      
REMARK 465     PRO A   384                                                      
REMARK 465     THR A   385                                                      
REMARK 465     LYS A   386                                                      
REMARK 465     LEU A   387                                                      
REMARK 465     ASN A   388                                                      
REMARK 465     ASP A   389                                                      
REMARK 465     LEU A   390                                                      
REMARK 465     CYS A   391                                                      
REMARK 465     PHE A   392                                                      
REMARK 465     THR A   393                                                      
REMARK 465     ASN A   394                                                      
REMARK 465     VAL A   395                                                      
REMARK 465     TYR A   396                                                      
REMARK 465     ALA A   397                                                      
REMARK 465     ASP A   398                                                      
REMARK 465     SER A   399                                                      
REMARK 465     PHE A   400                                                      
REMARK 465     VAL A   401                                                      
REMARK 465     ILE A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     GLY A   404                                                      
REMARK 465     ASP A   405                                                      
REMARK 465     GLU A   406                                                      
REMARK 465     VAL A   407                                                      
REMARK 465     ARG A   408                                                      
REMARK 465     GLN A   409                                                      
REMARK 465     ILE A   410                                                      
REMARK 465     ALA A   411                                                      
REMARK 465     PRO A   412                                                      
REMARK 465     GLY A   413                                                      
REMARK 465     GLN A   414                                                      
REMARK 465     THR A   415                                                      
REMARK 465     GLY A   416                                                      
REMARK 465     LYS A   417                                                      
REMARK 465     ILE A   418                                                      
REMARK 465     ALA A   419                                                      
REMARK 465     ASP A   420                                                      
REMARK 465     TYR A   421                                                      
REMARK 465     ASN A   422                                                      
REMARK 465     TYR A   423                                                      
REMARK 465     LYS A   424                                                      
REMARK 465     LEU A   425                                                      
REMARK 465     PRO A   426                                                      
REMARK 465     ASP A   427                                                      
REMARK 465     ASP A   428                                                      
REMARK 465     PHE A   429                                                      
REMARK 465     THR A   430                                                      
REMARK 465     GLY A   431                                                      
REMARK 465     CYS A   432                                                      
REMARK 465     VAL A   433                                                      
REMARK 465     ILE A   434                                                      
REMARK 465     ALA A   435                                                      
REMARK 465     TRP A   436                                                      
REMARK 465     ASN A   437                                                      
REMARK 465     SER A   438                                                      
REMARK 465     ASN A   439                                                      
REMARK 465     ASN A   440                                                      
REMARK 465     LEU A   441                                                      
REMARK 465     ASP A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     LYS A   444                                                      
REMARK 465     VAL A   445                                                      
REMARK 465     GLY A   446                                                      
REMARK 465     GLY A   447                                                      
REMARK 465     ASN A   448                                                      
REMARK 465     TYR A   449                                                      
REMARK 465     ASN A   450                                                      
REMARK 465     TYR A   451                                                      
REMARK 465     LEU A   452                                                      
REMARK 465     TYR A   453                                                      
REMARK 465     ARG A   454                                                      
REMARK 465     LEU A   455                                                      
REMARK 465     PHE A   456                                                      
REMARK 465     ARG A   457                                                      
REMARK 465     LYS A   458                                                      
REMARK 465     SER A   459                                                      
REMARK 465     ASN A   460                                                      
REMARK 465     LEU A   461                                                      
REMARK 465     LYS A   462                                                      
REMARK 465     PRO A   463                                                      
REMARK 465     PHE A   464                                                      
REMARK 465     GLU A   465                                                      
REMARK 465     ARG A   466                                                      
REMARK 465     ASP A   467                                                      
REMARK 465     ILE A   468                                                      
REMARK 465     SER A   469                                                      
REMARK 465     THR A   470                                                      
REMARK 465     GLU A   471                                                      
REMARK 465     ILE A   472                                                      
REMARK 465     TYR A   473                                                      
REMARK 465     GLN A   474                                                      
REMARK 465     ALA A   475                                                      
REMARK 465     GLY A   476                                                      
REMARK 465     SER A   477                                                      
REMARK 465     THR A   478                                                      
REMARK 465     PRO A   479                                                      
REMARK 465     CYS A   480                                                      
REMARK 465     ASN A   481                                                      
REMARK 465     GLY A   482                                                      
REMARK 465     VAL A   483                                                      
REMARK 465     GLU A   484                                                      
REMARK 465     GLY A   485                                                      
REMARK 465     PHE A   486                                                      
REMARK 465     ASN A   487                                                      
REMARK 465     CYS A   488                                                      
REMARK 465     TYR A   489                                                      
REMARK 465     PHE A   490                                                      
REMARK 465     PRO A   491                                                      
REMARK 465     LEU A   492                                                      
REMARK 465     GLN A   493                                                      
REMARK 465     SER A   494                                                      
REMARK 465     TYR A   495                                                      
REMARK 465     GLY A   496                                                      
REMARK 465     PHE A   497                                                      
REMARK 465     GLN A   498                                                      
REMARK 465     PRO A   499                                                      
REMARK 465     THR A   500                                                      
REMARK 465     ASN A   501                                                      
REMARK 465     GLY A   502                                                      
REMARK 465     VAL A   503                                                      
REMARK 465     GLY A   504                                                      
REMARK 465     TYR A   505                                                      
REMARK 465     GLN A   506                                                      
REMARK 465     PRO A   507                                                      
REMARK 465     TYR A   508                                                      
REMARK 465     ARG A   509                                                      
REMARK 465     VAL A   510                                                      
REMARK 465     VAL A   511                                                      
REMARK 465     VAL A   512                                                      
REMARK 465     LEU A   513                                                      
REMARK 465     SER A   514                                                      
REMARK 465     PHE A   515                                                      
REMARK 465     GLU A   516                                                      
REMARK 465     LEU A   517                                                      
REMARK 465     LEU A   518                                                      
REMARK 465     HIS A   519                                                      
REMARK 465     ALA A   520                                                      
REMARK 465     PRO A   521                                                      
REMARK 465     ALA A   522                                                      
REMARK 465     THR A   523                                                      
REMARK 465     VAL A   524                                                      
REMARK 465     CYS A   525                                                      
REMARK 465     GLY A   526                                                      
REMARK 465     PRO A   527                                                      
REMARK 465     LYS A   528                                                      
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     ARG A   682                                                      
REMARK 465     ARG A   683                                                      
REMARK 465     ALA A   684                                                      
REMARK 465     ARG A   685                                                      
REMARK 465     SER A   686                                                      
REMARK 465     VAL A   687                                                      
REMARK 465     ALA A   688                                                      
REMARK 465     SER A   689                                                      
REMARK 465     GLN A   690                                                      
REMARK 465     SER A   691                                                      
REMARK 465     ILE A   692                                                      
REMARK 465     ILE A   693                                                      
REMARK 465     ALA A   694                                                      
REMARK 465     TYR A   695                                                      
REMARK 465     THR A   696                                                      
REMARK 465     MET A   697                                                      
REMARK 465     SER A   698                                                      
REMARK 465     LEU A   699                                                      
REMARK 465     GLY A   700                                                      
REMARK 465     ALA A   701                                                      
REMARK 465     GLU A   702                                                      
REMARK 465     ALA A   771                                                      
REMARK 465     VAL A   772                                                      
REMARK 465     GLU A   773                                                      
REMARK 465     GLN A   774                                                      
REMARK 465     ASP A   775                                                      
REMARK 465     LYS A   776                                                      
REMARK 465     ASN A   777                                                      
REMARK 465     THR A   778                                                      
REMARK 465     GLN A   779                                                      
REMARK 465     GLU A   780                                                      
REMARK 465     VAL A   781                                                      
REMARK 465     PHE A   782                                                      
REMARK 465     ALA A   783                                                      
REMARK 465     GLN A   784                                                      
REMARK 465     VAL A   785                                                      
REMARK 465     LYS A   786                                                      
REMARK 465     GLN A   787                                                      
REMARK 465     ILE A   788                                                      
REMARK 465     TYR A   789                                                      
REMARK 465     LYS A   790                                                      
REMARK 465     THR A   791                                                      
REMARK 465     PRO A   792                                                      
REMARK 465     PRO A   793                                                      
REMARK 465     ILE A   794                                                      
REMARK 465     LYS A   795                                                      
REMARK 465     ASP A   796                                                      
REMARK 465     PHE A   797                                                      
REMARK 465     GLY A   798                                                      
REMARK 465     GLY A   799                                                      
REMARK 465     PHE A   800                                                      
REMARK 465     ASN A   801                                                      
REMARK 465     PHE A   802                                                      
REMARK 465     SER A   803                                                      
REMARK 465     GLN A   804                                                      
REMARK 465     ILE A   805                                                      
REMARK 465     LEU A   806                                                      
REMARK 465     PRO A   807                                                      
REMARK 465     ASP A   808                                                      
REMARK 465     PRO A   809                                                      
REMARK 465     SER A   810                                                      
REMARK 465     LYS A   811                                                      
REMARK 465     PRO A   812                                                      
REMARK 465     SER A   813                                                      
REMARK 465     LYS A   814                                                      
REMARK 465     ARG A   815                                                      
REMARK 465     SER A   816                                                      
REMARK 465     PHE A   817                                                      
REMARK 465     ILE A   818                                                      
REMARK 465     GLU A   819                                                      
REMARK 465     ASP A   820                                                      
REMARK 465     LEU A   821                                                      
REMARK 465     LEU A   822                                                      
REMARK 465     PHE A   823                                                      
REMARK 465     ASN A   824                                                      
REMARK 465     LYS A   825                                                      
REMARK 465     VAL A   826                                                      
REMARK 465     THR A   827                                                      
REMARK 465     LEU A   828                                                      
REMARK 465     ALA A   829                                                      
REMARK 465     ASP A   830                                                      
REMARK 465     ALA A   831                                                      
REMARK 465     GLY A   832                                                      
REMARK 465     PHE A   833                                                      
REMARK 465     ILE A   834                                                      
REMARK 465     LYS A   835                                                      
REMARK 465     GLN A   836                                                      
REMARK 465     TYR A   837                                                      
REMARK 465     GLY A   838                                                      
REMARK 465     ASP A   839                                                      
REMARK 465     CYS A   840                                                      
REMARK 465     LEU A   841                                                      
REMARK 465     GLY A   842                                                      
REMARK 465     ASP A   843                                                      
REMARK 465     ILE A   844                                                      
REMARK 465     ALA A   845                                                      
REMARK 465     ALA A   846                                                      
REMARK 465     ARG A   847                                                      
REMARK 465     ASP A   848                                                      
REMARK 465     LEU A   849                                                      
REMARK 465     ILE A   850                                                      
REMARK 465     CYS A   851                                                      
REMARK 465     ALA A   852                                                      
REMARK 465     GLN A   853                                                      
REMARK 465     LYS A   854                                                      
REMARK 465     PHE A   855                                                      
REMARK 465     ASN A   856                                                      
REMARK 465     GLY A   857                                                      
REMARK 465     LEU A   858                                                      
REMARK 465     THR A   859                                                      
REMARK 465     VAL A   860                                                      
REMARK 465     LEU A   861                                                      
REMARK 465     PRO A   862                                                      
REMARK 465     PRO A   863                                                      
REMARK 465     LEU A   864                                                      
REMARK 465     LEU A   865                                                      
REMARK 465     THR A   866                                                      
REMARK 465     ASP A   867                                                      
REMARK 465     GLU A   868                                                      
REMARK 465     MET A   869                                                      
REMARK 465     ILE A   870                                                      
REMARK 465     ALA A   871                                                      
REMARK 465     GLN A   872                                                      
REMARK 465     TYR A   873                                                      
REMARK 465     THR A   874                                                      
REMARK 465     SER A   875                                                      
REMARK 465     ALA A   876                                                      
REMARK 465     LEU A   877                                                      
REMARK 465     LEU A   878                                                      
REMARK 465     ALA A   879                                                      
REMARK 465     GLY A   880                                                      
REMARK 465     THR A   881                                                      
REMARK 465     ILE A   882                                                      
REMARK 465     THR A   883                                                      
REMARK 465     SER A   884                                                      
REMARK 465     GLY A   885                                                      
REMARK 465     TRP A   886                                                      
REMARK 465     THR A   887                                                      
REMARK 465     PHE A   888                                                      
REMARK 465     GLY A   889                                                      
REMARK 465     ALA A   890                                                      
REMARK 465     GLY A   891                                                      
REMARK 465     ALA A   892                                                      
REMARK 465     ALA A   893                                                      
REMARK 465     LEU A   894                                                      
REMARK 465     GLN A   895                                                      
REMARK 465     ILE A   896                                                      
REMARK 465     PRO A   897                                                      
REMARK 465     PHE A   898                                                      
REMARK 465     ALA A   899                                                      
REMARK 465     MET A   900                                                      
REMARK 465     GLN A   901                                                      
REMARK 465     MET A   902                                                      
REMARK 465     ALA A   903                                                      
REMARK 465     TYR A   904                                                      
REMARK 465     ARG A   905                                                      
REMARK 465     PHE A   906                                                      
REMARK 465     ASN A   907                                                      
REMARK 465     GLY A   908                                                      
REMARK 465     ILE A   909                                                      
REMARK 465     GLY A   910                                                      
REMARK 465     VAL A   911                                                      
REMARK 465     ALA A  1174                                                      
REMARK 465     SER A  1175                                                      
REMARK 465     VAL A  1176                                                      
REMARK 465     VAL A  1177                                                      
REMARK 465     ASN A  1178                                                      
REMARK 465     ILE A  1179                                                      
REMARK 465     ILE A  1198                                                      
REMARK 465     ASP A  1199                                                      
REMARK 465     LEU A  1200                                                      
REMARK 465     GLN A  1201                                                      
REMARK 465     GLU A  1202                                                      
REMARK 465     LEU A  1203                                                      
REMARK 465     GLY A  1204                                                      
REMARK 465     LYS A  1205                                                      
REMARK 465     TYR A  1206                                                      
REMARK 465     GLU A  1207                                                      
REMARK 465     GLN A  1208                                                      
REMARK 465     TYR A  1209                                                      
REMARK 465     ILE A  1210                                                      
REMARK 465     LYS A  1211                                                      
REMARK 465     TRP A  1212                                                      
REMARK 465     PRO A  1213                                                      
REMARK 465     TRP A  1214                                                      
REMARK 465     TYR A  1215                                                      
REMARK 465     ILE A  1216                                                      
REMARK 465     TRP A  1217                                                      
REMARK 465     LEU A  1218                                                      
REMARK 465     GLY A  1219                                                      
REMARK 465     PHE A  1220                                                      
REMARK 465     ILE A  1221                                                      
REMARK 465     ALA A  1222                                                      
REMARK 465     GLY A  1223                                                      
REMARK 465     LEU A  1224                                                      
REMARK 465     ILE A  1225                                                      
REMARK 465     ALA A  1226                                                      
REMARK 465     ILE A  1227                                                      
REMARK 465     VAL A  1228                                                      
REMARK 465     MET A  1229                                                      
REMARK 465     VAL A  1230                                                      
REMARK 465     THR A  1231                                                      
REMARK 465     ILE A  1232                                                      
REMARK 465     MET A  1233                                                      
REMARK 465     LEU A  1234                                                      
REMARK 465     CYS A  1235                                                      
REMARK 465     CYS A  1236                                                      
REMARK 465     MET A  1237                                                      
REMARK 465     THR A  1238                                                      
REMARK 465     SER A  1239                                                      
REMARK 465     CYS A  1240                                                      
REMARK 465     CYS A  1241                                                      
REMARK 465     SER A  1242                                                      
REMARK 465     CYS A  1243                                                      
REMARK 465     LEU A  1244                                                      
REMARK 465     LYS A  1245                                                      
REMARK 465     GLY A  1246                                                      
REMARK 465     CYS A  1247                                                      
REMARK 465     CYS A  1248                                                      
REMARK 465     SER A  1249                                                      
REMARK 465     CYS A  1250                                                      
REMARK 465     GLY A  1251                                                      
REMARK 465     SER A  1252                                                      
REMARK 465     CYS A  1253                                                      
REMARK 465     CYS A  1254                                                      
REMARK 465     LYS A  1255                                                      
REMARK 465     PHE A  1256                                                      
REMARK 465     ASP A  1257                                                      
REMARK 465     GLU A  1258                                                      
REMARK 465     ASP A  1259                                                      
REMARK 465     ASP A  1260                                                      
REMARK 465     SER A  1261                                                      
REMARK 465     GLU A  1262                                                      
REMARK 465     PRO A  1263                                                      
REMARK 465     VAL A  1264                                                      
REMARK 465     LEU A  1265                                                      
REMARK 465     LYS A  1266                                                      
REMARK 465     GLY A  1267                                                      
REMARK 465     VAL A  1268                                                      
REMARK 465     LYS A  1269                                                      
REMARK 465     LEU A  1270                                                      
REMARK 465     HIS A  1271                                                      
REMARK 465     TYR A  1272                                                      
REMARK 465     THR A  1273                                                      
REMARK 465     LEU A  1274                                                      
REMARK 465     GLU A  1275                                                      
REMARK 465     SER A  1276                                                      
REMARK 465     GLY A  1277                                                      
REMARK 465     GLY A  1278                                                      
REMARK 465     GLY A  1279                                                      
REMARK 465     SER A  1280                                                      
REMARK 465     ALA A  1281                                                      
REMARK 465     TRP A  1282                                                      
REMARK 465     SER A  1283                                                      
REMARK 465     HIS A  1284                                                      
REMARK 465     PRO A  1285                                                      
REMARK 465     GLN A  1286                                                      
REMARK 465     PHE A  1287                                                      
REMARK 465     GLU A  1288                                                      
REMARK 465     LYS A  1289                                                      
REMARK 465     GLY A  1290                                                      
REMARK 465     GLY A  1291                                                      
REMARK 465     GLY A  1292                                                      
REMARK 465     SER A  1293                                                      
REMARK 465     GLY A  1294                                                      
REMARK 465     GLY A  1295                                                      
REMARK 465     GLY A  1296                                                      
REMARK 465     SER A  1297                                                      
REMARK 465     GLY A  1298                                                      
REMARK 465     GLY A  1299                                                      
REMARK 465     SER A  1300                                                      
REMARK 465     SER A  1301                                                      
REMARK 465     ALA A  1302                                                      
REMARK 465     TRP A  1303                                                      
REMARK 465     SER A  1304                                                      
REMARK 465     HIS A  1305                                                      
REMARK 465     PRO A  1306                                                      
REMARK 465     GLN A  1307                                                      
REMARK 465     PHE A  1308                                                      
REMARK 465     GLU A  1309                                                      
REMARK 465     LYS A  1310                                                      
REMARK 465     MET B     1                                                      
REMARK 465     PHE B     2                                                      
REMARK 465     VAL B     3                                                      
REMARK 465     PHE B     4                                                      
REMARK 465     LEU B     5                                                      
REMARK 465     VAL B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     LEU B     8                                                      
REMARK 465     PRO B     9                                                      
REMARK 465     LEU B    10                                                      
REMARK 465     VAL B    11                                                      
REMARK 465     SER B    12                                                      
REMARK 465     SER B    13                                                      
REMARK 465     GLN B    14                                                      
REMARK 465     CYS B    15                                                      
REMARK 465     VAL B    16                                                      
REMARK 465     ASN B    17                                                      
REMARK 465     LEU B    18                                                      
REMARK 465     THR B    19                                                      
REMARK 465     THR B    20                                                      
REMARK 465     ARG B    21                                                      
REMARK 465     THR B    22                                                      
REMARK 465     GLN B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     PRO B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     TYR B    28                                                      
REMARK 465     THR B    29                                                      
REMARK 465     ASN B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     PHE B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     ARG B    34                                                      
REMARK 465     GLY B    35                                                      
REMARK 465     VAL B    36                                                      
REMARK 465     TYR B    37                                                      
REMARK 465     TYR B    38                                                      
REMARK 465     PRO B    39                                                      
REMARK 465     ASP B    40                                                      
REMARK 465     LYS B    41                                                      
REMARK 465     VAL B    42                                                      
REMARK 465     PHE B    43                                                      
REMARK 465     ARG B    44                                                      
REMARK 465     SER B    45                                                      
REMARK 465     SER B    46                                                      
REMARK 465     VAL B    47                                                      
REMARK 465     LEU B    48                                                      
REMARK 465     HIS B    49                                                      
REMARK 465     SER B    50                                                      
REMARK 465     THR B    51                                                      
REMARK 465     GLN B    52                                                      
REMARK 465     ASP B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     PHE B    55                                                      
REMARK 465     LEU B    56                                                      
REMARK 465     PRO B    57                                                      
REMARK 465     PHE B    58                                                      
REMARK 465     PHE B    59                                                      
REMARK 465     SER B    60                                                      
REMARK 465     ASN B    61                                                      
REMARK 465     VAL B    62                                                      
REMARK 465     THR B    63                                                      
REMARK 465     TRP B    64                                                      
REMARK 465     PHE B    65                                                      
REMARK 465     HIS B    66                                                      
REMARK 465     ALA B    67                                                      
REMARK 465     ILE B    68                                                      
REMARK 465     HIS B    69                                                      
REMARK 465     VAL B    70                                                      
REMARK 465     SER B    71                                                      
REMARK 465     GLY B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ASN B    74                                                      
REMARK 465     GLY B    75                                                      
REMARK 465     THR B    76                                                      
REMARK 465     LYS B    77                                                      
REMARK 465     ARG B    78                                                      
REMARK 465     PHE B    79                                                      
REMARK 465     ASP B    80                                                      
REMARK 465     ASN B    81                                                      
REMARK 465     PRO B    82                                                      
REMARK 465     VAL B    83                                                      
REMARK 465     LEU B    84                                                      
REMARK 465     PRO B    85                                                      
REMARK 465     PHE B    86                                                      
REMARK 465     ASN B    87                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     GLY B    89                                                      
REMARK 465     VAL B    90                                                      
REMARK 465     TYR B    91                                                      
REMARK 465     PHE B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     SER B    94                                                      
REMARK 465     THR B    95                                                      
REMARK 465     GLU B    96                                                      
REMARK 465     LYS B    97                                                      
REMARK 465     SER B    98                                                      
REMARK 465     ASN B    99                                                      
REMARK 465     ILE B   100                                                      
REMARK 465     ILE B   101                                                      
REMARK 465     ARG B   102                                                      
REMARK 465     GLY B   103                                                      
REMARK 465     TRP B   104                                                      
REMARK 465     ILE B   105                                                      
REMARK 465     PHE B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     THR B   108                                                      
REMARK 465     THR B   109                                                      
REMARK 465     LEU B   110                                                      
REMARK 465     ASP B   111                                                      
REMARK 465     SER B   112                                                      
REMARK 465     LYS B   113                                                      
REMARK 465     THR B   114                                                      
REMARK 465     GLN B   115                                                      
REMARK 465     SER B   116                                                      
REMARK 465     LEU B   117                                                      
REMARK 465     LEU B   118                                                      
REMARK 465     ILE B   119                                                      
REMARK 465     VAL B   120                                                      
REMARK 465     ASN B   121                                                      
REMARK 465     ASN B   122                                                      
REMARK 465     ALA B   123                                                      
REMARK 465     THR B   124                                                      
REMARK 465     ASN B   125                                                      
REMARK 465     VAL B   126                                                      
REMARK 465     VAL B   127                                                      
REMARK 465     ILE B   128                                                      
REMARK 465     LYS B   129                                                      
REMARK 465     VAL B   130                                                      
REMARK 465     CYS B   131                                                      
REMARK 465     GLU B   132                                                      
REMARK 465     PHE B   133                                                      
REMARK 465     GLN B   134                                                      
REMARK 465     PHE B   135                                                      
REMARK 465     CYS B   136                                                      
REMARK 465     ASN B   137                                                      
REMARK 465     ASP B   138                                                      
REMARK 465     PRO B   139                                                      
REMARK 465     PHE B   140                                                      
REMARK 465     LEU B   141                                                      
REMARK 465     GLY B   142                                                      
REMARK 465     VAL B   143                                                      
REMARK 465     TYR B   144                                                      
REMARK 465     TYR B   145                                                      
REMARK 465     HIS B   146                                                      
REMARK 465     LYS B   147                                                      
REMARK 465     ASN B   148                                                      
REMARK 465     ASN B   149                                                      
REMARK 465     LYS B   150                                                      
REMARK 465     SER B   151                                                      
REMARK 465     TRP B   152                                                      
REMARK 465     MET B   153                                                      
REMARK 465     GLU B   154                                                      
REMARK 465     SER B   155                                                      
REMARK 465     GLU B   156                                                      
REMARK 465     PHE B   157                                                      
REMARK 465     ARG B   158                                                      
REMARK 465     VAL B   159                                                      
REMARK 465     TYR B   160                                                      
REMARK 465     SER B   161                                                      
REMARK 465     SER B   162                                                      
REMARK 465     ALA B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     ASN B   165                                                      
REMARK 465     CYS B   166                                                      
REMARK 465     THR B   167                                                      
REMARK 465     PHE B   168                                                      
REMARK 465     GLU B   169                                                      
REMARK 465     TYR B   170                                                      
REMARK 465     VAL B   171                                                      
REMARK 465     SER B   172                                                      
REMARK 465     GLN B   173                                                      
REMARK 465     PRO B   174                                                      
REMARK 465     PHE B   175                                                      
REMARK 465     LEU B   176                                                      
REMARK 465     MET B   177                                                      
REMARK 465     ASP B   178                                                      
REMARK 465     LEU B   179                                                      
REMARK 465     GLU B   180                                                      
REMARK 465     GLY B   181                                                      
REMARK 465     LYS B   182                                                      
REMARK 465     GLN B   183                                                      
REMARK 465     GLY B   184                                                      
REMARK 465     ASN B   185                                                      
REMARK 465     PHE B   186                                                      
REMARK 465     LYS B   187                                                      
REMARK 465     ASN B   188                                                      
REMARK 465     LEU B   189                                                      
REMARK 465     ARG B   190                                                      
REMARK 465     GLU B   191                                                      
REMARK 465     PHE B   192                                                      
REMARK 465     VAL B   193                                                      
REMARK 465     PHE B   194                                                      
REMARK 465     LYS B   195                                                      
REMARK 465     ASN B   196                                                      
REMARK 465     ILE B   197                                                      
REMARK 465     ASP B   198                                                      
REMARK 465     GLY B   199                                                      
REMARK 465     TYR B   200                                                      
REMARK 465     PHE B   201                                                      
REMARK 465     LYS B   202                                                      
REMARK 465     ILE B   203                                                      
REMARK 465     TYR B   204                                                      
REMARK 465     SER B   205                                                      
REMARK 465     LYS B   206                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     THR B   208                                                      
REMARK 465     PRO B   209                                                      
REMARK 465     ILE B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     VAL B   213                                                      
REMARK 465     ARG B   214                                                      
REMARK 465     ASP B   215                                                      
REMARK 465     LEU B   216                                                      
REMARK 465     PRO B   217                                                      
REMARK 465     GLN B   218                                                      
REMARK 465     GLY B   219                                                      
REMARK 465     PHE B   220                                                      
REMARK 465     SER B   221                                                      
REMARK 465     ALA B   222                                                      
REMARK 465     LEU B   223                                                      
REMARK 465     GLU B   224                                                      
REMARK 465     PRO B   225                                                      
REMARK 465     LEU B   226                                                      
REMARK 465     VAL B   227                                                      
REMARK 465     ASP B   228                                                      
REMARK 465     LEU B   229                                                      
REMARK 465     PRO B   230                                                      
REMARK 465     ILE B   231                                                      
REMARK 465     GLY B   232                                                      
REMARK 465     ILE B   233                                                      
REMARK 465     ASN B   234                                                      
REMARK 465     ILE B   235                                                      
REMARK 465     THR B   236                                                      
REMARK 465     ARG B   237                                                      
REMARK 465     PHE B   238                                                      
REMARK 465     GLN B   239                                                      
REMARK 465     THR B   240                                                      
REMARK 465     LEU B   241                                                      
REMARK 465     LEU B   242                                                      
REMARK 465     ALA B   243                                                      
REMARK 465     LEU B   244                                                      
REMARK 465     HIS B   245                                                      
REMARK 465     ARG B   246                                                      
REMARK 465     SER B   247                                                      
REMARK 465     TYR B   248                                                      
REMARK 465     LEU B   249                                                      
REMARK 465     THR B   250                                                      
REMARK 465     PRO B   251                                                      
REMARK 465     GLY B   252                                                      
REMARK 465     ASP B   253                                                      
REMARK 465     SER B   254                                                      
REMARK 465     SER B   255                                                      
REMARK 465     SER B   256                                                      
REMARK 465     GLY B   257                                                      
REMARK 465     TRP B   258                                                      
REMARK 465     THR B   259                                                      
REMARK 465     ALA B   260                                                      
REMARK 465     GLY B   261                                                      
REMARK 465     ALA B   262                                                      
REMARK 465     ALA B   263                                                      
REMARK 465     ALA B   264                                                      
REMARK 465     TYR B   265                                                      
REMARK 465     TYR B   266                                                      
REMARK 465     VAL B   267                                                      
REMARK 465     GLY B   268                                                      
REMARK 465     TYR B   269                                                      
REMARK 465     LEU B   270                                                      
REMARK 465     GLN B   271                                                      
REMARK 465     PRO B   272                                                      
REMARK 465     ARG B   273                                                      
REMARK 465     THR B   274                                                      
REMARK 465     PHE B   275                                                      
REMARK 465     LEU B   276                                                      
REMARK 465     LEU B   277                                                      
REMARK 465     LYS B   278                                                      
REMARK 465     TYR B   279                                                      
REMARK 465     ASN B   280                                                      
REMARK 465     GLU B   281                                                      
REMARK 465     ASN B   282                                                      
REMARK 465     GLY B   283                                                      
REMARK 465     THR B   284                                                      
REMARK 465     ILE B   285                                                      
REMARK 465     THR B   286                                                      
REMARK 465     ASP B   287                                                      
REMARK 465     ALA B   288                                                      
REMARK 465     VAL B   289                                                      
REMARK 465     ASP B   290                                                      
REMARK 465     CYS B   291                                                      
REMARK 465     ALA B   292                                                      
REMARK 465     LEU B   293                                                      
REMARK 465     ASP B   294                                                      
REMARK 465     PRO B   295                                                      
REMARK 465     LEU B   296                                                      
REMARK 465     SER B   297                                                      
REMARK 465     GLU B   298                                                      
REMARK 465     THR B   299                                                      
REMARK 465     LYS B   300                                                      
REMARK 465     CYS B   301                                                      
REMARK 465     THR B   302                                                      
REMARK 465     LEU B   303                                                      
REMARK 465     LYS B   304                                                      
REMARK 465     SER B   305                                                      
REMARK 465     PHE B   306                                                      
REMARK 465     THR B   307                                                      
REMARK 465     VAL B   308                                                      
REMARK 465     GLU B   309                                                      
REMARK 465     LYS B   310                                                      
REMARK 465     GLY B   311                                                      
REMARK 465     ILE B   312                                                      
REMARK 465     TYR B   313                                                      
REMARK 465     GLN B   314                                                      
REMARK 465     THR B   315                                                      
REMARK 465     SER B   316                                                      
REMARK 465     ASN B   317                                                      
REMARK 465     PHE B   318                                                      
REMARK 465     ARG B   319                                                      
REMARK 465     VAL B   320                                                      
REMARK 465     GLN B   321                                                      
REMARK 465     PRO B   322                                                      
REMARK 465     THR B   323                                                      
REMARK 465     GLU B   324                                                      
REMARK 465     SER B   325                                                      
REMARK 465     ILE B   326                                                      
REMARK 465     VAL B   327                                                      
REMARK 465     ARG B   328                                                      
REMARK 465     PHE B   329                                                      
REMARK 465     PRO B   330                                                      
REMARK 465     ASN B   331                                                      
REMARK 465     ILE B   332                                                      
REMARK 465     THR B   333                                                      
REMARK 465     ASN B   334                                                      
REMARK 465     LEU B   335                                                      
REMARK 465     CYS B   336                                                      
REMARK 465     PRO B   337                                                      
REMARK 465     PHE B   338                                                      
REMARK 465     GLY B   339                                                      
REMARK 465     GLU B   340                                                      
REMARK 465     VAL B   341                                                      
REMARK 465     PHE B   342                                                      
REMARK 465     ASN B   343                                                      
REMARK 465     ALA B   344                                                      
REMARK 465     THR B   345                                                      
REMARK 465     ARG B   346                                                      
REMARK 465     PHE B   347                                                      
REMARK 465     ALA B   348                                                      
REMARK 465     SER B   349                                                      
REMARK 465     VAL B   350                                                      
REMARK 465     TYR B   351                                                      
REMARK 465     ALA B   352                                                      
REMARK 465     TRP B   353                                                      
REMARK 465     ASN B   354                                                      
REMARK 465     ARG B   355                                                      
REMARK 465     LYS B   356                                                      
REMARK 465     ARG B   357                                                      
REMARK 465     ILE B   358                                                      
REMARK 465     SER B   359                                                      
REMARK 465     ASN B   360                                                      
REMARK 465     CYS B   361                                                      
REMARK 465     VAL B   362                                                      
REMARK 465     ALA B   363                                                      
REMARK 465     ASP B   364                                                      
REMARK 465     TYR B   365                                                      
REMARK 465     SER B   366                                                      
REMARK 465     VAL B   367                                                      
REMARK 465     LEU B   368                                                      
REMARK 465     TYR B   369                                                      
REMARK 465     ASN B   370                                                      
REMARK 465     SER B   371                                                      
REMARK 465     ALA B   372                                                      
REMARK 465     SER B   373                                                      
REMARK 465     PHE B   374                                                      
REMARK 465     SER B   375                                                      
REMARK 465     THR B   376                                                      
REMARK 465     PHE B   377                                                      
REMARK 465     LYS B   378                                                      
REMARK 465     CYS B   379                                                      
REMARK 465     TYR B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     VAL B   382                                                      
REMARK 465     SER B   383                                                      
REMARK 465     PRO B   384                                                      
REMARK 465     THR B   385                                                      
REMARK 465     LYS B   386                                                      
REMARK 465     LEU B   387                                                      
REMARK 465     ASN B   388                                                      
REMARK 465     ASP B   389                                                      
REMARK 465     LEU B   390                                                      
REMARK 465     CYS B   391                                                      
REMARK 465     PHE B   392                                                      
REMARK 465     THR B   393                                                      
REMARK 465     ASN B   394                                                      
REMARK 465     VAL B   395                                                      
REMARK 465     TYR B   396                                                      
REMARK 465     ALA B   397                                                      
REMARK 465     ASP B   398                                                      
REMARK 465     SER B   399                                                      
REMARK 465     PHE B   400                                                      
REMARK 465     VAL B   401                                                      
REMARK 465     ILE B   402                                                      
REMARK 465     ARG B   403                                                      
REMARK 465     GLY B   404                                                      
REMARK 465     ASP B   405                                                      
REMARK 465     GLU B   406                                                      
REMARK 465     VAL B   407                                                      
REMARK 465     ARG B   408                                                      
REMARK 465     GLN B   409                                                      
REMARK 465     ILE B   410                                                      
REMARK 465     ALA B   411                                                      
REMARK 465     PRO B   412                                                      
REMARK 465     GLY B   413                                                      
REMARK 465     GLN B   414                                                      
REMARK 465     THR B   415                                                      
REMARK 465     GLY B   416                                                      
REMARK 465     LYS B   417                                                      
REMARK 465     ILE B   418                                                      
REMARK 465     ALA B   419                                                      
REMARK 465     ASP B   420                                                      
REMARK 465     TYR B   421                                                      
REMARK 465     ASN B   422                                                      
REMARK 465     TYR B   423                                                      
REMARK 465     LYS B   424                                                      
REMARK 465     LEU B   425                                                      
REMARK 465     PRO B   426                                                      
REMARK 465     ASP B   427                                                      
REMARK 465     ASP B   428                                                      
REMARK 465     PHE B   429                                                      
REMARK 465     THR B   430                                                      
REMARK 465     GLY B   431                                                      
REMARK 465     CYS B   432                                                      
REMARK 465     VAL B   433                                                      
REMARK 465     ILE B   434                                                      
REMARK 465     ALA B   435                                                      
REMARK 465     TRP B   436                                                      
REMARK 465     ASN B   437                                                      
REMARK 465     SER B   438                                                      
REMARK 465     ASN B   439                                                      
REMARK 465     ASN B   440                                                      
REMARK 465     LEU B   441                                                      
REMARK 465     ASP B   442                                                      
REMARK 465     SER B   443                                                      
REMARK 465     LYS B   444                                                      
REMARK 465     VAL B   445                                                      
REMARK 465     GLY B   446                                                      
REMARK 465     GLY B   447                                                      
REMARK 465     ASN B   448                                                      
REMARK 465     TYR B   449                                                      
REMARK 465     ASN B   450                                                      
REMARK 465     TYR B   451                                                      
REMARK 465     LEU B   452                                                      
REMARK 465     TYR B   453                                                      
REMARK 465     ARG B   454                                                      
REMARK 465     LEU B   455                                                      
REMARK 465     PHE B   456                                                      
REMARK 465     ARG B   457                                                      
REMARK 465     LYS B   458                                                      
REMARK 465     SER B   459                                                      
REMARK 465     ASN B   460                                                      
REMARK 465     LEU B   461                                                      
REMARK 465     LYS B   462                                                      
REMARK 465     PRO B   463                                                      
REMARK 465     PHE B   464                                                      
REMARK 465     GLU B   465                                                      
REMARK 465     ARG B   466                                                      
REMARK 465     ASP B   467                                                      
REMARK 465     ILE B   468                                                      
REMARK 465     SER B   469                                                      
REMARK 465     THR B   470                                                      
REMARK 465     GLU B   471                                                      
REMARK 465     ILE B   472                                                      
REMARK 465     TYR B   473                                                      
REMARK 465     GLN B   474                                                      
REMARK 465     ALA B   475                                                      
REMARK 465     GLY B   476                                                      
REMARK 465     SER B   477                                                      
REMARK 465     THR B   478                                                      
REMARK 465     PRO B   479                                                      
REMARK 465     CYS B   480                                                      
REMARK 465     ASN B   481                                                      
REMARK 465     GLY B   482                                                      
REMARK 465     VAL B   483                                                      
REMARK 465     GLU B   484                                                      
REMARK 465     GLY B   485                                                      
REMARK 465     PHE B   486                                                      
REMARK 465     ASN B   487                                                      
REMARK 465     CYS B   488                                                      
REMARK 465     TYR B   489                                                      
REMARK 465     PHE B   490                                                      
REMARK 465     PRO B   491                                                      
REMARK 465     LEU B   492                                                      
REMARK 465     GLN B   493                                                      
REMARK 465     SER B   494                                                      
REMARK 465     TYR B   495                                                      
REMARK 465     GLY B   496                                                      
REMARK 465     PHE B   497                                                      
REMARK 465     GLN B   498                                                      
REMARK 465     PRO B   499                                                      
REMARK 465     THR B   500                                                      
REMARK 465     ASN B   501                                                      
REMARK 465     GLY B   502                                                      
REMARK 465     VAL B   503                                                      
REMARK 465     GLY B   504                                                      
REMARK 465     TYR B   505                                                      
REMARK 465     GLN B   506                                                      
REMARK 465     PRO B   507                                                      
REMARK 465     TYR B   508                                                      
REMARK 465     ARG B   509                                                      
REMARK 465     VAL B   510                                                      
REMARK 465     VAL B   511                                                      
REMARK 465     VAL B   512                                                      
REMARK 465     LEU B   513                                                      
REMARK 465     SER B   514                                                      
REMARK 465     PHE B   515                                                      
REMARK 465     GLU B   516                                                      
REMARK 465     LEU B   517                                                      
REMARK 465     LEU B   518                                                      
REMARK 465     HIS B   519                                                      
REMARK 465     ALA B   520                                                      
REMARK 465     PRO B   521                                                      
REMARK 465     ALA B   522                                                      
REMARK 465     THR B   523                                                      
REMARK 465     VAL B   524                                                      
REMARK 465     CYS B   525                                                      
REMARK 465     GLY B   526                                                      
REMARK 465     PRO B   527                                                      
REMARK 465     LYS B   528                                                      
REMARK 465     LYS B   529                                                      
REMARK 465     SER B   530                                                      
REMARK 465     THR B   531                                                      
REMARK 465     ASN B   532                                                      
REMARK 465     LEU B   533                                                      
REMARK 465     VAL B   534                                                      
REMARK 465     LYS B   535                                                      
REMARK 465     ASN B   536                                                      
REMARK 465     LYS B   537                                                      
REMARK 465     CYS B   538                                                      
REMARK 465     VAL B   539                                                      
REMARK 465     ASN B   540                                                      
REMARK 465     PHE B   541                                                      
REMARK 465     ASN B   542                                                      
REMARK 465     PHE B   543                                                      
REMARK 465     ASN B   544                                                      
REMARK 465     GLY B   545                                                      
REMARK 465     LEU B   546                                                      
REMARK 465     THR B   547                                                      
REMARK 465     GLY B   548                                                      
REMARK 465     THR B   549                                                      
REMARK 465     GLY B   550                                                      
REMARK 465     VAL B   551                                                      
REMARK 465     LEU B   552                                                      
REMARK 465     THR B   553                                                      
REMARK 465     GLU B   554                                                      
REMARK 465     SER B   555                                                      
REMARK 465     ASN B   556                                                      
REMARK 465     LYS B   557                                                      
REMARK 465     LYS B   558                                                      
REMARK 465     PHE B   559                                                      
REMARK 465     LEU B   560                                                      
REMARK 465     PRO B   561                                                      
REMARK 465     PHE B   562                                                      
REMARK 465     GLN B   563                                                      
REMARK 465     GLN B   564                                                      
REMARK 465     PHE B   565                                                      
REMARK 465     GLY B   566                                                      
REMARK 465     ARG B   567                                                      
REMARK 465     ASP B   568                                                      
REMARK 465     ILE B   569                                                      
REMARK 465     ALA B   570                                                      
REMARK 465     ASP B   571                                                      
REMARK 465     THR B   572                                                      
REMARK 465     THR B   573                                                      
REMARK 465     ASP B   574                                                      
REMARK 465     ALA B   575                                                      
REMARK 465     VAL B   576                                                      
REMARK 465     ARG B   577                                                      
REMARK 465     ASP B   578                                                      
REMARK 465     PRO B   579                                                      
REMARK 465     GLN B   580                                                      
REMARK 465     THR B   581                                                      
REMARK 465     LEU B   582                                                      
REMARK 465     GLU B   583                                                      
REMARK 465     ILE B   584                                                      
REMARK 465     LEU B   585                                                      
REMARK 465     ASP B   586                                                      
REMARK 465     ILE B   587                                                      
REMARK 465     THR B   588                                                      
REMARK 465     PRO B   589                                                      
REMARK 465     CYS B   590                                                      
REMARK 465     SER B   591                                                      
REMARK 465     PHE B   592                                                      
REMARK 465     GLY B   593                                                      
REMARK 465     GLY B   594                                                      
REMARK 465     VAL B   595                                                      
REMARK 465     SER B   596                                                      
REMARK 465     VAL B   597                                                      
REMARK 465     ILE B   598                                                      
REMARK 465     THR B   599                                                      
REMARK 465     PRO B   600                                                      
REMARK 465     GLY B   601                                                      
REMARK 465     THR B   602                                                      
REMARK 465     ASN B   603                                                      
REMARK 465     THR B   604                                                      
REMARK 465     SER B   605                                                      
REMARK 465     ASN B   606                                                      
REMARK 465     GLN B   607                                                      
REMARK 465     VAL B   608                                                      
REMARK 465     ALA B   609                                                      
REMARK 465     VAL B   610                                                      
REMARK 465     LEU B   611                                                      
REMARK 465     TYR B   612                                                      
REMARK 465     GLN B   613                                                      
REMARK 465     ASP B   614                                                      
REMARK 465     VAL B   615                                                      
REMARK 465     ASN B   616                                                      
REMARK 465     CYS B   617                                                      
REMARK 465     THR B   618                                                      
REMARK 465     GLU B   619                                                      
REMARK 465     VAL B   620                                                      
REMARK 465     PRO B   621                                                      
REMARK 465     VAL B   622                                                      
REMARK 465     ALA B   623                                                      
REMARK 465     ILE B   624                                                      
REMARK 465     HIS B   625                                                      
REMARK 465     ALA B   626                                                      
REMARK 465     ASP B   627                                                      
REMARK 465     GLN B   628                                                      
REMARK 465     LEU B   629                                                      
REMARK 465     THR B   630                                                      
REMARK 465     PRO B   631                                                      
REMARK 465     THR B   632                                                      
REMARK 465     TRP B   633                                                      
REMARK 465     ARG B   634                                                      
REMARK 465     VAL B   635                                                      
REMARK 465     TYR B   636                                                      
REMARK 465     SER B   637                                                      
REMARK 465     THR B   638                                                      
REMARK 465     GLY B   639                                                      
REMARK 465     SER B   640                                                      
REMARK 465     ASN B   641                                                      
REMARK 465     VAL B   642                                                      
REMARK 465     PHE B   643                                                      
REMARK 465     GLN B   644                                                      
REMARK 465     THR B   645                                                      
REMARK 465     ARG B   646                                                      
REMARK 465     ALA B   647                                                      
REMARK 465     GLY B   648                                                      
REMARK 465     CYS B   649                                                      
REMARK 465     LEU B   650                                                      
REMARK 465     ILE B   651                                                      
REMARK 465     GLY B   652                                                      
REMARK 465     ALA B   653                                                      
REMARK 465     GLU B   654                                                      
REMARK 465     HIS B   655                                                      
REMARK 465     VAL B   656                                                      
REMARK 465     ASN B   657                                                      
REMARK 465     ASN B   658                                                      
REMARK 465     SER B   659                                                      
REMARK 465     TYR B   660                                                      
REMARK 465     GLU B   661                                                      
REMARK 465     CYS B   662                                                      
REMARK 465     ASP B   663                                                      
REMARK 465     ILE B   664                                                      
REMARK 465     PRO B   665                                                      
REMARK 465     ILE B   666                                                      
REMARK 465     GLY B   667                                                      
REMARK 465     ALA B   668                                                      
REMARK 465     GLY B   669                                                      
REMARK 465     ILE B   670                                                      
REMARK 465     CYS B   671                                                      
REMARK 465     ALA B   672                                                      
REMARK 465     SER B   673                                                      
REMARK 465     TYR B   674                                                      
REMARK 465     GLN B   675                                                      
REMARK 465     THR B   676                                                      
REMARK 465     GLN B   677                                                      
REMARK 465     THR B   678                                                      
REMARK 465     ASN B   679                                                      
REMARK 465     SER B   680                                                      
REMARK 465     PRO B   681                                                      
REMARK 465     ARG B   682                                                      
REMARK 465     ARG B   683                                                      
REMARK 465     ALA B   684                                                      
REMARK 465     ARG B   685                                                      
REMARK 465     SER B   686                                                      
REMARK 465     VAL B   687                                                      
REMARK 465     ALA B   688                                                      
REMARK 465     SER B   689                                                      
REMARK 465     GLN B   690                                                      
REMARK 465     SER B   691                                                      
REMARK 465     ILE B   692                                                      
REMARK 465     ILE B   693                                                      
REMARK 465     ALA B   694                                                      
REMARK 465     TYR B   695                                                      
REMARK 465     THR B   696                                                      
REMARK 465     MET B   697                                                      
REMARK 465     SER B   698                                                      
REMARK 465     LEU B   699                                                      
REMARK 465     GLY B   700                                                      
REMARK 465     ALA B   701                                                      
REMARK 465     GLU B   702                                                      
REMARK 465     ALA B   771                                                      
REMARK 465     VAL B   772                                                      
REMARK 465     GLU B   773                                                      
REMARK 465     GLN B   774                                                      
REMARK 465     ASP B   775                                                      
REMARK 465     LYS B   776                                                      
REMARK 465     ASN B   777                                                      
REMARK 465     THR B   778                                                      
REMARK 465     GLN B   779                                                      
REMARK 465     GLU B   780                                                      
REMARK 465     VAL B   781                                                      
REMARK 465     PHE B   782                                                      
REMARK 465     ALA B   783                                                      
REMARK 465     GLN B   784                                                      
REMARK 465     VAL B   785                                                      
REMARK 465     LYS B   786                                                      
REMARK 465     GLN B   787                                                      
REMARK 465     ILE B   788                                                      
REMARK 465     TYR B   789                                                      
REMARK 465     LYS B   790                                                      
REMARK 465     THR B   791                                                      
REMARK 465     PRO B   792                                                      
REMARK 465     PRO B   793                                                      
REMARK 465     ILE B   794                                                      
REMARK 465     LYS B   795                                                      
REMARK 465     ASP B   796                                                      
REMARK 465     PHE B   797                                                      
REMARK 465     GLY B   798                                                      
REMARK 465     GLY B   799                                                      
REMARK 465     PHE B   800                                                      
REMARK 465     ASN B   801                                                      
REMARK 465     PHE B   802                                                      
REMARK 465     SER B   803                                                      
REMARK 465     GLN B   804                                                      
REMARK 465     ILE B   805                                                      
REMARK 465     LEU B   806                                                      
REMARK 465     PRO B   807                                                      
REMARK 465     ASP B   808                                                      
REMARK 465     PRO B   809                                                      
REMARK 465     SER B   810                                                      
REMARK 465     LYS B   811                                                      
REMARK 465     PRO B   812                                                      
REMARK 465     SER B   813                                                      
REMARK 465     LYS B   814                                                      
REMARK 465     ARG B   815                                                      
REMARK 465     SER B   816                                                      
REMARK 465     PHE B   817                                                      
REMARK 465     ILE B   818                                                      
REMARK 465     GLU B   819                                                      
REMARK 465     ASP B   820                                                      
REMARK 465     LEU B   821                                                      
REMARK 465     LEU B   822                                                      
REMARK 465     PHE B   823                                                      
REMARK 465     ASN B   824                                                      
REMARK 465     LYS B   825                                                      
REMARK 465     VAL B   826                                                      
REMARK 465     THR B   827                                                      
REMARK 465     LEU B   828                                                      
REMARK 465     ALA B   829                                                      
REMARK 465     ASP B   830                                                      
REMARK 465     ALA B   831                                                      
REMARK 465     GLY B   832                                                      
REMARK 465     PHE B   833                                                      
REMARK 465     ILE B   834                                                      
REMARK 465     LYS B   835                                                      
REMARK 465     GLN B   836                                                      
REMARK 465     TYR B   837                                                      
REMARK 465     GLY B   838                                                      
REMARK 465     ASP B   839                                                      
REMARK 465     CYS B   840                                                      
REMARK 465     LEU B   841                                                      
REMARK 465     GLY B   842                                                      
REMARK 465     ASP B   843                                                      
REMARK 465     ILE B   844                                                      
REMARK 465     ALA B   845                                                      
REMARK 465     ALA B   846                                                      
REMARK 465     ARG B   847                                                      
REMARK 465     ASP B   848                                                      
REMARK 465     LEU B   849                                                      
REMARK 465     ILE B   850                                                      
REMARK 465     CYS B   851                                                      
REMARK 465     ALA B   852                                                      
REMARK 465     GLN B   853                                                      
REMARK 465     LYS B   854                                                      
REMARK 465     PHE B   855                                                      
REMARK 465     ASN B   856                                                      
REMARK 465     GLY B   857                                                      
REMARK 465     LEU B   858                                                      
REMARK 465     THR B   859                                                      
REMARK 465     VAL B   860                                                      
REMARK 465     LEU B   861                                                      
REMARK 465     PRO B   862                                                      
REMARK 465     PRO B   863                                                      
REMARK 465     LEU B   864                                                      
REMARK 465     LEU B   865                                                      
REMARK 465     THR B   866                                                      
REMARK 465     ASP B   867                                                      
REMARK 465     GLU B   868                                                      
REMARK 465     MET B   869                                                      
REMARK 465     ILE B   870                                                      
REMARK 465     ALA B   871                                                      
REMARK 465     GLN B   872                                                      
REMARK 465     TYR B   873                                                      
REMARK 465     THR B   874                                                      
REMARK 465     SER B   875                                                      
REMARK 465     ALA B   876                                                      
REMARK 465     LEU B   877                                                      
REMARK 465     LEU B   878                                                      
REMARK 465     ALA B   879                                                      
REMARK 465     GLY B   880                                                      
REMARK 465     THR B   881                                                      
REMARK 465     ILE B   882                                                      
REMARK 465     THR B   883                                                      
REMARK 465     SER B   884                                                      
REMARK 465     GLY B   885                                                      
REMARK 465     TRP B   886                                                      
REMARK 465     THR B   887                                                      
REMARK 465     PHE B   888                                                      
REMARK 465     GLY B   889                                                      
REMARK 465     ALA B   890                                                      
REMARK 465     GLY B   891                                                      
REMARK 465     ALA B   892                                                      
REMARK 465     ALA B   893                                                      
REMARK 465     LEU B   894                                                      
REMARK 465     GLN B   895                                                      
REMARK 465     ILE B   896                                                      
REMARK 465     PRO B   897                                                      
REMARK 465     PHE B   898                                                      
REMARK 465     ALA B   899                                                      
REMARK 465     MET B   900                                                      
REMARK 465     GLN B   901                                                      
REMARK 465     MET B   902                                                      
REMARK 465     ALA B   903                                                      
REMARK 465     TYR B   904                                                      
REMARK 465     ARG B   905                                                      
REMARK 465     PHE B   906                                                      
REMARK 465     ASN B   907                                                      
REMARK 465     GLY B   908                                                      
REMARK 465     ILE B   909                                                      
REMARK 465     GLY B   910                                                      
REMARK 465     VAL B   911                                                      
REMARK 465     ALA B  1174                                                      
REMARK 465     SER B  1175                                                      
REMARK 465     VAL B  1176                                                      
REMARK 465     VAL B  1177                                                      
REMARK 465     ASN B  1178                                                      
REMARK 465     ILE B  1179                                                      
REMARK 465     ILE B  1198                                                      
REMARK 465     ASP B  1199                                                      
REMARK 465     LEU B  1200                                                      
REMARK 465     GLN B  1201                                                      
REMARK 465     GLU B  1202                                                      
REMARK 465     LEU B  1203                                                      
REMARK 465     GLY B  1204                                                      
REMARK 465     LYS B  1205                                                      
REMARK 465     TYR B  1206                                                      
REMARK 465     GLU B  1207                                                      
REMARK 465     GLN B  1208                                                      
REMARK 465     TYR B  1209                                                      
REMARK 465     ILE B  1210                                                      
REMARK 465     LYS B  1211                                                      
REMARK 465     TRP B  1212                                                      
REMARK 465     PRO B  1213                                                      
REMARK 465     TRP B  1214                                                      
REMARK 465     TYR B  1215                                                      
REMARK 465     ILE B  1216                                                      
REMARK 465     TRP B  1217                                                      
REMARK 465     LEU B  1218                                                      
REMARK 465     GLY B  1219                                                      
REMARK 465     PHE B  1220                                                      
REMARK 465     ILE B  1221                                                      
REMARK 465     ALA B  1222                                                      
REMARK 465     GLY B  1223                                                      
REMARK 465     LEU B  1224                                                      
REMARK 465     ILE B  1225                                                      
REMARK 465     ALA B  1226                                                      
REMARK 465     ILE B  1227                                                      
REMARK 465     VAL B  1228                                                      
REMARK 465     MET B  1229                                                      
REMARK 465     VAL B  1230                                                      
REMARK 465     THR B  1231                                                      
REMARK 465     ILE B  1232                                                      
REMARK 465     MET B  1233                                                      
REMARK 465     LEU B  1234                                                      
REMARK 465     CYS B  1235                                                      
REMARK 465     CYS B  1236                                                      
REMARK 465     MET B  1237                                                      
REMARK 465     THR B  1238                                                      
REMARK 465     SER B  1239                                                      
REMARK 465     CYS B  1240                                                      
REMARK 465     CYS B  1241                                                      
REMARK 465     SER B  1242                                                      
REMARK 465     CYS B  1243                                                      
REMARK 465     LEU B  1244                                                      
REMARK 465     LYS B  1245                                                      
REMARK 465     GLY B  1246                                                      
REMARK 465     CYS B  1247                                                      
REMARK 465     CYS B  1248                                                      
REMARK 465     SER B  1249                                                      
REMARK 465     CYS B  1250                                                      
REMARK 465     GLY B  1251                                                      
REMARK 465     SER B  1252                                                      
REMARK 465     CYS B  1253                                                      
REMARK 465     CYS B  1254                                                      
REMARK 465     LYS B  1255                                                      
REMARK 465     PHE B  1256                                                      
REMARK 465     ASP B  1257                                                      
REMARK 465     GLU B  1258                                                      
REMARK 465     ASP B  1259                                                      
REMARK 465     ASP B  1260                                                      
REMARK 465     SER B  1261                                                      
REMARK 465     GLU B  1262                                                      
REMARK 465     PRO B  1263                                                      
REMARK 465     VAL B  1264                                                      
REMARK 465     LEU B  1265                                                      
REMARK 465     LYS B  1266                                                      
REMARK 465     GLY B  1267                                                      
REMARK 465     VAL B  1268                                                      
REMARK 465     LYS B  1269                                                      
REMARK 465     LEU B  1270                                                      
REMARK 465     HIS B  1271                                                      
REMARK 465     TYR B  1272                                                      
REMARK 465     THR B  1273                                                      
REMARK 465     LEU B  1274                                                      
REMARK 465     GLU B  1275                                                      
REMARK 465     SER B  1276                                                      
REMARK 465     GLY B  1277                                                      
REMARK 465     GLY B  1278                                                      
REMARK 465     GLY B  1279                                                      
REMARK 465     SER B  1280                                                      
REMARK 465     ALA B  1281                                                      
REMARK 465     TRP B  1282                                                      
REMARK 465     SER B  1283                                                      
REMARK 465     HIS B  1284                                                      
REMARK 465     PRO B  1285                                                      
REMARK 465     GLN B  1286                                                      
REMARK 465     PHE B  1287                                                      
REMARK 465     GLU B  1288                                                      
REMARK 465     LYS B  1289                                                      
REMARK 465     GLY B  1290                                                      
REMARK 465     GLY B  1291                                                      
REMARK 465     GLY B  1292                                                      
REMARK 465     SER B  1293                                                      
REMARK 465     GLY B  1294                                                      
REMARK 465     GLY B  1295                                                      
REMARK 465     GLY B  1296                                                      
REMARK 465     SER B  1297                                                      
REMARK 465     GLY B  1298                                                      
REMARK 465     GLY B  1299                                                      
REMARK 465     SER B  1300                                                      
REMARK 465     SER B  1301                                                      
REMARK 465     ALA B  1302                                                      
REMARK 465     TRP B  1303                                                      
REMARK 465     SER B  1304                                                      
REMARK 465     HIS B  1305                                                      
REMARK 465     PRO B  1306                                                      
REMARK 465     GLN B  1307                                                      
REMARK 465     PHE B  1308                                                      
REMARK 465     GLU B  1309                                                      
REMARK 465     LYS B  1310                                                      
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   ND2  ASN B   717     O5   NAG B  1402              2.14            
REMARK 500   ND2  ASN C   717     O5   NAG C  1402              2.14            
REMARK 500   ND2  ASN A   717     O5   NAG A  1402              2.14            
REMARK 500   OD1  ASN C  1173     C1   NAG C  1417              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    CYS C 749   CA  -  CB  -  SG  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    CYS A 749   CA  -  CB  -  SG  ANGL. DEV. =  12.1 DEGREES          
REMARK 500    CYS B 749   CA  -  CB  -  SG  ANGL. DEV. =  12.1 DEGREES          
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    SER C 758       37.22    -85.26                                   
REMARK 500    ASP C1041       -5.94     84.94                                   
REMARK 500    ASP C1084       39.06     38.76                                   
REMARK 500    PRO C1090      170.66    -58.65                                   
REMARK 500    GLU C1111       85.11   -154.31                                   
REMARK 500    SER C1123     -161.62   -127.91                                   
REMARK 500    THR C1136       95.73    -62.73                                   
REMARK 500    LEU C1141       90.35    -65.83                                   
REMARK 500    ASN C1158       48.72    -88.42                                   
REMARK 500    ASP C1168       75.45   -106.67                                   
REMARK 500    SER A 758       37.27    -85.33                                   
REMARK 500    ASP A1041       -5.96     84.98                                   
REMARK 500    ASP A1084       39.07     38.74                                   
REMARK 500    PRO A1090      170.66    -58.60                                   
REMARK 500    GLU A1111       85.08   -154.25                                   
REMARK 500    SER A1123     -161.66   -127.90                                   
REMARK 500    THR A1136       95.70    -62.72                                   
REMARK 500    LEU A1141       90.36    -65.84                                   
REMARK 500    ASN A1158       48.72    -88.40                                   
REMARK 500    ASP A1168       75.40   -106.69                                   
REMARK 500    SER B 758       37.19    -85.26                                   
REMARK 500    ASP B1041       -5.90     84.88                                   
REMARK 500    ASP B1084       39.05     38.76                                   
REMARK 500    PRO B1090      170.68    -58.71                                   
REMARK 500    GLU B1111       85.18   -154.31                                   
REMARK 500    SER B1123     -161.61   -127.90                                   
REMARK 500    THR B1136       95.67    -62.75                                   
REMARK 500    LEU B1141       90.32    -65.87                                   
REMARK 500    ASN B1158       48.75    -88.47                                   
REMARK 500    ASP B1168       75.47   -106.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     NAG E    1                                                       
REMARK 610     NAG J    1                                                       
REMARK 610     NAG O    1                                                       
REMARK 610     MAN C 1409                                                       
REMARK 610     NAG C 1417                                                       
REMARK 610     MAN A 1409                                                       
REMARK 610     NAG A 1417                                                       
REMARK 610     MAN B 1409                                                       
REMARK 610     NAG B 1417                                                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-22293   RELATED DB: EMDB                             
REMARK 900 DISTINCT CONFORMATIONAL STATES OF SARS-COV-2 SPIKE PROTEIN           
DBREF  6XRA C    1  1273  UNP    P0DTC2   SPIKE_SARS2      1   1273             
DBREF  6XRA A    1  1273  UNP    P0DTC2   SPIKE_SARS2      1   1273             
DBREF  6XRA B    1  1273  UNP    P0DTC2   SPIKE_SARS2      1   1273             
SEQADV 6XRA LEU C 1274  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU C 1275  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1276  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1277  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1278  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1279  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1280  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA C 1281  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP C 1282  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1283  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS C 1284  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO C 1285  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN C 1286  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE C 1287  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU C 1288  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS C 1289  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1290  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1291  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1292  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1293  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1294  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1295  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1296  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1297  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1298  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY C 1299  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1300  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1301  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA C 1302  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP C 1303  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER C 1304  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS C 1305  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO C 1306  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN C 1307  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE C 1308  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU C 1309  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS C 1310  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LEU A 1274  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU A 1275  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1276  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1277  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1278  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1279  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1280  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA A 1281  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP A 1282  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1283  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS A 1284  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO A 1285  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN A 1286  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE A 1287  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU A 1288  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS A 1289  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1290  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1291  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1292  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1293  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1294  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1295  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1296  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1297  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1298  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY A 1299  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1300  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1301  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA A 1302  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP A 1303  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER A 1304  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS A 1305  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO A 1306  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN A 1307  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE A 1308  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU A 1309  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS A 1310  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LEU B 1274  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU B 1275  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1276  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1277  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1278  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1279  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1280  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA B 1281  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP B 1282  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1283  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS B 1284  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO B 1285  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN B 1286  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE B 1287  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU B 1288  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS B 1289  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1290  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1291  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1292  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1293  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1294  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1295  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1296  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1297  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1298  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLY B 1299  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1300  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1301  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA ALA B 1302  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA TRP B 1303  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA SER B 1304  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA HIS B 1305  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PRO B 1306  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLN B 1307  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA PHE B 1308  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA GLU B 1309  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 6XRA LYS B 1310  UNP  P0DTC2              EXPRESSION TAG                 
SEQRES   1 C 1310  MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER          
SEQRES   2 C 1310  GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO          
SEQRES   3 C 1310  ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO          
SEQRES   4 C 1310  ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN          
SEQRES   5 C 1310  ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE          
SEQRES   6 C 1310  HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG          
SEQRES   7 C 1310  PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR          
SEQRES   8 C 1310  PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP          
SEQRES   9 C 1310  ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU          
SEQRES  10 C 1310  LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL          
SEQRES  11 C 1310  CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL          
SEQRES  12 C 1310  TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU          
SEQRES  13 C 1310  PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU          
SEQRES  14 C 1310  TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS          
SEQRES  15 C 1310  GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS          
SEQRES  16 C 1310  ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR          
SEQRES  17 C 1310  PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER          
SEQRES  18 C 1310  ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN          
SEQRES  19 C 1310  ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER          
SEQRES  20 C 1310  TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA          
SEQRES  21 C 1310  GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG          
SEQRES  22 C 1310  THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR          
SEQRES  23 C 1310  ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR          
SEQRES  24 C 1310  LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE          
SEQRES  25 C 1310  TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER          
SEQRES  26 C 1310  ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE          
SEQRES  27 C 1310  GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR          
SEQRES  28 C 1310  ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP          
SEQRES  29 C 1310  TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE          
SEQRES  30 C 1310  LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU          
SEQRES  31 C 1310  CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG          
SEQRES  32 C 1310  GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY          
SEQRES  33 C 1310  LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE          
SEQRES  34 C 1310  THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP          
SEQRES  35 C 1310  SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU          
SEQRES  36 C 1310  PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE          
SEQRES  37 C 1310  SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN          
SEQRES  38 C 1310  GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER          
SEQRES  39 C 1310  TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO          
SEQRES  40 C 1310  TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA          
SEQRES  41 C 1310  PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU          
SEQRES  42 C 1310  VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU          
SEQRES  43 C 1310  THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE          
SEQRES  44 C 1310  LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR          
SEQRES  45 C 1310  THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU          
SEQRES  46 C 1310  ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE          
SEQRES  47 C 1310  THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU          
SEQRES  48 C 1310  TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE          
SEQRES  49 C 1310  HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER          
SEQRES  50 C 1310  THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU          
SEQRES  51 C 1310  ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP          
SEQRES  52 C 1310  ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR          
SEQRES  53 C 1310  GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER          
SEQRES  54 C 1310  GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU          
SEQRES  55 C 1310  ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO          
SEQRES  56 C 1310  THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO          
SEQRES  57 C 1310  VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR          
SEQRES  58 C 1310  ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU          
SEQRES  59 C 1310  GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU          
SEQRES  60 C 1310  THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU          
SEQRES  61 C 1310  VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO          
SEQRES  62 C 1310  ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU          
SEQRES  63 C 1310  PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU          
SEQRES  64 C 1310  ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY          
SEQRES  65 C 1310  PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA          
SEQRES  66 C 1310  ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU          
SEQRES  67 C 1310  THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA          
SEQRES  68 C 1310  GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER          
SEQRES  69 C 1310  GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO          
SEQRES  70 C 1310  PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY          
SEQRES  71 C 1310  VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE          
SEQRES  72 C 1310  ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP          
SEQRES  73 C 1310  SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN          
SEQRES  74 C 1310  ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU          
SEQRES  75 C 1310  VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER          
SEQRES  76 C 1310  VAL LEU ASN ASP ILE LEU SER ARG LEU ASP LYS VAL GLU          
SEQRES  77 C 1310  ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU          
SEQRES  78 C 1310  GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG          
SEQRES  79 C 1310  ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR          
SEQRES  80 C 1310  LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL          
SEQRES  81 C 1310  ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO          
SEQRES  82 C 1310  GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR          
SEQRES  83 C 1310  TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO          
SEQRES  84 C 1310  ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU          
SEQRES  85 C 1310  GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR          
SEQRES  86 C 1310  GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP          
SEQRES  87 C 1310  ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY          
SEQRES  88 C 1310  ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU          
SEQRES  89 C 1310  LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS          
SEQRES  90 C 1310  ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER          
SEQRES  91 C 1310  GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE          
SEQRES  92 C 1310  ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER          
SEQRES  93 C 1310  LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR          
SEQRES  94 C 1310  ILE LYS TRP PRO TRP TYR ILE TRP LEU GLY PHE ILE ALA          
SEQRES  95 C 1310  GLY LEU ILE ALA ILE VAL MET VAL THR ILE MET LEU CYS          
SEQRES  96 C 1310  CYS MET THR SER CYS CYS SER CYS LEU LYS GLY CYS CYS          
SEQRES  97 C 1310  SER CYS GLY SER CYS CYS LYS PHE ASP GLU ASP ASP SER          
SEQRES  98 C 1310  GLU PRO VAL LEU LYS GLY VAL LYS LEU HIS TYR THR LEU          
SEQRES  99 C 1310  GLU SER GLY GLY GLY SER ALA TRP SER HIS PRO GLN PHE          
SEQRES 100 C 1310  GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER          
SEQRES 101 C 1310  SER ALA TRP SER HIS PRO GLN PHE GLU LYS                      
SEQRES   1 A 1310  MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER          
SEQRES   2 A 1310  GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO          
SEQRES   3 A 1310  ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO          
SEQRES   4 A 1310  ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN          
SEQRES   5 A 1310  ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE          
SEQRES   6 A 1310  HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG          
SEQRES   7 A 1310  PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR          
SEQRES   8 A 1310  PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP          
SEQRES   9 A 1310  ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU          
SEQRES  10 A 1310  LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL          
SEQRES  11 A 1310  CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL          
SEQRES  12 A 1310  TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU          
SEQRES  13 A 1310  PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU          
SEQRES  14 A 1310  TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS          
SEQRES  15 A 1310  GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS          
SEQRES  16 A 1310  ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR          
SEQRES  17 A 1310  PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER          
SEQRES  18 A 1310  ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN          
SEQRES  19 A 1310  ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER          
SEQRES  20 A 1310  TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA          
SEQRES  21 A 1310  GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG          
SEQRES  22 A 1310  THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR          
SEQRES  23 A 1310  ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR          
SEQRES  24 A 1310  LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE          
SEQRES  25 A 1310  TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER          
SEQRES  26 A 1310  ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE          
SEQRES  27 A 1310  GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR          
SEQRES  28 A 1310  ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP          
SEQRES  29 A 1310  TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE          
SEQRES  30 A 1310  LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU          
SEQRES  31 A 1310  CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG          
SEQRES  32 A 1310  GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY          
SEQRES  33 A 1310  LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE          
SEQRES  34 A 1310  THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP          
SEQRES  35 A 1310  SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU          
SEQRES  36 A 1310  PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE          
SEQRES  37 A 1310  SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN          
SEQRES  38 A 1310  GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER          
SEQRES  39 A 1310  TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO          
SEQRES  40 A 1310  TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA          
SEQRES  41 A 1310  PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU          
SEQRES  42 A 1310  VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU          
SEQRES  43 A 1310  THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE          
SEQRES  44 A 1310  LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR          
SEQRES  45 A 1310  THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU          
SEQRES  46 A 1310  ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE          
SEQRES  47 A 1310  THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU          
SEQRES  48 A 1310  TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE          
SEQRES  49 A 1310  HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER          
SEQRES  50 A 1310  THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU          
SEQRES  51 A 1310  ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP          
SEQRES  52 A 1310  ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR          
SEQRES  53 A 1310  GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER          
SEQRES  54 A 1310  GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU          
SEQRES  55 A 1310  ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO          
SEQRES  56 A 1310  THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO          
SEQRES  57 A 1310  VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR          
SEQRES  58 A 1310  ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU          
SEQRES  59 A 1310  GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU          
SEQRES  60 A 1310  THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU          
SEQRES  61 A 1310  VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO          
SEQRES  62 A 1310  ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU          
SEQRES  63 A 1310  PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU          
SEQRES  64 A 1310  ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY          
SEQRES  65 A 1310  PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA          
SEQRES  66 A 1310  ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU          
SEQRES  67 A 1310  THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA          
SEQRES  68 A 1310  GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER          
SEQRES  69 A 1310  GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO          
SEQRES  70 A 1310  PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY          
SEQRES  71 A 1310  VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE          
SEQRES  72 A 1310  ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP          
SEQRES  73 A 1310  SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN          
SEQRES  74 A 1310  ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU          
SEQRES  75 A 1310  VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER          
SEQRES  76 A 1310  VAL LEU ASN ASP ILE LEU SER ARG LEU ASP LYS VAL GLU          
SEQRES  77 A 1310  ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU          
SEQRES  78 A 1310  GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG          
SEQRES  79 A 1310  ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR          
SEQRES  80 A 1310  LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL          
SEQRES  81 A 1310  ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO          
SEQRES  82 A 1310  GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR          
SEQRES  83 A 1310  TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO          
SEQRES  84 A 1310  ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU          
SEQRES  85 A 1310  GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR          
SEQRES  86 A 1310  GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP          
SEQRES  87 A 1310  ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY          
SEQRES  88 A 1310  ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU          
SEQRES  89 A 1310  LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS          
SEQRES  90 A 1310  ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER          
SEQRES  91 A 1310  GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE          
SEQRES  92 A 1310  ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER          
SEQRES  93 A 1310  LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR          
SEQRES  94 A 1310  ILE LYS TRP PRO TRP TYR ILE TRP LEU GLY PHE ILE ALA          
SEQRES  95 A 1310  GLY LEU ILE ALA ILE VAL MET VAL THR ILE MET LEU CYS          
SEQRES  96 A 1310  CYS MET THR SER CYS CYS SER CYS LEU LYS GLY CYS CYS          
SEQRES  97 A 1310  SER CYS GLY SER CYS CYS LYS PHE ASP GLU ASP ASP SER          
SEQRES  98 A 1310  GLU PRO VAL LEU LYS GLY VAL LYS LEU HIS TYR THR LEU          
SEQRES  99 A 1310  GLU SER GLY GLY GLY SER ALA TRP SER HIS PRO GLN PHE          
SEQRES 100 A 1310  GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER          
SEQRES 101 A 1310  SER ALA TRP SER HIS PRO GLN PHE GLU LYS                      
SEQRES   1 B 1310  MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER          
SEQRES   2 B 1310  GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO          
SEQRES   3 B 1310  ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO          
SEQRES   4 B 1310  ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN          
SEQRES   5 B 1310  ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE          
SEQRES   6 B 1310  HIS ALA ILE HIS VAL SER GLY THR ASN GLY THR LYS ARG          
SEQRES   7 B 1310  PHE ASP ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR          
SEQRES   8 B 1310  PHE ALA SER THR GLU LYS SER ASN ILE ILE ARG GLY TRP          
SEQRES   9 B 1310  ILE PHE GLY THR THR LEU ASP SER LYS THR GLN SER LEU          
SEQRES  10 B 1310  LEU ILE VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL          
SEQRES  11 B 1310  CYS GLU PHE GLN PHE CYS ASN ASP PRO PHE LEU GLY VAL          
SEQRES  12 B 1310  TYR TYR HIS LYS ASN ASN LYS SER TRP MET GLU SER GLU          
SEQRES  13 B 1310  PHE ARG VAL TYR SER SER ALA ASN ASN CYS THR PHE GLU          
SEQRES  14 B 1310  TYR VAL SER GLN PRO PHE LEU MET ASP LEU GLU GLY LYS          
SEQRES  15 B 1310  GLN GLY ASN PHE LYS ASN LEU ARG GLU PHE VAL PHE LYS          
SEQRES  16 B 1310  ASN ILE ASP GLY TYR PHE LYS ILE TYR SER LYS HIS THR          
SEQRES  17 B 1310  PRO ILE ASN LEU VAL ARG ASP LEU PRO GLN GLY PHE SER          
SEQRES  18 B 1310  ALA LEU GLU PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN          
SEQRES  19 B 1310  ILE THR ARG PHE GLN THR LEU LEU ALA LEU HIS ARG SER          
SEQRES  20 B 1310  TYR LEU THR PRO GLY ASP SER SER SER GLY TRP THR ALA          
SEQRES  21 B 1310  GLY ALA ALA ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG          
SEQRES  22 B 1310  THR PHE LEU LEU LYS TYR ASN GLU ASN GLY THR ILE THR          
SEQRES  23 B 1310  ASP ALA VAL ASP CYS ALA LEU ASP PRO LEU SER GLU THR          
SEQRES  24 B 1310  LYS CYS THR LEU LYS SER PHE THR VAL GLU LYS GLY ILE          
SEQRES  25 B 1310  TYR GLN THR SER ASN PHE ARG VAL GLN PRO THR GLU SER          
SEQRES  26 B 1310  ILE VAL ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE          
SEQRES  27 B 1310  GLY GLU VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR          
SEQRES  28 B 1310  ALA TRP ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP          
SEQRES  29 B 1310  TYR SER VAL LEU TYR ASN SER ALA SER PHE SER THR PHE          
SEQRES  30 B 1310  LYS CYS TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU          
SEQRES  31 B 1310  CYS PHE THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG          
SEQRES  32 B 1310  GLY ASP GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY          
SEQRES  33 B 1310  LYS ILE ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE          
SEQRES  34 B 1310  THR GLY CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP          
SEQRES  35 B 1310  SER LYS VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU          
SEQRES  36 B 1310  PHE ARG LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE          
SEQRES  37 B 1310  SER THR GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN          
SEQRES  38 B 1310  GLY VAL GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER          
SEQRES  39 B 1310  TYR GLY PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO          
SEQRES  40 B 1310  TYR ARG VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA          
SEQRES  41 B 1310  PRO ALA THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU          
SEQRES  42 B 1310  VAL LYS ASN LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU          
SEQRES  43 B 1310  THR GLY THR GLY VAL LEU THR GLU SER ASN LYS LYS PHE          
SEQRES  44 B 1310  LEU PRO PHE GLN GLN PHE GLY ARG ASP ILE ALA ASP THR          
SEQRES  45 B 1310  THR ASP ALA VAL ARG ASP PRO GLN THR LEU GLU ILE LEU          
SEQRES  46 B 1310  ASP ILE THR PRO CYS SER PHE GLY GLY VAL SER VAL ILE          
SEQRES  47 B 1310  THR PRO GLY THR ASN THR SER ASN GLN VAL ALA VAL LEU          
SEQRES  48 B 1310  TYR GLN ASP VAL ASN CYS THR GLU VAL PRO VAL ALA ILE          
SEQRES  49 B 1310  HIS ALA ASP GLN LEU THR PRO THR TRP ARG VAL TYR SER          
SEQRES  50 B 1310  THR GLY SER ASN VAL PHE GLN THR ARG ALA GLY CYS LEU          
SEQRES  51 B 1310  ILE GLY ALA GLU HIS VAL ASN ASN SER TYR GLU CYS ASP          
SEQRES  52 B 1310  ILE PRO ILE GLY ALA GLY ILE CYS ALA SER TYR GLN THR          
SEQRES  53 B 1310  GLN THR ASN SER PRO ARG ARG ALA ARG SER VAL ALA SER          
SEQRES  54 B 1310  GLN SER ILE ILE ALA TYR THR MET SER LEU GLY ALA GLU          
SEQRES  55 B 1310  ASN SER VAL ALA TYR SER ASN ASN SER ILE ALA ILE PRO          
SEQRES  56 B 1310  THR ASN PHE THR ILE SER VAL THR THR GLU ILE LEU PRO          
SEQRES  57 B 1310  VAL SER MET THR LYS THR SER VAL ASP CYS THR MET TYR          
SEQRES  58 B 1310  ILE CYS GLY ASP SER THR GLU CYS SER ASN LEU LEU LEU          
SEQRES  59 B 1310  GLN TYR GLY SER PHE CYS THR GLN LEU ASN ARG ALA LEU          
SEQRES  60 B 1310  THR GLY ILE ALA VAL GLU GLN ASP LYS ASN THR GLN GLU          
SEQRES  61 B 1310  VAL PHE ALA GLN VAL LYS GLN ILE TYR LYS THR PRO PRO          
SEQRES  62 B 1310  ILE LYS ASP PHE GLY GLY PHE ASN PHE SER GLN ILE LEU          
SEQRES  63 B 1310  PRO ASP PRO SER LYS PRO SER LYS ARG SER PHE ILE GLU          
SEQRES  64 B 1310  ASP LEU LEU PHE ASN LYS VAL THR LEU ALA ASP ALA GLY          
SEQRES  65 B 1310  PHE ILE LYS GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA          
SEQRES  66 B 1310  ALA ARG ASP LEU ILE CYS ALA GLN LYS PHE ASN GLY LEU          
SEQRES  67 B 1310  THR VAL LEU PRO PRO LEU LEU THR ASP GLU MET ILE ALA          
SEQRES  68 B 1310  GLN TYR THR SER ALA LEU LEU ALA GLY THR ILE THR SER          
SEQRES  69 B 1310  GLY TRP THR PHE GLY ALA GLY ALA ALA LEU GLN ILE PRO          
SEQRES  70 B 1310  PHE ALA MET GLN MET ALA TYR ARG PHE ASN GLY ILE GLY          
SEQRES  71 B 1310  VAL THR GLN ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE          
SEQRES  72 B 1310  ALA ASN GLN PHE ASN SER ALA ILE GLY LYS ILE GLN ASP          
SEQRES  73 B 1310  SER LEU SER SER THR ALA SER ALA LEU GLY LYS LEU GLN          
SEQRES  74 B 1310  ASP VAL VAL ASN GLN ASN ALA GLN ALA LEU ASN THR LEU          
SEQRES  75 B 1310  VAL LYS GLN LEU SER SER ASN PHE GLY ALA ILE SER SER          
SEQRES  76 B 1310  VAL LEU ASN ASP ILE LEU SER ARG LEU ASP LYS VAL GLU          
SEQRES  77 B 1310  ALA GLU VAL GLN ILE ASP ARG LEU ILE THR GLY ARG LEU          
SEQRES  78 B 1310  GLN SER LEU GLN THR TYR VAL THR GLN GLN LEU ILE ARG          
SEQRES  79 B 1310  ALA ALA GLU ILE ARG ALA SER ALA ASN LEU ALA ALA THR          
SEQRES  80 B 1310  LYS MET SER GLU CYS VAL LEU GLY GLN SER LYS ARG VAL          
SEQRES  81 B 1310  ASP PHE CYS GLY LYS GLY TYR HIS LEU MET SER PHE PRO          
SEQRES  82 B 1310  GLN SER ALA PRO HIS GLY VAL VAL PHE LEU HIS VAL THR          
SEQRES  83 B 1310  TYR VAL PRO ALA GLN GLU LYS ASN PHE THR THR ALA PRO          
SEQRES  84 B 1310  ALA ILE CYS HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU          
SEQRES  85 B 1310  GLY VAL PHE VAL SER ASN GLY THR HIS TRP PHE VAL THR          
SEQRES  86 B 1310  GLN ARG ASN PHE TYR GLU PRO GLN ILE ILE THR THR ASP          
SEQRES  87 B 1310  ASN THR PHE VAL SER GLY ASN CYS ASP VAL VAL ILE GLY          
SEQRES  88 B 1310  ILE VAL ASN ASN THR VAL TYR ASP PRO LEU GLN PRO GLU          
SEQRES  89 B 1310  LEU ASP SER PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS          
SEQRES  90 B 1310  ASN HIS THR SER PRO ASP VAL ASP LEU GLY ASP ILE SER          
SEQRES  91 B 1310  GLY ILE ASN ALA SER VAL VAL ASN ILE GLN LYS GLU ILE          
SEQRES  92 B 1310  ASP ARG LEU ASN GLU VAL ALA LYS ASN LEU ASN GLU SER          
SEQRES  93 B 1310  LEU ILE ASP LEU GLN GLU LEU GLY LYS TYR GLU GLN TYR          
SEQRES  94 B 1310  ILE LYS TRP PRO TRP TYR ILE TRP LEU GLY PHE ILE ALA          
SEQRES  95 B 1310  GLY LEU ILE ALA ILE VAL MET VAL THR ILE MET LEU CYS          
SEQRES  96 B 1310  CYS MET THR SER CYS CYS SER CYS LEU LYS GLY CYS CYS          
SEQRES  97 B 1310  SER CYS GLY SER CYS CYS LYS PHE ASP GLU ASP ASP SER          
SEQRES  98 B 1310  GLU PRO VAL LEU LYS GLY VAL LYS LEU HIS TYR THR LEU          
SEQRES  99 B 1310  GLU SER GLY GLY GLY SER ALA TRP SER HIS PRO GLN PHE          
SEQRES 100 B 1310  GLU LYS GLY GLY GLY SER GLY GLY GLY SER GLY GLY SER          
SEQRES 101 B 1310  SER ALA TRP SER HIS PRO GLN PHE GLU LYS                      
HET    NAG  D   1      14                                                       
HET    NAG  D   2      14                                                       
HET    NAG  E   1      14                                                       
HET    NAG  E   2      14                                                       
HET    MAN  E   3      11                                                       
HET    MAN  E   4      11                                                       
HET    NAG  F   1      14                                                       
HET    NAG  F   2      14                                                       
HET    MAN  F   3      11                                                       
HET    MAN  F   4      11                                                       
HET    NAG  G   1      14                                                       
HET    NAG  G   2      14                                                       
HET    MAN  G   3      11                                                       
HET    NAG  H   1      14                                                       
HET    NAG  H   2      14                                                       
HET    NAG  I   1      14                                                       
HET    NAG  I   2      14                                                       
HET    NAG  J   1      14                                                       
HET    NAG  J   2      14                                                       
HET    MAN  J   3      11                                                       
HET    MAN  J   4      11                                                       
HET    NAG  K   1      14                                                       
HET    NAG  K   2      14                                                       
HET    MAN  K   3      11                                                       
HET    MAN  K   4      11                                                       
HET    NAG  L   1      14                                                       
HET    NAG  L   2      14                                                       
HET    MAN  L   3      11                                                       
HET    NAG  M   1      14                                                       
HET    NAG  M   2      14                                                       
HET    NAG  N   1      14                                                       
HET    NAG  N   2      14                                                       
HET    NAG  O   1      14                                                       
HET    NAG  O   2      14                                                       
HET    MAN  O   3      11                                                       
HET    MAN  O   4      11                                                       
HET    NAG  P   1      14                                                       
HET    NAG  P   2      14                                                       
HET    MAN  P   3      11                                                       
HET    MAN  P   4      11                                                       
HET    NAG  Q   1      14                                                       
HET    NAG  Q   2      14                                                       
HET    MAN  Q   3      11                                                       
HET    NAG  R   1      14                                                       
HET    NAG  R   2      14                                                       
HET    NAG  C1401      14                                                       
HET    NAG  C1402      14                                                       
HET    MAN  C1409      11                                                       
HET    NAG  C1417      14                                                       
HET    NAG  A1401      14                                                       
HET    NAG  A1402      14                                                       
HET    MAN  A1409      11                                                       
HET    NAG  A1417      14                                                       
HET    NAG  B1401      14                                                       
HET    NAG  B1402      14                                                       
HET    MAN  B1409      11                                                       
HET    NAG  B1417      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     MAN ALPHA-D-MANNOPYRANOSE                                            
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                         
HETSYN     MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE                              
FORMUL   4  NAG    39(C8 H15 N O6)                                              
FORMUL   5  MAN    18(C6 H12 O6)                                                
HELIX    1 AA1 ASP C  737  CYS C  743  1                                   7    
HELIX    2 AA2 SER C  746  LEU C  754  1                                   9    
HELIX    3 AA3 GLN C  755  GLY C  757  5                                   3    
HELIX    4 AA4 SER C  758  GLY C  769  1                                  12    
HELIX    5 AA5 GLN C  913  LEU C 1034  1                                 122    
HELIX    6 AA6 SER C 1147  LYS C 1154  1                                   8    
HELIX    7 AA7 ASP C 1168  ILE C 1172  5                                   5    
HELIX    8 AA8 LYS C 1181  LEU C 1193  1                                  13    
HELIX    9 AA9 ASN C 1194  LEU C 1197  5                                   4    
HELIX   10 AB1 ASP A  737  CYS A  743  1                                   7    
HELIX   11 AB2 SER A  746  LEU A  754  1                                   9    
HELIX   12 AB3 GLN A  755  GLY A  757  5                                   3    
HELIX   13 AB4 SER A  758  GLY A  769  1                                  12    
HELIX   14 AB5 GLN A  913  LEU A 1034  1                                 122    
HELIX   15 AB6 SER A 1147  LYS A 1154  1                                   8    
HELIX   16 AB7 ASP A 1168  ILE A 1172  5                                   5    
HELIX   17 AB8 LYS A 1181  LEU A 1193  1                                  13    
HELIX   18 AB9 ASN A 1194  LEU A 1197  5                                   4    
HELIX   19 AC1 ASP B  737  CYS B  743  1                                   7    
HELIX   20 AC2 SER B  746  LEU B  754  1                                   9    
HELIX   21 AC3 GLN B  755  GLY B  757  5                                   3    
HELIX   22 AC4 SER B  758  GLY B  769  1                                  12    
HELIX   23 AC5 GLN B  913  LEU B 1034  1                                 122    
HELIX   24 AC6 SER B 1147  LYS B 1154  1                                   8    
HELIX   25 AC7 ASP B 1168  ILE B 1172  5                                   5    
HELIX   26 AC8 LYS B 1181  LEU B 1193  1                                  13    
HELIX   27 AC9 ASN B 1194  LEU B 1197  5                                   4    
SHEET    1 AA1 4 TYR C1047  ALA C1056  0                                        
SHEET    2 AA1 4 GLY C1059  ALA C1078 -1  O  VAL C1065   N  MET C1050           
SHEET    3 AA1 4 VAL C1094  SER C1097 -1  O  SER C1097   N  THR C1076           
SHEET    4 AA1 4 TRP C1102  THR C1105 -1  O  THR C1105   N  VAL C1094           
SHEET    1 AA2 4 TYR C1047  ALA C1056  0                                        
SHEET    2 AA2 4 GLY C1059  ALA C1078 -1  O  VAL C1065   N  MET C1050           
SHEET    3 AA2 4 ASN C 710  PRO C 728 -1  N  ILE C 712   O  PHE C1075           
SHEET    4 AA2 4 VAL A1129  ASN A1134  1  O  VAL A1133   N  ILE C 726           
SHEET    1 AA3 3 ILE C1081  HIS C1083  0                                        
SHEET    2 AA3 3 LYS C1086  PRO C1090 -1  O  HIS C1088   N  ILE C1081           
SHEET    3 AA3 3 THR C1120  VAL C1122 -1  O  PHE C1121   N  PHE C1089           
SHEET    1 AA4 4 VAL C1129  ASN C1134  0                                        
SHEET    2 AA4 4 ASN B 710  PRO B 728  1  O  VAL B 722   N  VAL C1129           
SHEET    3 AA4 4 GLY B1059  ALA B1078 -1  O  PHE B1075   N  ILE B 712           
SHEET    4 AA4 4 TYR B1047  ALA B1056 -1  N  MET B1050   O  VAL B1065           
SHEET    1 AA5 5 VAL C1129  ASN C1134  0                                        
SHEET    2 AA5 5 ASN B 710  PRO B 728  1  O  VAL B 722   N  VAL C1129           
SHEET    3 AA5 5 GLY B1059  ALA B1078 -1  O  PHE B1075   N  ILE B 712           
SHEET    4 AA5 5 VAL B1094  SER B1097 -1  O  SER B1097   N  THR B1076           
SHEET    5 AA5 5 TRP B1102  THR B1105 -1  O  THR B1105   N  VAL B1094           
SHEET    1 AA6 4 TYR A1047  ALA A1056  0                                        
SHEET    2 AA6 4 GLY A1059  ALA A1078 -1  O  VAL A1065   N  MET A1050           
SHEET    3 AA6 4 VAL A1094  SER A1097 -1  O  SER A1097   N  THR A1076           
SHEET    4 AA6 4 TRP A1102  THR A1105 -1  O  THR A1105   N  VAL A1094           
SHEET    1 AA7 4 TYR A1047  ALA A1056  0                                        
SHEET    2 AA7 4 GLY A1059  ALA A1078 -1  O  VAL A1065   N  MET A1050           
SHEET    3 AA7 4 ASN A 710  PRO A 728 -1  N  ILE A 712   O  PHE A1075           
SHEET    4 AA7 4 VAL B1129  ASN B1134  1  O  VAL B1133   N  ILE A 726           
SHEET    1 AA8 3 ILE A1081  HIS A1083  0                                        
SHEET    2 AA8 3 LYS A1086  PRO A1090 -1  O  HIS A1088   N  ILE A1081           
SHEET    3 AA8 3 THR A1120  VAL A1122 -1  O  PHE A1121   N  PHE A1089           
SHEET    1 AA9 3 ILE B1081  HIS B1083  0                                        
SHEET    2 AA9 3 LYS B1086  PRO B1090 -1  O  HIS B1088   N  ILE B1081           
SHEET    3 AA9 3 THR B1120  VAL B1122 -1  O  PHE B1121   N  PHE B1089           
SSBOND   1 CYS C  738    CYS C  760                          1555   1555  2.02  
SSBOND   2 CYS C  743    CYS C  749                          1555   1555  2.04  
SSBOND   3 CYS C 1032    CYS C 1043                          1555   1555  2.09  
SSBOND   4 CYS C 1082    CYS C 1126                          1555   1555  2.02  
SSBOND   5 CYS A  738    CYS A  760                          1555   1555  2.02  
SSBOND   6 CYS A  743    CYS A  749                          1555   1555  2.04  
SSBOND   7 CYS A 1032    CYS A 1043                          1555   1555  2.09  
SSBOND   8 CYS A 1082    CYS A 1126                          1555   1555  2.02  
SSBOND   9 CYS B  738    CYS B  760                          1555   1555  2.02  
SSBOND  10 CYS B  743    CYS B  749                          1555   1555  2.04  
SSBOND  11 CYS B 1032    CYS B 1043                          1555   1555  2.09  
SSBOND  12 CYS B 1082    CYS B 1126                          1555   1555  2.02  
LINK         ND2 ASN C 709                 C1  NAG C1401     1555   1555  1.53  
LINK         ND2 ASN C 717                 C1  NAG C1402     1555   1555  1.47  
LINK         ND2 ASN C1074                 C1  NAG D   1     1555   1555  1.58  
LINK         ND2 ASN C1134                 C1  NAG F   1     1555   1555  1.59  
LINK         ND2 ASN C1158                 C1  NAG G   1     1555   1555  1.55  
LINK         ND2 ASN C1194                 C1  NAG H   1     1555   1555  1.55  
LINK         ND2 ASN A 709                 C1  NAG A1401     1555   1555  1.53  
LINK         ND2 ASN A 717                 C1  NAG A1402     1555   1555  1.47  
LINK         ND2 ASN A1074                 C1  NAG I   1     1555   1555  1.58  
LINK         ND2 ASN A1134                 C1  NAG K   1     1555   1555  1.59  
LINK         ND2 ASN A1158                 C1  NAG L   1     1555   1555  1.55  
LINK         ND2 ASN A1194                 C1  NAG M   1     1555   1555  1.54  
LINK         ND2 ASN B 709                 C1  NAG B1401     1555   1555  1.53  
LINK         ND2 ASN B 717                 C1  NAG B1402     1555   1555  1.47  
LINK         ND2 ASN B1074                 C1  NAG N   1     1555   1555  1.58  
LINK         ND2 ASN B1134                 C1  NAG P   1     1555   1555  1.59  
LINK         ND2 ASN B1158                 C1  NAG Q   1     1555   1555  1.55  
LINK         ND2 ASN B1194                 C1  NAG R   1     1555   1555  1.51  
LINK         O4  NAG D   1                 C1  NAG D   2     1555   1555  1.45  
LINK         O4  NAG E   1                 C1  NAG E   2     1555   1555  1.45  
LINK         O4  NAG E   2                 C1  MAN E   3     1555   1555  1.44  
LINK         O3  MAN E   3                 C1  MAN E   4     1555   1555  1.45  
LINK         O4  NAG F   1                 C1  NAG F   2     1555   1555  1.45  
LINK         O4  NAG F   2                 C1  MAN F   3     1555   1555  1.44  
LINK         O3  MAN F   3                 C1  MAN F   4     1555   1555  1.44  
LINK         O4  NAG G   1                 C1  NAG G   2     1555   1555  1.45  
LINK         O4  NAG G   2                 C1  MAN G   3     1555   1555  1.45  
LINK         O4  NAG H   1                 C1  NAG H   2     1555   1555  1.44  
LINK         O4  NAG I   1                 C1  NAG I   2     1555   1555  1.45  
LINK         O4  NAG J   1                 C1  NAG J   2     1555   1555  1.45  
LINK         O4  NAG J   2                 C1  MAN J   3     1555   1555  1.44  
LINK         O3  MAN J   3                 C1  MAN J   4     1555   1555  1.45  
LINK         O4  NAG K   1                 C1  NAG K   2     1555   1555  1.45  
LINK         O4  NAG K   2                 C1  MAN K   3     1555   1555  1.44  
LINK         O3  MAN K   3                 C1  MAN K   4     1555   1555  1.44  
LINK         O4  NAG L   1                 C1  NAG L   2     1555   1555  1.45  
LINK         O4  NAG L   2                 C1  MAN L   3     1555   1555  1.45  
LINK         O4  NAG M   1                 C1  NAG M   2     1555   1555  1.44  
LINK         O4  NAG N   1                 C1  NAG N   2     1555   1555  1.45  
LINK         O4  NAG O   1                 C1  NAG O   2     1555   1555  1.45  
LINK         O4  NAG O   2                 C1  MAN O   3     1555   1555  1.44  
LINK         O3  MAN O   3                 C1  MAN O   4     1555   1555  1.45  
LINK         O4  NAG P   1                 C1  NAG P   2     1555   1555  1.45  
LINK         O4  NAG P   2                 C1  MAN P   3     1555   1555  1.44  
LINK         O3  MAN P   3                 C1  MAN P   4     1555   1555  1.45  
LINK         O4  NAG Q   1                 C1  NAG Q   2     1555   1555  1.45  
LINK         O4  NAG Q   2                 C1  MAN Q   3     1555   1555  1.45  
LINK         O4  NAG R   1                 C1  NAG R   2     1555   1555  1.44  
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   ASN C 703     174.394 217.387 262.012  1.00 82.27           N  
ATOM      2  CA  ASN C 703     174.799 216.194 262.802  1.00 81.85           C  
ATOM      3  C   ASN C 703     174.504 214.890 262.037  1.00 80.68           C  
ATOM      4  O   ASN C 703     173.640 214.108 262.433  1.00 74.86           O  
ATOM      5  CB  ASN C 703     174.145 216.200 264.210  1.00 86.36           C  
ATOM      6  CG  ASN C 703     172.614 216.173 264.212  1.00 88.41           C  
ATOM      7  OD1 ASN C 703     171.963 216.646 263.293  1.00 85.42           O  
ATOM      8  ND2 ASN C 703     171.980 215.643 265.237  1.00 88.87           N  
ATOM      9  N   SER C 704     175.191 214.632 260.919  1.00 80.81           N  
ATOM     10  CA  SER C 704     174.692 213.692 259.894  1.00 81.48           C  
ATOM     11  C   SER C 704     174.741 212.213 260.303  1.00 73.55           C  
ATOM     12  O   SER C 704     173.693 211.593 260.502  1.00 75.66           O  
ATOM     13  CB  SER C 704     175.417 213.927 258.565  1.00 78.48           C  
ATOM     14  OG  SER C 704     176.816 213.768 258.694  1.00 79.15           O  
ATOM     15  N   VAL C 705     175.937 211.630 260.442  1.00 66.59           N  
ATOM     16  CA  VAL C 705     176.107 210.180 260.673  1.00 66.26           C  
ATOM     17  C   VAL C 705     177.013 209.845 261.859  1.00 67.45           C  
ATOM     18  O   VAL C 705     176.827 208.804 262.480  1.00 66.08           O  
ATOM     19  CB  VAL C 705     176.495 209.472 259.353  1.00 68.53           C  
ATOM     20  CG1 VAL C 705     177.916 209.786 258.872  1.00 65.14           C  
ATOM     21  CG2 VAL C 705     176.326 207.957 259.469  1.00 65.68           C  
ATOM     22  N   ALA C 706     177.905 210.757 262.253  1.00 67.41           N  
ATOM     23  CA  ALA C 706     178.872 210.556 263.332  1.00 58.96           C  
ATOM     24  C   ALA C 706     178.271 210.219 264.700  1.00 58.84           C  
ATOM     25  O   ALA C 706     178.984 209.690 265.546  1.00 54.38           O  
ATOM     26  CB  ALA C 706     179.746 211.808 263.446  1.00 56.49           C  
ATOM     27  N   TYR C 707     176.979 210.497 264.900  1.00 60.15           N  
ATOM     28  CA  TYR C 707     176.228 210.271 266.138  1.00 54.42           C  
ATOM     29  C   TYR C 707     174.957 209.414 265.953  1.00 59.61           C  
ATOM     30  O   TYR C 707     174.151 209.279 266.871  1.00 65.85           O  
ATOM     31  CB  TYR C 707     175.882 211.629 266.756  1.00 51.18           C  
ATOM     32  CG  TYR C 707     177.005 212.647 266.777  1.00 53.78           C  
ATOM     33  CD1 TYR C 707     176.954 213.777 265.946  1.00 51.60           C  
ATOM     34  CD2 TYR C 707     178.071 212.494 267.679  1.00 59.96           C  
ATOM     35  CE1 TYR C 707     177.922 214.792 266.074  1.00 63.00           C  
ATOM     36  CE2 TYR C 707     179.048 213.499 267.806  1.00 56.03           C  
ATOM     37  CZ  TYR C 707     178.955 214.664 267.023  1.00 63.86           C  
ATOM     38  OH  TYR C 707     179.820 215.686 267.220  1.00 66.20           O  
ATOM     39  N   SER C 708     174.730 208.850 264.767  1.00 62.06           N  
ATOM     40  CA  SER C 708     173.605 207.934 264.517  1.00 61.51           C  
ATOM     41  C   SER C 708     173.853 206.580 265.170  1.00 56.03           C  
ATOM     42  O   SER C 708     174.989 206.107 265.218  1.00 60.50           O  
ATOM     43  CB  SER C 708     173.378 207.771 263.012  1.00 72.51           C  
ATOM     44  OG  SER C 708     174.470 207.138 262.363  1.00 71.13           O  
ATOM     45  N   ASN C 709     172.837 205.929 265.720  1.00 53.40           N  
ATOM     46  CA  ASN C 709     173.134 204.579 266.206  1.00 59.93           C  
ATOM     47  C   ASN C 709     172.406 203.494 265.515  1.00 59.34           C  
ATOM     48  O   ASN C 709     171.188 203.481 265.334  1.00 58.48           O  
ATOM     49  CB  ASN C 709     173.297 204.406 267.683  1.00 62.40           C  
ATOM     50  CG  ASN C 709     172.065 204.698 268.397  1.00 63.97           C  
ATOM     51  OD1 ASN C 709     170.975 204.442 267.908  1.00 69.35           O  
ATOM     52  ND2 ASN C 709     172.207 205.219 269.559  1.00 65.58           N  
ATOM     53  N   ASN C 710     173.251 202.573 265.136  1.00 53.61           N  
ATOM     54  CA  ASN C 710     172.880 201.444 264.284  1.00 49.49           C  
ATOM     55  C   ASN C 710     173.497 200.152 264.833  1.00 43.37           C  
ATOM     56  O   ASN C 710     174.515 200.169 265.525  1.00 46.39           O  
ATOM     57  CB  ASN C 710     173.231 201.721 262.815  1.00 62.71           C  
ATOM     58  CG  ASN C 710     174.695 202.028 262.545  1.00 60.13           C  
ATOM     59  OD1 ASN C 710     175.519 202.266 263.407  1.00 45.15           O  
ATOM     60  ND2 ASN C 710     175.063 202.031 261.294  1.00 62.61           N  
ATOM     61  N   SER C 711     172.841 199.022 264.568  1.00 46.67           N  
ATOM     62  CA  SER C 711     173.248 197.685 265.012  1.00 53.79           C  
ATOM     63  C   SER C 711     174.501 197.216 264.264  1.00 50.99           C  
ATOM     64  O   SER C 711     174.465 197.027 263.047  1.00 52.70           O  
ATOM     65  CB  SER C 711     172.108 196.684 264.782  1.00 56.71           C  
ATOM     66  OG  SER C 711     170.873 197.137 265.303  1.00 61.25           O  
ATOM     67  N   ILE C 712     175.605 196.994 264.976  1.00 50.20           N  
ATOM     68  CA  ILE C 712     176.887 196.548 264.425  1.00 41.05           C  
ATOM     69  C   ILE C 712     177.265 195.198 265.003  1.00 44.15           C  
ATOM     70  O   ILE C 712     177.272 195.031 266.218  1.00 51.04           O  
ATOM     71  CB  ILE C 712     177.961 197.613 264.693  1.00 40.26           C  
ATOM     72  CG1 ILE C 712     177.718 198.750 263.685  1.00 45.89           C  
ATOM     73  CG2 ILE C 712     179.392 197.055 264.578  1.00 45.78           C  
ATOM     74  CD1 ILE C 712     178.782 199.836 263.705  1.00 53.18           C  
ATOM     75  N   ALA C 713     177.616 194.236 264.151  1.00 45.77           N  
ATOM     76  CA  ALA C 713     178.132 192.954 264.603  1.00 45.99           C  
ATOM     77  C   ALA C 713     179.527 193.127 265.206  1.00 50.03           C  
ATOM     78  O   ALA C 713     180.428 193.713 264.599  1.00 43.43           O  
ATOM     79  CB  ALA C 713     178.115 191.942 263.457  1.00 48.09           C  
ATOM     80  N   ILE C 714     179.683 192.631 266.429  1.00 60.35           N  
ATOM     81  CA  ILE C 714     180.925 192.636 267.197  1.00 55.33           C  
ATOM     82  C   ILE C 714     181.190 191.181 267.595  1.00 55.28           C  
ATOM     83  O   ILE C 714     180.274 190.543 268.115  1.00 57.16           O  
ATOM     84  CB  ILE C 714     180.831 193.587 268.407  1.00 42.76           C  
ATOM     85  CG1 ILE C 714     180.516 195.028 267.931  1.00 41.05           C  
ATOM     86  CG2 ILE C 714     182.134 193.518 269.216  1.00 47.00           C  
ATOM     87  CD1 ILE C 714     180.518 196.103 269.014  1.00 37.07           C  
ATOM     88  N   PRO C 715     182.386 190.620 267.341  1.00 53.90           N  
ATOM     89  CA  PRO C 715     182.668 189.215 267.601  1.00 55.87           C  
ATOM     90  C   PRO C 715     182.378 188.794 269.038  1.00 57.66           C  
ATOM     91  O   PRO C 715     182.973 189.304 269.988  1.00 57.52           O  
ATOM     92  CB  PRO C 715     184.128 189.009 267.236  1.00 48.13           C  
ATOM     93  CG  PRO C 715     184.333 190.041 266.131  1.00 55.61           C  
ATOM     94  CD  PRO C 715     183.487 191.212 266.610  1.00 54.07           C  
ATOM     95  N   THR C 716     181.448 187.858 269.202  1.00 63.71           N  
ATOM     96  CA  THR C 716     181.069 187.324 270.506  1.00 61.66           C  
ATOM     97  C   THR C 716     182.063 186.242 270.872  1.00 53.68           C  
ATOM     98  O   THR C 716     182.534 186.200 272.003  1.00 50.00           O  
ATOM     99  CB  THR C 716     179.654 186.734 270.534  1.00 64.82           C  
ATOM    100  OG1 THR C 716     178.707 187.717 270.206  1.00 75.19           O  
ATOM    101  CG2 THR C 716     179.253 186.218 271.909  1.00 54.44           C  
ATOM    102  N   ASN C 717     182.417 185.405 269.896  1.00 61.46           N  
ATOM    103  CA  ASN C 717     183.310 184.273 270.149  1.00 66.84           C  
ATOM    104  C   ASN C 717     184.111 183.788 268.952  1.00 60.09           C  
ATOM    105  O   ASN C 717     183.822 184.142 267.810  1.00 65.97           O  
ATOM    106  CB  ASN C 717     182.540 183.100 270.733  1.00 65.86           C  
ATOM    107  CG  ASN C 717     182.707 182.998 272.222  1.00 68.81           C  
ATOM    108  OD1 ASN C 717     183.694 183.505 272.772  1.00 68.95           O  
ATOM    109  ND2 ASN C 717     181.727 182.348 272.878  1.00 72.12           N  
ATOM    110  N   PHE C 718     185.147 182.993 269.193  1.00 53.36           N  
ATOM    111  CA  PHE C 718     185.997 182.565 268.083  1.00 55.29           C  
ATOM    112  C   PHE C 718     186.114 181.075 267.816  1.00 58.77           C  
ATOM    113  O   PHE C 718     186.183 180.267 268.736  1.00 70.72           O  
ATOM    114  CB  PHE C 718     187.375 183.184 268.260  1.00 52.92           C  
ATOM    115  CG  PHE C 718     187.340 184.680 268.434  1.00 47.79           C  
ATOM    116  CD1 PHE C 718     186.976 185.516 267.372  1.00 46.20           C  
ATOM    117  CD2 PHE C 718     187.646 185.229 269.684  1.00 50.14           C  
ATOM    118  CE1 PHE C 718     186.937 186.901 267.554  1.00 38.09           C  
ATOM    119  CE2 PHE C 718     187.603 186.613 269.869  1.00 51.92           C  
ATOM    120  CZ  PHE C 718     187.245 187.447 268.806  1.00 45.33           C  
ATOM    121  N   THR C 719     186.233 180.741 266.536  1.00 57.34           N  
ATOM    122  CA  THR C 719     186.672 179.447 266.020  1.00 56.91           C  
ATOM    123  C   THR C 719     188.045 179.630 265.392  1.00 56.41           C  
ATOM    124  O   THR C 719     188.297 180.611 264.695  1.00 54.42           O  
ATOM    125  CB  THR C 719     185.655 178.881 265.023  1.00 57.29           C  
ATOM    126  OG1 THR C 719     184.600 178.289 265.738  1.00 74.01           O  
ATOM    127  CG2 THR C 719     186.175 177.783 264.104  1.00 58.18           C  
ATOM    128  N   ILE C 720     188.950 178.700 265.659  1.00 64.71           N  
ATOM    129  CA  ILE C 720     190.246 178.636 264.990  1.00 51.67           C  
ATOM    130  C   ILE C 720     190.100 178.077 263.570  1.00 54.73           C  
ATOM    131  O   ILE C 720     189.279 177.208 263.294  1.00 57.03           O  
ATOM    132  CB  ILE C 720     191.252 177.901 265.888  1.00 54.47           C  
ATOM    133  CG1 ILE C 720     192.672 177.833 265.307  1.00 44.48           C  
ATOM    134  CG2 ILE C 720     190.807 176.489 266.250  1.00 59.72           C  
ATOM    135  CD1 ILE C 720     193.357 179.197 265.380  1.00 40.54           C  
ATOM    136  N   SER C 721     190.861 178.630 262.637  1.00 60.43           N  
ATOM    137  CA  SER C 721     190.716 178.397 261.205  1.00 53.89           C  
ATOM    138  C   SER C 721     192.052 178.515 260.478  1.00 54.21           C  
ATOM    139  O   SER C 721     193.000 179.095 261.001  1.00 58.33           O  
ATOM    140  CB  SER C 721     189.702 179.378 260.635  1.00 52.28           C  
ATOM    141  OG  SER C 721     190.155 180.697 260.738  1.00 51.32           O  
ATOM    142  N   VAL C 722     192.150 177.963 259.273  1.00 54.15           N  
ATOM    143  CA  VAL C 722     193.315 178.134 258.407  1.00 54.56           C  
ATOM    144  C   VAL C 722     192.882 178.478 256.998  1.00 57.39           C  
ATOM    145  O   VAL C 722     191.859 178.000 256.521  1.00 63.63           O  
ATOM    146  CB  VAL C 722     194.271 176.935 258.431  1.00 50.30           C  
ATOM    147  CG1 VAL C 722     194.718 176.621 259.854  1.00 54.62           C  
ATOM    148  CG2 VAL C 722     193.675 175.675 257.818  1.00 52.97           C  
ATOM    149  N   THR C 723     193.651 179.308 256.315  1.00 51.07           N  
ATOM    150  CA  THR C 723     193.410 179.679 254.919  1.00 50.72           C  
ATOM    151  C   THR C 723     194.541 179.141 254.059  1.00 55.64           C  
ATOM    152  O   THR C 723     195.692 179.169 254.479  1.00 60.05           O  
ATOM    153  CB  THR C 723     193.263 181.193 254.766  1.00 51.57           C  
ATOM    154  OG1 THR C 723     192.189 181.622 255.572  1.00 58.45           O  
ATOM    155  CG2 THR C 723     192.956 181.621 253.335  1.00 55.07           C  
ATOM    156  N   THR C 724     194.229 178.655 252.866  1.00 57.28           N  
ATOM    157  CA  THR C 724     195.206 178.488 251.789  1.00 55.52           C  
ATOM    158  C   THR C 724     194.947 179.626 250.814  1.00 55.14           C  
ATOM    159  O   THR C 724     193.865 179.687 250.244  1.00 57.71           O  
ATOM    160  CB  THR C 724     195.035 177.127 251.106  1.00 64.09           C  
ATOM    161  OG1 THR C 724     195.161 176.087 252.049  1.00 73.02           O  
ATOM    162  CG2 THR C 724     196.087 176.858 250.037  1.00 62.30           C  
ATOM    163  N   GLU C 725     195.879 180.557 250.650  1.00 50.42           N  
ATOM    164  CA  GLU C 725     195.734 181.698 249.741  1.00 48.47           C  
ATOM    165  C   GLU C 725     196.765 181.596 248.623  1.00 51.89           C  
ATOM    166  O   GLU C 725     197.955 181.604 248.910  1.00 50.94           O  
ATOM    167  CB  GLU C 725     195.862 183.022 250.514  1.00 47.20           C  
ATOM    168  CG  GLU C 725     196.092 184.236 249.597  1.00 41.08           C  
ATOM    169  CD  GLU C 725     195.643 185.611 250.121  1.00 46.48           C  
ATOM    170  OE1 GLU C 725     195.651 185.910 251.333  1.00 43.37           O  
ATOM    171  OE2 GLU C 725     195.353 186.494 249.286  1.00 53.54           O1-
ATOM    172  N   ILE C 726     196.336 181.533 247.360  1.00 56.15           N  
ATOM    173  CA  ILE C 726     197.224 181.391 246.194  1.00 48.68           C  
ATOM    174  C   ILE C 726     197.392 182.742 245.482  1.00 49.07           C  
ATOM    175  O   ILE C 726     196.405 183.352 245.079  1.00 53.03           O  
ATOM    176  CB  ILE C 726     196.664 180.321 245.230  1.00 53.80           C  
ATOM    177  CG1 ILE C 726     196.442 178.947 245.903  1.00 53.75           C  
ATOM    178  CG2 ILE C 726     197.589 180.128 244.019  1.00 57.49           C  
ATOM    179  CD1 ILE C 726     195.099 178.328 245.543  1.00 55.48           C  
ATOM    180  N   LEU C 727     198.632 183.205 245.310  1.00 44.62           N  
ATOM    181  CA  LEU C 727     199.007 184.385 244.520  1.00 43.83           C  
ATOM    182  C   LEU C 727     199.995 184.002 243.407  1.00 48.92           C  
ATOM    183  O   LEU C 727     201.087 183.528 243.717  1.00 54.18           O  
ATOM    184  CB  LEU C 727     199.705 185.439 245.393  1.00 37.49           C  
ATOM    185  CG  LEU C 727     198.803 186.423 246.128  1.00 34.82           C  
ATOM    186  CD1 LEU C 727     198.079 185.774 247.285  1.00 40.58           C  
ATOM    187  CD2 LEU C 727     199.664 187.527 246.727  1.00 21.93           C  
ATOM    188  N   PRO C 728     199.716 184.284 242.126  1.00 46.45           N  
ATOM    189  CA  PRO C 728     200.734 184.220 241.094  1.00 41.65           C  
ATOM    190  C   PRO C 728     201.723 185.378 241.240  1.00 40.28           C  
ATOM    191  O   PRO C 728     201.327 186.528 241.413  1.00 39.34           O  
ATOM    192  CB  PRO C 728     199.971 184.259 239.782  1.00 43.82           C  
ATOM    193  CG  PRO C 728     198.700 185.021 240.123  1.00 41.00           C  
ATOM    194  CD  PRO C 728     198.432 184.665 241.571  1.00 42.26           C  
ATOM    195  N   VAL C 729     203.016 185.073 241.169  1.00 42.28           N  
ATOM    196  CA  VAL C 729     204.127 186.032 241.313  1.00 39.67           C  
ATOM    197  C   VAL C 729     204.937 186.190 240.027  1.00 50.00           C  
ATOM    198  O   VAL C 729     205.684 187.153 239.877  1.00 52.34           O  
ATOM    199  CB  VAL C 729     205.050 185.681 242.491  1.00 47.98           C  
ATOM    200  CG1 VAL C 729     204.256 185.535 243.789  1.00 56.97           C  
ATOM    201  CG2 VAL C 729     205.881 184.413 242.280  1.00 48.89           C  
ATOM    202  N   SER C 730     204.802 185.276 239.076  1.00 57.97           N  
ATOM    203  CA  SER C 730     205.494 185.303 237.787  1.00 56.31           C  
ATOM    204  C   SER C 730     204.588 184.791 236.674  1.00 53.98           C  
ATOM    205  O   SER C 730     203.527 184.214 236.911  1.00 51.15           O  
ATOM    206  CB  SER C 730     206.816 184.528 237.869  1.00 57.14           C  
ATOM    207  OG  SER C 730     206.656 183.216 238.356  1.00 58.55           O  
ATOM    208  N   MET C 731     204.980 185.079 235.438  1.00 50.24           N  
ATOM    209  CA  MET C 731     204.276 184.674 234.227  1.00 50.08           C  
ATOM    210  C   MET C 731     205.276 184.060 233.249  1.00 52.66           C  
ATOM    211  O   MET C 731     206.284 184.689 232.924  1.00 62.00           O  
ATOM    212  CB  MET C 731     203.579 185.918 233.662  1.00 44.46           C  
ATOM    213  CG  MET C 731     202.805 185.695 232.372  1.00 48.71           C  
ATOM    214  SD  MET C 731     201.673 187.046 232.036  1.00 31.12           S  
ATOM    215  CE  MET C 731     200.871 186.477 230.534  1.00 30.20           C  
ATOM    216  N   THR C 732     205.008 182.848 232.768  1.00 47.26           N  
ATOM    217  CA  THR C 732     205.838 182.217 231.731  1.00 46.65           C  
ATOM    218  C   THR C 732     205.770 183.010 230.423  1.00 53.65           C  
ATOM    219  O   THR C 732     204.728 183.575 230.079  1.00 51.87           O  
ATOM    220  CB  THR C 732     205.490 180.737 231.528  1.00 44.76           C  
ATOM    221  OG1 THR C 732     206.444 180.137 230.681  1.00 52.36           O  
ATOM    222  CG2 THR C 732     204.120 180.502 230.900  1.00 40.45           C  
ATOM    223  N   LYS C 733     206.896 183.104 229.708  1.00 51.43           N  
ATOM    224  CA  LYS C 733     207.061 183.994 228.555  1.00 49.07           C  
ATOM    225  C   LYS C 733     206.450 183.384 227.299  1.00 54.80           C  
ATOM    226  O   LYS C 733     207.087 182.634 226.561  1.00 55.02           O  
ATOM    227  CB  LYS C 733     208.539 184.360 228.374  1.00 54.58           C  
ATOM    228  CG  LYS C 733     209.197 184.963 229.625  1.00 58.09           C  
ATOM    229  CD  LYS C 733     208.512 186.214 230.191  1.00 53.74           C  
ATOM    230  CE  LYS C 733     209.195 186.706 231.476  1.00 51.43           C  
ATOM    231  NZ  LYS C 733     210.606 187.101 231.264  1.00 51.80           N  
ATOM    232  N   THR C 734     205.185 183.699 227.069  1.00 57.49           N  
ATOM    233  CA  THR C 734     204.362 183.260 225.941  1.00 52.06           C  
ATOM    234  C   THR C 734     204.757 183.936 224.624  1.00 48.20           C  
ATOM    235  O   THR C 734     203.922 184.583 223.989  1.00 50.15           O  
ATOM    236  CB  THR C 734     202.881 183.504 226.271  1.00 53.98           C  
ATOM    237  OG1 THR C 734     202.692 184.846 226.666  1.00 46.29           O  
ATOM    238  CG2 THR C 734     202.380 182.615 227.405  1.00 55.05           C  
ATOM    239  N   SER C 735     206.020 183.815 224.204  1.00 48.22           N  
ATOM    240  CA  SER C 735     206.499 184.286 222.898  1.00 44.96           C  
ATOM    241  C   SER C 735     205.672 183.694 221.752  1.00 43.09           C  
ATOM    242  O   SER C 735     205.153 182.580 221.844  1.00 44.07           O  
ATOM    243  CB  SER C 735     207.993 183.978 222.737  1.00 45.88           C  
ATOM    244  OG  SER C 735     208.287 182.599 222.882  1.00 52.86           O  
ATOM    245  N   VAL C 736     205.489 184.454 220.677  1.00 44.46           N  
ATOM    246  CA  VAL C 736     204.586 184.115 219.569  1.00 46.61           C  
ATOM    247  C   VAL C 736     205.332 184.137 218.241  1.00 52.97           C  
ATOM    248  O   VAL C 736     205.992 185.119 217.913  1.00 50.16           O  
ATOM    249  CB  VAL C 736     203.329 185.009 219.607  1.00 38.66           C  
ATOM    250  CG1 VAL C 736     203.603 186.509 219.496  1.00 33.87           C  
ATOM    251  CG2 VAL C 736     202.321 184.640 218.530  1.00 34.73           C  
ATOM    252  N   ASP C 737     205.155 183.079 217.460  1.00 56.84           N  
ATOM    253  CA  ASP C 737     205.721 183.023 216.129  1.00 48.73           C  
ATOM    254  C   ASP C 737     204.695 183.804 215.325  1.00 51.16           C  
ATOM    255  O   ASP C 737     203.540 183.394 215.231  1.00 50.58           O  
ATOM    256  CB  ASP C 737     205.802 181.583 215.636  1.00 46.52           C  
ATOM    257  CG  ASP C 737     206.350 181.482 214.233  1.00 58.27           C  
ATOM    258  OD1 ASP C 737     206.551 182.537 213.598  1.00 62.03           O  
ATOM    259  OD2 ASP C 737     206.579 180.350 213.762  1.00 63.80           O1-
ATOM    260  N   CYS C 738     205.103 184.831 214.632  1.00 53.86           N  
ATOM    261  CA  CYS C 738     204.090 185.677 214.025  1.00 46.34           C  
ATOM    262  C   CYS C 738     203.543 185.190 212.707  1.00 47.22           C  
ATOM    263  O   CYS C 738     202.437 185.549 212.304  1.00 38.47           O  
ATOM    264  CB  CYS C 738     204.549 187.114 214.104  1.00 44.00           C  
ATOM    265  SG  CYS C 738     205.483 187.186 215.654  1.00 56.11           S  
ATOM    266  N   THR C 739     204.326 184.364 212.036  1.00 52.09           N  
ATOM    267  CA  THR C 739     203.804 183.701 210.849  1.00 51.06           C  
ATOM    268  C   THR C 739     202.652 182.758 211.182  1.00 49.51           C  
ATOM    269  O   THR C 739     201.544 182.916 210.673  1.00 56.43           O  
ATOM    270  CB  THR C 739     204.899 182.916 210.105  1.00 53.56           C  
ATOM    271  OG1 THR C 739     205.512 181.980 210.999  1.00 61.45           O  
ATOM    272  CG2 THR C 739     205.956 183.863 209.564  1.00 44.21           C  
ATOM    273  N   MET C 740     202.918 181.779 212.039  1.00 43.37           N  
ATOM    274  CA  MET C 740     201.897 180.801 212.427  1.00 42.73           C  
ATOM    275  C   MET C 740     200.655 181.446 213.054  1.00 41.55           C  
ATOM    276  O   MET C 740     199.552 180.959 212.812  1.00 43.72           O  
ATOM    277  CB  MET C 740     202.472 179.739 213.370  1.00 40.81           C  
ATOM    278  CG  MET C 740     203.412 178.799 212.614  1.00 52.95           C  
ATOM    279  SD  MET C 740     203.930 177.341 213.555  1.00 70.84           S  
ATOM    280  CE  MET C 740     205.022 176.566 212.331  1.00 53.29           C  
ATOM    281  N   TYR C 741     200.787 182.543 213.809  1.00 43.56           N  
ATOM    282  CA  TYR C 741     199.616 183.245 214.350  1.00 38.84           C  
ATOM    283  C   TYR C 741     198.744 183.852 213.247  1.00 43.76           C  
ATOM    284  O   TYR C 741     197.566 183.529 213.147  1.00 43.85           O  
ATOM    285  CB  TYR C 741     200.035 184.325 215.358  1.00 36.35           C  
ATOM    286  CG  TYR C 741     198.873 184.793 216.213  1.00 31.81           C  
ATOM    287  CD1 TYR C 741     197.928 185.706 215.708  1.00 31.77           C  
ATOM    288  CD2 TYR C 741     198.707 184.263 217.503  1.00 29.81           C  
ATOM    289  CE1 TYR C 741     196.799 186.062 216.467  1.00 26.67           C  
ATOM    290  CE2 TYR C 741     197.587 184.622 218.271  1.00 26.71           C  
ATOM    291  CZ  TYR C 741     196.621 185.504 217.746  1.00 28.42           C  
ATOM    292  OH  TYR C 741     195.512 185.780 218.479  1.00 35.06           O  
ATOM    293  N   ILE C 742     199.310 184.728 212.416  1.00 47.63           N  
ATOM    294  CA  ILE C 742     198.572 185.483 211.397  1.00 42.04           C  
ATOM    295  C   ILE C 742     198.211 184.609 210.205  1.00 43.35           C  
ATOM    296  O   ILE C 742     197.042 184.517 209.863  1.00 40.67           O  
ATOM    297  CB  ILE C 742     199.379 186.717 210.956  1.00 30.92           C  
ATOM    298  CG1 ILE C 742     199.393 187.763 212.081  1.00 31.25           C  
ATOM    299  CG2 ILE C 742     198.827 187.343 209.670  1.00 35.01           C  
ATOM    300  CD1 ILE C 742     200.667 188.592 212.043  1.00 33.93           C  
ATOM    301  N   CYS C 743     199.212 184.104 209.486  1.00 48.47           N  
ATOM    302  CA  CYS C 743     198.972 183.349 208.247  1.00 35.79           C  
ATOM    303  C   CYS C 743     198.815 181.831 208.383  1.00 40.64           C  
ATOM    304  O   CYS C 743     198.010 181.226 207.675  1.00 46.89           O  
ATOM    305  CB  CYS C 743     200.046 183.715 207.199  1.00 41.59           C  
ATOM    306  SG  CYS C 743     199.835 183.109 205.497  1.00 94.54           S  
ATOM    307  N   GLY C 744     199.574 181.216 209.283  1.00 48.16           N  
ATOM    308  CA  GLY C 744     199.487 179.779 209.477  1.00 49.17           C  
ATOM    309  C   GLY C 744     200.222 178.996 208.405  1.00 54.24           C  
ATOM    310  O   GLY C 744     201.413 179.214 208.183  1.00 52.09           O  
ATOM    311  N   ASP C 745     199.520 178.084 207.737  1.00 62.72           N  
ATOM    312  CA  ASP C 745     200.149 177.273 206.681  1.00 62.84           C  
ATOM    313  C   ASP C 745     200.217 177.985 205.318  1.00 59.49           C  
ATOM    314  O   ASP C 745     200.966 177.568 204.436  1.00 60.42           O  
ATOM    315  CB  ASP C 745     199.356 175.959 206.521  1.00 60.61           C  
ATOM    316  CG  ASP C 745     197.875 176.124 206.136  1.00 63.90           C  
ATOM    317  OD1 ASP C 745     197.303 175.205 205.512  1.00 64.90           O  
ATOM    318  OD2 ASP C 745     197.243 177.150 206.466  1.00 65.30           O1-
ATOM    319  N   SER C 746     199.400 179.014 205.104  1.00 52.84           N  
ATOM    320  CA  SER C 746     199.109 179.537 203.771  1.00 52.66           C  
ATOM    321  C   SER C 746     200.264 180.360 203.199  1.00 53.17           C  
ATOM    322  O   SER C 746     200.630 181.427 203.704  1.00 51.24           O  
ATOM    323  CB  SER C 746     197.783 180.282 203.812  1.00 47.53           C  
ATOM    324  OG  SER C 746     197.209 180.331 202.526  1.00 56.29           O  
ATOM    325  N   THR C 747     200.897 179.811 202.165  1.00 59.80           N  
ATOM    326  CA  THR C 747     202.236 180.220 201.730  1.00 55.89           C  
ATOM    327  C   THR C 747     202.258 181.583 201.049  1.00 55.50           C  
ATOM    328  O   THR C 747     203.181 182.353 201.284  1.00 56.27           O  
ATOM    329  CB  THR C 747     202.862 179.124 200.870  1.00 46.78           C  
ATOM    330  OG1 THR C 747     203.110 178.009 201.700  1.00 47.44           O  
ATOM    331  CG2 THR C 747     204.196 179.511 200.260  1.00 50.50           C  
ATOM    332  N   GLU C 748     201.227 181.965 200.302  1.00 54.61           N  
ATOM    333  CA  GLU C 748     201.195 183.274 199.640  1.00 54.23           C  
ATOM    334  C   GLU C 748     201.220 184.435 200.648  1.00 59.73           C  
ATOM    335  O   GLU C 748     201.974 185.390 200.475  1.00 60.41           O  
ATOM    336  CB  GLU C 748     200.024 183.378 198.644  1.00 58.62           C  
ATOM    337  CG  GLU C 748     198.601 183.480 199.221  1.00 57.67           C  
ATOM    338  CD  GLU C 748     198.112 182.230 199.960  1.00 66.41           C  
ATOM    339  OE1 GLU C 748     198.635 181.116 199.749  1.00 65.11           O  
ATOM    340  OE2 GLU C 748     197.174 182.358 200.773  1.00 75.03           O1-
ATOM    341  N   CYS C 749     200.460 184.330 201.747  1.00 54.99           N  
ATOM    342  CA  CYS C 749     200.518 185.395 202.766  1.00 47.40           C  
ATOM    343  C   CYS C 749     201.786 185.310 203.619  1.00 46.88           C  
ATOM    344  O   CYS C 749     202.275 186.323 204.120  1.00 47.53           O  
ATOM    345  CB  CYS C 749     199.234 185.586 203.627  1.00 48.24           C  
ATOM    346  SG  CYS C 749     198.417 184.308 204.651  1.00 68.13           S  
ATOM    347  N   SER C 750     202.311 184.099 203.777  1.00 46.00           N  
ATOM    348  CA  SER C 750     203.533 183.900 204.544  1.00 45.34           C  
ATOM    349  C   SER C 750     204.634 184.712 203.878  1.00 45.97           C  
ATOM    350  O   SER C 750     205.271 185.556 204.509  1.00 46.19           O  
ATOM    351  CB  SER C 750     203.913 182.420 204.582  1.00 50.37           C  
ATOM    352  OG  SER C 750     202.894 181.649 205.195  1.00 50.01           O  
ATOM    353  N   ASN C 751     204.849 184.448 202.593  1.00 51.46           N  
ATOM    354  CA  ASN C 751     205.845 185.173 201.810  1.00 52.42           C  
ATOM    355  C   ASN C 751     205.623 186.688 201.844  1.00 55.36           C  
ATOM    356  O   ASN C 751     206.593 187.441 201.839  1.00 55.53           O  
ATOM    357  CB  ASN C 751     205.828 184.642 200.372  1.00 53.48           C  
ATOM    358  CG  ASN C 751     206.228 183.185 200.227  1.00 71.36           C  
ATOM    359  OD1 ASN C 751     205.828 182.514 199.302  1.00 72.50           O  
ATOM    360  ND2 ASN C 751     207.037 182.646 201.094  1.00 72.26           N  
ATOM    361  N   LEU C 752     204.378 187.159 201.935  1.00 54.36           N  
ATOM    362  CA  LEU C 752     204.098 188.582 202.152  1.00 48.14           C  
ATOM    363  C   LEU C 752     204.573 189.088 203.517  1.00 42.87           C  
ATOM    364  O   LEU C 752     205.066 190.208 203.593  1.00 42.87           O  
ATOM    365  CB  LEU C 752     202.599 188.854 201.984  1.00 41.88           C  
ATOM    366  CG  LEU C 752     202.155 188.844 200.520  1.00 32.47           C  
ATOM    367  CD1 LEU C 752     200.639 188.829 200.462  1.00 31.88           C  
ATOM    368  CD2 LEU C 752     202.612 190.100 199.800  1.00 31.84           C  
ATOM    369  N   LEU C 753     204.478 188.280 204.575  1.00 35.78           N  
ATOM    370  CA  LEU C 753     204.901 188.655 205.927  1.00 40.54           C  
ATOM    371  C   LEU C 753     206.355 189.176 205.965  1.00 44.39           C  
ATOM    372  O   LEU C 753     206.607 190.141 206.677  1.00 43.75           O  
ATOM    373  CB  LEU C 753     204.691 187.470 206.904  1.00 41.70           C  
ATOM    374  CG  LEU C 753     203.484 187.538 207.861  1.00 37.61           C  
ATOM    375  CD1 LEU C 753     203.587 188.728 208.798  1.00 38.01           C  
ATOM    376  CD2 LEU C 753     202.122 187.584 207.174  1.00 37.04           C  
ATOM    377  N   LEU C 754     207.291 188.630 205.177  1.00 41.73           N  
ATOM    378  CA  LEU C 754     208.692 189.098 205.155  1.00 38.47           C  
ATOM    379  C   LEU C 754     208.820 190.592 204.821  1.00 38.66           C  
ATOM    380  O   LEU C 754     209.666 191.284 205.377  1.00 43.21           O  
ATOM    381  CB  LEU C 754     209.499 188.239 204.166  1.00 38.36           C  
ATOM    382  CG  LEU C 754     210.115 186.971 204.772  1.00 36.50           C  
ATOM    383  CD1 LEU C 754     209.168 186.153 205.636  1.00 40.65           C  
ATOM    384  CD2 LEU C 754     210.616 186.059 203.659  1.00 42.43           C  
ATOM    385  N   GLN C 755     207.957 191.129 203.966  1.00 33.46           N  
ATOM    386  CA  GLN C 755     207.975 192.545 203.627  1.00 42.29           C  
ATOM    387  C   GLN C 755     207.323 193.445 204.684  1.00 43.20           C  
ATOM    388  O   GLN C 755     207.559 194.645 204.650  1.00 50.19           O  
ATOM    389  CB  GLN C 755     207.355 192.736 202.242  1.00 48.88           C  
ATOM    390  CG  GLN C 755     208.321 192.343 201.103  1.00 55.18           C  
ATOM    391  CD  GLN C 755     208.693 193.501 200.173  1.00 58.11           C  
ATOM    392  OE1 GLN C 755     208.960 194.623 200.575  1.00 54.57           O  
ATOM    393  NE2 GLN C 755     208.729 193.258 198.880  1.00 54.46           N  
ATOM    394  N   TYR C 756     206.597 192.908 205.674  1.00 39.86           N  
ATOM    395  CA  TYR C 756     206.171 193.660 206.871  1.00 29.05           C  
ATOM    396  C   TYR C 756     207.325 193.890 207.860  1.00 31.83           C  
ATOM    397  O   TYR C 756     207.147 194.523 208.896  1.00 36.43           O  
ATOM    398  CB  TYR C 756     204.977 192.987 207.565  1.00 23.23           C  
ATOM    399  CG  TYR C 756     203.674 193.038 206.793  1.00 27.69           C  
ATOM    400  CD1 TYR C 756     202.677 193.958 207.146  1.00 22.34           C  
ATOM    401  CD2 TYR C 756     203.445 192.155 205.728  1.00 37.44           C  
ATOM    402  CE1 TYR C 756     201.473 194.003 206.419  1.00 18.26           C  
ATOM    403  CE2 TYR C 756     202.239 192.184 205.010  1.00 29.37           C  
ATOM    404  CZ  TYR C 756     201.256 193.121 205.349  1.00 21.36           C  
ATOM    405  OH  TYR C 756     200.134 193.197 204.607  1.00 33.44           O  
ATOM    406  N   GLY C 757     208.527 193.407 207.544  1.00 36.69           N  
ATOM    407  CA  GLY C 757     209.718 193.631 208.347  1.00 33.27           C  
ATOM    408  C   GLY C 757     209.781 192.743 209.578  1.00 43.23           C  
ATOM    409  O   GLY C 757     209.036 191.776 209.716  1.00 42.51           O  
ATOM    410  N   SER C 758     210.690 193.066 210.493  1.00 52.06           N  
ATOM    411  CA  SER C 758     210.865 192.268 211.708  1.00 40.72           C  
ATOM    412  C   SER C 758     209.916 192.650 212.840  1.00 41.95           C  
ATOM    413  O   SER C 758     210.253 192.518 214.022  1.00 47.25           O  
ATOM    414  CB  SER C 758     212.315 192.334 212.191  1.00 45.31           C  
ATOM    415  OG  SER C 758     213.175 191.631 211.312  1.00 59.48           O  
ATOM    416  N   PHE C 759     208.683 192.991 212.483  1.00 40.68           N  
ATOM    417  CA  PHE C 759     207.690 193.422 213.465  1.00 31.73           C  
ATOM    418  C   PHE C 759     207.393 192.358 214.527  1.00 36.51           C  
ATOM    419  O   PHE C 759     207.120 192.695 215.671  1.00 45.00           O  
ATOM    420  CB  PHE C 759     206.419 193.987 212.800  1.00 26.14           C  
ATOM    421  CG  PHE C 759     205.384 192.955 212.467  1.00 26.17           C  
ATOM    422  CD1 PHE C 759     204.353 192.691 213.346  1.00 22.08           C  
ATOM    423  CD2 PHE C 759     205.451 192.243 211.285  1.00 35.01           C  
ATOM    424  CE1 PHE C 759     203.399 191.739 213.049  1.00 30.42           C  
ATOM    425  CE2 PHE C 759     204.501 191.289 210.981  1.00 36.45           C  
ATOM    426  CZ  PHE C 759     203.472 191.037 211.864  1.00 37.73           C  
ATOM    427  N   CYS C 760     207.514 191.103 214.112  1.00 38.00           N  
ATOM    428  CA  CYS C 760     207.305 189.944 214.958  1.00 37.11           C  
ATOM    429  C   CYS C 760     208.273 189.955 216.133  1.00 38.04           C  
ATOM    430  O   CYS C 760     207.900 189.668 217.270  1.00 52.28           O  
ATOM    431  CB  CYS C 760     207.552 188.686 214.128  1.00 57.90           C  
ATOM    432  SG  CYS C 760     207.414 187.148 215.053  1.00 69.67           S  
ATOM    433  N   THR C 761     209.522 190.292 215.835  1.00 35.70           N  
ATOM    434  CA  THR C 761     210.600 190.330 216.830  1.00 41.01           C  
ATOM    435  C   THR C 761     210.247 191.392 217.863  1.00 37.87           C  
ATOM    436  O   THR C 761     210.260 191.156 219.069  1.00 39.91           O  
ATOM    437  CB  THR C 761     211.958 190.666 216.197  1.00 48.22           C  
ATOM    438  OG1 THR C 761     212.310 189.651 215.250  1.00 58.85           O  
ATOM    439  CG2 THR C 761     213.031 190.745 217.265  1.00 48.54           C  
ATOM    440  N   GLN C 762     209.933 192.569 217.344  1.00 40.24           N  
ATOM    441  CA  GLN C 762     209.484 193.739 218.104  1.00 35.02           C  
ATOM    442  C   GLN C 762     208.362 193.433 219.111  1.00 39.85           C  
ATOM    443  O   GLN C 762     208.441 193.858 220.257  1.00 39.70           O  
ATOM    444  CB  GLN C 762     209.040 194.828 217.118  1.00 38.23           C  
ATOM    445  CG  GLN C 762     210.127 195.237 216.123  1.00 41.05           C  
ATOM    446  CD  GLN C 762     211.516 195.330 216.717  1.00 44.53           C  
ATOM    447  OE1 GLN C 762     212.301 194.394 216.698  1.00 47.01           O  
ATOM    448  NE2 GLN C 762     211.884 196.473 217.237  1.00 44.68           N  
ATOM    449  N   LEU C 763     207.362 192.644 218.722  1.00 31.91           N  
ATOM    450  CA  LEU C 763     206.332 192.127 219.621  1.00 30.90           C  
ATOM    451  C   LEU C 763     206.920 191.110 220.609  1.00 31.12           C  
ATOM    452  O   LEU C 763     206.504 191.064 221.764  1.00 44.94           O  
ATOM    453  CB  LEU C 763     205.219 191.512 218.759  1.00 28.58           C  
ATOM    454  CG  LEU C 763     204.164 192.518 218.267  1.00 20.70           C  
ATOM    455  CD1 LEU C 763     204.699 193.722 217.503  1.00 24.92           C  
ATOM    456  CD2 LEU C 763     203.181 191.792 217.358  1.00 27.22           C  
ATOM    457  N   ASN C 764     207.915 190.322 220.207  1.00 28.25           N  
ATOM    458  CA  ASN C 764     208.566 189.379 221.104  1.00 27.42           C  
ATOM    459  C   ASN C 764     209.554 190.029 222.074  1.00 35.94           C  
ATOM    460  O   ASN C 764     209.724 189.491 223.158  1.00 46.02           O  
ATOM    461  CB  ASN C 764     209.159 188.219 220.312  1.00 29.92           C  
ATOM    462  CG  ASN C 764     208.071 187.259 219.886  1.00 37.53           C  
ATOM    463  OD1 ASN C 764     207.571 186.473 220.671  1.00 41.90           O  
ATOM    464  ND2 ASN C 764     207.642 187.293 218.655  1.00 40.50           N  
ATOM    465  N   ARG C 765     210.133 191.207 221.791  1.00 36.90           N  
ATOM    466  CA  ARG C 765     210.860 192.001 222.804  1.00 32.29           C  
ATOM    467  C   ARG C 765     209.943 192.318 223.970  1.00 36.50           C  
ATOM    468  O   ARG C 765     210.358 192.203 225.116  1.00 41.15           O  
ATOM    469  CB  ARG C 765     211.418 193.315 222.226  1.00 33.37           C  
ATOM    470  CG  ARG C 765     212.803 193.140 221.604  1.00 34.07           C  
ATOM    471  CD  ARG C 765     213.303 194.411 220.907  1.00 43.94           C  
ATOM    472  NE  ARG C 765     213.531 195.557 221.815  1.00 41.11           N  
ATOM    473  CZ  ARG C 765     214.595 195.776 222.566  1.00 43.94           C  
ATOM    474  NH1 ARG C 765     214.739 196.892 223.209  1.00 42.43           N  
ATOM    475  NH2 ARG C 765     215.549 194.906 222.703  1.00 50.30           N  
ATOM    476  N   ALA C 766     208.695 192.671 223.686  1.00 34.45           N  
ATOM    477  CA  ALA C 766     207.705 192.976 224.696  1.00 30.93           C  
ATOM    478  C   ALA C 766     207.366 191.738 225.542  1.00 39.45           C  
ATOM    479  O   ALA C 766     207.641 191.709 226.739  1.00 49.00           O  
ATOM    480  CB  ALA C 766     206.496 193.585 223.982  1.00 34.83           C  
ATOM    481  N   LEU C 767     206.836 190.685 224.912  1.00 35.98           N  
ATOM    482  CA  LEU C 767     206.378 189.460 225.585  1.00 35.83           C  
ATOM    483  C   LEU C 767     207.512 188.632 226.224  1.00 40.67           C  
ATOM    484  O   LEU C 767     207.268 187.989 227.235  1.00 54.71           O  
ATOM    485  CB  LEU C 767     205.549 188.610 224.588  1.00 32.25           C  
ATOM    486  CG  LEU C 767     204.043 188.923 224.596  1.00 32.13           C  
ATOM    487  CD1 LEU C 767     203.752 190.401 224.396  1.00 37.95           C  
ATOM    488  CD2 LEU C 767     203.320 188.167 223.490  1.00 32.83           C  
ATOM    489  N   THR C 768     208.739 188.639 225.698  1.00 37.15           N  
ATOM    490  CA  THR C 768     209.893 187.962 226.320  1.00 45.28           C  
ATOM    491  C   THR C 768     210.470 188.729 227.520  1.00 48.55           C  
ATOM    492  O   THR C 768     211.105 188.145 228.400  1.00 60.49           O  
ATOM    493  CB  THR C 768     210.984 187.656 225.277  1.00 52.10           C  
ATOM    494  OG1 THR C 768     211.720 186.516 225.651  1.00 60.78           O  
ATOM    495  CG2 THR C 768     212.014 188.771 225.076  1.00 63.10           C  
ATOM    496  N   GLY C 769     210.202 190.031 227.607  1.00 40.64           N  
ATOM    497  CA  GLY C 769     210.407 190.830 228.808  1.00 50.29           C  
ATOM    498  C   GLY C 769     209.282 190.615 229.829  1.00 58.92           C  
ATOM    499  O   GLY C 769     208.932 189.494 230.192  1.00 57.17           O  
ATOM    500  N   ILE C 770     208.727 191.722 230.307  1.00 55.22           N  
ATOM    501  CA  ILE C 770     207.472 191.852 231.049  1.00 57.34           C  
ATOM    502  C   ILE C 770     207.284 190.779 232.134  1.00 62.09           C  
ATOM    503  O   ILE C 770     207.222 191.096 233.322  1.00 59.44           O  
ATOM    504  CB  ILE C 770     206.295 191.983 230.057  1.00 43.35           C  
ATOM    505  CG1 ILE C 770     205.188 192.904 230.609  1.00 49.03           C  
ATOM    506  CG2 ILE C 770     205.729 190.611 229.642  1.00 32.45           C  
ATOM    507  CD1 ILE C 770     205.528 194.395 230.534  1.00 45.99           C  
ATOM    508  N   THR C 912     194.914 204.905  81.501  1.00 73.30           N  
ATOM    509  CA  THR C 912     194.583 203.953  82.574  1.00 75.24           C  
ATOM    510  C   THR C 912     195.823 203.520  83.369  1.00 73.30           C  
ATOM    511  O   THR C 912     195.791 203.461  84.601  1.00 73.30           O  
ATOM    512  CB  THR C 912     193.813 202.737  82.012  1.00 73.30           C  
ATOM    513  OG1 THR C 912     193.611 201.748  82.998  1.00 73.30           O  
ATOM    514  CG2 THR C 912     194.492 202.029  80.838  1.00 73.30           C  
ATOM    515  N   GLN C 913     196.945 203.276  82.681  1.00 71.67           N  
ATOM    516  CA  GLN C 913     198.172 202.768  83.305  1.00 71.67           C  
ATOM    517  C   GLN C 913     198.748 203.759  84.327  1.00 73.67           C  
ATOM    518  O   GLN C 913     199.236 203.359  85.383  1.00 75.90           O  
ATOM    519  CB  GLN C 913     199.188 202.419  82.202  1.00 71.67           C  
ATOM    520  CG  GLN C 913     200.302 201.465  82.670  1.00 71.67           C  
ATOM    521  CD  GLN C 913     199.812 200.048  82.949  1.00 71.67           C  
ATOM    522  OE1 GLN C 913     198.638 199.723  82.852  1.00 71.67           O  
ATOM    523  NE2 GLN C 913     200.691 199.152  83.309  1.00 71.67           N  
ATOM    524  N   ASN C 914     198.618 205.056  84.039  1.00 75.57           N  
ATOM    525  CA  ASN C 914     198.989 206.152  84.925  1.00 73.54           C  
ATOM    526  C   ASN C 914     198.168 206.200  86.226  1.00 75.17           C  
ATOM    527  O   ASN C 914     198.749 206.187  87.307  1.00 73.87           O  
ATOM    528  CB  ASN C 914     198.942 207.486  84.151  1.00 73.54           C  
ATOM    529  CG  ASN C 914     197.653 207.797  83.397  1.00 74.26           C  
ATOM    530  OD1 ASN C 914     196.677 207.085  83.416  1.00 73.54           O  
ATOM    531  ND2 ASN C 914     197.624 208.870  82.686  1.00 73.54           N  
ATOM    532  N   VAL C 915     196.832 206.225  86.169  1.00 77.47           N  
ATOM    533  CA  VAL C 915     195.994 206.274  87.388  1.00 76.43           C  
ATOM    534  C   VAL C 915     196.061 204.985  88.210  1.00 73.17           C  
ATOM    535  O   VAL C 915     196.019 205.049  89.439  1.00 73.17           O  
ATOM    536  CB  VAL C 915     194.532 206.671  87.112  1.00 73.17           C  
ATOM    537  CG1 VAL C 915     194.476 208.099  86.560  1.00 73.17           C  
ATOM    538  CG2 VAL C 915     193.778 205.740  86.165  1.00 73.17           C  
ATOM    539  N   LEU C 916     196.258 203.822  87.583  1.00 73.77           N  
ATOM    540  CA  LEU C 916     196.469 202.566  88.311  1.00 72.79           C  
ATOM    541  C   LEU C 916     197.803 202.576  89.085  1.00 73.91           C  
ATOM    542  O   LEU C 916     197.872 202.056  90.198  1.00 74.29           O  
ATOM    543  CB  LEU C 916     196.359 201.390  87.320  1.00 72.56           C  
ATOM    544  CG  LEU C 916     196.231 200.004  87.954  1.00 71.58           C  
ATOM    545  CD1 LEU C 916     194.989 199.853  88.800  1.00 71.58           C  
ATOM    546  CD2 LEU C 916     196.130 198.958  86.848  1.00 71.58           C  
ATOM    547  N   TYR C 917     198.830 203.230  88.537  1.00 74.53           N  
ATOM    548  CA  TYR C 917     200.135 203.417  89.178  1.00 74.10           C  
ATOM    549  C   TYR C 917     200.107 204.512  90.255  1.00 74.81           C  
ATOM    550  O   TYR C 917     200.673 204.336  91.328  1.00 74.60           O  
ATOM    551  CB  TYR C 917     201.178 203.707  88.091  1.00 74.07           C  
ATOM    552  CG  TYR C 917     202.623 203.655  88.546  1.00 74.76           C  
ATOM    553  CD1 TYR C 917     203.206 204.761  89.194  1.00 72.24           C  
ATOM    554  CD2 TYR C 917     203.399 202.508  88.286  1.00 73.66           C  
ATOM    555  CE1 TYR C 917     204.549 204.706  89.620  1.00 72.87           C  
ATOM    556  CE2 TYR C 917     204.741 202.449  88.706  1.00 74.46           C  
ATOM    557  CZ  TYR C 917     205.321 203.549  89.376  1.00 75.86           C  
ATOM    558  OH  TYR C 917     206.619 203.494  89.776  1.00 77.18           O  
ATOM    559  N   GLU C 918     199.402 205.623  90.046  1.00 73.35           N  
ATOM    560  CA  GLU C 918     199.229 206.636  91.096  1.00 75.84           C  
ATOM    561  C   GLU C 918     198.387 206.101  92.275  1.00 76.80           C  
ATOM    562  O   GLU C 918     198.686 206.410  93.425  1.00 76.40           O  
ATOM    563  CB  GLU C 918     198.647 207.935  90.512  1.00 75.08           C  
ATOM    564  CG  GLU C 918     199.659 208.692  89.632  1.00 79.42           C  
ATOM    565  CD  GLU C 918     200.939 209.082  90.378  1.00 80.79           C  
ATOM    566  OE1 GLU C 918     200.847 209.609  91.509  1.00 77.31           O  
ATOM    567  OE2 GLU C 918     202.042 208.888  89.826  1.00 79.44           O1-
ATOM    568  N   ASN C 919     197.403 205.225  92.033  1.00 79.78           N  
ATOM    569  CA  ASN C 919     196.764 204.442  93.097  1.00 76.96           C  
ATOM    570  C   ASN C 919     197.749 203.468  93.782  1.00 72.76           C  
ATOM    571  O   ASN C 919     197.623 203.236  94.982  1.00 72.10           O  
ATOM    572  CB  ASN C 919     195.535 203.693  92.550  1.00 75.57           C  
ATOM    573  CG  ASN C 919     194.292 204.562  92.512  1.00 80.03           C  
ATOM    574  OD1 ASN C 919     193.556 204.675  93.476  1.00 79.43           O  
ATOM    575  ND2 ASN C 919     194.005 205.182  91.400  1.00 79.55           N  
ATOM    576  N   GLN C 920     198.752 202.945  93.066  1.00 70.38           N  
ATOM    577  CA  GLN C 920     199.816 202.115  93.638  1.00 73.66           C  
ATOM    578  C   GLN C 920     200.757 202.925  94.552  1.00 70.23           C  
ATOM    579  O   GLN C 920     201.082 202.486  95.659  1.00 69.64           O  
ATOM    580  CB  GLN C 920     200.555 201.379  92.495  1.00 71.93           C  
ATOM    581  CG  GLN C 920     201.340 200.116  92.887  1.00 71.93           C  
ATOM    582  CD  GLN C 920     200.429 198.950  93.251  1.00 69.64           C  
ATOM    583  OE1 GLN C 920     199.478 199.101  93.990  1.00 69.64           O  
ATOM    584  NE2 GLN C 920     200.636 197.751  92.771  1.00 69.64           N  
ATOM    585  N   LYS C 921     201.113 204.154  94.149  1.00 71.28           N  
ATOM    586  CA  LYS C 921     201.801 205.139  95.016  1.00 72.07           C  
ATOM    587  C   LYS C 921     200.951 205.514  96.240  1.00 75.33           C  
ATOM    588  O   LYS C 921     201.453 205.501  97.362  1.00 69.92           O  
ATOM    589  CB  LYS C 921     202.162 206.409  94.215  1.00 71.62           C  
ATOM    590  CG  LYS C 921     203.212 206.238  93.101  1.00 72.71           C  
ATOM    591  CD  LYS C 921     204.619 205.846  93.586  1.00 73.70           C  
ATOM    592  CE  LYS C 921     205.295 206.874  94.507  1.00 69.92           C  
ATOM    593  NZ  LYS C 921     205.744 208.081  93.773  1.00 73.56           N  
ATOM    594  N   LEU C 922     199.665 205.804  96.032  1.00 73.73           N  
ATOM    595  CA  LEU C 922     198.705 206.188  97.072  1.00 73.06           C  
ATOM    596  C   LEU C 922     198.617 205.138  98.182  1.00 73.44           C  
ATOM    597  O   LEU C 922     198.891 205.454  99.339  1.00 69.65           O  
ATOM    598  CB  LEU C 922     197.340 206.464  96.413  1.00 75.57           C  
ATOM    599  CG  LEU C 922     196.208 207.021  97.301  1.00 75.42           C  
ATOM    600  CD1 LEU C 922     195.042 207.448  96.408  1.00 74.67           C  
ATOM    601  CD2 LEU C 922     195.629 206.010  98.293  1.00 69.65           C  
ATOM    602  N   ILE C 923     198.250 203.894  97.853  1.00 76.16           N  
ATOM    603  CA  ILE C 923     197.957 202.884  98.882  1.00 69.39           C  
ATOM    604  C   ILE C 923     199.211 202.506  99.675  1.00 66.09           C  
ATOM    605  O   ILE C 923     199.158 202.361 100.894  1.00 69.79           O  
ATOM    606  CB  ILE C 923     197.242 201.654  98.279  1.00 65.37           C  
ATOM    607  CG1 ILE C 923     196.686 200.704  99.359  1.00 65.37           C  
ATOM    608  CG2 ILE C 923     198.150 200.818  97.366  1.00 66.29           C  
ATOM    609  CD1 ILE C 923     195.668 201.350 100.301  1.00 65.37           C  
ATOM    610  N   ALA C 924     200.370 202.445  99.014  1.00 66.03           N  
ATOM    611  CA  ALA C 924     201.660 202.248  99.661  1.00 66.12           C  
ATOM    612  C   ALA C 924     202.038 203.412 100.588  1.00 66.45           C  
ATOM    613  O   ALA C 924     202.564 203.178 101.673  1.00 66.96           O  
ATOM    614  CB  ALA C 924     202.714 202.034  98.571  1.00 69.28           C  
ATOM    615  N   ASN C 925     201.752 204.663 100.205  1.00 71.14           N  
ATOM    616  CA  ASN C 925     201.981 205.839 101.051  1.00 69.53           C  
ATOM    617  C   ASN C 925     201.034 205.869 102.264  1.00 70.51           C  
ATOM    618  O   ASN C 925     201.454 206.219 103.364  1.00 66.33           O  
ATOM    619  CB  ASN C 925     201.872 207.118 100.197  1.00 74.59           C  
ATOM    620  CG  ASN C 925     203.036 207.372  99.254  1.00 76.28           C  
ATOM    621  OD1 ASN C 925     203.136 208.426  98.650  1.00 80.15           O  
ATOM    622  ND2 ASN C 925     203.985 206.473  99.137  1.00 72.74           N  
ATOM    623  N   GLN C 926     199.781 205.442 102.100  1.00 73.50           N  
ATOM    624  CA  GLN C 926     198.853 205.257 103.218  1.00 68.74           C  
ATOM    625  C   GLN C 926     199.315 204.144 104.176  1.00 64.17           C  
ATOM    626  O   GLN C 926     199.285 204.341 105.393  1.00 61.70           O  
ATOM    627  CB  GLN C 926     197.445 204.966 102.688  1.00 68.57           C  
ATOM    628  CG  GLN C 926     196.810 206.147 101.934  1.00 68.37           C  
ATOM    629  CD  GLN C 926     196.350 207.252 102.871  1.00 71.94           C  
ATOM    630  OE1 GLN C 926     195.254 207.227 103.400  1.00 78.02           O  
ATOM    631  NE2 GLN C 926     197.156 208.254 103.136  1.00 72.29           N  
ATOM    632  N   PHE C 927     199.789 203.006 103.655  1.00 62.86           N  
ATOM    633  CA  PHE C 927     200.294 201.886 104.457  1.00 59.85           C  
ATOM    634  C   PHE C 927     201.604 202.192 105.190  1.00 65.06           C  
ATOM    635  O   PHE C 927     201.692 202.004 106.401  1.00 70.29           O  
ATOM    636  CB  PHE C 927     200.432 200.657 103.555  1.00 61.32           C  
ATOM    637  CG  PHE C 927     201.075 199.465 104.228  1.00 62.96           C  
ATOM    638  CD1 PHE C 927     200.306 198.644 105.068  1.00 59.63           C  
ATOM    639  CD2 PHE C 927     202.439 199.182 104.031  1.00 64.05           C  
ATOM    640  CE1 PHE C 927     200.886 197.529 105.689  1.00 66.67           C  
ATOM    641  CE2 PHE C 927     203.019 198.063 104.653  1.00 60.29           C  
ATOM    642  CZ  PHE C 927     202.238 197.228 105.470  1.00 64.08           C  
ATOM    643  N   ASN C 928     202.603 202.726 104.486  1.00 62.39           N  
ATOM    644  CA  ASN C 928     203.904 203.109 105.041  1.00 63.73           C  
ATOM    645  C   ASN C 928     203.757 204.145 106.170  1.00 64.65           C  
ATOM    646  O   ASN C 928     204.401 204.022 107.215  1.00 67.37           O  
ATOM    647  CB  ASN C 928     204.768 203.607 103.863  1.00 68.57           C  
ATOM    648  CG  ASN C 928     206.087 204.237 104.267  1.00 71.82           C  
ATOM    649  OD1 ASN C 928     206.128 205.327 104.819  1.00 70.15           O  
ATOM    650  ND2 ASN C 928     207.203 203.627 103.950  1.00 75.18           N  
ATOM    651  N   SER C 929     202.857 205.122 106.010  1.00 67.77           N  
ATOM    652  CA  SER C 929     202.518 206.081 107.065  1.00 65.37           C  
ATOM    653  C   SER C 929     201.730 205.444 108.222  1.00 67.99           C  
ATOM    654  O   SER C 929     201.993 205.761 109.385  1.00 62.54           O  
ATOM    655  CB  SER C 929     201.747 207.241 106.436  1.00 64.80           C  
ATOM    656  OG  SER C 929     201.374 208.206 107.405  1.00 63.79           O  
ATOM    657  N   ALA C 930     200.828 204.489 107.945  1.00 66.55           N  
ATOM    658  CA  ALA C 930     200.073 203.791 108.986  1.00 63.90           C  
ATOM    659  C   ALA C 930     200.977 202.948 109.891  1.00 65.81           C  
ATOM    660  O   ALA C 930     200.919 203.105 111.102  1.00 68.53           O  
ATOM    661  CB  ALA C 930     198.965 202.944 108.362  1.00 63.61           C  
ATOM    662  N   ILE C 931     201.859 202.115 109.328  1.00 61.55           N  
ATOM    663  CA  ILE C 931     202.809 201.290 110.093  1.00 61.55           C  
ATOM    664  C   ILE C 931     203.717 202.143 111.001  1.00 66.22           C  
ATOM    665  O   ILE C 931     203.911 201.791 112.164  1.00 67.64           O  
ATOM    666  CB  ILE C 931     203.627 200.372 109.157  1.00 59.18           C  
ATOM    667  CG1 ILE C 931     202.765 199.320 108.429  1.00 61.72           C  
ATOM    668  CG2 ILE C 931     204.753 199.672 109.929  1.00 62.54           C  
ATOM    669  CD1 ILE C 931     201.960 198.372 109.318  1.00 56.26           C  
ATOM    670  N   GLY C 932     204.202 203.306 110.552  1.00 68.93           N  
ATOM    671  CA  GLY C 932     204.974 204.208 111.424  1.00 65.00           C  
ATOM    672  C   GLY C 932     204.183 204.732 112.636  1.00 64.26           C  
ATOM    673  O   GLY C 932     204.714 204.888 113.737  1.00 69.54           O  
ATOM    674  N   LYS C 933     202.872 204.929 112.460  1.00 63.23           N  
ATOM    675  CA  LYS C 933     201.923 205.265 113.527  1.00 63.87           C  
ATOM    676  C   LYS C 933     201.568 204.045 114.389  1.00 67.73           C  
ATOM    677  O   LYS C 933     201.336 204.199 115.588  1.00 69.98           O  
ATOM    678  CB  LYS C 933     200.712 205.954 112.874  1.00 66.28           C  
ATOM    679  CG  LYS C 933     199.779 206.659 113.873  1.00 66.22           C  
ATOM    680  CD  LYS C 933     198.849 207.664 113.166  1.00 61.39           C  
ATOM    681  CE  LYS C 933     199.590 208.976 112.840  1.00 61.94           C  
ATOM    682  NZ  LYS C 933     198.966 209.747 111.728  1.00 62.48           N  
ATOM    683  N   ILE C 934     201.599 202.820 113.851  1.00 65.81           N  
ATOM    684  CA  ILE C 934     201.540 201.586 114.657  1.00 63.48           C  
ATOM    685  C   ILE C 934     202.756 201.474 115.580  1.00 65.48           C  
ATOM    686  O   ILE C 934     202.584 201.157 116.750  1.00 70.76           O  
ATOM    687  CB  ILE C 934     201.411 200.309 113.790  1.00 65.59           C  
ATOM    688  CG1 ILE C 934     200.180 200.278 112.861  1.00 66.71           C  
ATOM    689  CG2 ILE C 934     201.385 199.056 114.671  1.00 60.02           C  
ATOM    690  CD1 ILE C 934     198.848 200.656 113.499  1.00 66.17           C  
ATOM    691  N   GLN C 935     203.965 201.758 115.105  1.00 66.83           N  
ATOM    692  CA  GLN C 935     205.163 201.690 115.946  1.00 68.24           C  
ATOM    693  C   GLN C 935     205.136 202.708 117.098  1.00 71.29           C  
ATOM    694  O   GLN C 935     205.486 202.358 118.221  1.00 69.66           O  
ATOM    695  CB  GLN C 935     206.412 201.840 115.069  1.00 73.97           C  
ATOM    696  CG  GLN C 935     206.569 200.618 114.151  1.00 73.94           C  
ATOM    697  CD  GLN C 935     207.655 200.811 113.108  1.00 83.25           C  
ATOM    698  OE1 GLN C 935     207.496 201.515 112.121  1.00 84.92           O  
ATOM    699  NE2 GLN C 935     208.792 200.182 113.260  1.00 83.91           N  
ATOM    700  N   ASP C 936     204.625 203.919 116.883  1.00 70.75           N  
ATOM    701  CA  ASP C 936     204.341 204.887 117.954  1.00 72.44           C  
ATOM    702  C   ASP C 936     203.276 204.370 118.945  1.00 69.47           C  
ATOM    703  O   ASP C 936     203.500 204.338 120.155  1.00 69.44           O  
ATOM    704  CB  ASP C 936     203.900 206.212 117.302  1.00 75.99           C  
ATOM    705  CG  ASP C 936     203.671 207.363 118.290  1.00 77.86           C  
ATOM    706  OD1 ASP C 936     202.968 208.326 117.912  1.00 70.17           O  
ATOM    707  OD2 ASP C 936     204.213 207.337 119.412  1.00 86.20           O1-
ATOM    708  N   SER C 937     202.148 203.875 118.430  1.00 67.93           N  
ATOM    709  CA  SER C 937     201.038 203.313 119.218  1.00 66.62           C  
ATOM    710  C   SER C 937     201.459 202.142 120.124  1.00 65.52           C  
ATOM    711  O   SER C 937     200.988 201.987 121.253  1.00 68.94           O  
ATOM    712  CB  SER C 937     199.981 202.780 118.254  1.00 68.21           C  
ATOM    713  OG  SER C 937     199.465 203.802 117.426  1.00 68.75           O  
ATOM    714  N   LEU C 938     202.354 201.301 119.615  1.00 62.53           N  
ATOM    715  CA  LEU C 938     202.822 200.101 120.283  1.00 64.33           C  
ATOM    716  C   LEU C 938     203.985 200.389 121.242  1.00 69.12           C  
ATOM    717  O   LEU C 938     203.989 199.894 122.364  1.00 74.44           O  
ATOM    718  CB  LEU C 938     203.160 199.109 119.175  1.00 67.60           C  
ATOM    719  CG  LEU C 938     203.431 197.685 119.669  1.00 68.13           C  
ATOM    720  CD1 LEU C 938     203.050 196.713 118.565  1.00 69.83           C  
ATOM    721  CD2 LEU C 938     204.901 197.465 119.998  1.00 72.19           C  
ATOM    722  N   SER C 939     204.957 201.216 120.849  1.00 69.26           N  
ATOM    723  CA  SER C 939     206.086 201.595 121.714  1.00 71.07           C  
ATOM    724  C   SER C 939     205.626 202.380 122.951  1.00 69.99           C  
ATOM    725  O   SER C 939     206.085 202.124 124.065  1.00 75.57           O  
ATOM    726  CB  SER C 939     207.131 202.396 120.925  1.00 72.81           C  
ATOM    727  OG  SER C 939     206.599 203.579 120.366  1.00 73.08           O  
ATOM    728  N   SER C 940     204.670 203.295 122.783  1.00 71.76           N  
ATOM    729  CA  SER C 940     204.031 204.003 123.897  1.00 68.15           C  
ATOM    730  C   SER C 940     203.259 203.050 124.814  1.00 64.66           C  
ATOM    731  O   SER C 940     203.467 203.095 126.021  1.00 67.68           O  
ATOM    732  CB  SER C 940     203.135 205.125 123.386  1.00 70.45           C  
ATOM    733  OG  SER C 940     202.191 204.620 122.466  1.00 75.01           O  
ATOM    734  N   THR C 941     202.455 202.122 124.278  1.00 65.47           N  
ATOM    735  CA  THR C 941     201.770 201.087 125.086  1.00 63.22           C  
ATOM    736  C   THR C 941     202.758 200.220 125.862  1.00 60.95           C  
ATOM    737  O   THR C 941     202.517 199.938 127.027  1.00 66.17           O  
ATOM    738  CB  THR C 941     200.858 200.170 124.254  1.00 67.40           C  
ATOM    739  OG1 THR C 941     199.892 200.902 123.541  1.00 75.15           O  
ATOM    740  CG2 THR C 941     200.080 199.186 125.134  1.00 59.17           C  
ATOM    741  N   ALA C 942     203.891 199.827 125.277  1.00 64.95           N  
ATOM    742  CA  ALA C 942     204.937 199.105 126.002  1.00 65.54           C  
ATOM    743  C   ALA C 942     205.554 199.940 127.144  1.00 69.76           C  
ATOM    744  O   ALA C 942     205.700 199.455 128.263  1.00 70.42           O  
ATOM    745  CB  ALA C 942     206.012 198.675 125.003  1.00 70.29           C  
ATOM    746  N   SER C 943     205.884 201.205 126.882  1.00 69.76           N  
ATOM    747  CA  SER C 943     206.410 202.141 127.885  1.00 68.97           C  
ATOM    748  C   SER C 943     205.401 202.454 129.004  1.00 64.88           C  
ATOM    749  O   SER C 943     205.787 202.618 130.155  1.00 64.41           O  
ATOM    750  CB  SER C 943     206.847 203.415 127.159  1.00 70.48           C  
ATOM    751  OG  SER C 943     207.567 204.278 128.008  1.00 72.59           O  
ATOM    752  N   ALA C 944     204.100 202.454 128.704  1.00 64.27           N  
ATOM    753  CA  ALA C 944     203.042 202.539 129.706  1.00 59.92           C  
ATOM    754  C   ALA C 944     202.896 201.235 130.503  1.00 58.06           C  
ATOM    755  O   ALA C 944     203.011 201.227 131.721  1.00 62.56           O  
ATOM    756  CB  ALA C 944     201.715 202.885 129.016  1.00 58.47           C  
ATOM    757  N   LEU C 945     202.655 200.106 129.841  1.00 57.07           N  
ATOM    758  CA  LEU C 945     202.397 198.826 130.506  1.00 55.55           C  
ATOM    759  C   LEU C 945     203.616 198.345 131.317  1.00 59.03           C  
ATOM    760  O   LEU C 945     203.467 197.737 132.374  1.00 71.13           O  
ATOM    761  CB  LEU C 945     201.894 197.831 129.447  1.00 61.73           C  
ATOM    762  CG  LEU C 945     201.385 196.513 130.060  1.00 61.38           C  
ATOM    763  CD1 LEU C 945     200.087 196.046 129.402  1.00 62.08           C  
ATOM    764  CD2 LEU C 945     202.438 195.427 129.906  1.00 62.75           C  
ATOM    765  N   GLY C 946     204.826 198.729 130.911  1.00 60.17           N  
ATOM    766  CA  GLY C 946     206.051 198.548 131.695  1.00 63.08           C  
ATOM    767  C   GLY C 946     206.198 199.468 132.917  1.00 59.88           C  
ATOM    768  O   GLY C 946     206.873 199.082 133.868  1.00 53.97           O  
ATOM    769  N   LYS C 947     205.546 200.642 132.958  1.00 65.50           N  
ATOM    770  CA  LYS C 947     205.424 201.481 134.176  1.00 60.04           C  
ATOM    771  C   LYS C 947     204.323 200.984 135.125  1.00 55.20           C  
ATOM    772  O   LYS C 947     204.471 201.097 136.340  1.00 55.08           O  
ATOM    773  CB  LYS C 947     205.291 202.980 133.804  1.00 62.41           C  
ATOM    774  CG  LYS C 947     203.882 203.594 133.881  1.00 62.59           C  
ATOM    775  CD  LYS C 947     203.839 205.006 133.288  1.00 65.29           C  
ATOM    776  CE  LYS C 947     202.391 205.515 133.266  1.00 59.81           C  
ATOM    777  NZ  LYS C 947     202.263 206.834 132.593  1.00 47.95           N  
ATOM    778  N   LEU C 948     203.261 200.371 134.594  1.00 57.67           N  
ATOM    779  CA  LEU C 948     202.207 199.721 135.388  1.00 56.72           C  
ATOM    780  C   LEU C 948     202.729 198.458 136.084  1.00 55.02           C  
ATOM    781  O   LEU C 948     202.516 198.292 137.278  1.00 62.72           O  
ATOM    782  CB  LEU C 948     200.997 199.388 134.490  1.00 65.02           C  
ATOM    783  CG  LEU C 948     199.869 200.437 134.429  1.00 63.88           C  
ATOM    784  CD1 LEU C 948     199.093 200.519 135.742  1.00 61.60           C  
ATOM    785  CD2 LEU C 948     200.351 201.841 134.070  1.00 62.90           C  
ATOM    786  N   GLN C 949     203.457 197.590 135.382  1.00 57.23           N  
ATOM    787  CA  GLN C 949     204.079 196.390 135.963  1.00 59.00           C  
ATOM    788  C   GLN C 949     205.204 196.710 136.964  1.00 57.80           C  
ATOM    789  O   GLN C 949     205.440 195.931 137.885  1.00 61.76           O  
ATOM    790  CB  GLN C 949     204.542 195.494 134.804  1.00 76.33           C  
ATOM    791  CG  GLN C 949     205.159 194.140 135.216  1.00 81.98           C  
ATOM    792  CD  GLN C 949     206.690 194.081 135.176  1.00 77.19           C  
ATOM    793  OE1 GLN C 949     207.405 195.066 135.108  1.00 75.26           O  
ATOM    794  NE2 GLN C 949     207.264 192.902 135.210  1.00 70.02           N  
ATOM    795  N   ASP C 950     205.856 197.871 136.843  1.00 58.77           N  
ATOM    796  CA  ASP C 950     206.822 198.392 137.821  1.00 58.27           C  
ATOM    797  C   ASP C 950     206.103 198.795 139.114  1.00 60.03           C  
ATOM    798  O   ASP C 950     206.318 198.197 140.174  1.00 60.08           O  
ATOM    799  CB  ASP C 950     207.572 199.577 137.183  1.00 60.57           C  
ATOM    800  CG  ASP C 950     208.476 200.391 138.120  1.00 59.26           C  
ATOM    801  OD1 ASP C 950     208.950 199.867 139.155  1.00 60.95           O  
ATOM    802  OD2 ASP C 950     208.734 201.573 137.803  1.00 58.69           O1-
ATOM    803  N   VAL C 951     205.174 199.751 139.012  1.00 59.23           N  
ATOM    804  CA  VAL C 951     204.447 200.299 140.164  1.00 45.08           C  
ATOM    805  C   VAL C 951     203.594 199.249 140.879  1.00 48.13           C  
ATOM    806  O   VAL C 951     203.569 199.246 142.109  1.00 59.78           O  
ATOM    807  CB  VAL C 951     203.657 201.555 139.750  1.00 46.79           C  
ATOM    808  CG1 VAL C 951     202.538 201.960 140.711  1.00 49.33           C  
ATOM    809  CG2 VAL C 951     204.626 202.739 139.673  1.00 49.33           C  
ATOM    810  N   VAL C 952     202.942 198.313 140.184  1.00 46.96           N  
ATOM    811  CA  VAL C 952     202.193 197.232 140.858  1.00 45.26           C  
ATOM    812  C   VAL C 952     203.106 196.311 141.677  1.00 51.14           C  
ATOM    813  O   VAL C 952     202.734 195.923 142.779  1.00 56.14           O  
ATOM    814  CB  VAL C 952     201.319 196.446 139.858  1.00 45.89           C  
ATOM    815  CG1 VAL C 952     200.727 195.144 140.410  1.00 38.90           C  
ATOM    816  CG2 VAL C 952     200.129 197.316 139.428  1.00 52.34           C  
ATOM    817  N   ASN C 953     204.327 196.001 141.228  1.00 52.70           N  
ATOM    818  CA  ASN C 953     205.253 195.172 142.006  1.00 57.85           C  
ATOM    819  C   ASN C 953     205.945 195.964 143.139  1.00 55.60           C  
ATOM    820  O   ASN C 953     206.233 195.396 144.189  1.00 54.53           O  
ATOM    821  CB  ASN C 953     206.236 194.478 141.048  1.00 62.67           C  
ATOM    822  CG  ASN C 953     206.501 193.035 141.438  1.00 61.29           C  
ATOM    823  OD1 ASN C 953     206.540 192.658 142.592  1.00 61.52           O  
ATOM    824  ND2 ASN C 953     206.668 192.161 140.484  1.00 52.01           N  
ATOM    825  N   GLN C 954     206.107 197.284 142.997  1.00 55.77           N  
ATOM    826  CA  GLN C 954     206.508 198.192 144.086  1.00 53.37           C  
ATOM    827  C   GLN C 954     205.427 198.305 145.185  1.00 52.41           C  
ATOM    828  O   GLN C 954     205.745 198.316 146.373  1.00 56.68           O  
ATOM    829  CB  GLN C 954     206.879 199.553 143.465  1.00 55.30           C  
ATOM    830  CG  GLN C 954     207.610 200.516 144.413  1.00 57.99           C  
ATOM    831  CD  GLN C 954     206.714 201.401 145.287  1.00 58.14           C  
ATOM    832  OE1 GLN C 954     205.492 201.370 145.259  1.00 45.95           O  
ATOM    833  NE2 GLN C 954     207.297 202.269 146.081  1.00 62.71           N  
ATOM    834  N   ASN C 955     204.143 198.265 144.814  1.00 47.80           N  
ATOM    835  CA  ASN C 955     203.039 198.110 145.763  1.00 48.81           C  
ATOM    836  C   ASN C 955     203.058 196.737 146.469  1.00 52.34           C  
ATOM    837  O   ASN C 955     202.892 196.666 147.684  1.00 55.44           O  
ATOM    838  CB  ASN C 955     201.697 198.336 145.048  1.00 50.09           C  
ATOM    839  CG  ASN C 955     201.318 199.793 144.926  1.00 50.77           C  
ATOM    840  OD1 ASN C 955     200.371 200.253 145.545  1.00 50.85           O  
ATOM    841  ND2 ASN C 955     202.021 200.570 144.143  1.00 52.93           N  
ATOM    842  N   ALA C 956     203.305 195.643 145.751  1.00 51.07           N  
ATOM    843  CA  ALA C 956     203.398 194.316 146.352  1.00 48.37           C  
ATOM    844  C   ALA C 956     204.564 194.223 147.348  1.00 57.11           C  
ATOM    845  O   ALA C 956     204.422 193.646 148.422  1.00 64.30           O  
ATOM    846  CB  ALA C 956     203.521 193.283 145.228  1.00 56.95           C  
ATOM    847  N   GLN C 957     205.694 194.861 147.043  1.00 62.82           N  
ATOM    848  CA  GLN C 957     206.808 195.056 147.980  1.00 59.81           C  
ATOM    849  C   GLN C 957     206.390 195.874 149.211  1.00 55.92           C  
ATOM    850  O   GLN C 957     206.654 195.457 150.336  1.00 58.61           O  
ATOM    851  CB  GLN C 957     207.992 195.678 147.215  1.00 68.05           C  
ATOM    852  CG  GLN C 957     209.136 196.207 148.096  1.00 64.70           C  
ATOM    853  CD  GLN C 957     208.998 197.687 148.448  1.00 65.17           C  
ATOM    854  OE1 GLN C 957     208.928 198.555 147.592  1.00 61.89           O  
ATOM    855  NE2 GLN C 957     208.977 198.042 149.715  1.00 70.65           N  
ATOM    856  N   ALA C 958     205.707 197.006 149.041  1.00 55.14           N  
ATOM    857  CA  ALA C 958     205.260 197.834 150.164  1.00 57.96           C  
ATOM    858  C   ALA C 958     204.308 197.092 151.120  1.00 59.22           C  
ATOM    859  O   ALA C 958     204.479 197.178 152.333  1.00 63.08           O  
ATOM    860  CB  ALA C 958     204.637 199.126 149.634  1.00 52.77           C  
ATOM    861  N   LEU C 959     203.364 196.299 150.612  1.00 61.67           N  
ATOM    862  CA  LEU C 959     202.459 195.522 151.462  1.00 51.49           C  
ATOM    863  C   LEU C 959     203.145 194.372 152.191  1.00 48.69           C  
ATOM    864  O   LEU C 959     202.825 194.152 153.353  1.00 55.46           O  
ATOM    865  CB  LEU C 959     201.266 195.002 150.652  1.00 62.77           C  
ATOM    866  CG  LEU C 959     200.031 195.906 150.691  1.00 60.67           C  
ATOM    867  CD1 LEU C 959     199.432 195.968 152.092  1.00 55.78           C  
ATOM    868  CD2 LEU C 959     200.323 197.318 150.191  1.00 58.32           C  
ATOM    869  N   ASN C 960     204.118 193.689 151.586  1.00 48.36           N  
ATOM    870  CA  ASN C 960     204.905 192.704 152.334  1.00 52.25           C  
ATOM    871  C   ASN C 960     205.820 193.372 153.380  1.00 56.66           C  
ATOM    872  O   ASN C 960     206.045 192.792 154.439  1.00 55.44           O  
ATOM    873  CB  ASN C 960     205.661 191.765 151.373  1.00 58.48           C  
ATOM    874  CG  ASN C 960     204.849 190.530 151.011  1.00 54.99           C  
ATOM    875  OD1 ASN C 960     203.655 190.581 150.753  1.00 54.36           O  
ATOM    876  ND2 ASN C 960     205.457 189.367 151.027  1.00 55.51           N  
ATOM    877  N   THR C 961     206.277 194.607 153.142  1.00 56.24           N  
ATOM    878  CA  THR C 961     206.982 195.404 154.161  1.00 54.93           C  
ATOM    879  C   THR C 961     206.048 195.758 155.324  1.00 59.03           C  
ATOM    880  O   THR C 961     206.393 195.535 156.482  1.00 67.02           O  
ATOM    881  CB  THR C 961     207.601 196.682 153.574  1.00 55.44           C  
ATOM    882  OG1 THR C 961     208.315 196.429 152.383  1.00 62.01           O  
ATOM    883  CG2 THR C 961     208.602 197.289 154.545  1.00 67.14           C  
ATOM    884  N   LEU C 962     204.838 196.237 155.026  1.00 52.45           N  
ATOM    885  CA  LEU C 962     203.808 196.531 156.013  1.00 40.74           C  
ATOM    886  C   LEU C 962     203.454 195.292 156.837  1.00 37.92           C  
ATOM    887  O   LEU C 962     203.474 195.364 158.054  1.00 42.62           O  
ATOM    888  CB  LEU C 962     202.584 197.107 155.288  1.00 45.99           C  
ATOM    889  CG  LEU C 962     201.613 197.833 156.229  1.00 36.86           C  
ATOM    890  CD1 LEU C 962     202.115 199.230 156.591  1.00 42.65           C  
ATOM    891  CD2 LEU C 962     200.227 197.971 155.608  1.00 33.41           C  
ATOM    892  N   VAL C 963     203.185 194.139 156.225  1.00 38.17           N  
ATOM    893  CA  VAL C 963     202.822 192.925 156.977  1.00 44.44           C  
ATOM    894  C   VAL C 963     203.945 192.464 157.904  1.00 48.61           C  
ATOM    895  O   VAL C 963     203.666 192.072 159.032  1.00 54.38           O  
ATOM    896  CB  VAL C 963     202.369 191.792 156.035  1.00 58.87           C  
ATOM    897  CG1 VAL C 963     202.325 190.426 156.728  1.00 58.19           C  
ATOM    898  CG2 VAL C 963     200.962 192.077 155.494  1.00 56.46           C  
ATOM    899  N   LYS C 964     205.219 192.554 157.509  1.00 48.93           N  
ATOM    900  CA  LYS C 964     206.332 192.186 158.402  1.00 50.63           C  
ATOM    901  C   LYS C 964     206.503 193.171 159.570  1.00 44.95           C  
ATOM    902  O   LYS C 964     206.761 192.738 160.694  1.00 43.82           O  
ATOM    903  CB  LYS C 964     207.633 192.023 157.602  1.00 67.54           C  
ATOM    904  CG  LYS C 964     207.695 190.751 156.741  1.00 71.19           C  
ATOM    905  CD  LYS C 964     207.662 189.408 157.492  1.00 69.81           C  
ATOM    906  CE  LYS C 964     208.804 189.254 158.508  1.00 65.89           C  
ATOM    907  NZ  LYS C 964     208.865 187.889 159.071  1.00 72.40           N  
ATOM    908  N   GLN C 965     206.304 194.473 159.352  1.00 43.15           N  
ATOM    909  CA  GLN C 965     206.302 195.461 160.437  1.00 44.25           C  
ATOM    910  C   GLN C 965     205.082 195.349 161.364  1.00 41.12           C  
ATOM    911  O   GLN C 965     205.244 195.461 162.577  1.00 45.59           O  
ATOM    912  CB  GLN C 965     206.400 196.878 159.867  1.00 50.34           C  
ATOM    913  CG  GLN C 965     207.800 197.177 159.296  1.00 53.58           C  
ATOM    914  CD  GLN C 965     208.421 198.458 159.841  1.00 62.51           C  
ATOM    915  OE1 GLN C 965     208.276 198.823 160.998  1.00 65.38           O  
ATOM    916  NE2 GLN C 965     209.152 199.200 159.047  1.00 62.07           N  
ATOM    917  N   LEU C 966     203.881 195.086 160.852  1.00 36.92           N  
ATOM    918  CA  LEU C 966     202.679 194.922 161.671  1.00 30.98           C  
ATOM    919  C   LEU C 966     202.657 193.585 162.415  1.00 35.51           C  
ATOM    920  O   LEU C 966     202.238 193.546 163.564  1.00 44.71           O  
ATOM    921  CB  LEU C 966     201.435 195.070 160.794  1.00 30.85           C  
ATOM    922  CG  LEU C 966     200.908 196.501 160.695  1.00 32.56           C  
ATOM    923  CD1 LEU C 966     201.939 197.549 160.300  1.00 33.68           C  
ATOM    924  CD2 LEU C 966     199.786 196.494 159.673  1.00 34.45           C  
ATOM    925  N   SER C 967     203.197 192.521 161.837  1.00 37.44           N  
ATOM    926  CA  SER C 967     203.478 191.285 162.571  1.00 38.87           C  
ATOM    927  C   SER C 967     204.386 191.567 163.773  1.00 42.86           C  
ATOM    928  O   SER C 967     204.157 191.031 164.857  1.00 46.48           O  
ATOM    929  CB  SER C 967     204.124 190.263 161.634  1.00 46.10           C  
ATOM    930  OG  SER C 967     204.482 189.085 162.323  1.00 36.76           O  
ATOM    931  N   SER C 968     205.351 192.483 163.631  1.00 46.23           N  
ATOM    932  CA  SER C 968     206.146 192.938 164.773  1.00 39.68           C  
ATOM    933  C   SER C 968     205.285 193.659 165.808  1.00 40.69           C  
ATOM    934  O   SER C 968     205.374 193.323 166.977  1.00 46.62           O  
ATOM    935  CB  SER C 968     207.379 193.756 164.353  1.00 47.37           C  
ATOM    936  OG  SER C 968     207.172 195.153 164.394  1.00 41.28           O  
ATOM    937  N   ASN C 969     204.404 194.587 165.429  1.00 39.20           N  
ATOM    938  CA  ASN C 969     203.566 195.329 166.378  1.00 31.08           C  
ATOM    939  C   ASN C 969     202.554 194.475 167.124  1.00 30.22           C  
ATOM    940  O   ASN C 969     202.455 194.583 168.343  1.00 37.09           O  
ATOM    941  CB  ASN C 969     202.853 196.500 165.685  1.00 34.30           C  
ATOM    942  CG  ASN C 969     203.778 197.680 165.539  1.00 45.67           C  
ATOM    943  OD1 ASN C 969     204.685 197.848 166.325  1.00 46.45           O  
ATOM    944  ND2 ASN C 969     203.607 198.527 164.556  1.00 44.01           N  
ATOM    945  N   PHE C 970     201.813 193.605 166.453  1.00 32.81           N  
ATOM    946  CA  PHE C 970     200.887 192.722 167.152  1.00 37.12           C  
ATOM    947  C   PHE C 970     201.611 191.624 167.944  1.00 38.51           C  
ATOM    948  O   PHE C 970     201.100 191.191 168.971  1.00 39.67           O  
ATOM    949  CB  PHE C 970     199.824 192.204 166.182  1.00 42.84           C  
ATOM    950  CG  PHE C 970     199.085 193.327 165.475  1.00 43.92           C  
ATOM    951  CD1 PHE C 970     199.048 193.372 164.072  1.00 42.55           C  
ATOM    952  CD2 PHE C 970     198.476 194.356 166.218  1.00 39.86           C  
ATOM    953  CE1 PHE C 970     198.427 194.451 163.419  1.00 46.36           C  
ATOM    954  CE2 PHE C 970     197.855 195.433 165.567  1.00 37.03           C  
ATOM    955  CZ  PHE C 970     197.841 195.488 164.166  1.00 40.30           C  
ATOM    956  N   GLY C 971     202.846 191.256 167.584  1.00 37.79           N  
ATOM    957  CA  GLY C 971     203.715 190.406 168.405  1.00 33.28           C  
ATOM    958  C   GLY C 971     204.314 191.121 169.627  1.00 35.52           C  
ATOM    959  O   GLY C 971     204.395 190.541 170.709  1.00 33.94           O  
ATOM    960  N   ALA C 972     204.702 192.388 169.489  1.00 36.94           N  
ATOM    961  CA  ALA C 972     205.229 193.205 170.579  1.00 30.09           C  
ATOM    962  C   ALA C 972     204.118 193.497 171.589  1.00 35.98           C  
ATOM    963  O   ALA C 972     204.255 193.185 172.770  1.00 42.30           O  
ATOM    964  CB  ALA C 972     205.835 194.497 170.014  1.00 29.88           C  
ATOM    965  N   ILE C 973     202.977 194.005 171.112  1.00 29.67           N  
ATOM    966  CA  ILE C 973     201.814 194.278 171.952  1.00 23.01           C  
ATOM    967  C   ILE C 973     201.289 192.990 172.583  1.00 28.30           C  
ATOM    968  O   ILE C 973     200.935 193.015 173.752  1.00 35.51           O  
ATOM    969  CB  ILE C 973     200.732 195.033 171.158  1.00 24.07           C  
ATOM    970  CG1 ILE C 973     201.223 196.458 170.833  1.00 21.72           C  
ATOM    971  CG2 ILE C 973     199.409 195.106 171.938  1.00 26.00           C  
ATOM    972  CD1 ILE C 973     200.353 197.178 169.799  1.00 26.22           C  
ATOM    973  N   SER C 974     201.316 191.850 171.890  1.00 34.82           N  
ATOM    974  CA  SER C 974     200.993 190.552 172.510  1.00 36.17           C  
ATOM    975  C   SER C 974     201.812 190.321 173.776  1.00 34.68           C  
ATOM    976  O   SER C 974     201.230 190.066 174.824  1.00 41.37           O  
ATOM    977  CB  SER C 974     201.207 189.410 171.509  1.00 52.23           C  
ATOM    978  OG  SER C 974     201.286 188.138 172.122  1.00 49.29           O  
ATOM    979  N   SER C 975     203.139 190.469 173.729  1.00 35.04           N  
ATOM    980  CA  SER C 975     204.000 190.211 174.890  1.00 37.99           C  
ATOM    981  C   SER C 975     203.897 191.282 175.990  1.00 36.50           C  
ATOM    982  O   SER C 975     203.703 190.955 177.163  1.00 38.45           O  
ATOM    983  CB  SER C 975     205.447 190.022 174.437  1.00 50.88           C  
ATOM    984  OG  SER C 975     206.260 189.664 175.541  1.00 51.77           O  
ATOM    985  N   VAL C 976     203.980 192.570 175.636  1.00 31.35           N  
ATOM    986  CA  VAL C 976     203.938 193.681 176.606  1.00 29.02           C  
ATOM    987  C   VAL C 976     202.577 193.805 177.298  1.00 25.37           C  
ATOM    988  O   VAL C 976     202.521 194.078 178.492  1.00 33.17           O  
ATOM    989  CB  VAL C 976     204.320 195.014 175.940  1.00 35.24           C  
ATOM    990  CG1 VAL C 976     204.377 196.165 176.947  1.00 30.75           C  
ATOM    991  CG2 VAL C 976     205.703 194.955 175.282  1.00 46.34           C  
ATOM    992  N   LEU C 977     201.475 193.586 176.579  1.00 23.58           N  
ATOM    993  CA  LEU C 977     200.115 193.651 177.107  1.00 23.72           C  
ATOM    994  C   LEU C 977     199.733 192.364 177.850  1.00 32.92           C  
ATOM    995  O   LEU C 977     199.034 192.456 178.854  1.00 38.88           O  
ATOM    996  CB  LEU C 977     199.171 194.000 175.942  1.00 23.57           C  
ATOM    997  CG  LEU C 977     197.918 194.795 176.308  1.00 27.08           C  
ATOM    998  CD1 LEU C 977     197.472 195.630 175.112  1.00 37.32           C  
ATOM    999  CD2 LEU C 977     196.753 193.895 176.677  1.00 31.81           C  
ATOM   1000  N   ASN C 978     200.250 191.189 177.470  1.00 33.01           N  
ATOM   1001  CA  ASN C 978     200.122 190.006 178.324  1.00 29.86           C  
ATOM   1002  C   ASN C 978     200.815 190.216 179.668  1.00 36.00           C  
ATOM   1003  O   ASN C 978     200.254 189.848 180.690  1.00 42.21           O  
ATOM   1004  CB  ASN C 978     200.665 188.729 177.658  1.00 36.14           C  
ATOM   1005  CG  ASN C 978     199.578 187.905 176.995  1.00 59.02           C  
ATOM   1006  OD1 ASN C 978     198.525 187.655 177.563  1.00 65.78           O  
ATOM   1007  ND2 ASN C 978     199.787 187.413 175.803  1.00 62.59           N  
ATOM   1008  N   ASP C 979     202.002 190.823 179.705  1.00 33.31           N  
ATOM   1009  CA  ASP C 979     202.680 191.111 180.974  1.00 26.01           C  
ATOM   1010  C   ASP C 979     201.916 192.112 181.836  1.00 27.08           C  
ATOM   1011  O   ASP C 979     201.678 191.813 182.999  1.00 35.50           O  
ATOM   1012  CB  ASP C 979     204.123 191.577 180.753  1.00 36.65           C  
ATOM   1013  CG  ASP C 979     205.096 190.434 180.435  1.00 56.26           C  
ATOM   1014  OD1 ASP C 979     204.781 189.251 180.704  1.00 62.04           O  
ATOM   1015  OD2 ASP C 979     206.225 190.728 179.979  1.00 67.78           O1-
ATOM   1016  N   ILE C 980     201.455 193.242 181.287  1.00 19.83           N  
ATOM   1017  CA  ILE C 980     200.547 194.170 181.989  1.00 17.87           C  
ATOM   1018  C   ILE C 980     199.319 193.435 182.555  1.00 19.88           C  
ATOM   1019  O   ILE C 980     198.960 193.673 183.698  1.00 27.23           O  
ATOM   1020  CB  ILE C 980     200.120 195.329 181.059  1.00 17.03           C  
ATOM   1021  CG1 ILE C 980     201.220 196.367 180.774  1.00 15.52           C  
ATOM   1022  CG2 ILE C 980     198.885 196.053 181.587  1.00 16.56           C  
ATOM   1023  CD1 ILE C 980     201.686 197.192 181.975  1.00 19.34           C  
ATOM   1024  N   LEU C 981     198.679 192.524 181.823  1.00 23.36           N  
ATOM   1025  CA  LEU C 981     197.540 191.737 182.313  1.00 27.81           C  
ATOM   1026  C   LEU C 981     197.944 190.788 183.452  1.00 28.04           C  
ATOM   1027  O   LEU C 981     197.301 190.742 184.495  1.00 29.61           O  
ATOM   1028  CB  LEU C 981     196.942 190.929 181.144  1.00 30.32           C  
ATOM   1029  CG  LEU C 981     196.015 191.744 180.239  1.00 35.06           C  
ATOM   1030  CD1 LEU C 981     195.779 191.015 178.917  1.00 38.11           C  
ATOM   1031  CD2 LEU C 981     194.656 191.941 180.902  1.00 31.52           C  
ATOM   1032  N   SER C 982     199.024 190.036 183.269  1.00 25.40           N  
ATOM   1033  CA  SER C 982     199.515 189.030 184.213  1.00 26.73           C  
ATOM   1034  C   SER C 982     200.033 189.632 185.521  1.00 28.01           C  
ATOM   1035  O   SER C 982     199.783 189.082 186.595  1.00 38.78           O  
ATOM   1036  CB  SER C 982     200.598 188.212 183.506  1.00 36.52           C  
ATOM   1037  OG  SER C 982     201.078 187.170 184.319  1.00 42.33           O  
ATOM   1038  N   ARG C 983     200.637 190.817 185.444  1.00 23.32           N  
ATOM   1039  CA  ARG C 983     201.138 191.489 186.642  1.00 21.81           C  
ATOM   1040  C   ARG C 983     200.027 192.294 187.354  1.00 24.34           C  
ATOM   1041  O   ARG C 983     200.028 192.385 188.577  1.00 31.26           O  
ATOM   1042  CB  ARG C 983     202.381 192.339 186.331  1.00 17.45           C  
ATOM   1043  CG  ARG C 983     202.110 193.737 185.816  1.00 19.16           C  
ATOM   1044  CD  ARG C 983     203.352 194.397 185.246  1.00 19.48           C  
ATOM   1045  NE  ARG C 983     204.099 195.126 186.264  1.00 24.32           N  
ATOM   1046  CZ  ARG C 983     205.004 196.061 185.998  1.00 29.89           C  
ATOM   1047  NH1 ARG C 983     205.277 196.386 184.744  1.00 26.95           N  
ATOM   1048  NH2 ARG C 983     205.635 196.674 186.988  1.00 40.42           N  
ATOM   1049  N   LEU C 984     199.086 192.873 186.606  1.00 19.62           N  
ATOM   1050  CA  LEU C 984     197.975 193.575 187.242  1.00 18.16           C  
ATOM   1051  C   LEU C 984     197.066 192.600 187.974  1.00 23.47           C  
ATOM   1052  O   LEU C 984     196.594 192.924 189.050  1.00 30.91           O  
ATOM   1053  CB  LEU C 984     197.230 194.430 186.212  1.00 21.16           C  
ATOM   1054  CG  LEU C 984     196.190 195.408 186.782  1.00 26.30           C  
ATOM   1055  CD1 LEU C 984     196.712 196.204 187.978  1.00 34.60           C  
ATOM   1056  CD2 LEU C 984     195.860 196.434 185.698  1.00 27.44           C  
ATOM   1057  N   ASP C 985     196.895 191.381 187.467  1.00 27.73           N  
ATOM   1058  CA  ASP C 985     196.212 190.296 188.191  1.00 27.32           C  
ATOM   1059  C   ASP C 985     196.928 189.929 189.501  1.00 27.80           C  
ATOM   1060  O   ASP C 985     196.281 189.731 190.528  1.00 31.27           O  
ATOM   1061  CB  ASP C 985     196.116 189.033 187.313  1.00 35.34           C  
ATOM   1062  CG  ASP C 985     195.161 189.083 186.118  1.00 40.88           C  
ATOM   1063  OD1 ASP C 985     194.361 190.028 185.949  1.00 36.50           O  
ATOM   1064  OD2 ASP C 985     195.164 188.099 185.350  1.00 42.33           O1-
ATOM   1065  N   LYS C 986     198.264 189.873 189.500  1.00 25.07           N  
ATOM   1066  CA  LYS C 986     199.047 189.647 190.723  1.00 25.20           C  
ATOM   1067  C   LYS C 986     198.845 190.791 191.720  1.00 28.44           C  
ATOM   1068  O   LYS C 986     198.456 190.539 192.849  1.00 34.75           O  
ATOM   1069  CB  LYS C 986     200.522 189.436 190.356  1.00 30.11           C  
ATOM   1070  CG  LYS C 986     201.471 189.209 191.540  1.00 29.14           C  
ATOM   1071  CD  LYS C 986     201.194 187.960 192.391  1.00 45.36           C  
ATOM   1072  CE  LYS C 986     201.291 186.614 191.657  1.00 43.05           C  
ATOM   1073  NZ  LYS C 986     202.659 186.312 191.171  1.00 51.71           N  
ATOM   1074  N   VAL C 987     199.032 192.048 191.326  1.00 27.75           N  
ATOM   1075  CA  VAL C 987     198.843 193.220 192.205  1.00 21.54           C  
ATOM   1076  C   VAL C 987     197.405 193.396 192.723  1.00 18.87           C  
ATOM   1077  O   VAL C 987     197.224 193.766 193.877  1.00 25.67           O  
ATOM   1078  CB  VAL C 987     199.338 194.491 191.502  1.00 30.90           C  
ATOM   1079  CG1 VAL C 987     199.096 195.764 192.319  1.00 22.39           C  
ATOM   1080  CG2 VAL C 987     200.847 194.390 191.271  1.00 30.98           C  
ATOM   1081  N   GLU C 988     196.372 193.090 191.943  1.00 22.20           N  
ATOM   1082  CA  GLU C 988     194.982 193.084 192.425  1.00 30.32           C  
ATOM   1083  C   GLU C 988     194.653 191.892 193.337  1.00 36.37           C  
ATOM   1084  O   GLU C 988     193.709 191.968 194.123  1.00 43.20           O  
ATOM   1085  CB  GLU C 988     194.016 193.174 191.228  1.00 30.28           C  
ATOM   1086  CG  GLU C 988     192.624 193.733 191.593  1.00 49.59           C  
ATOM   1087  CD  GLU C 988     191.572 192.735 192.116  1.00 57.09           C  
ATOM   1088  OE1 GLU C 988     191.584 191.550 191.728  1.00 64.90           O  
ATOM   1089  OE2 GLU C 988     190.663 193.161 192.867  1.00 51.37           O1-
ATOM   1090  N   ALA C 989     195.431 190.802 193.297  1.00 29.15           N  
ATOM   1091  CA  ALA C 989     195.359 189.736 194.300  1.00 29.48           C  
ATOM   1092  C   ALA C 989     196.063 190.134 195.594  1.00 32.04           C  
ATOM   1093  O   ALA C 989     195.478 190.040 196.670  1.00 41.35           O  
ATOM   1094  CB  ALA C 989     195.963 188.444 193.748  1.00 29.89           C  
ATOM   1095  N   GLU C 990     197.312 190.595 195.511  1.00 30.29           N  
ATOM   1096  CA  GLU C 990     198.145 190.878 196.684  1.00 24.29           C  
ATOM   1097  C   GLU C 990     197.492 191.939 197.567  1.00 25.57           C  
ATOM   1098  O   GLU C 990     197.416 191.749 198.778  1.00 37.40           O  
ATOM   1099  CB  GLU C 990     199.554 191.331 196.266  1.00 23.79           C  
ATOM   1100  CG  GLU C 990     200.355 190.333 195.411  1.00 31.51           C  
ATOM   1101  CD  GLU C 990     201.135 189.290 196.207  1.00 46.95           C  
ATOM   1102  OE1 GLU C 990     202.381 189.369 196.235  1.00 52.28           O  
ATOM   1103  OE2 GLU C 990     200.517 188.359 196.762  1.00 58.77           O1-
ATOM   1104  N   VAL C 991     196.917 193.000 196.983  1.00 25.33           N  
ATOM   1105  CA  VAL C 991     196.259 194.095 197.723  1.00 29.15           C  
ATOM   1106  C   VAL C 991     195.062 193.630 198.573  1.00 29.75           C  
ATOM   1107  O   VAL C 991     194.760 194.262 199.578  1.00 43.08           O  
ATOM   1108  CB  VAL C 991     195.919 195.262 196.768  1.00 34.61           C  
ATOM   1109  CG1 VAL C 991     194.587 195.103 196.038  1.00 43.72           C  
ATOM   1110  CG2 VAL C 991     195.916 196.611 197.477  1.00 53.73           C  
ATOM   1111  N   GLN C 992     194.421 192.500 198.247  1.00 33.16           N  
ATOM   1112  CA  GLN C 992     193.366 191.864 199.057  1.00 34.32           C  
ATOM   1113  C   GLN C 992     193.909 190.939 200.160  1.00 30.73           C  
ATOM   1114  O   GLN C 992     193.291 190.773 201.205  1.00 35.45           O  
ATOM   1115  CB  GLN C 992     192.481 190.978 198.179  1.00 42.78           C  
ATOM   1116  CG  GLN C 992     191.740 191.675 197.044  1.00 42.62           C  
ATOM   1117  CD  GLN C 992     191.044 190.618 196.197  1.00 48.08           C  
ATOM   1118  OE1 GLN C 992     190.032 190.046 196.581  1.00 54.76           O  
ATOM   1119  NE2 GLN C 992     191.600 190.263 195.066  1.00 52.51           N  
ATOM   1120  N   ILE C 993     195.058 190.303 199.946  1.00 29.18           N  
ATOM   1121  CA  ILE C 993     195.706 189.443 200.936  1.00 24.83           C  
ATOM   1122  C   ILE C 993     196.411 190.312 201.989  1.00 26.85           C  
ATOM   1123  O   ILE C 993     196.335 190.015 203.177  1.00 34.79           O  
ATOM   1124  CB  ILE C 993     196.636 188.439 200.231  1.00 30.77           C  
ATOM   1125  CG1 ILE C 993     195.796 187.460 199.390  1.00 37.50           C  
ATOM   1126  CG2 ILE C 993     197.462 187.640 201.242  1.00 37.96           C  
ATOM   1127  CD1 ILE C 993     196.612 186.633 198.403  1.00 51.52           C  
ATOM   1128  N   ASP C 994     197.017 191.434 201.592  1.00 24.09           N  
ATOM   1129  CA  ASP C 994     197.538 192.464 202.497  1.00 22.48           C  
ATOM   1130  C   ASP C 994     196.447 193.080 203.367  1.00 25.02           C  
ATOM   1131  O   ASP C 994     196.703 193.490 204.501  1.00 25.03           O  
ATOM   1132  CB  ASP C 994     198.161 193.608 201.687  1.00 25.58           C  
ATOM   1133  CG  ASP C 994     199.550 193.309 201.137  1.00 37.26           C  
ATOM   1134  OD1 ASP C 994     199.860 193.783 200.025  1.00 33.41           O  
ATOM   1135  OD2 ASP C 994     200.387 192.736 201.872  1.00 49.07           O1-
ATOM   1136  N   ARG C 995     195.231 193.142 202.849  1.00 25.15           N  
ATOM   1137  CA  ARG C 995     194.139 193.720 203.611  1.00 18.79           C  
ATOM   1138  C   ARG C 995     193.878 192.835 204.831  1.00 20.95           C  
ATOM   1139  O   ARG C 995     193.851 193.310 205.960  1.00 30.51           O  
ATOM   1140  CB  ARG C 995     192.901 193.874 202.721  1.00 28.87           C  
ATOM   1141  CG  ARG C 995     192.160 195.180 202.928  1.00 38.83           C  
ATOM   1142  CD  ARG C 995     190.987 195.313 201.972  1.00 39.07           C  
ATOM   1143  NE  ARG C 995     191.215 196.275 200.899  1.00 36.92           N  
ATOM   1144  CZ  ARG C 995     191.330 195.939 199.621  1.00 37.56           C  
ATOM   1145  NH1 ARG C 995     191.220 194.671 199.254  1.00 41.49           N  
ATOM   1146  NH2 ARG C 995     191.539 196.872 198.706  1.00 49.26           N  
ATOM   1147  N   LEU C 996     193.704 191.543 204.579  1.00 22.23           N  
ATOM   1148  CA  LEU C 996     193.458 190.564 205.622  1.00 16.60           C  
ATOM   1149  C   LEU C 996     194.659 190.367 206.535  1.00 22.72           C  
ATOM   1150  O   LEU C 996     194.457 190.229 207.728  1.00 24.92           O  
ATOM   1151  CB  LEU C 996     193.002 189.259 204.972  1.00 19.93           C  
ATOM   1152  CG  LEU C 996     192.590 188.193 205.987  1.00 22.00           C  
ATOM   1153  CD1 LEU C 996     191.413 188.640 206.840  1.00 31.99           C  
ATOM   1154  CD2 LEU C 996     192.170 186.947 205.234  1.00 31.79           C  
ATOM   1155  N   ILE C 997     195.900 190.398 206.051  1.00 13.85           N  
ATOM   1156  CA  ILE C 997     197.067 190.405 206.958  1.00 14.09           C  
ATOM   1157  C   ILE C 997     196.985 191.597 207.912  1.00 15.30           C  
ATOM   1158  O   ILE C 997     197.070 191.400 209.114  1.00 18.72           O  
ATOM   1159  CB  ILE C 997     198.410 190.374 206.203  1.00 19.74           C  
ATOM   1160  CG1 ILE C 997     198.635 189.025 205.486  1.00 24.81           C  
ATOM   1161  CG2 ILE C 997     199.579 190.615 207.168  1.00 18.64           C  
ATOM   1162  CD1 ILE C 997     199.700 189.082 204.381  1.00 28.77           C  
ATOM   1163  N   THR C 998     196.716 192.802 207.424  1.00 15.01           N  
ATOM   1164  CA  THR C 998     196.618 194.018 208.246  1.00 13.30           C  
ATOM   1165  C   THR C 998     195.485 194.010 209.285  1.00 14.40           C  
ATOM   1166  O   THR C 998     195.657 194.562 210.365  1.00 16.74           O  
ATOM   1167  CB  THR C 998     196.515 195.231 207.325  1.00 19.00           C  
ATOM   1168  OG1 THR C 998     197.594 195.219 206.418  1.00 20.40           O  
ATOM   1169  CG2 THR C 998     196.548 196.541 208.097  1.00 14.21           C  
ATOM   1170  N   GLY C 999     194.356 193.345 209.047  1.00 13.12           N  
ATOM   1171  CA  GLY C 999     193.349 193.091 210.080  1.00 13.60           C  
ATOM   1172  C   GLY C 999     193.684 191.936 211.038  1.00 16.44           C  
ATOM   1173  O   GLY C 999     193.232 191.913 212.186  1.00 26.88           O  
ATOM   1174  N   ARG C1000     194.558 191.042 210.616  1.00 14.04           N  
ATOM   1175  CA  ARG C1000     195.062 190.051 211.551  1.00 11.08           C  
ATOM   1176  C   ARG C1000     196.206 190.661 212.398  1.00 16.05           C  
ATOM   1177  O   ARG C1000     196.438 190.219 213.517  1.00 27.42           O  
ATOM   1178  CB  ARG C1000     195.456 188.784 210.848  1.00 11.68           C  
ATOM   1179  CG  ARG C1000     194.241 187.926 210.611  1.00 20.60           C  
ATOM   1180  CD  ARG C1000     194.512 186.907 209.550  1.00 16.69           C  
ATOM   1181  NE  ARG C1000     193.513 185.856 209.553  1.00 25.11           N  
ATOM   1182  CZ  ARG C1000     193.643 184.729 210.236  1.00 27.27           C  
ATOM   1183  NH1 ARG C1000     194.724 184.513 210.965  1.00 28.68           N  
ATOM   1184  NH2 ARG C1000     192.691 183.822 210.194  1.00 30.38           N  
ATOM   1185  N   LEU C1001     196.920 191.659 211.868  1.00 14.74           N  
ATOM   1186  CA  LEU C1001     197.895 192.373 212.685  1.00  8.73           C  
ATOM   1187  C   LEU C1001     197.221 192.941 213.923  1.00 11.77           C  
ATOM   1188  O   LEU C1001     197.756 192.767 215.001  1.00 19.52           O  
ATOM   1189  CB  LEU C1001     198.599 193.492 211.905  1.00 12.66           C  
ATOM   1190  CG  LEU C1001     199.525 193.068 210.763  1.00 12.96           C  
ATOM   1191  CD1 LEU C1001     200.274 194.265 210.207  1.00 12.48           C  
ATOM   1192  CD2 LEU C1001     200.552 192.050 211.210  1.00 12.54           C  
ATOM   1193  N   GLN C1002     196.025 193.522 213.810  1.00 11.73           N  
ATOM   1194  CA  GLN C1002     195.301 194.089 214.956  1.00  9.80           C  
ATOM   1195  C   GLN C1002     194.868 193.022 215.957  1.00 17.63           C  
ATOM   1196  O   GLN C1002     194.860 193.244 217.163  1.00 24.82           O  
ATOM   1197  CB  GLN C1002     194.047 194.862 214.509  1.00 10.21           C  
ATOM   1198  CG  GLN C1002     194.208 195.784 213.300  1.00 13.83           C  
ATOM   1199  CD  GLN C1002     195.468 196.632 213.318  1.00 12.28           C  
ATOM   1200  OE1 GLN C1002     195.771 197.335 214.263  1.00 12.37           O  
ATOM   1201  NE2 GLN C1002     196.254 196.596 212.271  1.00  8.85           N  
ATOM   1202  N   SER C1003     194.514 191.836 215.471  1.00 20.46           N  
ATOM   1203  CA  SER C1003     194.190 190.697 216.336  1.00 16.68           C  
ATOM   1204  C   SER C1003     195.420 190.240 217.115  1.00 16.42           C  
ATOM   1205  O   SER C1003     195.334 190.010 218.310  1.00 23.63           O  
ATOM   1206  CB  SER C1003     193.616 189.544 215.516  1.00 28.56           C  
ATOM   1207  OG  SER C1003     192.454 189.934 214.810  1.00 39.32           O  
ATOM   1208  N   LEU C1004     196.591 190.172 216.489  1.00 16.52           N  
ATOM   1209  CA  LEU C1004     197.854 189.919 217.177  1.00 16.92           C  
ATOM   1210  C   LEU C1004     198.285 191.096 218.094  1.00 18.41           C  
ATOM   1211  O   LEU C1004     198.871 190.859 219.141  1.00 25.84           O  
ATOM   1212  CB  LEU C1004     198.909 189.567 216.122  1.00 16.66           C  
ATOM   1213  CG  LEU C1004     200.309 189.356 216.702  1.00 14.31           C  
ATOM   1214  CD1 LEU C1004     200.406 188.147 217.611  1.00 18.30           C  
ATOM   1215  CD2 LEU C1004     201.313 189.150 215.588  1.00 32.24           C  
ATOM   1216  N   GLN C1005     197.969 192.354 217.779  1.00 18.29           N  
ATOM   1217  CA  GLN C1005     198.227 193.496 218.665  1.00 11.98           C  
ATOM   1218  C   GLN C1005     197.270 193.552 219.869  1.00 20.86           C  
ATOM   1219  O   GLN C1005     197.673 193.953 220.957  1.00 27.50           O  
ATOM   1220  CB  GLN C1005     198.160 194.794 217.856  1.00 15.29           C  
ATOM   1221  CG  GLN C1005     198.771 195.969 218.616  1.00 16.51           C  
ATOM   1222  CD  GLN C1005     200.249 195.781 218.908  1.00 19.98           C  
ATOM   1223  OE1 GLN C1005     201.034 195.398 218.062  1.00 26.73           O  
ATOM   1224  NE2 GLN C1005     200.693 196.042 220.113  1.00 28.83           N  
ATOM   1225  N   THR C1006     196.032 193.076 219.733  1.00 22.61           N  
ATOM   1226  CA  THR C1006     195.145 192.797 220.870  1.00 16.87           C  
ATOM   1227  C   THR C1006     195.652 191.631 221.707  1.00 17.79           C  
ATOM   1228  O   THR C1006     195.614 191.715 222.929  1.00 25.43           O  
ATOM   1229  CB  THR C1006     193.720 192.536 220.406  1.00 22.55           C  
ATOM   1230  OG1 THR C1006     193.239 193.739 219.888  1.00 31.52           O  
ATOM   1231  CG2 THR C1006     192.752 192.141 221.517  1.00 23.78           C  
ATOM   1232  N   TYR C1007     196.207 190.591 221.084  1.00 19.19           N  
ATOM   1233  CA  TYR C1007     196.886 189.530 221.802  1.00 14.35           C  
ATOM   1234  C   TYR C1007     198.042 190.083 222.610  1.00 15.95           C  
ATOM   1235  O   TYR C1007     198.061 189.889 223.815  1.00 25.42           O  
ATOM   1236  CB  TYR C1007     197.314 188.425 220.845  1.00 19.89           C  
ATOM   1237  CG  TYR C1007     198.137 187.335 221.483  1.00 16.82           C  
ATOM   1238  CD1 TYR C1007     197.503 186.253 222.107  1.00 22.33           C  
ATOM   1239  CD2 TYR C1007     199.537 187.406 221.458  1.00 17.39           C  
ATOM   1240  CE1 TYR C1007     198.267 185.243 222.710  1.00 26.81           C  
ATOM   1241  CE2 TYR C1007     200.307 186.400 222.059  1.00 25.04           C  
ATOM   1242  CZ  TYR C1007     199.673 185.308 222.676  1.00 30.16           C  
ATOM   1243  OH  TYR C1007     200.411 184.285 223.175  1.00 35.10           O  
ATOM   1244  N   VAL C1008     198.961 190.831 222.006  1.00 12.14           N  
ATOM   1245  CA  VAL C1008     200.128 191.408 222.687  1.00 12.00           C  
ATOM   1246  C   VAL C1008     199.726 192.390 223.783  1.00 20.48           C  
ATOM   1247  O   VAL C1008     200.265 192.323 224.880  1.00 26.04           O  
ATOM   1248  CB  VAL C1008     201.062 192.039 221.642  1.00 18.34           C  
ATOM   1249  CG1 VAL C1008     202.076 193.041 222.189  1.00 13.57           C  
ATOM   1250  CG2 VAL C1008     201.823 190.911 220.942  1.00 23.13           C  
ATOM   1251  N   THR C1009     198.730 193.243 223.565  1.00 31.46           N  
ATOM   1252  CA  THR C1009     198.230 194.149 224.607  1.00 13.43           C  
ATOM   1253  C   THR C1009     197.650 193.391 225.800  1.00 11.35           C  
ATOM   1254  O   THR C1009     198.102 193.625 226.907  1.00 16.66           O  
ATOM   1255  CB  THR C1009     197.192 195.138 224.068  1.00 21.46           C  
ATOM   1256  OG1 THR C1009     197.678 195.830 222.941  1.00 26.68           O  
ATOM   1257  CG2 THR C1009     196.799 196.168 225.124  1.00 15.32           C  
ATOM   1258  N   GLN C1010     196.728 192.441 225.620  1.00 14.83           N  
ATOM   1259  CA  GLN C1010     196.171 191.628 226.714  1.00 14.98           C  
ATOM   1260  C   GLN C1010     197.211 190.731 227.417  1.00 17.05           C  
ATOM   1261  O   GLN C1010     197.047 190.418 228.591  1.00 18.90           O  
ATOM   1262  CB  GLN C1010     195.010 190.790 226.169  1.00 14.35           C  
ATOM   1263  CG  GLN C1010     193.715 191.585 225.973  1.00 24.82           C  
ATOM   1264  CD  GLN C1010     192.471 190.728 225.719  1.00 35.67           C  
ATOM   1265  OE1 GLN C1010     191.415 190.926 226.295  1.00 41.59           O  
ATOM   1266  NE2 GLN C1010     192.524 189.712 224.900  1.00 30.85           N  
ATOM   1267  N   GLN C1011     198.298 190.352 226.754  1.00 13.60           N  
ATOM   1268  CA  GLN C1011     199.414 189.615 227.337  1.00  9.62           C  
ATOM   1269  C   GLN C1011     200.395 190.520 228.096  1.00 13.24           C  
ATOM   1270  O   GLN C1011     201.030 190.053 229.036  1.00 18.32           O  
ATOM   1271  CB  GLN C1011     200.120 188.823 226.223  1.00 17.31           C  
ATOM   1272  CG  GLN C1011     200.683 187.473 226.666  1.00 20.80           C  
ATOM   1273  CD  GLN C1011     199.624 186.437 227.048  1.00 28.65           C  
ATOM   1274  OE1 GLN C1011     198.426 186.584 226.862  1.00 24.94           O  
ATOM   1275  NE2 GLN C1011     200.027 185.323 227.604  1.00 46.38           N  
ATOM   1276  N   LEU C1012     200.518 191.810 227.752  1.00 14.96           N  
ATOM   1277  CA  LEU C1012     201.260 192.803 228.536  1.00 12.27           C  
ATOM   1278  C   LEU C1012     200.431 193.331 229.706  1.00 14.30           C  
ATOM   1279  O   LEU C1012     200.947 193.491 230.802  1.00 16.93           O  
ATOM   1280  CB  LEU C1012     201.682 193.984 227.654  1.00 15.22           C  
ATOM   1281  CG  LEU C1012     202.722 193.679 226.567  1.00 15.60           C  
ATOM   1282  CD1 LEU C1012     202.954 194.953 225.765  1.00  9.18           C  
ATOM   1283  CD2 LEU C1012     204.047 193.208 227.139  1.00 38.32           C  
ATOM   1284  N   ILE C1013     199.136 193.560 229.505  1.00 15.55           N  
ATOM   1285  CA  ILE C1013     198.185 193.953 230.541  1.00  6.35           C  
ATOM   1286  C   ILE C1013     198.247 192.934 231.670  1.00 13.85           C  
ATOM   1287  O   ILE C1013     198.508 193.305 232.810  1.00 16.96           O  
ATOM   1288  CB  ILE C1013     196.776 194.093 229.916  1.00 11.24           C  
ATOM   1289  CG1 ILE C1013     196.617 195.400 229.107  1.00 11.71           C  
ATOM   1290  CG2 ILE C1013     195.611 193.932 230.900  1.00 20.21           C  
ATOM   1291  CD1 ILE C1013     196.408 196.681 229.914  1.00 15.63           C  
ATOM   1292  N   ARG C1014     198.109 191.634 231.375  1.00 13.10           N  
ATOM   1293  CA  ARG C1014     198.159 190.570 232.388  1.00 10.47           C  
ATOM   1294  C   ARG C1014     199.498 190.513 233.092  1.00 10.37           C  
ATOM   1295  O   ARG C1014     199.514 190.355 234.300  1.00 23.53           O  
ATOM   1296  CB  ARG C1014     197.774 189.226 231.764  1.00 12.66           C  
ATOM   1297  CG  ARG C1014     197.813 188.091 232.792  1.00 13.86           C  
ATOM   1298  CD  ARG C1014     197.436 186.744 232.177  1.00 27.52           C  
ATOM   1299  NE  ARG C1014     197.624 185.651 233.147  1.00 38.63           N  
ATOM   1300  CZ  ARG C1014     196.778 185.285 234.084  1.00 46.13           C  
ATOM   1301  NH1 ARG C1014     197.052 184.308 234.883  1.00 53.05           N  
ATOM   1302  NH2 ARG C1014     195.652 185.898 234.246  1.00 48.37           N  
ATOM   1303  N   ALA C1015     200.607 190.701 232.396  1.00 10.29           N  
ATOM   1304  CA  ALA C1015     201.926 190.729 233.025  1.00 11.12           C  
ATOM   1305  C   ALA C1015     202.174 191.943 233.959  1.00 15.54           C  
ATOM   1306  O   ALA C1015     202.913 191.835 234.935  1.00 26.48           O  
ATOM   1307  CB  ALA C1015     202.954 190.622 231.909  1.00 17.72           C  
ATOM   1308  N   ALA C1016     201.527 193.081 233.719  1.00 13.93           N  
ATOM   1309  CA  ALA C1016     201.508 194.220 234.633  1.00 14.19           C  
ATOM   1310  C   ALA C1016     200.525 194.063 235.819  1.00 13.29           C  
ATOM   1311  O   ALA C1016     200.727 194.691 236.859  1.00 22.99           O  
ATOM   1312  CB  ALA C1016     201.220 195.483 233.828  1.00 17.15           C  
ATOM   1313  N   GLU C1017     199.501 193.201 235.736  1.00 14.12           N  
ATOM   1314  CA  GLU C1017     198.787 192.688 236.918  1.00 13.90           C  
ATOM   1315  C   GLU C1017     199.626 191.670 237.693  1.00 16.20           C  
ATOM   1316  O   GLU C1017     199.703 191.741 238.912  1.00 25.11           O  
ATOM   1317  CB  GLU C1017     197.469 192.001 236.558  1.00 16.96           C  
ATOM   1318  CG  GLU C1017     196.449 192.940 235.933  1.00 27.18           C  
ATOM   1319  CD  GLU C1017     195.140 192.202 235.645  1.00 38.93           C  
ATOM   1320  OE1 GLU C1017     194.560 192.406 234.559  1.00 32.40           O  
ATOM   1321  OE2 GLU C1017     194.600 191.479 236.515  1.00 56.40           O1-
ATOM   1322  N   ILE C1018     200.305 190.746 237.021  1.00 11.96           N  
ATOM   1323  CA  ILE C1018     201.187 189.782 237.679  1.00 13.60           C  
ATOM   1324  C   ILE C1018     202.241 190.506 238.499  1.00 18.00           C  
ATOM   1325  O   ILE C1018     202.448 190.148 239.653  1.00 30.74           O  
ATOM   1326  CB  ILE C1018     201.829 188.843 236.648  1.00 16.62           C  
ATOM   1327  CG1 ILE C1018     200.789 187.877 236.062  1.00 16.99           C  
ATOM   1328  CG2 ILE C1018     203.056 188.091 237.175  1.00 24.62           C  
ATOM   1329  CD1 ILE C1018     200.490 186.637 236.891  1.00 27.66           C  
ATOM   1330  N   ARG C1019     202.873 191.564 237.976  1.00 19.64           N  
ATOM   1331  CA  ARG C1019     203.885 192.313 238.737  1.00 18.79           C  
ATOM   1332  C   ARG C1019     203.316 193.119 239.909  1.00 19.02           C  
ATOM   1333  O   ARG C1019     204.044 193.372 240.862  1.00 29.69           O  
ATOM   1334  CB  ARG C1019     204.765 193.128 237.780  1.00 26.76           C  
ATOM   1335  CG  ARG C1019     205.762 192.196 237.065  1.00 43.00           C  
ATOM   1336  CD  ARG C1019     206.837 192.885 236.216  1.00 41.13           C  
ATOM   1337  NE  ARG C1019     206.269 193.581 235.049  1.00 38.93           N  
ATOM   1338  CZ  ARG C1019     205.855 194.832 235.021  1.00 40.38           C  
ATOM   1339  NH1 ARG C1019     205.947 195.591 236.066  1.00 40.30           N  
ATOM   1340  NH2 ARG C1019     205.344 195.366 233.957  1.00 49.74           N  
ATOM   1341  N   ALA C1020     202.020 193.423 239.941  1.00 18.81           N  
ATOM   1342  CA  ALA C1020     201.352 193.942 241.140  1.00 18.74           C  
ATOM   1343  C   ALA C1020     201.015 192.831 242.140  1.00 23.57           C  
ATOM   1344  O   ALA C1020     201.116 193.034 243.343  1.00 32.95           O  
ATOM   1345  CB  ALA C1020     200.087 194.698 240.740  1.00 22.51           C  
ATOM   1346  N   SER C1021     200.668 191.634 241.670  1.00 21.09           N  
ATOM   1347  CA  SER C1021     200.450 190.456 242.514  1.00 16.80           C  
ATOM   1348  C   SER C1021     201.747 189.929 243.139  1.00 18.07           C  
ATOM   1349  O   SER C1021     201.728 189.429 244.252  1.00 27.77           O  
ATOM   1350  CB  SER C1021     199.737 189.394 241.691  1.00 19.00           C  
ATOM   1351  OG  SER C1021     199.487 188.241 242.447  1.00 24.98           O  
ATOM   1352  N   ALA C1022     202.899 190.124 242.504  1.00 18.67           N  
ATOM   1353  CA  ALA C1022     204.215 189.941 243.109  1.00 21.53           C  
ATOM   1354  C   ALA C1022     204.598 191.030 244.141  1.00 25.92           C  
ATOM   1355  O   ALA C1022     205.292 190.734 245.113  1.00 33.34           O  
ATOM   1356  CB  ALA C1022     205.235 189.893 241.979  1.00 26.67           C  
ATOM   1357  N   ASN C1023     204.106 192.267 244.008  1.00 25.24           N  
ATOM   1358  CA  ASN C1023     204.135 193.239 245.106  1.00 21.69           C  
ATOM   1359  C   ASN C1023     203.169 192.881 246.240  1.00 22.37           C  
ATOM   1360  O   ASN C1023     203.546 193.026 247.398  1.00 29.60           O  
ATOM   1361  CB  ASN C1023     203.825 194.652 244.597  1.00 31.08           C  
ATOM   1362  CG  ASN C1023     205.009 195.367 244.017  1.00 40.02           C  
ATOM   1363  OD1 ASN C1023     206.075 194.837 243.835  1.00 39.83           O  
ATOM   1364  ND2 ASN C1023     204.862 196.629 243.729  1.00 41.47           N  
ATOM   1365  N   LEU C1024     201.968 192.371 245.955  1.00 23.17           N  
ATOM   1366  CA  LEU C1024     201.061 191.883 246.988  1.00 18.04           C  
ATOM   1367  C   LEU C1024     201.675 190.698 247.727  1.00 16.36           C  
ATOM   1368  O   LEU C1024     201.643 190.668 248.944  1.00 23.99           O  
ATOM   1369  CB  LEU C1024     199.692 191.529 246.401  1.00 20.73           C  
ATOM   1370  CG  LEU C1024     198.644 191.158 247.459  1.00 14.16           C  
ATOM   1371  CD1 LEU C1024     198.291 192.329 248.370  1.00 20.25           C  
ATOM   1372  CD2 LEU C1024     197.374 190.679 246.763  1.00 13.56           C  
ATOM   1373  N   ALA C1025     202.296 189.749 247.033  1.00 17.47           N  
ATOM   1374  CA  ALA C1025     203.038 188.661 247.639  1.00 18.56           C  
ATOM   1375  C   ALA C1025     204.211 189.156 248.480  1.00 20.13           C  
ATOM   1376  O   ALA C1025     204.541 188.489 249.444  1.00 28.09           O  
ATOM   1377  CB  ALA C1025     203.533 187.744 246.525  1.00 24.23           C  
ATOM   1378  N   ALA C1026     204.820 190.306 248.184  1.00 20.60           N  
ATOM   1379  CA  ALA C1026     205.905 190.864 248.998  1.00 20.07           C  
ATOM   1380  C   ALA C1026     205.404 191.435 250.331  1.00 24.74           C  
ATOM   1381  O   ALA C1026     205.895 191.045 251.385  1.00 31.30           O  
ATOM   1382  CB  ALA C1026     206.676 191.924 248.204  1.00 35.13           C  
ATOM   1383  N   THR C1027     204.400 192.316 250.306  1.00 23.41           N  
ATOM   1384  CA  THR C1027     203.787 192.868 251.526  1.00 19.60           C  
ATOM   1385  C   THR C1027     203.095 191.776 252.344  1.00 21.94           C  
ATOM   1386  O   THR C1027     203.328 191.675 253.543  1.00 31.78           O  
ATOM   1387  CB  THR C1027     202.862 194.049 251.212  1.00 20.00           C  
ATOM   1388  OG1 THR C1027     202.204 194.506 252.354  1.00 30.19           O  
ATOM   1389  CG2 THR C1027     201.714 193.735 250.264  1.00 31.37           C  
ATOM   1390  N   LYS C1028     202.334 190.874 251.718  1.00 22.02           N  
ATOM   1391  CA  LYS C1028     201.644 189.751 252.373  1.00 20.19           C  
ATOM   1392  C   LYS C1028     202.590 188.656 252.895  1.00 21.38           C  
ATOM   1393  O   LYS C1028     202.257 187.991 253.866  1.00 34.35           O  
ATOM   1394  CB  LYS C1028     200.606 189.201 251.386  1.00 15.90           C  
ATOM   1395  CG  LYS C1028     199.661 188.219 252.058  1.00 16.30           C  
ATOM   1396  CD  LYS C1028     198.405 187.861 251.268  1.00 19.84           C  
ATOM   1397  CE  LYS C1028     197.457 189.053 251.195  1.00 21.71           C  
ATOM   1398  NZ  LYS C1028     196.098 188.635 250.773  1.00 23.73           N  
ATOM   1399  N   MET C1029     203.780 188.476 252.325  1.00 20.04           N  
ATOM   1400  CA  MET C1029     204.855 187.693 252.942  1.00 24.52           C  
ATOM   1401  C   MET C1029     205.386 188.432 254.154  1.00 34.09           C  
ATOM   1402  O   MET C1029     205.448 187.870 255.237  1.00 48.25           O  
ATOM   1403  CB  MET C1029     205.989 187.449 251.935  1.00 25.67           C  
ATOM   1404  CG  MET C1029     207.289 186.878 252.509  1.00 35.13           C  
ATOM   1405  SD  MET C1029     207.340 185.080 252.591  1.00 64.02           S  
ATOM   1406  CE  MET C1029     209.015 184.874 253.260  1.00 72.20           C  
ATOM   1407  N   SER C1030     205.768 189.694 253.996  1.00 33.73           N  
ATOM   1408  CA  SER C1030     206.455 190.434 255.048  1.00 32.61           C  
ATOM   1409  C   SER C1030     205.614 190.573 256.307  1.00 30.79           C  
ATOM   1410  O   SER C1030     206.025 190.142 257.375  1.00 37.64           O  
ATOM   1411  CB  SER C1030     206.867 191.797 254.528  1.00 36.01           C  
ATOM   1412  OG  SER C1030     207.630 192.420 255.516  1.00 42.70           O  
ATOM   1413  N   GLU C1031     204.406 191.104 256.200  1.00 29.08           N  
ATOM   1414  CA  GLU C1031     203.580 191.464 257.355  1.00 31.47           C  
ATOM   1415  C   GLU C1031     203.004 190.283 258.124  1.00 32.00           C  
ATOM   1416  O   GLU C1031     202.418 190.480 259.186  1.00 38.87           O  
ATOM   1417  CB  GLU C1031     202.464 192.399 256.892  1.00 31.29           C  
ATOM   1418  CG  GLU C1031     203.061 193.756 256.526  1.00 31.69           C  
ATOM   1419  CD  GLU C1031     202.103 194.613 255.706  1.00 35.59           C  
ATOM   1420  OE1 GLU C1031     200.871 194.579 255.921  1.00 42.78           O  
ATOM   1421  OE2 GLU C1031     202.609 195.410 254.883  1.00 37.70           O1-
ATOM   1422  N   CYS C1032     203.149 189.060 257.613  1.00 29.30           N  
ATOM   1423  CA  CYS C1032     202.422 187.890 258.111  1.00 39.64           C  
ATOM   1424  C   CYS C1032     203.258 186.611 258.265  1.00 47.30           C  
ATOM   1425  O   CYS C1032     202.921 185.746 259.074  1.00 51.01           O  
ATOM   1426  CB  CYS C1032     201.227 187.669 257.193  1.00 28.96           C  
ATOM   1427  SG  CYS C1032     200.292 189.214 257.096  1.00 38.85           S  
ATOM   1428  N   VAL C1033     204.362 186.504 257.528  1.00 38.08           N  
ATOM   1429  CA  VAL C1033     205.417 185.525 257.773  1.00 35.49           C  
ATOM   1430  C   VAL C1033     206.485 186.110 258.686  1.00 46.31           C  
ATOM   1431  O   VAL C1033     206.913 185.419 259.607  1.00 56.11           O  
ATOM   1432  CB  VAL C1033     206.026 184.990 256.469  1.00 36.59           C  
ATOM   1433  CG1 VAL C1033     207.083 183.919 256.727  1.00 45.43           C  
ATOM   1434  CG2 VAL C1033     204.924 184.404 255.582  1.00 40.18           C  
ATOM   1435  N   LEU C1034     206.900 187.373 258.512  1.00 43.50           N  
ATOM   1436  CA  LEU C1034     207.881 188.008 259.413  1.00 36.09           C  
ATOM   1437  C   LEU C1034     207.220 188.697 260.614  1.00 37.40           C  
ATOM   1438  O   LEU C1034     207.899 188.993 261.593  1.00 40.85           O  
ATOM   1439  CB  LEU C1034     208.793 188.992 258.655  1.00 43.01           C  
ATOM   1440  CG  LEU C1034     209.451 188.429 257.383  1.00 51.31           C  
ATOM   1441  CD1 LEU C1034     210.200 189.545 256.665  1.00 48.72           C  
ATOM   1442  CD2 LEU C1034     210.445 187.314 257.704  1.00 56.00           C  
ATOM   1443  N   GLY C1035     205.911 188.934 260.549  1.00 33.01           N  
ATOM   1444  CA  GLY C1035     205.127 189.685 261.525  1.00 34.07           C  
ATOM   1445  C   GLY C1035     203.838 188.998 261.954  1.00 36.01           C  
ATOM   1446  O   GLY C1035     203.697 187.785 261.865  1.00 40.40           O  
ATOM   1447  N   GLN C1036     202.881 189.782 262.429  1.00 30.23           N  
ATOM   1448  CA  GLN C1036     201.505 189.364 262.660  1.00 34.55           C  
ATOM   1449  C   GLN C1036     200.611 190.570 262.416  1.00 35.15           C  
ATOM   1450  O   GLN C1036     200.726 191.574 263.123  1.00 35.62           O  
ATOM   1451  CB  GLN C1036     201.343 188.831 264.080  1.00 36.57           C  
ATOM   1452  CG  GLN C1036     199.888 188.541 264.466  1.00 40.31           C  
ATOM   1453  CD  GLN C1036     199.752 188.193 265.935  1.00 36.59           C  
ATOM   1454  OE1 GLN C1036     200.521 188.609 266.785  1.00 49.62           O  
ATOM   1455  NE2 GLN C1036     198.749 187.443 266.303  1.00 33.43           N  
ATOM   1456  N   SER C1037     199.752 190.490 261.408  1.00 34.85           N  
ATOM   1457  CA  SER C1037     198.954 191.631 260.988  1.00 36.30           C  
ATOM   1458  C   SER C1037     197.771 191.891 261.918  1.00 40.93           C  
ATOM   1459  O   SER C1037     197.152 190.964 262.436  1.00 41.06           O  
ATOM   1460  CB  SER C1037     198.486 191.479 259.549  1.00 39.04           C  
ATOM   1461  OG  SER C1037     198.012 192.738 259.133  1.00 38.02           O  
ATOM   1462  N   LYS C1038     197.436 193.168 262.120  1.00 41.81           N  
ATOM   1463  CA  LYS C1038     196.282 193.617 262.923  1.00 40.39           C  
ATOM   1464  C   LYS C1038     195.054 193.950 262.058  1.00 50.76           C  
ATOM   1465  O   LYS C1038     194.033 194.388 262.582  1.00 51.94           O  
ATOM   1466  CB  LYS C1038     196.743 194.767 263.838  1.00 40.30           C  
ATOM   1467  CG  LYS C1038     197.758 194.247 264.882  1.00 44.48           C  
ATOM   1468  CD  LYS C1038     198.708 195.327 265.405  1.00 46.40           C  
ATOM   1469  CE  LYS C1038     199.949 194.724 266.092  1.00 38.37           C  
ATOM   1470  NZ  LYS C1038     200.887 194.060 265.143  1.00 41.96           N  
ATOM   1471  N   ARG C1039     195.161 193.695 260.746  1.00 45.05           N  
ATOM   1472  CA  ARG C1039     194.109 193.940 259.762  1.00 37.82           C  
ATOM   1473  C   ARG C1039     193.157 192.747 259.695  1.00 34.85           C  
ATOM   1474  O   ARG C1039     193.569 191.610 259.908  1.00 31.87           O  
ATOM   1475  CB  ARG C1039     194.757 194.180 258.401  1.00 42.62           C  
ATOM   1476  CG  ARG C1039     195.581 195.456 258.340  1.00 45.29           C  
ATOM   1477  CD  ARG C1039     196.691 195.382 257.303  1.00 48.48           C  
ATOM   1478  NE  ARG C1039     196.181 195.210 255.948  1.00 49.44           N  
ATOM   1479  CZ  ARG C1039     196.880 195.499 254.857  1.00 49.68           C  
ATOM   1480  NH1 ARG C1039     198.115 195.968 254.961  1.00 52.93           N  
ATOM   1481  NH2 ARG C1039     196.345 195.319 253.660  1.00 50.83           N  
ATOM   1482  N   VAL C1040     191.887 193.002 259.394  1.00 32.13           N  
ATOM   1483  CA  VAL C1040     190.868 191.955 259.384  1.00 29.80           C  
ATOM   1484  C   VAL C1040     190.631 191.453 257.958  1.00 47.12           C  
ATOM   1485  O   VAL C1040     190.262 192.262 257.102  1.00 57.94           O  
ATOM   1486  CB  VAL C1040     189.534 192.485 259.936  1.00 26.66           C  
ATOM   1487  CG1 VAL C1040     188.480 191.390 259.918  1.00 33.58           C  
ATOM   1488  CG2 VAL C1040     189.724 193.024 261.345  1.00 43.59           C  
ATOM   1489  N   ASP C1041     190.910 190.161 257.700  1.00 44.75           N  
ATOM   1490  CA  ASP C1041     190.803 189.410 256.412  1.00 39.84           C  
ATOM   1491  C   ASP C1041     192.028 189.526 255.477  1.00 46.65           C  
ATOM   1492  O   ASP C1041     192.077 188.853 254.448  1.00 57.88           O  
ATOM   1493  CB  ASP C1041     189.465 189.532 255.643  1.00 41.75           C  
ATOM   1494  CG  ASP C1041     188.253 189.475 256.557  1.00 53.55           C  
ATOM   1495  OD1 ASP C1041     187.153 189.866 256.114  1.00 54.57           O  
ATOM   1496  OD2 ASP C1041     188.404 189.040 257.718  1.00 58.75           O1-
ATOM   1497  N   PHE C1042     193.008 190.362 255.823  1.00 46.54           N  
ATOM   1498  CA  PHE C1042     194.279 190.370 255.117  1.00 36.43           C  
ATOM   1499  C   PHE C1042     194.957 189.170 255.819  1.00 40.17           C  
ATOM   1500  O   PHE C1042     194.843 189.019 257.065  1.00 48.86           O  
ATOM   1501  CB  PHE C1042     195.060 191.654 255.344  1.00 34.46           C  
ATOM   1502  CG  PHE C1042     196.367 191.706 254.604  1.00 39.45           C  
ATOM   1503  CD1 PHE C1042     196.413 192.088 253.274  1.00 57.80           C  
ATOM   1504  CD2 PHE C1042     197.551 191.373 255.242  1.00 34.77           C  
ATOM   1505  CE1 PHE C1042     197.615 192.136 252.594  1.00 44.53           C  
ATOM   1506  CE2 PHE C1042     198.756 191.419 254.568  1.00 31.62           C  
ATOM   1507  CZ  PHE C1042     198.788 191.801 253.241  1.00 35.77           C  
ATOM   1508  N   CYS C1043     195.684 188.326 255.095  1.00 38.80           N  
ATOM   1509  CA  CYS C1043     196.313 187.123 255.689  1.00 31.89           C  
ATOM   1510  C   CYS C1043     195.235 186.138 256.303  1.00 34.97           C  
ATOM   1511  O   CYS C1043     195.305 185.789 257.481  1.00 40.54           O  
ATOM   1512  CB  CYS C1043     197.560 187.438 256.641  1.00 27.00           C  
ATOM   1513  SG  CYS C1043     198.986 188.217 255.801  1.00 31.48           S  
ATOM   1514  N   GLY C1044     194.258 185.713 255.471  1.00 39.93           N  
ATOM   1515  CA  GLY C1044     193.282 184.693 255.810  1.00 44.46           C  
ATOM   1516  C   GLY C1044     192.030 185.280 256.413  1.00 47.73           C  
ATOM   1517  O   GLY C1044     192.069 186.351 257.002  1.00 53.08           O  
ATOM   1518  N   LYS C1045     190.889 184.606 256.264  1.00 52.45           N  
ATOM   1519  CA  LYS C1045     189.629 185.098 256.837  1.00 52.50           C  
ATOM   1520  C   LYS C1045     189.770 185.280 258.359  1.00 51.24           C  
ATOM   1521  O   LYS C1045     190.391 184.450 259.022  1.00 57.38           O  
ATOM   1522  CB  LYS C1045     188.500 184.140 256.445  1.00 64.22           C  
ATOM   1523  CG  LYS C1045     187.111 184.708 256.723  1.00 64.42           C  
ATOM   1524  CD  LYS C1045     186.030 183.681 256.394  1.00 65.38           C  
ATOM   1525  CE  LYS C1045     184.655 184.308 256.630  1.00 64.25           C  
ATOM   1526  NZ  LYS C1045     183.549 183.378 256.326  1.00 52.01           N  
ATOM   1527  N   GLY C1046     189.181 186.336 258.911  1.00 49.02           N  
ATOM   1528  CA  GLY C1046     189.211 186.648 260.339  1.00 44.13           C  
ATOM   1529  C   GLY C1046     190.433 187.460 260.762  1.00 41.33           C  
ATOM   1530  O   GLY C1046     190.794 188.429 260.092  1.00 43.31           O  
ATOM   1531  N   TYR C1047     191.016 187.087 261.903  1.00 37.04           N  
ATOM   1532  CA  TYR C1047     192.113 187.774 262.589  1.00 32.41           C  
ATOM   1533  C   TYR C1047     193.356 186.892 262.642  1.00 34.29           C  
ATOM   1534  O   TYR C1047     193.271 185.689 262.856  1.00 45.12           O  
ATOM   1535  CB  TYR C1047     191.671 188.178 263.995  1.00 33.14           C  
ATOM   1536  CG  TYR C1047     190.455 189.068 264.020  1.00 32.94           C  
ATOM   1537  CD1 TYR C1047     189.166 188.504 264.065  1.00 29.62           C  
ATOM   1538  CD2 TYR C1047     190.620 190.459 263.926  1.00 34.32           C  
ATOM   1539  CE1 TYR C1047     188.039 189.331 263.947  1.00 35.58           C  
ATOM   1540  CE2 TYR C1047     189.493 191.285 263.803  1.00 41.51           C  
ATOM   1541  CZ  TYR C1047     188.203 190.722 263.785  1.00 44.76           C  
ATOM   1542  OH  TYR C1047     187.118 191.520 263.634  1.00 52.70           O  
ATOM   1543  N   HIS C1048     194.526 187.476 262.427  1.00 28.65           N  
ATOM   1544  CA  HIS C1048     195.751 186.726 262.160  1.00 32.76           C  
ATOM   1545  C   HIS C1048     196.478 186.232 263.409  1.00 40.06           C  
ATOM   1546  O   HIS C1048     196.697 186.973 264.363  1.00 45.32           O  
ATOM   1547  CB  HIS C1048     196.650 187.609 261.300  1.00 37.69           C  
ATOM   1548  CG  HIS C1048     197.917 186.956 260.844  1.00 35.74           C  
ATOM   1549  ND1 HIS C1048     199.196 187.402 261.151  1.00 35.19           N  
ATOM   1550  CD2 HIS C1048     198.012 185.899 260.000  1.00 33.70           C  
ATOM   1551  CE1 HIS C1048     200.040 186.579 260.532  1.00 38.15           C  
ATOM   1552  NE2 HIS C1048     199.355 185.693 259.813  1.00 35.99           N  
ATOM   1553  N   LEU C1049     196.924 184.983 263.380  1.00 38.84           N  
ATOM   1554  CA  LEU C1049     197.851 184.436 264.365  1.00 40.01           C  
ATOM   1555  C   LEU C1049     199.243 184.283 263.773  1.00 42.95           C  
ATOM   1556  O   LEU C1049     200.204 184.809 264.321  1.00 43.03           O  
ATOM   1557  CB  LEU C1049     197.326 183.106 264.941  1.00 42.24           C  
ATOM   1558  CG  LEU C1049     196.023 183.240 265.750  1.00 36.56           C  
ATOM   1559  CD1 LEU C1049     195.390 181.870 265.927  1.00 33.02           C  
ATOM   1560  CD2 LEU C1049     196.291 183.848 267.121  1.00 35.19           C  
ATOM   1561  N   MET C1050     199.368 183.523 262.695  1.00 39.85           N  
ATOM   1562  CA  MET C1050     200.662 183.028 262.230  1.00 45.70           C  
ATOM   1563  C   MET C1050     200.583 182.584 260.772  1.00 49.30           C  
ATOM   1564  O   MET C1050     199.493 182.294 260.288  1.00 50.72           O  
ATOM   1565  CB  MET C1050     201.029 181.852 263.133  1.00 52.28           C  
ATOM   1566  CG  MET C1050     202.501 181.475 263.121  1.00 50.97           C  
ATOM   1567  SD  MET C1050     202.859 180.265 264.400  1.00 57.36           S  
ATOM   1568  CE  MET C1050     202.786 181.289 265.879  1.00 59.74           C  
ATOM   1569  N   SER C1051     201.692 182.492 260.036  1.00 51.53           N  
ATOM   1570  CA  SER C1051     201.660 181.991 258.650  1.00 42.38           C  
ATOM   1571  C   SER C1051     202.912 181.267 258.186  1.00 44.16           C  
ATOM   1572  O   SER C1051     204.002 181.482 258.709  1.00 48.48           O  
ATOM   1573  CB  SER C1051     201.377 183.100 257.641  1.00 41.19           C  
ATOM   1574  OG  SER C1051     200.165 183.714 257.968  1.00 47.13           O  
ATOM   1575  N   PHE C1052     202.727 180.447 257.154  1.00 41.98           N  
ATOM   1576  CA  PHE C1052     203.733 179.577 256.567  1.00 46.93           C  
ATOM   1577  C   PHE C1052     203.604 179.636 255.029  1.00 50.15           C  
ATOM   1578  O   PHE C1052     202.595 179.196 254.472  1.00 52.19           O  
ATOM   1579  CB  PHE C1052     203.551 178.150 257.112  1.00 52.29           C  
ATOM   1580  CG  PHE C1052     203.243 178.077 258.598  1.00 51.18           C  
ATOM   1581  CD1 PHE C1052     204.271 178.304 259.527  1.00 50.11           C  
ATOM   1582  CD2 PHE C1052     201.925 177.862 259.046  1.00 55.69           C  
ATOM   1583  CE1 PHE C1052     203.983 178.314 260.897  1.00 45.62           C  
ATOM   1584  CE2 PHE C1052     201.644 177.869 260.422  1.00 47.87           C  
ATOM   1585  CZ  PHE C1052     202.674 178.098 261.345  1.00 49.12           C  
ATOM   1586  N   PRO C1053     204.558 180.247 254.313  1.00 47.04           N  
ATOM   1587  CA  PRO C1053     204.533 180.317 252.866  1.00 44.24           C  
ATOM   1588  C   PRO C1053     205.046 179.007 252.263  1.00 52.22           C  
ATOM   1589  O   PRO C1053     205.962 178.372 252.783  1.00 64.66           O  
ATOM   1590  CB  PRO C1053     205.431 181.501 252.512  1.00 51.79           C  
ATOM   1591  CG  PRO C1053     206.505 181.410 253.584  1.00 50.51           C  
ATOM   1592  CD  PRO C1053     205.752 180.905 254.812  1.00 53.73           C  
ATOM   1593  N   GLN C1054     204.513 178.630 251.119  1.00 52.65           N  
ATOM   1594  CA  GLN C1054     205.017 177.550 250.292  1.00 53.80           C  
ATOM   1595  C   GLN C1054     204.999 177.994 248.835  1.00 58.50           C  
ATOM   1596  O   GLN C1054     204.127 178.741 248.398  1.00 62.20           O  
ATOM   1597  CB  GLN C1054     204.225 176.263 250.557  1.00 55.49           C  
ATOM   1598  CG  GLN C1054     202.761 176.337 250.112  1.00 58.75           C  
ATOM   1599  CD  GLN C1054     201.909 175.251 250.747  1.00 55.94           C  
ATOM   1600  OE1 GLN C1054     201.855 175.078 251.949  1.00 53.63           O  
ATOM   1601  NE2 GLN C1054     201.173 174.492 249.981  1.00 57.90           N  
ATOM   1602  N   SER C1055     205.996 177.576 248.073  1.00 64.72           N  
ATOM   1603  CA  SER C1055     206.073 177.893 246.653  1.00 59.27           C  
ATOM   1604  C   SER C1055     205.087 177.065 245.827  1.00 60.69           C  
ATOM   1605  O   SER C1055     204.599 176.012 246.235  1.00 57.15           O  
ATOM   1606  CB  SER C1055     207.512 177.706 246.164  1.00 59.11           C  
ATOM   1607  OG  SER C1055     207.973 176.393 246.401  1.00 69.62           O  
ATOM   1608  N   ALA C1056     204.831 177.563 244.627  1.00 57.73           N  
ATOM   1609  CA  ALA C1056     204.179 176.915 243.499  1.00 65.43           C  
ATOM   1610  C   ALA C1056     204.962 177.325 242.225  1.00 67.52           C  
ATOM   1611  O   ALA C1056     205.804 178.226 242.315  1.00 71.87           O  
ATOM   1612  CB  ALA C1056     202.703 177.340 243.503  1.00 56.80           C  
ATOM   1613  N   PRO C1057     204.761 176.702 241.051  1.00 62.81           N  
ATOM   1614  CA  PRO C1057     205.644 176.882 239.895  1.00 59.61           C  
ATOM   1615  C   PRO C1057     205.865 178.338 239.460  1.00 62.62           C  
ATOM   1616  O   PRO C1057     206.986 178.713 239.122  1.00 67.03           O  
ATOM   1617  CB  PRO C1057     205.014 176.060 238.772  1.00 63.86           C  
ATOM   1618  CG  PRO C1057     204.209 174.992 239.505  1.00 56.90           C  
ATOM   1619  CD  PRO C1057     203.755 175.691 240.774  1.00 64.26           C  
ATOM   1620  N   HIS C1058     204.822 179.171 239.529  1.00 58.70           N  
ATOM   1621  CA  HIS C1058     204.854 180.617 239.236  1.00 60.48           C  
ATOM   1622  C   HIS C1058     204.163 181.445 240.327  1.00 60.03           C  
ATOM   1623  O   HIS C1058     203.599 182.510 240.087  1.00 56.97           O  
ATOM   1624  CB  HIS C1058     204.272 180.883 237.834  1.00 62.78           C  
ATOM   1625  CG  HIS C1058     205.240 180.581 236.725  1.00 59.39           C  
ATOM   1626  ND1 HIS C1058     206.241 181.448 236.281  1.00 55.91           N  
ATOM   1627  CD2 HIS C1058     205.325 179.414 236.033  1.00 56.56           C  
ATOM   1628  CE1 HIS C1058     206.912 180.777 235.331  1.00 54.01           C  
ATOM   1629  NE2 HIS C1058     206.380 179.557 235.162  1.00 53.74           N  
ATOM   1630  N   GLY C1059     204.142 180.944 241.556  1.00 61.06           N  
ATOM   1631  CA  GLY C1059     203.326 181.521 242.616  1.00 53.48           C  
ATOM   1632  C   GLY C1059     203.902 181.345 244.008  1.00 56.58           C  
ATOM   1633  O   GLY C1059     204.868 180.616 244.249  1.00 60.34           O  
ATOM   1634  N   VAL C1060     203.236 181.993 244.948  1.00 51.74           N  
ATOM   1635  CA  VAL C1060     203.358 181.739 246.373  1.00 46.55           C  
ATOM   1636  C   VAL C1060     201.985 181.364 246.886  1.00 47.54           C  
ATOM   1637  O   VAL C1060     200.974 181.900 246.449  1.00 50.79           O  
ATOM   1638  CB  VAL C1060     203.975 182.939 247.110  1.00 47.06           C  
ATOM   1639  CG1 VAL C1060     203.042 184.141 247.203  1.00 51.52           C  
ATOM   1640  CG2 VAL C1060     204.424 182.567 248.527  1.00 54.11           C  
ATOM   1641  N   VAL C1061     201.945 180.424 247.808  1.00 45.40           N  
ATOM   1642  CA  VAL C1061     200.745 180.014 248.509  1.00 46.42           C  
ATOM   1643  C   VAL C1061     201.006 180.210 249.984  1.00 52.44           C  
ATOM   1644  O   VAL C1061     202.052 179.817 250.490  1.00 58.93           O  
ATOM   1645  CB  VAL C1061     200.357 178.568 248.180  1.00 44.09           C  
ATOM   1646  CG1 VAL C1061     199.096 178.148 248.930  1.00 50.41           C  
ATOM   1647  CG2 VAL C1061     200.121 178.394 246.683  1.00 49.27           C  
ATOM   1648  N   PHE C1062     200.076 180.830 250.692  1.00 42.22           N  
ATOM   1649  CA  PHE C1062     200.184 181.035 252.127  1.00 40.34           C  
ATOM   1650  C   PHE C1062     199.236 180.097 252.852  1.00 46.37           C  
ATOM   1651  O   PHE C1062     198.054 180.035 252.524  1.00 53.65           O  
ATOM   1652  CB  PHE C1062     199.889 182.483 252.488  1.00 41.91           C  
ATOM   1653  CG  PHE C1062     200.791 183.479 251.799  1.00 38.27           C  
ATOM   1654  CD1 PHE C1062     202.107 183.674 252.249  1.00 34.59           C  
ATOM   1655  CD2 PHE C1062     200.330 184.177 250.673  1.00 43.74           C  
ATOM   1656  CE1 PHE C1062     202.951 184.579 251.586  1.00 35.04           C  
ATOM   1657  CE2 PHE C1062     201.170 185.092 250.022  1.00 35.77           C  
ATOM   1658  CZ  PHE C1062     202.478 185.295 250.482  1.00 31.59           C  
ATOM   1659  N   LEU C1063     199.761 179.407 253.860  1.00 43.50           N  
ATOM   1660  CA  LEU C1063     198.985 178.859 254.954  1.00 52.24           C  
ATOM   1661  C   LEU C1063     198.888 179.932 256.034  1.00 53.35           C  
ATOM   1662  O   LEU C1063     199.876 180.207 256.704  1.00 50.21           O  
ATOM   1663  CB  LEU C1063     199.692 177.617 255.505  1.00 58.02           C  
ATOM   1664  CG  LEU C1063     199.785 176.455 254.512  1.00 59.97           C  
ATOM   1665  CD1 LEU C1063     200.736 175.401 255.074  1.00 68.46           C  
ATOM   1666  CD2 LEU C1063     198.416 175.809 254.298  1.00 66.52           C  
ATOM   1667  N   HIS C1064     197.729 180.551 256.208  1.00 46.38           N  
ATOM   1668  CA  HIS C1064     197.492 181.488 257.302  1.00 43.24           C  
ATOM   1669  C   HIS C1064     196.725 180.785 258.387  1.00 57.58           C  
ATOM   1670  O   HIS C1064     195.690 180.200 258.102  1.00 64.57           O  
ATOM   1671  CB  HIS C1064     196.661 182.700 256.890  1.00 39.15           C  
ATOM   1672  CG  HIS C1064     197.070 183.339 255.609  1.00 35.26           C  
ATOM   1673  ND1 HIS C1064     196.278 183.377 254.478  1.00 41.89           N  
ATOM   1674  CD2 HIS C1064     198.190 184.064 255.391  1.00 32.02           C  
ATOM   1675  CE1 HIS C1064     196.945 184.132 253.608  1.00 38.97           C  
ATOM   1676  NE2 HIS C1064     198.101 184.543 254.119  1.00 35.52           N  
ATOM   1677  N   VAL C1065     197.178 180.893 259.628  1.00 51.32           N  
ATOM   1678  CA  VAL C1065     196.416 180.456 260.785  1.00 45.69           C  
ATOM   1679  C   VAL C1065     195.776 181.666 261.420  1.00 48.34           C  
ATOM   1680  O   VAL C1065     196.461 182.631 261.754  1.00 54.02           O  
ATOM   1681  CB  VAL C1065     197.288 179.712 261.792  1.00 42.80           C  
ATOM   1682  CG1 VAL C1065     196.375 179.111 262.855  1.00 47.94           C  
ATOM   1683  CG2 VAL C1065     198.095 178.599 261.126  1.00 47.24           C  
ATOM   1684  N   THR C1066     194.459 181.620 261.568  1.00 49.98           N  
ATOM   1685  CA  THR C1066     193.617 182.767 261.909  1.00 48.89           C  
ATOM   1686  C   THR C1066     192.436 182.329 262.773  1.00 53.90           C  
ATOM   1687  O   THR C1066     192.041 181.169 262.756  1.00 64.15           O  
ATOM   1688  CB  THR C1066     193.093 183.475 260.642  1.00 50.54           C  
ATOM   1689  OG1 THR C1066     192.221 182.678 259.894  1.00 56.84           O  
ATOM   1690  CG2 THR C1066     194.164 183.885 259.653  1.00 47.75           C  
ATOM   1691  N   TYR C1067     191.829 183.238 263.523  1.00 42.32           N  
ATOM   1692  CA  TYR C1067     190.552 182.975 264.182  1.00 37.32           C  
ATOM   1693  C   TYR C1067     189.438 183.823 263.571  1.00 45.50           C  
ATOM   1694  O   TYR C1067     189.601 185.017 263.326  1.00 49.66           O  
ATOM   1695  CB  TYR C1067     190.679 183.094 265.704  1.00 44.90           C  
ATOM   1696  CG  TYR C1067     191.191 184.405 266.260  1.00 42.78           C  
ATOM   1697  CD1 TYR C1067     190.303 185.451 266.521  1.00 42.10           C  
ATOM   1698  CD2 TYR C1067     192.557 184.571 266.531  1.00 37.54           C  
ATOM   1699  CE1 TYR C1067     190.774 186.676 267.007  1.00 34.99           C  
ATOM   1700  CE2 TYR C1067     193.042 185.800 267.006  1.00 29.19           C  
ATOM   1701  CZ  TYR C1067     192.148 186.866 267.223  1.00 28.07           C  
ATOM   1702  OH  TYR C1067     192.609 188.095 267.567  1.00 28.18           O  
ATOM   1703  N   VAL C1068     188.297 183.200 263.305  1.00 44.61           N  
ATOM   1704  CA  VAL C1068     187.074 183.852 262.824  1.00 48.52           C  
ATOM   1705  C   VAL C1068     186.040 183.866 263.947  1.00 52.25           C  
ATOM   1706  O   VAL C1068     186.092 182.998 264.815  1.00 56.67           O  
ATOM   1707  CB  VAL C1068     186.485 183.144 261.585  1.00 48.00           C  
ATOM   1708  CG1 VAL C1068     187.367 183.343 260.360  1.00 47.60           C  
ATOM   1709  CG2 VAL C1068     186.213 181.651 261.780  1.00 48.43           C  
ATOM   1710  N   PRO C1069     185.066 184.802 263.792  1.00 46.72           N  
ATOM   1711  CA  PRO C1069     183.944 184.845 264.710  1.00 52.27           C  
ATOM   1712  C   PRO C1069     182.987 183.685 264.493  1.00 54.45           C  
ATOM   1713  O   PRO C1069     182.234 183.701 263.522  1.00 55.06           O  
ATOM   1714  CB  PRO C1069     183.211 186.149 264.380  1.00 52.04           C  
ATOM   1715  CG  PRO C1069     183.851 186.724 263.193  1.00 53.33           C  
ATOM   1716  CD  PRO C1069     185.153 186.040 262.977  1.00 48.30           C  
ATOM   1717  N   ALA C1070     183.013 182.687 265.378  1.00 55.70           N  
ATOM   1718  CA  ALA C1070     182.080 181.570 265.311  1.00 57.23           C  
ATOM   1719  C   ALA C1070     180.687 182.128 265.559  1.00 62.82           C  
ATOM   1720  O   ALA C1070     179.727 181.766 264.880  1.00 64.47           O  
ATOM   1721  CB  ALA C1070     182.429 180.525 266.356  1.00 63.11           C  
ATOM   1722  N   GLN C1071     180.594 183.021 266.545  1.00 59.49           N  
ATOM   1723  CA  GLN C1071     179.359 183.691 266.866  1.00 58.87           C  
ATOM   1724  C   GLN C1071     179.648 185.200 267.023  1.00 57.81           C  
ATOM   1725  O   GLN C1071     180.759 185.592 267.373  1.00 52.98           O  
ATOM   1726  CB  GLN C1071     178.767 183.127 268.158  1.00 59.05           C  
ATOM   1727  CG  GLN C1071     177.279 183.385 268.325  1.00 64.70           C  
ATOM   1728  CD  GLN C1071     176.742 182.849 269.637  1.00 68.25           C  
ATOM   1729  OE1 GLN C1071     177.378 182.986 270.682  1.00 62.98           O  
ATOM   1730  NE2 GLN C1071     175.563 182.239 269.591  1.00 73.73           N  
ATOM   1731  N   GLU C1072     178.645 186.031 266.765  1.00 60.40           N  
ATOM   1732  CA  GLU C1072     178.730 187.478 266.905  1.00 56.38           C  
ATOM   1733  C   GLU C1072     177.334 188.046 267.157  1.00 58.96           C  
ATOM   1734  O   GLU C1072     176.329 187.487 266.710  1.00 66.36           O  
ATOM   1735  CB  GLU C1072     179.431 188.104 265.686  1.00 55.38           C  
ATOM   1736  CG  GLU C1072     178.787 187.756 264.334  1.00 61.17           C  
ATOM   1737  CD  GLU C1072     179.628 188.190 263.129  1.00 66.85           C  
ATOM   1738  OE1 GLU C1072     180.484 189.090 263.240  1.00 69.96           O  
ATOM   1739  OE2 GLU C1072     179.419 187.631 262.030  1.00 67.74           O1-
ATOM   1740  N   LYS C1073     177.270 189.167 267.868  1.00 55.64           N  
ATOM   1741  CA  LYS C1073     176.012 189.806 268.257  1.00 55.99           C  
ATOM   1742  C   LYS C1073     175.997 191.237 267.749  1.00 58.01           C  
ATOM   1743  O   LYS C1073     177.019 191.914 267.773  1.00 57.75           O  
ATOM   1744  CB  LYS C1073     175.824 189.678 269.776  1.00 56.13           C  
ATOM   1745  CG  LYS C1073     174.527 190.337 270.273  1.00 62.40           C  
ATOM   1746  CD  LYS C1073     174.253 190.048 271.756  1.00 59.72           C  
ATOM   1747  CE  LYS C1073     173.003 190.808 272.209  1.00 59.61           C  
ATOM   1748  NZ  LYS C1073     172.616 190.462 273.588  1.00 66.35           N  
ATOM   1749  N   ASN C1074     174.851 191.694 267.259  1.00 55.93           N  
ATOM   1750  CA  ASN C1074     174.647 193.088 266.897  1.00 59.64           C  
ATOM   1751  C   ASN C1074     174.365 193.900 268.161  1.00 63.62           C  
ATOM   1752  O   ASN C1074     173.305 193.758 268.773  1.00 64.97           O  
ATOM   1753  CB  ASN C1074     173.540 193.310 265.849  1.00 62.27           C  
ATOM   1754  CG  ASN C1074     173.007 192.078 265.145  1.00 73.96           C  
ATOM   1755  OD1 ASN C1074     172.432 191.206 265.789  1.00 71.59           O  
ATOM   1756  ND2 ASN C1074     173.042 192.080 263.822  1.00 80.20           N  
ATOM   1757  N   PHE C1075     175.292 194.770 268.534  1.00114.01           N  
ATOM   1758  CA  PHE C1075     175.022 195.821 269.509  1.00 56.22           C  
ATOM   1759  C   PHE C1075     174.694 197.104 268.764  1.00 48.05           C  
ATOM   1760  O   PHE C1075     175.336 197.424 267.769  1.00 58.12           O  
ATOM   1761  CB  PHE C1075     176.226 196.017 270.415  1.00 50.36           C  
ATOM   1762  CG  PHE C1075     176.634 194.746 271.112  1.00 57.69           C  
ATOM   1763  CD1 PHE C1075     176.087 194.417 272.361  1.00 59.18           C  
ATOM   1764  CD2 PHE C1075     177.531 193.870 270.484  1.00 54.61           C  
ATOM   1765  CE1 PHE C1075     176.447 193.210 272.986  1.00 63.34           C  
ATOM   1766  CE2 PHE C1075     177.889 192.666 271.107  1.00 62.52           C  
ATOM   1767  CZ  PHE C1075     177.349 192.337 272.357  1.00 57.74           C  
ATOM   1768  N   THR C1076     173.704 197.862 269.213  1.00 43.40           N  
ATOM   1769  CA  THR C1076     173.634 199.251 268.775  1.00 44.08           C  
ATOM   1770  C   THR C1076     174.870 199.981 269.280  1.00 44.96           C  
ATOM   1771  O   THR C1076     175.480 199.609 270.282  1.00 50.01           O  
ATOM   1772  CB  THR C1076     172.344 199.947 269.203  1.00 47.75           C  
ATOM   1773  OG1 THR C1076     172.171 199.912 270.595  1.00 52.42           O  
ATOM   1774  CG2 THR C1076     171.123 199.300 268.556  1.00 54.84           C  
ATOM   1775  N   THR C1077     175.289 200.982 268.528  1.00 45.28           N  
ATOM   1776  CA  THR C1077     176.516 201.740 268.744  1.00 41.50           C  
ATOM   1777  C   THR C1077     176.345 203.166 268.236  1.00 43.50           C  
ATOM   1778  O   THR C1077     175.403 203.485 267.511  1.00 50.69           O  
ATOM   1779  CB  THR C1077     177.723 201.104 268.022  1.00 42.75           C  
ATOM   1780  OG1 THR C1077     177.474 201.052 266.644  1.00 51.34           O  
ATOM   1781  CG2 THR C1077     178.099 199.694 268.454  1.00 39.65           C  
ATOM   1782  N   ALA C1078     177.291 204.018 268.601  1.00 43.04           N  
ATOM   1783  CA  ALA C1078     177.620 205.220 267.862  1.00 47.87           C  
ATOM   1784  C   ALA C1078     179.155 205.326 267.785  1.00 50.55           C  
ATOM   1785  O   ALA C1078     179.845 204.846 268.688  1.00 50.48           O  
ATOM   1786  CB  ALA C1078     176.988 206.435 268.546  1.00 49.62           C  
ATOM   1787  N   PRO C1079     179.732 205.912 266.728  1.00 53.73           N  
ATOM   1788  CA  PRO C1079     181.169 206.158 266.652  1.00 61.05           C  
ATOM   1789  C   PRO C1079     181.639 207.200 267.671  1.00 53.98           C  
ATOM   1790  O   PRO C1079     182.701 207.057 268.261  1.00 52.66           O  
ATOM   1791  CB  PRO C1079     181.439 206.658 265.239  1.00 59.93           C  
ATOM   1792  CG  PRO C1079     180.126 206.545 264.487  1.00 54.90           C  
ATOM   1793  CD  PRO C1079     179.049 206.290 265.517  1.00 53.72           C  
ATOM   1794  N   ALA C1080     180.747 208.154 267.973  1.00 50.76           N  
ATOM   1795  CA  ALA C1080     180.979 209.227 268.961  1.00 52.04           C  
ATOM   1796  C   ALA C1080     179.668 209.803 269.565  1.00 57.27           C  
ATOM   1797  O   ALA C1080     178.598 209.660 268.974  1.00 59.72           O  
ATOM   1798  CB  ALA C1080     181.817 210.339 268.349  1.00 50.01           C  
ATOM   1799  N   ILE C1081     179.763 210.449 270.735  1.00 58.32           N  
ATOM   1800  CA  ILE C1081     178.626 211.049 271.417  1.00 56.13           C  
ATOM   1801  C   ILE C1081     179.008 212.465 271.817  1.00 58.94           C  
ATOM   1802  O   ILE C1081     180.143 212.733 272.224  1.00 60.48           O  
ATOM   1803  CB  ILE C1081     178.176 210.228 272.647  1.00 52.56           C  
ATOM   1804  CG1 ILE C1081     179.366 209.907 273.554  1.00 56.30           C  
ATOM   1805  CG2 ILE C1081     177.477 208.951 272.208  1.00 52.14           C  
ATOM   1806  CD1 ILE C1081     178.990 209.113 274.790  1.00 61.63           C  
ATOM   1807  N   CYS C1082     178.049 213.376 271.692  1.00 61.18           N  
ATOM   1808  CA  CYS C1082     178.270 214.801 271.925  1.00 68.40           C  
ATOM   1809  C   CYS C1082     177.451 215.212 273.146  1.00 73.25           C  
ATOM   1810  O   CYS C1082     176.252 215.491 273.041  1.00 72.88           O  
ATOM   1811  CB  CYS C1082     177.915 215.608 270.674  1.00 69.18           C  
ATOM   1812  SG  CYS C1082     177.394 217.326 270.909  1.00 74.43           S  
ATOM   1813  N   HIS C1083     178.105 215.242 274.305  1.00 73.87           N  
ATOM   1814  CA  HIS C1083     177.458 215.587 275.564  1.00 74.43           C  
ATOM   1815  C   HIS C1083     177.506 217.097 275.755  1.00 78.58           C  
ATOM   1816  O   HIS C1083     178.590 217.692 275.750  1.00 82.23           O  
ATOM   1817  CB  HIS C1083     178.137 214.881 276.736  1.00 69.82           C  
ATOM   1818  CG  HIS C1083     177.827 213.419 276.826  1.00 64.30           C  
ATOM   1819  ND1 HIS C1083     178.700 212.506 277.380  1.00 65.17           N  
ATOM   1820  CD2 HIS C1083     176.739 212.712 276.442  1.00 65.78           C  
ATOM   1821  CE1 HIS C1083     178.164 211.300 277.328  1.00 64.50           C  
ATOM   1822  NE2 HIS C1083     176.974 211.397 276.763  1.00 65.37           N  
ATOM   1823  N   ASP C1084     176.344 217.713 275.959  1.00 77.44           N  
ATOM   1824  CA  ASP C1084     176.214 219.168 276.159  1.00 78.42           C  
ATOM   1825  C   ASP C1084     177.121 220.078 275.306  1.00 79.64           C  
ATOM   1826  O   ASP C1084     177.635 221.090 275.782  1.00 79.97           O  
ATOM   1827  CB  ASP C1084     176.254 219.558 277.650  1.00 81.39           C  
ATOM   1828  CG  ASP C1084     177.644 219.475 278.251  1.00 83.66           C  
ATOM   1829  OD1 ASP C1084     178.329 220.517 278.313  1.00 81.41           O  
ATOM   1830  OD2 ASP C1084     178.052 218.368 278.663  1.00 81.05           O1-
ATOM   1831  N   GLY C1085     177.299 219.691 274.047  1.00 78.35           N  
ATOM   1832  CA  GLY C1085     178.077 220.444 273.045  1.00 78.33           C  
ATOM   1833  C   GLY C1085     179.560 220.054 272.902  1.00 64.92           C  
ATOM   1834  O   GLY C1085     180.287 220.689 272.142  1.00 60.00           O  
ATOM   1835  N   LYS C1086     180.020 219.010 273.597  1.00 65.60           N  
ATOM   1836  CA  LYS C1086     181.353 218.410 273.449  1.00 66.53           C  
ATOM   1837  C   LYS C1086     181.228 216.985 272.890  1.00 64.21           C  
ATOM   1838  O   LYS C1086     180.452 216.191 273.414  1.00 64.07           O  
ATOM   1839  CB  LYS C1086     182.069 218.448 274.809  1.00 68.17           C  
ATOM   1840  CG  LYS C1086     182.384 219.891 275.251  1.00 72.99           C  
ATOM   1841  CD  LYS C1086     183.034 220.011 276.641  1.00 69.08           C  
ATOM   1842  CE  LYS C1086     184.400 219.323 276.794  1.00 70.77           C  
ATOM   1843  NZ  LYS C1086     185.468 219.942 275.965  1.00 62.69           N  
ATOM   1844  N   ALA C1087     181.971 216.665 271.833  1.00 61.98           N  
ATOM   1845  CA  ALA C1087     181.999 215.323 271.258  1.00 53.00           C  
ATOM   1846  C   ALA C1087     183.005 214.440 271.999  1.00 50.35           C  
ATOM   1847  O   ALA C1087     184.146 214.834 272.195  1.00 54.04           O  
ATOM   1848  CB  ALA C1087     182.276 215.413 269.756  1.00 66.82           C  
ATOM   1849  N   HIS C1088     182.586 213.255 272.419  1.00 50.18           N  
ATOM   1850  CA  HIS C1088     183.400 212.237 273.080  1.00 51.65           C  
ATOM   1851  C   HIS C1088     183.480 211.007 272.190  1.00 49.43           C  
ATOM   1852  O   HIS C1088     182.456 210.564 271.677  1.00 53.71           O  
ATOM   1853  CB  HIS C1088     182.767 211.857 274.425  1.00 61.95           C  
ATOM   1854  CG  HIS C1088     182.618 213.000 275.392  1.00 63.60           C  
ATOM   1855  ND1 HIS C1088     183.522 213.342 276.396  1.00 58.51           N  
ATOM   1856  CD2 HIS C1088     181.615 213.918 275.365  1.00 64.55           C  
ATOM   1857  CE1 HIS C1088     183.047 214.473 276.937  1.00 61.35           C  
ATOM   1858  NE2 HIS C1088     181.907 214.838 276.337  1.00 64.18           N  
ATOM   1859  N   PHE C1089     184.668 210.435 271.999  1.00 45.58           N  
ATOM   1860  CA  PHE C1089     184.860 209.260 271.141  1.00 40.15           C  
ATOM   1861  C   PHE C1089     185.972 208.332 271.637  1.00 44.96           C  
ATOM   1862  O   PHE C1089     186.872 208.787 272.335  1.00 51.24           O  
ATOM   1863  CB  PHE C1089     185.070 209.672 269.683  1.00 37.68           C  
ATOM   1864  CG  PHE C1089     185.808 210.967 269.457  1.00 34.66           C  
ATOM   1865  CD1 PHE C1089     185.075 212.156 269.315  1.00 40.18           C  
ATOM   1866  CD2 PHE C1089     187.206 210.986 269.376  1.00 33.77           C  
ATOM   1867  CE1 PHE C1089     185.737 213.365 269.077  1.00 43.13           C  
ATOM   1868  CE2 PHE C1089     187.869 212.195 269.124  1.00 31.45           C  
ATOM   1869  CZ  PHE C1089     187.133 213.381 268.971  1.00 39.01           C  
ATOM   1870  N   PRO C1090     185.928 207.025 271.329  1.00 39.01           N  
ATOM   1871  CA  PRO C1090     186.887 206.049 271.828  1.00 40.42           C  
ATOM   1872  C   PRO C1090     188.358 206.292 271.497  1.00 41.66           C  
ATOM   1873  O   PRO C1090     188.718 206.908 270.498  1.00 43.66           O  
ATOM   1874  CB  PRO C1090     186.457 204.712 271.234  1.00 38.87           C  
ATOM   1875  CG  PRO C1090     184.951 204.860 271.082  1.00 42.20           C  
ATOM   1876  CD  PRO C1090     184.830 206.322 270.673  1.00 43.49           C  
ATOM   1877  N   ARG C1091     189.140 205.446 272.177  1.00 43.62           N  
ATOM   1878  CA  ARG C1091     190.552 205.280 271.977  1.00 49.43           C  
ATOM   1879  C   ARG C1091     190.645 203.745 271.746  1.00 54.06           C  
ATOM   1880  O   ARG C1091     190.394 202.988 272.687  1.00 54.82           O  
ATOM   1881  CB  ARG C1091     191.364 205.642 273.217  1.00 54.66           C  
ATOM   1882  CG  ARG C1091     191.320 207.104 273.611  1.00 60.36           C  
ATOM   1883  CD  ARG C1091     192.673 207.584 274.111  1.00 63.12           C  
ATOM   1884  NE  ARG C1091     192.553 208.706 275.037  1.00 60.51           N  
ATOM   1885  CZ  ARG C1091     193.573 209.467 275.420  1.00 56.22           C  
ATOM   1886  NH1 ARG C1091     193.375 210.467 276.268  1.00 52.52           N  
ATOM   1887  NH2 ARG C1091     194.791 209.230 274.954  1.00 57.42           N  
ATOM   1888  N   GLU C1092     190.950 203.295 270.522  1.00 45.79           N  
ATOM   1889  CA  GLU C1092     191.135 201.865 270.211  1.00 41.25           C  
ATOM   1890  C   GLU C1092     189.914 200.976 270.562  1.00 40.54           C  
ATOM   1891  O   GLU C1092     190.043 199.954 271.230  1.00 38.88           O  
ATOM   1892  CB  GLU C1092     192.446 201.348 270.845  1.00 45.56           C  
ATOM   1893  CG  GLU C1092     193.707 202.157 270.496  1.00 46.77           C  
ATOM   1894  CD  GLU C1092     194.872 201.806 271.431  1.00 68.34           C  
ATOM   1895  OE1 GLU C1092     195.637 202.719 271.817  1.00 71.84           O  
ATOM   1896  OE2 GLU C1092     195.028 200.627 271.818  1.00 82.11           O1-
ATOM   1897  N   GLY C1093     188.704 201.358 270.149  1.00 37.59           N  
ATOM   1898  CA  GLY C1093     187.471 200.598 270.400  1.00 40.87           C  
ATOM   1899  C   GLY C1093     186.238 201.213 269.740  1.00 38.11           C  
ATOM   1900  O   GLY C1093     186.375 202.134 268.939  1.00 38.20           O  
ATOM   1901  N   VAL C1094     185.037 200.761 270.120  1.00 37.07           N  
ATOM   1902  CA  VAL C1094     183.737 201.404 269.801  1.00 40.50           C  
ATOM   1903  C   VAL C1094     182.847 201.534 271.045  1.00 48.64           C  
ATOM   1904  O   VAL C1094     182.978 200.727 271.964  1.00 54.74           O  
ATOM   1905  CB  VAL C1094     182.973 200.713 268.653  1.00 39.73           C  
ATOM   1906  CG1 VAL C1094     183.874 200.531 267.433  1.00 50.59           C  
ATOM   1907  CG2 VAL C1094     182.357 199.361 269.012  1.00 38.76           C  
ATOM   1908  N   PHE C1095     181.925 202.503 271.082  1.00 49.15           N  
ATOM   1909  CA  PHE C1095     180.885 202.559 272.116  1.00 43.33           C  
ATOM   1910  C   PHE C1095     179.832 201.449 271.939  1.00 45.41           C  
ATOM   1911  O   PHE C1095     178.779 201.656 271.341  1.00 49.01           O  
ATOM   1912  CB  PHE C1095     180.201 203.934 272.130  1.00 36.10           C  
ATOM   1913  CG  PHE C1095     181.027 205.135 272.537  1.00 39.30           C  
ATOM   1914  CD1 PHE C1095     181.880 205.084 273.653  1.00 47.62           C  
ATOM   1915  CD2 PHE C1095     180.857 206.344 271.851  1.00 45.13           C  
ATOM   1916  CE1 PHE C1095     182.599 206.220 274.049  1.00 48.21           C  
ATOM   1917  CE2 PHE C1095     181.546 207.489 272.270  1.00 46.11           C  
ATOM   1918  CZ  PHE C1095     182.422 207.432 273.364  1.00 49.96           C  
ATOM   1919  N   VAL C1096     180.089 200.258 272.473  1.00 47.21           N  
ATOM   1920  CA  VAL C1096     179.070 199.205 272.574  1.00 50.87           C  
ATOM   1921  C   VAL C1096     177.949 199.661 273.493  1.00 54.59           C  
ATOM   1922  O   VAL C1096     178.197 200.178 274.585  1.00 61.25           O  
ATOM   1923  CB  VAL C1096     179.644 197.844 273.000  1.00 56.21           C  
ATOM   1924  CG1 VAL C1096     180.082 197.690 274.453  1.00 54.78           C  
ATOM   1925  CG2 VAL C1096     178.650 196.733 272.712  1.00 57.33           C  
ATOM   1926  N   SER C1097     176.708 199.485 273.047  1.00 53.31           N  
ATOM   1927  CA  SER C1097     175.562 200.028 273.753  1.00 57.20           C  
ATOM   1928  C   SER C1097     174.727 199.011 274.486  1.00 58.90           C  
ATOM   1929  O   SER C1097     174.018 198.189 273.905  1.00 55.69           O  
ATOM   1930  CB  SER C1097     174.659 200.845 272.833  1.00 61.81           C  
ATOM   1931  OG  SER C1097     173.762 201.643 273.590  1.00 58.80           O  
ATOM   1932  N   ASN C1098     174.838 199.124 275.800  1.00 65.19           N  
ATOM   1933  CA  ASN C1098     174.092 198.348 276.767  1.00 70.51           C  
ATOM   1934  C   ASN C1098     172.733 199.084 276.951  1.00 76.04           C  
ATOM   1935  O   ASN C1098     172.596 200.252 276.554  1.00 79.10           O  
ATOM   1936  CB  ASN C1098     174.940 198.280 278.037  1.00 69.29           C  
ATOM   1937  CG  ASN C1098     174.363 197.378 279.095  1.00 72.76           C  
ATOM   1938  OD1 ASN C1098     173.986 196.232 278.848  1.00 75.37           O  
ATOM   1939  ND2 ASN C1098     174.292 197.909 280.292  1.00 78.15           N  
ATOM   1940  N   GLY C1099     171.731 198.433 277.540  1.00 75.33           N  
ATOM   1941  CA  GLY C1099     170.417 199.041 277.653  1.00 82.29           C  
ATOM   1942  C   GLY C1099     170.446 200.399 278.352  1.00 83.21           C  
ATOM   1943  O   GLY C1099     169.559 201.221 278.129  1.00 81.95           O  
ATOM   1944  N   THR C1100     171.460 200.650 279.191  1.00 80.66           N  
ATOM   1945  CA  THR C1100     171.471 201.797 280.124  1.00 79.77           C  
ATOM   1946  C   THR C1100     172.797 202.570 280.152  1.00 77.90           C  
ATOM   1947  O   THR C1100     172.833 203.708 280.621  1.00 81.17           O  
ATOM   1948  CB  THR C1100     171.052 201.321 281.529  1.00 83.89           C  
ATOM   1949  OG1 THR C1100     169.856 200.578 281.450  1.00 88.46           O  
ATOM   1950  CG2 THR C1100     170.772 202.444 282.523  1.00 79.19           C  
ATOM   1951  N   HIS C1101     173.881 202.011 279.605  1.00 70.41           N  
ATOM   1952  CA  HIS C1101     175.235 202.579 279.673  1.00 70.61           C  
ATOM   1953  C   HIS C1101     176.039 202.411 278.378  1.00 66.42           C  
ATOM   1954  O   HIS C1101     175.803 201.506 277.579  1.00 68.83           O  
ATOM   1955  CB  HIS C1101     175.996 201.954 280.855  1.00 79.37           C  
ATOM   1956  CG  HIS C1101     175.340 202.213 282.182  1.00 81.52           C  
ATOM   1957  ND1 HIS C1101     175.335 203.438 282.852  1.00 82.69           N  
ATOM   1958  CD2 HIS C1101     174.595 201.317 282.884  1.00 77.24           C  
ATOM   1959  CE1 HIS C1101     174.585 203.251 283.946  1.00 84.50           C  
ATOM   1960  NE2 HIS C1101     174.126 201.992 283.984  1.00 84.07           N  
ATOM   1961  N   TRP C1102     177.045 203.271 278.209  1.00 62.69           N  
ATOM   1962  CA  TRP C1102     178.031 203.199 277.130  1.00 53.67           C  
ATOM   1963  C   TRP C1102     179.320 202.566 277.647  1.00 49.77           C  
ATOM   1964  O   TRP C1102     179.877 203.018 278.649  1.00 53.86           O  
ATOM   1965  CB  TRP C1102     178.351 204.606 276.614  1.00 49.44           C  
ATOM   1966  CG  TRP C1102     177.272 205.342 275.888  1.00 56.39           C  
ATOM   1967  CD1 TRP C1102     176.733 206.520 276.263  1.00 57.52           C  
ATOM   1968  CD2 TRP C1102     176.705 205.047 274.578  1.00 57.39           C  
ATOM   1969  NE1 TRP C1102     175.870 206.971 275.283  1.00 62.18           N  
ATOM   1970  CE2 TRP C1102     175.848 206.124 274.205  1.00 54.79           C  
ATOM   1971  CE3 TRP C1102     176.863 204.002 273.650  1.00 48.21           C  
ATOM   1972  CZ2 TRP C1102     175.216 206.190 272.958  1.00 48.87           C  
ATOM   1973  CZ3 TRP C1102     176.251 204.064 272.389  1.00 45.60           C  
ATOM   1974  CH2 TRP C1102     175.432 205.152 272.039  1.00 51.26           C  
ATOM   1975  N   PHE C1103     179.840 201.573 276.925  1.00 47.70           N  
ATOM   1976  CA  PHE C1103     181.127 200.951 277.219  1.00 48.10           C  
ATOM   1977  C   PHE C1103     182.028 200.978 275.986  1.00 54.10           C  
ATOM   1978  O   PHE C1103     181.560 200.733 274.882  1.00 57.68           O  
ATOM   1979  CB  PHE C1103     180.903 199.511 277.678  1.00 55.67           C  
ATOM   1980  CG  PHE C1103     179.954 199.288 278.845  1.00 60.66           C  
ATOM   1981  CD1 PHE C1103     180.396 199.497 280.164  1.00 58.48           C  
ATOM   1982  CD2 PHE C1103     178.662 198.775 278.621  1.00 57.44           C  
ATOM   1983  CE1 PHE C1103     179.550 199.194 281.241  1.00 65.08           C  
ATOM   1984  CE2 PHE C1103     177.820 198.467 279.701  1.00 58.42           C  
ATOM   1985  CZ  PHE C1103     178.269 198.670 281.012  1.00 70.85           C  
ATOM   1986  N   VAL C1104     183.324 201.246 276.133  1.00 47.08           N  
ATOM   1987  CA  VAL C1104     184.282 201.164 275.029  1.00 40.97           C  
ATOM   1988  C   VAL C1104     184.741 199.716 274.876  1.00 50.19           C  
ATOM   1989  O   VAL C1104     185.705 199.285 275.512  1.00 53.56           O  
ATOM   1990  CB  VAL C1104     185.437 202.162 275.206  1.00 41.59           C  
ATOM   1991  CG1 VAL C1104     186.505 202.009 274.122  1.00 46.37           C  
ATOM   1992  CG2 VAL C1104     184.910 203.594 275.117  1.00 44.15           C  
ATOM   1993  N   THR C1105     184.031 198.937 274.059  1.00 48.11           N  
ATOM   1994  CA  THR C1105     184.494 197.597 273.671  1.00 49.37           C  
ATOM   1995  C   THR C1105     185.610 197.688 272.638  1.00 53.33           C  
ATOM   1996  O   THR C1105     185.678 198.618 271.838  1.00 53.82           O  
ATOM   1997  CB  THR C1105     183.348 196.688 273.210  1.00 48.69           C  
ATOM   1998  OG1 THR C1105     183.675 195.331 273.371  1.00 52.67           O  
ATOM   1999  CG2 THR C1105     182.925 196.829 271.762  1.00 47.22           C  
ATOM   2000  N   GLN C1106     186.507 196.712 272.641  1.00 54.89           N  
ATOM   2001  CA  GLN C1106     187.481 196.532 271.571  1.00 53.50           C  
ATOM   2002  C   GLN C1106     186.725 196.161 270.281  1.00 56.91           C  
ATOM   2003  O   GLN C1106     185.858 195.297 270.320  1.00 59.31           O  
ATOM   2004  CB  GLN C1106     188.445 195.439 272.041  1.00 54.13           C  
ATOM   2005  CG  GLN C1106     189.625 195.262 271.101  1.00 54.25           C  
ATOM   2006  CD  GLN C1106     190.641 194.227 271.582  1.00 66.42           C  
ATOM   2007  OE1 GLN C1106     190.491 193.542 272.586  1.00 60.24           O  
ATOM   2008  NE2 GLN C1106     191.747 194.087 270.895  1.00 71.90           N  
ATOM   2009  N   ARG C1107     186.960 196.841 269.159  1.00 53.48           N  
ATOM   2010  CA  ARG C1107     186.188 196.585 267.919  1.00 45.43           C  
ATOM   2011  C   ARG C1107     185.969 195.120 267.501  1.00 42.99           C  
ATOM   2012  O   ARG C1107     184.883 194.728 267.072  1.00 43.64           O  
ATOM   2013  CB  ARG C1107     186.825 197.325 266.740  1.00 39.79           C  
ATOM   2014  CG  ARG C1107     186.111 197.082 265.418  1.00 40.53           C  
ATOM   2015  CD  ARG C1107     184.737 197.733 265.408  1.00 39.09           C  
ATOM   2016  NE  ARG C1107     184.010 197.474 264.168  1.00 33.26           N  
ATOM   2017  CZ  ARG C1107     183.150 196.475 264.001  1.00 32.85           C  
ATOM   2018  NH1 ARG C1107     182.532 196.317 262.839  1.00 42.96           N  
ATOM   2019  NH2 ARG C1107     182.907 195.634 264.997  1.00 30.13           N  
ATOM   2020  N   ASN C1108     187.026 194.340 267.639  1.00 48.09           N  
ATOM   2021  CA  ASN C1108     187.058 192.926 267.269  1.00 50.35           C  
ATOM   2022  C   ASN C1108     186.621 191.932 268.361  1.00 52.36           C  
ATOM   2023  O   ASN C1108     186.843 190.740 268.173  1.00 45.98           O  
ATOM   2024  CB  ASN C1108     188.436 192.562 266.699  1.00 54.21           C  
ATOM   2025  CG  ASN C1108     189.594 192.587 267.669  1.00 56.79           C  
ATOM   2026  OD1 ASN C1108     189.936 193.592 268.236  1.00 65.49           O  
ATOM   2027  ND2 ASN C1108     190.259 191.497 267.873  1.00 47.22           N  
ATOM   2028  N   PHE C1109     186.030 192.371 269.484  1.00 58.38           N  
ATOM   2029  CA  PHE C1109     185.520 191.467 270.530  1.00 53.44           C  
ATOM   2030  C   PHE C1109     184.500 192.140 271.462  1.00 54.98           C  
ATOM   2031  O   PHE C1109     184.692 193.292 271.837  1.00 53.15           O  
ATOM   2032  CB  PHE C1109     186.702 190.947 271.357  1.00 45.47           C  
ATOM   2033  CG  PHE C1109     186.333 189.909 272.389  1.00 45.46           C  
ATOM   2034  CD1 PHE C1109     185.599 188.768 272.021  1.00 49.73           C  
ATOM   2035  CD2 PHE C1109     186.791 190.047 273.705  1.00 52.53           C  
ATOM   2036  CE1 PHE C1109     185.330 187.775 272.973  1.00 47.87           C  
ATOM   2037  CE2 PHE C1109     186.538 189.041 274.647  1.00 52.51           C  
ATOM   2038  CZ  PHE C1109     185.798 187.908 274.285  1.00 42.74           C  
ATOM   2039  N   TYR C1110     183.444 191.449 271.901  1.00 56.62           N  
ATOM   2040  CA  TYR C1110     182.567 191.948 272.972  1.00 55.48           C  
ATOM   2041  C   TYR C1110     183.163 191.742 274.378  1.00 56.02           C  
ATOM   2042  O   TYR C1110     183.121 190.652 274.946  1.00 53.00           O  
ATOM   2043  CB  TYR C1110     181.153 191.360 272.878  1.00 57.32           C  
ATOM   2044  CG  TYR C1110     180.279 191.874 274.008  1.00 63.51           C  
ATOM   2045  CD1 TYR C1110     179.990 193.252 274.094  1.00 61.59           C  
ATOM   2046  CD2 TYR C1110     179.835 191.004 275.019  1.00 65.78           C  
ATOM   2047  CE1 TYR C1110     179.243 193.755 275.178  1.00 59.91           C  
ATOM   2048  CE2 TYR C1110     179.101 191.505 276.110  1.00 67.30           C  
ATOM   2049  CZ  TYR C1110     178.794 192.877 276.188  1.00 63.65           C  
ATOM   2050  OH  TYR C1110     178.089 193.348 277.247  1.00 73.58           O  
ATOM   2051  N   GLU C1111     183.716 192.817 274.939  1.00 50.61           N  
ATOM   2052  CA  GLU C1111     184.320 192.887 276.273  1.00 50.02           C  
ATOM   2053  C   GLU C1111     184.248 194.336 276.786  1.00 58.35           C  
ATOM   2054  O   GLU C1111     185.177 195.120 276.576  1.00 57.25           O  
ATOM   2055  CB  GLU C1111     185.762 192.362 276.199  1.00 50.64           C  
ATOM   2056  CG  GLU C1111     186.499 192.387 277.540  1.00 63.33           C  
ATOM   2057  CD  GLU C1111     187.920 191.850 277.380  1.00 64.96           C  
ATOM   2058  OE1 GLU C1111     188.139 190.624 277.474  1.00 63.58           O  
ATOM   2059  OE2 GLU C1111     188.855 192.650 277.164  1.00 70.20           O1-
ATOM   2060  N   PRO C1112     183.128 194.743 277.399  1.00 56.17           N  
ATOM   2061  CA  PRO C1112     182.879 196.136 277.733  1.00 53.99           C  
ATOM   2062  C   PRO C1112     183.821 196.672 278.816  1.00 55.96           C  
ATOM   2063  O   PRO C1112     184.181 195.960 279.752  1.00 64.37           O  
ATOM   2064  CB  PRO C1112     181.413 196.194 278.152  1.00 55.83           C  
ATOM   2065  CG  PRO C1112     181.096 194.783 278.607  1.00 54.65           C  
ATOM   2066  CD  PRO C1112     181.982 193.915 277.728  1.00 57.70           C  
ATOM   2067  N   GLN C1113     184.183 197.955 278.705  1.00 54.65           N  
ATOM   2068  CA  GLN C1113     184.896 198.736 279.721  1.00 53.71           C  
ATOM   2069  C   GLN C1113     184.297 200.148 279.824  1.00 53.90           C  
ATOM   2070  O   GLN C1113     183.855 200.707 278.825  1.00 53.62           O  
ATOM   2071  CB  GLN C1113     186.403 198.789 279.422  1.00 50.38           C  
ATOM   2072  CG  GLN C1113     187.030 197.384 279.367  1.00 55.80           C  
ATOM   2073  CD  GLN C1113     188.552 197.373 279.338  1.00 61.28           C  
ATOM   2074  OE1 GLN C1113     189.242 198.364 279.539  1.00 56.45           O  
ATOM   2075  NE2 GLN C1113     189.153 196.228 279.109  1.00 62.35           N  
ATOM   2076  N   ILE C1114     184.263 200.724 281.024  1.00 49.82           N  
ATOM   2077  CA  ILE C1114     183.558 201.981 281.339  1.00 48.54           C  
ATOM   2078  C   ILE C1114     184.177 203.176 280.588  1.00 50.70           C  
ATOM   2079  O   ILE C1114     185.384 203.213 280.360  1.00 50.52           O  
ATOM   2080  CB  ILE C1114     183.525 202.148 282.883  1.00 51.69           C  
ATOM   2081  CG1 ILE C1114     182.446 201.265 283.550  1.00 50.64           C  
ATOM   2082  CG2 ILE C1114     183.265 203.590 283.350  1.00 52.28           C  
ATOM   2083  CD1 ILE C1114     182.647 199.750 283.472  1.00 45.98           C  
ATOM   2084  N   ILE C1115     183.384 204.179 280.195  1.00 46.38           N  
ATOM   2085  CA  ILE C1115     183.937 205.448 279.698  1.00 45.11           C  
ATOM   2086  C   ILE C1115     184.767 206.118 280.798  1.00 53.66           C  
ATOM   2087  O   ILE C1115     184.263 206.439 281.871  1.00 71.46           O  
ATOM   2088  CB  ILE C1115     182.835 206.401 279.182  1.00 46.90           C  
ATOM   2089  CG1 ILE C1115     182.275 205.851 277.855  1.00 60.41           C  
ATOM   2090  CG2 ILE C1115     183.363 207.841 278.986  1.00 41.93           C  
ATOM   2091  CD1 ILE C1115     181.233 206.749 277.172  1.00 52.02           C  
ATOM   2092  N   THR C1116     186.029 206.390 280.481  1.00 46.11           N  
ATOM   2093  CA  THR C1116     186.970 207.177 281.285  1.00 49.95           C  
ATOM   2094  C   THR C1116     187.786 208.069 280.350  1.00 50.37           C  
ATOM   2095  O   THR C1116     187.855 207.802 279.144  1.00 63.23           O  
ATOM   2096  CB  THR C1116     187.921 206.298 282.124  1.00 52.26           C  
ATOM   2097  OG1 THR C1116     188.927 205.723 281.324  1.00 47.79           O  
ATOM   2098  CG2 THR C1116     187.275 205.136 282.865  1.00 54.66           C  
ATOM   2099  N   THR C1117     188.459 209.098 280.871  1.00 49.18           N  
ATOM   2100  CA  THR C1117     189.355 209.953 280.053  1.00 53.39           C  
ATOM   2101  C   THR C1117     190.589 209.180 279.536  1.00 55.53           C  
ATOM   2102  O   THR C1117     191.301 209.655 278.659  1.00 55.15           O  
ATOM   2103  CB  THR C1117     189.759 211.227 280.820  1.00 55.85           C  
ATOM   2104  OG1 THR C1117     188.610 211.909 281.273  1.00 56.97           O  
ATOM   2105  CG2 THR C1117     190.501 212.269 279.985  1.00 54.61           C  
ATOM   2106  N   ASP C1118     190.824 207.948 280.005  1.00 49.71           N  
ATOM   2107  CA  ASP C1118     191.841 207.026 279.481  1.00 57.36           C  
ATOM   2108  C   ASP C1118     191.294 206.021 278.430  1.00 64.26           C  
ATOM   2109  O   ASP C1118     192.073 205.395 277.708  1.00 62.62           O  
ATOM   2110  CB  ASP C1118     192.465 206.313 280.679  1.00 60.17           C  
ATOM   2111  CG  ASP C1118     193.661 205.436 280.305  1.00 73.72           C  
ATOM   2112  OD1 ASP C1118     194.580 205.910 279.604  1.00 75.74           O  
ATOM   2113  OD2 ASP C1118     193.706 204.266 280.748  1.00 73.38           O1-
ATOM   2114  N   ASN C1119     189.969 205.857 278.313  1.00 59.03           N  
ATOM   2115  CA  ASN C1119     189.287 205.087 277.254  1.00 47.61           C  
ATOM   2116  C   ASN C1119     188.757 205.965 276.109  1.00 46.94           C  
ATOM   2117  O   ASN C1119     188.370 205.440 275.069  1.00 56.38           O  
ATOM   2118  CB  ASN C1119     188.134 204.259 277.868  1.00 45.81           C  
ATOM   2119  CG  ASN C1119     188.578 202.921 278.414  1.00 51.26           C  
ATOM   2120  OD1 ASN C1119     189.633 202.398 278.094  1.00 58.77           O  
ATOM   2121  ND2 ASN C1119     187.795 202.300 279.262  1.00 54.57           N  
ATOM   2122  N   THR C1120     188.710 207.287 276.265  1.00 41.59           N  
ATOM   2123  CA  THR C1120     188.132 208.201 275.265  1.00 42.52           C  
ATOM   2124  C   THR C1120     188.996 209.432 275.044  1.00 47.49           C  
ATOM   2125  O   THR C1120     189.812 209.801 275.888  1.00 55.08           O  
ATOM   2126  CB  THR C1120     186.709 208.632 275.634  1.00 41.50           C  
ATOM   2127  OG1 THR C1120     186.704 209.284 276.879  1.00 43.07           O  
ATOM   2128  CG2 THR C1120     185.712 207.480 275.698  1.00 47.42           C  
ATOM   2129  N   PHE C1121     188.831 210.049 273.882  1.00 48.63           N  
ATOM   2130  CA  PHE C1121     189.232 211.415 273.589  1.00 48.71           C  
ATOM   2131  C   PHE C1121     188.015 212.339 273.673  1.00 46.01           C  
ATOM   2132  O   PHE C1121     186.869 211.885 273.672  1.00 47.52           O  
ATOM   2133  CB  PHE C1121     189.866 211.471 272.193  1.00 47.14           C  
ATOM   2134  CG  PHE C1121     191.192 210.753 272.047  1.00 45.46           C  
ATOM   2135  CD1 PHE C1121     191.386 209.794 271.035  1.00 48.54           C  
ATOM   2136  CD2 PHE C1121     192.254 211.078 272.906  1.00 52.45           C  
ATOM   2137  CE1 PHE C1121     192.633 209.162 270.889  1.00 54.77           C  
ATOM   2138  CE2 PHE C1121     193.492 210.439 272.757  1.00 51.48           C  
ATOM   2139  CZ  PHE C1121     193.690 209.484 271.752  1.00 51.76           C  
ATOM   2140  N   VAL C1122     188.272 213.644 273.715  1.00 43.04           N  
ATOM   2141  CA  VAL C1122     187.256 214.685 273.882  1.00 43.87           C  
ATOM   2142  C   VAL C1122     187.537 215.850 272.936  1.00 50.01           C  
ATOM   2143  O   VAL C1122     188.682 216.089 272.563  1.00 50.11           O  
ATOM   2144  CB  VAL C1122     187.188 215.143 275.356  1.00 50.78           C  
ATOM   2145  CG1 VAL C1122     186.075 216.163 275.607  1.00 54.73           C  
ATOM   2146  CG2 VAL C1122     186.967 213.967 276.314  1.00 49.97           C  
ATOM   2147  N   SER C1123     186.494 216.569 272.544  1.00 50.46           N  
ATOM   2148  CA  SER C1123     186.521 217.626 271.532  1.00 51.30           C  
ATOM   2149  C   SER C1123     185.898 218.942 272.035  1.00 59.35           C  
ATOM   2150  O   SER C1123     185.746 219.150 273.239  1.00 64.12           O  
ATOM   2151  CB  SER C1123     185.796 217.059 270.309  1.00 52.86           C  
ATOM   2152  OG  SER C1123     186.001 217.868 269.179  1.00 58.25           O  
ATOM   2153  N   GLY C1124     185.542 219.805 271.089  1.00 62.47           N  
ATOM   2154  CA  GLY C1124     184.944 221.085 271.406  1.00 62.16           C  
ATOM   2155  C   GLY C1124     184.029 221.615 270.319  1.00 69.77           C  
ATOM   2156  O   GLY C1124     184.330 221.484 269.128  1.00 69.81           O  
ATOM   2157  N   ASN C1125     182.883 222.132 270.771  1.00 77.38           N  
ATOM   2158  CA  ASN C1125     181.806 222.773 269.988  1.00 80.97           C  
ATOM   2159  C   ASN C1125     180.807 221.885 269.232  1.00 76.91           C  
ATOM   2160  O   ASN C1125     179.890 222.415 268.615  1.00 76.23           O  
ATOM   2161  CB  ASN C1125     182.294 223.953 269.121  1.00 76.82           C  
ATOM   2162  CG  ASN C1125     183.087 224.971 269.917  1.00 78.13           C  
ATOM   2163  OD1 ASN C1125     183.306 224.804 271.116  1.00 77.23           O  
ATOM   2164  ND2 ASN C1125     183.524 226.033 269.250  1.00 77.63           N  
ATOM   2165  N   CYS C1126     180.967 220.563 269.330  1.00 72.53           N  
ATOM   2166  CA  CYS C1126     180.077 219.553 268.713  1.00 72.93           C  
ATOM   2167  C   CYS C1126     179.843 219.539 267.183  1.00 76.20           C  
ATOM   2168  O   CYS C1126     178.791 219.097 266.724  1.00 75.07           O  
ATOM   2169  CB  CYS C1126     178.722 219.545 269.438  1.00 73.94           C  
ATOM   2170  SG  CYS C1126     177.649 218.144 269.079  1.00 77.69           S  
ATOM   2171  N   ASP C1127     180.803 220.020 266.395  1.00 76.14           N  
ATOM   2172  CA  ASP C1127     180.679 220.043 264.921  1.00 68.32           C  
ATOM   2173  C   ASP C1127     181.335 218.910 264.113  1.00 66.43           C  
ATOM   2174  O   ASP C1127     182.412 218.437 264.476  1.00 63.98           O  
ATOM   2175  CB  ASP C1127     181.152 221.396 264.378  1.00 68.46           C  
ATOM   2176  CG  ASP C1127     180.330 222.556 264.906  1.00 76.65           C  
ATOM   2177  OD1 ASP C1127     179.352 222.307 265.641  1.00 84.78           O  
ATOM   2178  OD2 ASP C1127     180.663 223.716 264.585  1.00 76.04           O1-
ATOM   2179  N   VAL C1128     180.692 218.475 263.019  1.00 66.46           N  
ATOM   2180  CA  VAL C1128     181.309 217.434 262.188  1.00 61.32           C  
ATOM   2181  C   VAL C1128     182.018 218.100 261.018  1.00 62.44           C  
ATOM   2182  O   VAL C1128     181.403 218.866 260.270  1.00 64.92           O  
ATOM   2183  CB  VAL C1128     180.243 216.449 261.684  1.00 51.62           C  
ATOM   2184  CG1 VAL C1128     180.712 215.561 260.530  1.00 57.27           C  
ATOM   2185  CG2 VAL C1128     179.822 215.518 262.819  1.00 55.98           C  
ATOM   2186  N   VAL C1129     183.299 217.787 260.834  1.00 57.46           N  
ATOM   2187  CA  VAL C1129     184.002 218.089 259.583  1.00 56.57           C  
ATOM   2188  C   VAL C1129     183.529 217.106 258.510  1.00 64.45           C  
ATOM   2189  O   VAL C1129     183.520 215.907 258.760  1.00 66.68           O  
ATOM   2190  CB  VAL C1129     185.520 218.017 259.815  1.00 50.98           C  
ATOM   2191  CG1 VAL C1129     186.350 217.926 258.530  1.00 56.83           C  
ATOM   2192  CG2 VAL C1129     185.999 219.250 260.588  1.00 64.62           C  
ATOM   2193  N   ILE C1130     183.169 217.567 257.311  1.00 63.79           N  
ATOM   2194  CA  ILE C1130     182.811 216.677 256.193  1.00 54.04           C  
ATOM   2195  C   ILE C1130     183.907 216.725 255.126  1.00 54.44           C  
ATOM   2196  O   ILE C1130     184.227 217.778 254.579  1.00 55.46           O  
ATOM   2197  CB  ILE C1130     181.402 216.984 255.637  1.00 54.37           C  
ATOM   2198  CG1 ILE C1130     180.353 216.751 256.748  1.00 58.64           C  
ATOM   2199  CG2 ILE C1130     181.108 216.104 254.410  1.00 62.20           C  
ATOM   2200  CD1 ILE C1130     178.885 216.774 256.309  1.00 62.80           C  
ATOM   2201  N   GLY C1131     184.477 215.564 254.824  1.00 54.61           N  
ATOM   2202  CA  GLY C1131     185.470 215.350 253.777  1.00 56.64           C  
ATOM   2203  C   GLY C1131     184.879 214.608 252.582  1.00 61.74           C  
ATOM   2204  O   GLY C1131     183.935 213.826 252.717  1.00 61.98           O  
ATOM   2205  N   ILE C1132     185.457 214.825 251.407  1.00 64.61           N  
ATOM   2206  CA  ILE C1132     185.101 214.140 250.164  1.00 57.70           C  
ATOM   2207  C   ILE C1132     186.363 213.600 249.487  1.00 56.23           C  
ATOM   2208  O   ILE C1132     187.360 214.310 249.328  1.00 51.46           O  
ATOM   2209  CB  ILE C1132     184.249 215.074 249.271  1.00 56.56           C  
ATOM   2210  CG1 ILE C1132     183.715 214.398 247.992  1.00 58.96           C  
ATOM   2211  CG2 ILE C1132     184.983 216.364 248.855  1.00 54.30           C  
ATOM   2212  CD1 ILE C1132     182.691 213.294 248.251  1.00 58.65           C  
ATOM   2213  N   VAL C1133     186.321 212.332 249.101  1.00 54.82           N  
ATOM   2214  CA  VAL C1133     187.373 211.654 248.355  1.00 53.92           C  
ATOM   2215  C   VAL C1133     186.730 210.991 247.155  1.00 60.00           C  
ATOM   2216  O   VAL C1133     185.759 210.246 247.281  1.00 62.45           O  
ATOM   2217  CB  VAL C1133     188.123 210.639 249.230  1.00 53.19           C  
ATOM   2218  CG1 VAL C1133     189.121 209.791 248.437  1.00 46.89           C  
ATOM   2219  CG2 VAL C1133     188.901 211.350 250.339  1.00 56.94           C  
ATOM   2220  N   ASN C1134     187.292 211.232 245.981  1.00 63.33           N  
ATOM   2221  CA  ASN C1134     186.800 210.651 244.748  1.00 61.34           C  
ATOM   2222  C   ASN C1134     187.968 210.056 243.972  1.00 66.29           C  
ATOM   2223  O   ASN C1134     188.756 210.781 243.367  1.00 72.49           O  
ATOM   2224  CB  ASN C1134     186.016 211.725 243.992  1.00 68.36           C  
ATOM   2225  CG  ASN C1134     185.179 211.142 242.876  1.00 76.54           C  
ATOM   2226  OD1 ASN C1134     185.341 209.992 242.475  1.00 76.56           O  
ATOM   2227  ND2 ASN C1134     184.302 211.985 242.359  1.00 79.76           N  
ATOM   2228  N   ASN C1135     188.142 208.743 244.074  1.00 59.52           N  
ATOM   2229  CA  ASN C1135     189.239 208.040 243.433  1.00 64.38           C  
ATOM   2230  C   ASN C1135     188.934 207.807 241.951  1.00 65.49           C  
ATOM   2231  O   ASN C1135     188.585 206.707 241.530  1.00 64.06           O  
ATOM   2232  CB  ASN C1135     189.551 206.768 244.216  1.00 57.02           C  
ATOM   2233  CG  ASN C1135     189.882 207.073 245.661  1.00 51.11           C  
ATOM   2234  OD1 ASN C1135     190.917 207.620 245.991  1.00 56.11           O  
ATOM   2235  ND2 ASN C1135     188.997 206.741 246.550  1.00 51.83           N  
ATOM   2236  N   THR C1136     189.087 208.861 241.161  1.00 64.98           N  
ATOM   2237  CA  THR C1136     189.117 208.817 239.706  1.00 58.29           C  
ATOM   2238  C   THR C1136     190.322 207.981 239.272  1.00 66.30           C  
ATOM   2239  O   THR C1136     191.429 208.502 239.164  1.00 68.98           O  
ATOM   2240  CB  THR C1136     189.221 210.257 239.170  1.00 68.02           C  
ATOM   2241  OG1 THR C1136     188.125 211.027 239.592  1.00 66.81           O  
ATOM   2242  CG2 THR C1136     189.297 210.357 237.649  1.00 66.35           C  
ATOM   2243  N   VAL C1137     190.136 206.689 238.994  1.00 63.49           N  
ATOM   2244  CA  VAL C1137     191.062 205.979 238.100  1.00 56.30           C  
ATOM   2245  C   VAL C1137     191.062 206.707 236.763  1.00 46.14           C  
ATOM   2246  O   VAL C1137     190.041 207.265 236.374  1.00 46.99           O  
ATOM   2247  CB  VAL C1137     190.732 204.496 237.911  1.00 48.40           C  
ATOM   2248  CG1 VAL C1137     190.814 203.737 239.236  1.00 48.39           C  
ATOM   2249  CG2 VAL C1137     189.364 204.237 237.291  1.00 42.22           C  
ATOM   2250  N   TYR C1138     192.203 206.781 236.092  1.00 44.13           N  
ATOM   2251  CA  TYR C1138     192.399 207.757 235.024  1.00 43.29           C  
ATOM   2252  C   TYR C1138     191.459 207.500 233.845  1.00 44.23           C  
ATOM   2253  O   TYR C1138     191.382 206.384 233.338  1.00 45.14           O  
ATOM   2254  CB  TYR C1138     193.858 207.720 234.589  1.00 41.45           C  
ATOM   2255  CG  TYR C1138     194.254 208.716 233.532  1.00 42.66           C  
ATOM   2256  CD1 TYR C1138     194.534 208.278 232.226  1.00 48.42           C  
ATOM   2257  CD2 TYR C1138     194.409 210.070 233.875  1.00 49.81           C  
ATOM   2258  CE1 TYR C1138     194.934 209.205 231.249  1.00 52.26           C  
ATOM   2259  CE2 TYR C1138     194.792 211.002 232.897  1.00 56.77           C  
ATOM   2260  CZ  TYR C1138     195.023 210.574 231.576  1.00 58.30           C  
ATOM   2261  OH  TYR C1138     195.291 211.487 230.611  1.00 58.84           O  
ATOM   2262  N   ASP C1139     190.706 208.511 233.416  1.00 46.70           N  
ATOM   2263  CA  ASP C1139     189.894 208.430 232.204  1.00 43.07           C  
ATOM   2264  C   ASP C1139     190.657 209.112 231.062  1.00 46.79           C  
ATOM   2265  O   ASP C1139     190.809 210.339 231.079  1.00 47.13           O  
ATOM   2266  CB  ASP C1139     188.498 209.031 232.429  1.00 47.74           C  
ATOM   2267  CG  ASP C1139     187.451 208.487 231.454  1.00 58.10           C  
ATOM   2268  OD1 ASP C1139     187.805 207.847 230.450  1.00 55.56           O  
ATOM   2269  OD2 ASP C1139     186.247 208.682 231.709  1.00 65.86           O1-
ATOM   2270  N   PRO C1140     191.182 208.343 230.096  1.00 37.04           N  
ATOM   2271  CA  PRO C1140     192.138 208.854 229.134  1.00 36.05           C  
ATOM   2272  C   PRO C1140     191.535 209.767 228.073  1.00 37.36           C  
ATOM   2273  O   PRO C1140     190.348 209.700 227.749  1.00 40.38           O  
ATOM   2274  CB  PRO C1140     192.780 207.622 228.506  1.00 40.48           C  
ATOM   2275  CG  PRO C1140     191.764 206.508 228.694  1.00 31.22           C  
ATOM   2276  CD  PRO C1140     191.067 206.903 229.980  1.00 26.61           C  
ATOM   2277  N   LEU C1141     192.397 210.580 227.460  1.00 38.82           N  
ATOM   2278  CA  LEU C1141     192.132 211.255 226.197  1.00 38.97           C  
ATOM   2279  C   LEU C1141     192.010 210.192 225.090  1.00 36.73           C  
ATOM   2280  O   LEU C1141     193.003 209.799 224.483  1.00 39.79           O  
ATOM   2281  CB  LEU C1141     193.278 212.239 225.899  1.00 42.75           C  
ATOM   2282  CG  LEU C1141     193.273 213.543 226.706  1.00 44.37           C  
ATOM   2283  CD1 LEU C1141     193.683 213.368 228.166  1.00 50.81           C  
ATOM   2284  CD2 LEU C1141     194.262 214.517 226.064  1.00 48.80           C  
ATOM   2285  N   GLN C1142     190.804 209.683 224.831  1.00 36.44           N  
ATOM   2286  CA  GLN C1142     190.593 208.689 223.778  1.00 34.59           C  
ATOM   2287  C   GLN C1142     190.698 209.320 222.377  1.00 41.22           C  
ATOM   2288  O   GLN C1142     190.341 210.488 222.190  1.00 49.63           O  
ATOM   2289  CB  GLN C1142     189.272 207.914 223.964  1.00 31.22           C  
ATOM   2290  CG  GLN C1142     189.289 206.827 225.063  1.00 28.68           C  
ATOM   2291  CD  GLN C1142     190.194 205.631 224.758  1.00 30.68           C  
ATOM   2292  OE1 GLN C1142     191.230 205.752 224.136  1.00 33.66           O  
ATOM   2293  NE2 GLN C1142     189.880 204.433 225.166  1.00 27.43           N  
ATOM   2294  N   PRO C1143     191.225 208.596 221.377  1.00 41.05           N  
ATOM   2295  CA  PRO C1143     191.612 209.135 220.079  1.00 38.18           C  
ATOM   2296  C   PRO C1143     190.426 209.389 219.140  1.00 33.72           C  
ATOM   2297  O   PRO C1143     190.191 208.646 218.189  1.00 40.45           O  
ATOM   2298  CB  PRO C1143     192.604 208.115 219.527  1.00 32.18           C  
ATOM   2299  CG  PRO C1143     192.124 206.802 220.110  1.00 27.29           C  
ATOM   2300  CD  PRO C1143     191.641 207.210 221.481  1.00 35.86           C  
ATOM   2301  N   GLU C1144     189.689 210.469 219.378  1.00 35.45           N  
ATOM   2302  CA  GLU C1144     188.586 210.898 218.513  1.00 47.65           C  
ATOM   2303  C   GLU C1144     189.073 211.524 217.199  1.00 49.79           C  
ATOM   2304  O   GLU C1144     189.989 212.346 217.180  1.00 53.98           O  
ATOM   2305  CB  GLU C1144     187.624 211.837 219.260  1.00 52.30           C  
ATOM   2306  CG  GLU C1144     186.469 212.436 218.429  1.00 57.44           C  
ATOM   2307  CD  GLU C1144     185.489 211.412 217.822  1.00 62.13           C  
ATOM   2308  OE1 GLU C1144     185.902 210.339 217.339  1.00 58.42           O  
ATOM   2309  OE2 GLU C1144     184.274 211.690 217.816  1.00 72.54           O1-
ATOM   2310  N   LEU C1145     188.399 211.152 216.116  1.00 43.41           N  
ATOM   2311  CA  LEU C1145     188.754 211.357 214.715  1.00 42.49           C  
ATOM   2312  C   LEU C1145     187.657 212.112 213.954  1.00 48.60           C  
ATOM   2313  O   LEU C1145     186.479 212.022 214.299  1.00 56.02           O  
ATOM   2314  CB  LEU C1145     188.908 209.979 214.065  1.00 31.58           C  
ATOM   2315  CG  LEU C1145     190.116 209.155 214.510  1.00 25.65           C  
ATOM   2316  CD1 LEU C1145     189.912 207.712 214.063  1.00 20.77           C  
ATOM   2317  CD2 LEU C1145     191.380 209.679 213.847  1.00 34.26           C  
ATOM   2318  N   ASP C1146     188.015 212.795 212.869  1.00 42.45           N  
ATOM   2319  CA  ASP C1146     187.039 213.318 211.902  1.00 47.55           C  
ATOM   2320  C   ASP C1146     186.203 212.193 211.273  1.00 49.98           C  
ATOM   2321  O   ASP C1146     186.558 211.021 211.402  1.00 52.00           O  
ATOM   2322  CB  ASP C1146     187.737 214.109 210.785  1.00 47.55           C  
ATOM   2323  CG  ASP C1146     188.844 215.039 211.268  1.00 50.82           C  
ATOM   2324  OD1 ASP C1146     188.640 216.270 211.246  1.00 49.58           O  
ATOM   2325  OD2 ASP C1146     189.930 214.543 211.638  1.00 55.51           O1-
ATOM   2326  N   SER C1147     185.150 212.503 210.512  1.00 54.78           N  
ATOM   2327  CA  SER C1147     184.592 211.481 209.610  1.00 54.01           C  
ATOM   2328  C   SER C1147     185.613 211.120 208.528  1.00 51.91           C  
ATOM   2329  O   SER C1147     186.444 211.939 208.143  1.00 54.45           O  
ATOM   2330  CB  SER C1147     183.267 211.906 208.969  1.00 52.54           C  
ATOM   2331  OG  SER C1147     182.237 212.041 209.924  1.00 53.81           O  
ATOM   2332  N   PHE C1148     185.556 209.895 208.006  1.00 50.74           N  
ATOM   2333  CA  PHE C1148     186.559 209.391 207.062  1.00 47.15           C  
ATOM   2334  C   PHE C1148     186.661 210.256 205.797  1.00 51.18           C  
ATOM   2335  O   PHE C1148     187.755 210.487 205.292  1.00 50.78           O  
ATOM   2336  CB  PHE C1148     186.201 207.944 206.716  1.00 41.79           C  
ATOM   2337  CG  PHE C1148     187.275 207.163 205.983  1.00 37.92           C  
ATOM   2338  CD1 PHE C1148     188.085 206.279 206.703  1.00 41.84           C  
ATOM   2339  CD2 PHE C1148     187.441 207.263 204.594  1.00 43.71           C  
ATOM   2340  CE1 PHE C1148     189.061 205.509 206.057  1.00 34.51           C  
ATOM   2341  CE2 PHE C1148     188.413 206.487 203.945  1.00 43.48           C  
ATOM   2342  CZ  PHE C1148     189.230 205.618 204.673  1.00 30.97           C  
ATOM   2343  N   LYS C1149     185.536 210.809 205.316  1.00 56.69           N  
ATOM   2344  CA  LYS C1149     185.480 211.703 204.151  1.00 54.52           C  
ATOM   2345  C   LYS C1149     186.397 212.917 204.307  1.00 53.93           C  
ATOM   2346  O   LYS C1149     187.134 213.212 203.379  1.00 55.60           O  
ATOM   2347  CB  LYS C1149     184.035 212.152 203.871  1.00 57.07           C  
ATOM   2348  CG  LYS C1149     183.056 210.986 203.639  1.00 51.98           C  
ATOM   2349  CD  LYS C1149     181.713 211.418 203.028  1.00 58.32           C  
ATOM   2350  CE  LYS C1149     180.956 212.528 203.773  1.00 54.48           C  
ATOM   2351  NZ  LYS C1149     180.352 212.082 205.057  1.00 58.96           N  
ATOM   2352  N   GLU C1150     186.433 213.571 205.467  1.00 49.19           N  
ATOM   2353  CA  GLU C1150     187.334 214.701 205.716  1.00 49.84           C  
ATOM   2354  C   GLU C1150     188.804 214.280 205.745  1.00 47.97           C  
ATOM   2355  O   GLU C1150     189.643 214.978 205.180  1.00 49.28           O  
ATOM   2356  CB  GLU C1150     186.998 215.409 207.038  1.00 65.07           C  
ATOM   2357  CG  GLU C1150     185.654 216.139 207.033  1.00 68.66           C  
ATOM   2358  CD  GLU C1150     184.497 215.257 207.525  1.00 67.24           C  
ATOM   2359  OE1 GLU C1150     184.298 215.173 208.758  1.00 71.21           O  
ATOM   2360  OE2 GLU C1150     183.782 214.662 206.685  1.00 63.73           O1-
ATOM   2361  N   GLU C1151     189.143 213.159 206.388  1.00 42.80           N  
ATOM   2362  CA  GLU C1151     190.543 212.732 206.514  1.00 46.85           C  
ATOM   2363  C   GLU C1151     191.063 212.065 205.225  1.00 48.48           C  
ATOM   2364  O   GLU C1151     192.267 212.034 204.981  1.00 42.94           O  
ATOM   2365  CB  GLU C1151     190.689 211.845 207.761  1.00 49.13           C  
ATOM   2366  CG  GLU C1151     192.105 211.892 208.366  1.00 55.59           C  
ATOM   2367  CD  GLU C1151     192.282 210.965 209.579  1.00 49.13           C  
ATOM   2368  OE1 GLU C1151     191.514 209.991 209.706  1.00 47.41           O  
ATOM   2369  OE2 GLU C1151     193.194 211.190 210.398  1.00 55.01           O1-
ATOM   2370  N   LEU C1152     190.164 211.591 204.356  1.00 46.73           N  
ATOM   2371  CA  LEU C1152     190.448 211.124 202.999  1.00 42.16           C  
ATOM   2372  C   LEU C1152     190.666 212.299 202.043  1.00 48.38           C  
ATOM   2373  O   LEU C1152     191.750 212.456 201.485  1.00 52.01           O  
ATOM   2374  CB  LEU C1152     189.304 210.197 202.557  1.00 41.79           C  
ATOM   2375  CG  LEU C1152     189.480 209.565 201.171  1.00 39.87           C  
ATOM   2376  CD1 LEU C1152     190.616 208.546 201.157  1.00 37.30           C  
ATOM   2377  CD2 LEU C1152     188.199 208.854 200.750  1.00 40.11           C  
ATOM   2378  N   ASP C1153     189.668 213.172 201.905  1.00 50.28           N  
ATOM   2379  CA  ASP C1153     189.657 214.303 200.975  1.00 43.18           C  
ATOM   2380  C   ASP C1153     190.815 215.282 201.185  1.00 43.40           C  
ATOM   2381  O   ASP C1153     191.174 216.010 200.265  1.00 41.45           O  
ATOM   2382  CB  ASP C1153     188.328 215.063 201.094  1.00 46.14           C  
ATOM   2383  CG  ASP C1153     187.086 214.309 200.597  1.00 52.88           C  
ATOM   2384  OD1 ASP C1153     187.219 213.356 199.800  1.00 51.59           O  
ATOM   2385  OD2 ASP C1153     185.955 214.715 200.944  1.00 46.44           O1-
ATOM   2386  N   LYS C1154     191.438 215.293 202.363  1.00 46.17           N  
ATOM   2387  CA  LYS C1154     192.640 216.087 202.638  1.00 49.15           C  
ATOM   2388  C   LYS C1154     193.780 215.784 201.663  1.00 50.07           C  
ATOM   2389  O   LYS C1154     194.487 216.709 201.271  1.00 56.00           O  
ATOM   2390  CB  LYS C1154     193.056 215.848 204.096  1.00 53.66           C  
ATOM   2391  CG  LYS C1154     194.212 216.769 204.510  1.00 61.00           C  
ATOM   2392  CD  LYS C1154     194.583 216.636 205.996  1.00 64.82           C  
ATOM   2393  CE  LYS C1154     193.519 217.222 206.939  1.00 69.13           C  
ATOM   2394  NZ  LYS C1154     193.452 218.703 206.847  1.00 73.90           N  
ATOM   2395  N   TYR C1155     193.933 214.523 201.240  1.00 45.75           N  
ATOM   2396  CA  TYR C1155     195.033 214.060 200.373  1.00 52.47           C  
ATOM   2397  C   TYR C1155     194.607 213.220 199.165  1.00 51.90           C  
ATOM   2398  O   TYR C1155     195.318 213.190 198.163  1.00 54.59           O  
ATOM   2399  CB  TYR C1155     196.056 213.280 201.215  1.00 55.96           C  
ATOM   2400  CG  TYR C1155     196.825 214.177 202.160  1.00 58.05           C  
ATOM   2401  CD1 TYR C1155     196.627 214.107 203.548  1.00 56.98           C  
ATOM   2402  CD2 TYR C1155     197.694 215.140 201.616  1.00 62.34           C  
ATOM   2403  CE1 TYR C1155     197.286 215.025 204.386  1.00 58.85           C  
ATOM   2404  CE2 TYR C1155     198.342 216.067 202.448  1.00 55.96           C  
ATOM   2405  CZ  TYR C1155     198.124 216.020 203.836  1.00 51.05           C  
ATOM   2406  OH  TYR C1155     198.709 216.937 204.648  1.00 51.13           O  
ATOM   2407  N   PHE C1156     193.464 212.549 199.255  1.00 48.19           N  
ATOM   2408  CA  PHE C1156     192.985 211.678 198.176  1.00 40.29           C  
ATOM   2409  C   PHE C1156     192.705 212.351 196.824  1.00 46.03           C  
ATOM   2410  O   PHE C1156     192.073 213.405 196.761  1.00 45.14           O  
ATOM   2411  CB  PHE C1156     191.737 210.918 198.642  1.00 30.00           C  
ATOM   2412  CG  PHE C1156     191.172 209.984 197.611  1.00 30.00           C  
ATOM   2413  CD1 PHE C1156     191.736 208.736 197.402  1.00 30.00           C  
ATOM   2414  CD2 PHE C1156     190.075 210.353 196.850  1.00 30.00           C  
ATOM   2415  CE1 PHE C1156     191.218 207.875 196.454  1.00 30.00           C  
ATOM   2416  CE2 PHE C1156     189.552 209.497 195.900  1.00 30.00           C  
ATOM   2417  CZ  PHE C1156     190.124 208.256 195.702  1.00 30.00           C  
ATOM   2418  N   LYS C1157     193.185 211.724 195.748  1.00 57.12           N  
ATOM   2419  CA  LYS C1157     192.962 212.210 194.381  1.00 49.75           C  
ATOM   2420  C   LYS C1157     192.147 211.202 193.578  1.00 44.43           C  
ATOM   2421  O   LYS C1157     192.590 210.079 193.344  1.00 38.11           O  
ATOM   2422  CB  LYS C1157     194.310 212.558 193.723  1.00 42.88           C  
ATOM   2423  CG  LYS C1157     194.849 213.870 194.303  1.00 51.21           C  
ATOM   2424  CD  LYS C1157     196.114 214.364 193.595  1.00 66.53           C  
ATOM   2425  CE  LYS C1157     196.569 215.654 194.282  1.00 72.69           C  
ATOM   2426  NZ  LYS C1157     197.813 216.192 193.701  1.00 73.42           N  
ATOM   2427  N   ASN C1158     190.967 211.619 193.128  1.00 45.90           N  
ATOM   2428  CA  ASN C1158     189.995 210.785 192.416  1.00 54.02           C  
ATOM   2429  C   ASN C1158     190.257 210.801 190.898  1.00 61.02           C  
ATOM   2430  O   ASN C1158     189.372 211.054 190.086  1.00 60.90           O  
ATOM   2431  CB  ASN C1158     188.575 211.239 192.823  1.00 56.64           C  
ATOM   2432  CG  ASN C1158     187.544 210.147 192.889  1.00 62.16           C  
ATOM   2433  OD1 ASN C1158     187.850 208.986 193.129  1.00 66.07           O  
ATOM   2434  ND2 ASN C1158     186.294 210.544 192.749  1.00 64.33           N  
ATOM   2435  N   HIS C1159     191.513 210.583 190.507  1.00 60.53           N  
ATOM   2436  CA  HIS C1159     191.971 210.631 189.119  1.00 57.95           C  
ATOM   2437  C   HIS C1159     191.379 209.466 188.316  1.00 58.34           C  
ATOM   2438  O   HIS C1159     191.649 208.299 188.607  1.00 55.98           O  
ATOM   2439  CB  HIS C1159     193.505 210.617 189.107  1.00 58.98           C  
ATOM   2440  CG  HIS C1159     194.147 210.426 187.757  1.00 64.09           C  
ATOM   2441  ND1 HIS C1159     194.334 211.413 186.792  1.00 64.94           N  
ATOM   2442  CD2 HIS C1159     194.704 209.270 187.310  1.00 63.54           C  
ATOM   2443  CE1 HIS C1159     195.018 210.834 185.796  1.00 64.66           C  
ATOM   2444  NE2 HIS C1159     195.244 209.546 186.078  1.00 61.59           N  
ATOM   2445  N   THR C1160     190.582 209.782 187.297  1.00 58.52           N  
ATOM   2446  CA  THR C1160     190.060 208.794 186.347  1.00 55.89           C  
ATOM   2447  C   THR C1160     190.712 209.012 184.987  1.00 60.23           C  
ATOM   2448  O   THR C1160     190.567 210.073 184.374  1.00 59.90           O  
ATOM   2449  CB  THR C1160     188.532 208.838 186.222  1.00 50.30           C  
ATOM   2450  OG1 THR C1160     188.102 210.083 185.729  1.00 62.41           O  
ATOM   2451  CG2 THR C1160     187.825 208.599 187.554  1.00 55.32           C  
ATOM   2452  N   SER C1161     191.398 207.992 184.489  1.00 58.27           N  
ATOM   2453  CA  SER C1161     192.016 208.002 183.173  1.00 48.08           C  
ATOM   2454  C   SER C1161     190.942 207.953 182.076  1.00 50.30           C  
ATOM   2455  O   SER C1161     189.945 207.238 182.229  1.00 52.50           O  
ATOM   2456  CB  SER C1161     192.996 206.839 183.047  1.00 46.87           C  
ATOM   2457  OG  SER C1161     192.345 205.591 183.133  1.00 47.27           O  
ATOM   2458  N   PRO C1162     191.093 208.715 180.978  1.00 55.10           N  
ATOM   2459  CA  PRO C1162     190.073 208.794 179.943  1.00 64.69           C  
ATOM   2460  C   PRO C1162     189.936 207.505 179.121  1.00 57.86           C  
ATOM   2461  O   PRO C1162     190.892 206.764 178.902  1.00 56.31           O  
ATOM   2462  CB  PRO C1162     190.462 210.003 179.093  1.00 60.96           C  
ATOM   2463  CG  PRO C1162     191.975 210.101 179.264  1.00 50.43           C  
ATOM   2464  CD  PRO C1162     192.174 209.649 180.705  1.00 55.64           C  
ATOM   2465  N   ASP C1163     188.716 207.266 178.635  1.00 54.26           N  
ATOM   2466  CA  ASP C1163     188.351 206.189 177.707  1.00 56.75           C  
ATOM   2467  C   ASP C1163     189.219 206.259 176.444  1.00 64.60           C  
ATOM   2468  O   ASP C1163     189.197 207.263 175.732  1.00 71.70           O  
ATOM   2469  CB  ASP C1163     186.847 206.348 177.398  1.00 60.13           C  
ATOM   2470  CG  ASP C1163     186.245 205.358 176.394  1.00 65.01           C  
ATOM   2471  OD1 ASP C1163     186.954 204.492 175.843  1.00 68.59           O  
ATOM   2472  OD2 ASP C1163     185.022 205.445 176.152  1.00 63.94           O1-
ATOM   2473  N   VAL C1164     190.031 205.231 176.192  1.00 60.66           N  
ATOM   2474  CA  VAL C1164     190.986 205.248 175.080  1.00 61.85           C  
ATOM   2475  C   VAL C1164     190.257 205.161 173.737  1.00 71.57           C  
ATOM   2476  O   VAL C1164     189.592 204.174 173.434  1.00 65.76           O  
ATOM   2477  CB  VAL C1164     192.114 204.212 175.242  1.00 58.32           C  
ATOM   2478  CG1 VAL C1164     191.638 202.797 175.552  1.00 58.15           C  
ATOM   2479  CG2 VAL C1164     193.035 204.171 174.017  1.00 50.09           C  
ATOM   2480  N   ASP C1165     190.437 206.193 172.918  1.00 74.01           N  
ATOM   2481  CA  ASP C1165     190.067 206.226 171.508  1.00 67.38           C  
ATOM   2482  C   ASP C1165     191.327 206.293 170.649  1.00 67.47           C  
ATOM   2483  O   ASP C1165     192.282 206.995 170.978  1.00 75.68           O  
ATOM   2484  CB  ASP C1165     189.133 207.400 171.206  1.00 67.94           C  
ATOM   2485  CG  ASP C1165     187.721 207.213 171.760  1.00 72.56           C  
ATOM   2486  OD1 ASP C1165     187.214 206.075 171.808  1.00 68.31           O  
ATOM   2487  OD2 ASP C1165     187.081 208.229 172.089  1.00 78.61           O1-
ATOM   2488  N   LEU C1166     191.307 205.546 169.552  1.00 58.06           N  
ATOM   2489  CA  LEU C1166     192.369 205.431 168.557  1.00 53.06           C  
ATOM   2490  C   LEU C1166     191.762 205.328 167.142  1.00 58.77           C  
ATOM   2491  O   LEU C1166     190.547 205.176 166.994  1.00 58.80           O  
ATOM   2492  CB  LEU C1166     193.342 204.304 168.965  1.00 53.32           C  
ATOM   2493  CG  LEU C1166     192.928 202.850 168.673  1.00 46.83           C  
ATOM   2494  CD1 LEU C1166     194.053 201.914 169.108  1.00 34.52           C  
ATOM   2495  CD2 LEU C1166     191.668 202.430 169.429  1.00 47.51           C  
ATOM   2496  N   GLY C1167     192.594 205.509 166.119  1.00 58.47           N  
ATOM   2497  CA  GLY C1167     192.256 205.589 164.695  1.00 57.63           C  
ATOM   2498  C   GLY C1167     191.289 204.511 164.192  1.00 58.79           C  
ATOM   2499  O   GLY C1167     191.471 203.316 164.434  1.00 48.20           O  
ATOM   2500  N   ASP C1168     190.254 204.970 163.489  1.00 64.60           N  
ATOM   2501  CA  ASP C1168     189.071 204.235 163.043  1.00 70.48           C  
ATOM   2502  C   ASP C1168     189.122 203.966 161.528  1.00 71.32           C  
ATOM   2503  O   ASP C1168     188.435 204.596 160.720  1.00 71.72           O  
ATOM   2504  CB  ASP C1168     187.797 204.983 163.475  1.00 80.35           C  
ATOM   2505  CG  ASP C1168     187.691 206.463 163.066  1.00 80.87           C  
ATOM   2506  OD1 ASP C1168     188.712 207.131 162.783  1.00 76.65           O  
ATOM   2507  OD2 ASP C1168     186.561 206.997 163.103  1.00 81.53           O1-
ATOM   2508  N   ILE C1169     189.956 203.003 161.138  1.00 72.40           N  
ATOM   2509  CA  ILE C1169     190.329 202.739 159.742  1.00 62.05           C  
ATOM   2510  C   ILE C1169     189.165 202.324 158.820  1.00 70.02           C  
ATOM   2511  O   ILE C1169     189.332 202.322 157.605  1.00 77.31           O  
ATOM   2512  CB  ILE C1169     191.492 201.728 159.701  1.00 53.26           C  
ATOM   2513  CG1 ILE C1169     191.125 200.407 160.400  1.00 56.88           C  
ATOM   2514  CG2 ILE C1169     192.766 202.344 160.308  1.00 48.30           C  
ATOM   2515  CD1 ILE C1169     191.988 199.253 159.902  1.00 54.97           C  
ATOM   2516  N   SER C1170     187.972 202.048 159.351  1.00 70.73           N  
ATOM   2517  CA  SER C1170     186.750 201.800 158.577  1.00 76.57           C  
ATOM   2518  C   SER C1170     186.227 203.018 157.797  1.00 84.68           C  
ATOM   2519  O   SER C1170     185.373 202.861 156.926  1.00 83.46           O  
ATOM   2520  CB  SER C1170     185.666 201.281 159.523  1.00 74.09           C  
ATOM   2521  OG  SER C1170     185.436 202.190 160.584  1.00 64.12           O  
ATOM   2522  N   GLY C1171     186.724 204.233 158.057  1.00 87.39           N  
ATOM   2523  CA  GLY C1171     186.298 205.458 157.354  1.00 90.98           C  
ATOM   2524  C   GLY C1171     187.064 205.771 156.061  1.00 94.92           C  
ATOM   2525  O   GLY C1171     186.747 206.735 155.366  1.00103.42           O  
ATOM   2526  N   ILE C1172     188.077 204.984 155.721  1.00 90.14           N  
ATOM   2527  CA  ILE C1172     188.984 205.204 154.591  1.00 94.28           C  
ATOM   2528  C   ILE C1172     188.328 204.675 153.301  1.00 94.63           C  
ATOM   2529  O   ILE C1172     188.998 204.591 152.272  1.00 92.96           O  
ATOM   2530  CB  ILE C1172     190.336 204.477 154.922  1.00 85.81           C  
ATOM   2531  CG1 ILE C1172     190.951 205.020 156.242  1.00 84.56           C  
ATOM   2532  CG2 ILE C1172     191.385 204.530 153.792  1.00 81.27           C  
ATOM   2533  CD1 ILE C1172     192.184 204.256 156.752  1.00 78.54           C  
ATOM   2534  N   ASN C1173     187.045 204.324 153.327  1.00 95.04           N  
ATOM   2535  CA  ASN C1173     186.394 203.820 152.084  1.00100.33           C  
ATOM   2536  C   ASN C1173     185.389 204.857 151.566  1.00100.91           C  
ATOM   2537  O   ASN C1173     185.189 205.869 152.269  1.00 97.77           O  
ATOM   2538  CB  ASN C1173     185.744 202.447 152.282  1.00101.08           C  
ATOM   2539  CG  ASN C1173     184.290 202.372 151.868  1.00102.06           C  
ATOM   2540  OD1 ASN C1173     183.458 203.135 152.353  1.00101.33           O  
ATOM   2541  ND2 ASN C1173     183.981 201.440 150.980  1.00100.06           N  
ATOM   2542  N   GLN C1180     187.347 193.643 132.368  1.00 76.35           N  
ATOM   2543  CA  GLN C1180     187.434 192.440 131.536  1.00 72.92           C  
ATOM   2544  C   GLN C1180     186.944 192.687 130.105  1.00 72.95           C  
ATOM   2545  O   GLN C1180     187.477 192.095 129.169  1.00 76.63           O  
ATOM   2546  CB  GLN C1180     186.674 191.299 132.239  1.00 77.19           C  
ATOM   2547  CG  GLN C1180     186.480 190.004 131.435  1.00 71.02           C  
ATOM   2548  CD  GLN C1180     187.761 189.283 131.014  1.00 68.16           C  
ATOM   2549  OE1 GLN C1180     188.850 189.497 131.514  1.00 71.17           O  
ATOM   2550  NE2 GLN C1180     187.679 188.350 130.099  1.00 67.60           N  
ATOM   2551  N   LYS C1181     185.979 193.594 129.904  1.00 76.14           N  
ATOM   2552  CA  LYS C1181     185.386 193.915 128.589  1.00 74.08           C  
ATOM   2553  C   LYS C1181     186.427 194.276 127.524  1.00 68.58           C  
ATOM   2554  O   LYS C1181     186.331 193.822 126.393  1.00 71.31           O  
ATOM   2555  CB  LYS C1181     184.355 195.041 128.771  1.00 75.42           C  
ATOM   2556  CG  LYS C1181     183.765 195.552 127.445  1.00 70.68           C  
ATOM   2557  CD  LYS C1181     182.520 196.438 127.636  1.00 75.21           C  
ATOM   2558  CE  LYS C1181     182.707 197.671 128.531  1.00 72.47           C  
ATOM   2559  NZ  LYS C1181     183.715 198.634 128.023  1.00 74.73           N  
ATOM   2560  N   GLU C1182     187.450 195.049 127.860  1.00 65.15           N  
ATOM   2561  CA  GLU C1182     188.512 195.368 126.907  1.00 62.44           C  
ATOM   2562  C   GLU C1182     189.381 194.147 126.574  1.00 62.50           C  
ATOM   2563  O   GLU C1182     189.777 193.991 125.425  1.00 70.01           O  
ATOM   2564  CB  GLU C1182     189.357 196.545 127.408  1.00 61.13           C  
ATOM   2565  CG  GLU C1182     188.513 197.832 127.508  1.00 64.66           C  
ATOM   2566  CD  GLU C1182     187.570 197.884 128.721  1.00 69.58           C  
ATOM   2567  OE1 GLU C1182     187.933 197.376 129.809  1.00 80.00           O  
ATOM   2568  OE2 GLU C1182     186.431 198.379 128.563  1.00 70.06           O1-
ATOM   2569  N   ILE C1183     189.618 193.230 127.519  1.00 62.09           N  
ATOM   2570  CA  ILE C1183     190.324 191.971 127.239  1.00 65.87           C  
ATOM   2571  C   ILE C1183     189.451 191.038 126.389  1.00 66.87           C  
ATOM   2572  O   ILE C1183     189.959 190.367 125.493  1.00 72.12           O  
ATOM   2573  CB  ILE C1183     190.818 191.300 128.544  1.00 72.20           C  
ATOM   2574  CG1 ILE C1183     191.703 192.264 129.375  1.00 76.39           C  
ATOM   2575  CG2 ILE C1183     191.606 190.017 128.227  1.00 62.81           C  
ATOM   2576  CD1 ILE C1183     190.976 192.814 130.613  1.00 73.28           C  
ATOM   2577  N   ASP C1184     188.130 191.039 126.584  1.00 69.11           N  
ATOM   2578  CA  ASP C1184     187.170 190.347 125.710  1.00 72.03           C  
ATOM   2579  C   ASP C1184     187.216 190.878 124.263  1.00 71.76           C  
ATOM   2580  O   ASP C1184     187.336 190.099 123.316  1.00 73.90           O  
ATOM   2581  CB  ASP C1184     185.752 190.453 126.303  1.00 78.73           C  
ATOM   2582  CG  ASP C1184     184.672 190.019 125.315  1.00 85.44           C  
ATOM   2583  OD1 ASP C1184     183.785 190.834 124.994  1.00 85.20           O  
ATOM   2584  OD2 ASP C1184     184.711 188.860 124.857  1.00 88.64           O1-
ATOM   2585  N   ARG C1185     187.226 192.201 124.115  1.00 74.60           N  
ATOM   2586  CA  ARG C1185     187.317 192.836 122.799  1.00 69.32           C  
ATOM   2587  C   ARG C1185     188.656 192.515 122.122  1.00 63.92           C  
ATOM   2588  O   ARG C1185     188.686 192.097 120.965  1.00 67.70           O  
ATOM   2589  CB  ARG C1185     187.145 194.351 122.920  1.00 67.78           C  
ATOM   2590  CG  ARG C1185     185.730 194.843 122.661  1.00 72.39           C  
ATOM   2591  CD  ARG C1185     184.697 194.048 123.443  1.00 79.61           C  
ATOM   2592  NE  ARG C1185     183.346 194.562 123.229  1.00 84.28           N  
ATOM   2593  CZ  ARG C1185     182.242 193.982 123.688  1.00 87.10           C  
ATOM   2594  NH1 ARG C1185     182.319 192.860 124.389  1.00 90.58           N  
ATOM   2595  NH2 ARG C1185     181.057 194.525 123.443  1.00 90.93           N  
ATOM   2596  N   LEU C1186     189.756 192.707 122.848  1.00 65.36           N  
ATOM   2597  CA  LEU C1186     191.081 192.399 122.295  1.00 66.04           C  
ATOM   2598  C   LEU C1186     191.231 190.909 121.900  1.00 64.30           C  
ATOM   2599  O   LEU C1186     191.851 190.621 120.883  1.00 68.78           O  
ATOM   2600  CB  LEU C1186     192.192 192.836 123.269  1.00 69.48           C  
ATOM   2601  CG  LEU C1186     192.781 194.243 123.038  1.00 69.94           C  
ATOM   2602  CD1 LEU C1186     191.806 195.390 123.263  1.00 67.15           C  
ATOM   2603  CD2 LEU C1186     193.989 194.452 123.949  1.00 64.46           C  
ATOM   2604  N   ASN C1187     190.630 189.962 122.625  1.00 64.89           N  
ATOM   2605  CA  ASN C1187     190.580 188.559 122.187  1.00 64.37           C  
ATOM   2606  C   ASN C1187     189.698 188.399 120.933  1.00 69.82           C  
ATOM   2607  O   ASN C1187     190.064 187.688 119.995  1.00 72.40           O  
ATOM   2608  CB  ASN C1187     190.083 187.660 123.335  1.00 63.27           C  
ATOM   2609  CG  ASN C1187     191.194 187.239 124.276  1.00 69.68           C  
ATOM   2610  OD1 ASN C1187     191.931 186.300 124.014  1.00 71.30           O  
ATOM   2611  ND2 ASN C1187     191.355 187.898 125.391  1.00 71.93           N  
ATOM   2612  N   GLU C1188     188.554 189.089 120.886  1.00 70.16           N  
ATOM   2613  CA  GLU C1188     187.646 189.086 119.734  1.00 66.83           C  
ATOM   2614  C   GLU C1188     188.304 189.654 118.465  1.00 70.10           C  
ATOM   2615  O   GLU C1188     188.262 188.996 117.430  1.00 76.06           O  
ATOM   2616  CB  GLU C1188     186.331 189.790 120.115  1.00 66.21           C  
ATOM   2617  CG  GLU C1188     185.334 189.982 118.958  1.00 73.00           C  
ATOM   2618  CD  GLU C1188     185.382 191.376 118.301  1.00 77.25           C  
ATOM   2619  OE1 GLU C1188     185.343 191.461 117.053  1.00 78.79           O  
ATOM   2620  OE2 GLU C1188     185.360 192.399 119.015  1.00 79.93           O1-
ATOM   2621  N   VAL C1189     188.964 190.815 118.508  1.00 68.83           N  
ATOM   2622  CA  VAL C1189     189.639 191.374 117.323  1.00 62.16           C  
ATOM   2623  C   VAL C1189     190.945 190.665 116.985  1.00 65.30           C  
ATOM   2624  O   VAL C1189     191.358 190.722 115.837  1.00 73.36           O  
ATOM   2625  CB  VAL C1189     189.856 192.890 117.396  1.00 57.87           C  
ATOM   2626  CG1 VAL C1189     188.539 193.634 117.599  1.00 58.63           C  
ATOM   2627  CG2 VAL C1189     190.862 193.268 118.470  1.00 62.40           C  
ATOM   2628  N   ALA C1190     191.578 189.926 117.899  1.00 64.28           N  
ATOM   2629  CA  ALA C1190     192.708 189.076 117.522  1.00 68.07           C  
ATOM   2630  C   ALA C1190     192.262 187.983 116.541  1.00 74.57           C  
ATOM   2631  O   ALA C1190     192.959 187.709 115.561  1.00 81.18           O  
ATOM   2632  CB  ALA C1190     193.344 188.454 118.765  1.00 70.55           C  
ATOM   2633  N   LYS C1191     191.064 187.419 116.743  1.00 75.79           N  
ATOM   2634  CA  LYS C1191     190.410 186.560 115.744  1.00 80.67           C  
ATOM   2635  C   LYS C1191     189.877 187.367 114.555  1.00 80.23           C  
ATOM   2636  O   LYS C1191     190.326 187.168 113.430  1.00 79.08           O  
ATOM   2637  CB  LYS C1191     189.331 185.668 116.385  1.00 80.35           C  
ATOM   2638  CG  LYS C1191     189.958 184.682 117.387  1.00 92.59           C  
ATOM   2639  CD  LYS C1191     188.959 183.623 117.873  1.00 98.69           C  
ATOM   2640  CE  LYS C1191     189.640 182.667 118.859  1.00105.64           C  
ATOM   2641  NZ  LYS C1191     188.768 181.529 119.235  1.00112.56           N  
ATOM   2642  N   ASN C1192     188.969 188.314 114.784  1.00 76.36           N  
ATOM   2643  CA  ASN C1192     188.272 189.059 113.733  1.00 73.96           C  
ATOM   2644  C   ASN C1192     189.145 189.995 112.877  1.00 73.41           C  
ATOM   2645  O   ASN C1192     188.656 190.538 111.892  1.00 72.74           O  
ATOM   2646  CB  ASN C1192     187.049 189.774 114.338  1.00 70.26           C  
ATOM   2647  CG  ASN C1192     185.943 188.816 114.740  1.00 72.57           C  
ATOM   2648  OD1 ASN C1192     185.945 187.634 114.434  1.00 70.62           O  
ATOM   2649  ND2 ASN C1192     184.929 189.297 115.408  1.00 74.08           N  
ATOM   2650  N   LEU C1193     190.430 190.188 113.178  1.00 70.23           N  
ATOM   2651  CA  LEU C1193     191.360 190.865 112.268  1.00 68.60           C  
ATOM   2652  C   LEU C1193     191.813 189.966 111.101  1.00 79.13           C  
ATOM   2653  O   LEU C1193     192.164 190.483 110.044  1.00 82.26           O  
ATOM   2654  CB  LEU C1193     192.510 191.477 113.086  1.00 68.63           C  
ATOM   2655  CG  LEU C1193     193.471 192.404 112.329  1.00 71.30           C  
ATOM   2656  CD1 LEU C1193     192.765 193.597 111.691  1.00 67.35           C  
ATOM   2657  CD2 LEU C1193     194.502 192.969 113.314  1.00 71.41           C  
ATOM   2658  N   ASN C1194     191.699 188.633 111.213  1.00 92.41           N  
ATOM   2659  CA  ASN C1194     191.925 187.711 110.086  1.00 82.04           C  
ATOM   2660  C   ASN C1194     190.896 187.866 108.949  1.00 77.85           C  
ATOM   2661  O   ASN C1194     191.191 187.589 107.784  1.00 73.52           O  
ATOM   2662  CB  ASN C1194     191.970 186.260 110.599  1.00 85.85           C  
ATOM   2663  CG  ASN C1194     193.273 185.595 110.215  1.00 91.67           C  
ATOM   2664  OD1 ASN C1194     194.320 186.144 110.523  1.00 91.40           O  
ATOM   2665  ND2 ASN C1194     193.250 184.372 109.712  1.00 92.90           N  
ATOM   2666  N   GLU C1195     189.716 188.401 109.268  1.00 72.21           N  
ATOM   2667  CA  GLU C1195     188.708 188.794 108.275  1.00 72.66           C  
ATOM   2668  C   GLU C1195     189.142 189.986 107.408  1.00 70.29           C  
ATOM   2669  O   GLU C1195     188.460 190.320 106.442  1.00 71.14           O  
ATOM   2670  CB  GLU C1195     187.377 189.114 108.964  1.00 70.04           C  
ATOM   2671  CG  GLU C1195     186.795 187.928 109.738  1.00 67.74           C  
ATOM   2672  CD  GLU C1195     185.337 188.202 110.108  1.00 70.30           C  
ATOM   2673  OE1 GLU C1195     185.085 189.070 110.972  1.00 73.59           O  
ATOM   2674  OE2 GLU C1195     184.429 187.563 109.533  1.00 73.00           O1-
ATOM   2675  N   SER C1196     190.282 190.612 107.718  1.00 67.01           N  
ATOM   2676  CA  SER C1196     190.892 191.672 106.911  1.00 65.85           C  
ATOM   2677  C   SER C1196     192.332 191.346 106.492  1.00 68.31           C  
ATOM   2678  O   SER C1196     193.079 192.240 106.108  1.00 75.01           O  
ATOM   2679  CB  SER C1196     190.757 193.013 107.641  1.00 67.73           C  
ATOM   2680  OG  SER C1196     190.315 194.012 106.752  1.00 67.94           O  
ATOM   2681  N   LEU C1197     192.746 190.078 106.567  1.00 69.27           N  
ATOM   2682  CA  LEU C1197     194.054 189.619 106.093  1.00 70.90           C  
ATOM   2683  C   LEU C1197     194.155 189.696 104.555  1.00 72.34           C  
ATOM   2684  O   LEU C1197     193.647 188.839 103.830  1.00 80.18           O  
ATOM   2685  CB  LEU C1197     194.301 188.206 106.651  1.00 74.57           C  
ATOM   2686  CG  LEU C1197     195.673 187.603 106.300  1.00 74.84           C  
ATOM   2687  CD1 LEU C1197     196.819 188.421 106.896  1.00 79.06           C  
ATOM   2688  CD2 LEU C1197     195.761 186.182 106.845  1.00 78.01           C  
TER    2689      LEU C1197                                                      
ATOM   2690  N   ASN A 703     193.053 167.910 262.047  1.00 78.04           N  
ATOM   2691  CA  ASN A 703     193.883 168.859 262.836  1.00 80.61           C  
ATOM   2692  C   ASN A 703     195.160 169.255 262.070  1.00 78.19           C  
ATOM   2693  O   ASN A 703     196.269 168.899 262.467  1.00 71.52           O  
ATOM   2694  CB  ASN A 703     194.205 168.291 264.244  1.00 84.75           C  
ATOM   2695  CG  ASN A 703     194.995 166.979 264.248  1.00 88.28           C  
ATOM   2696  OD1 ASN A 703     194.911 166.178 263.330  1.00 83.75           O  
ATOM   2697  ND2 ASN A 703     195.771 166.697 265.273  1.00 89.69           N  
ATOM   2698  N   SER A 704     195.039 169.978 260.952  1.00 78.14           N  
ATOM   2699  CA  SER A 704     196.103 170.015 259.927  1.00 77.89           C  
ATOM   2700  C   SER A 704     197.358 170.799 260.335  1.00 71.25           C  
ATOM   2701  O   SER A 704     198.420 170.202 260.535  1.00 75.70           O  
ATOM   2702  CB  SER A 704     195.536 170.524 258.597  1.00 74.79           C  
ATOM   2703  OG  SER A 704     194.974 171.815 258.724  1.00 74.07           O  
ATOM   2704  N   VAL A 705     197.264 172.126 260.472  1.00 63.48           N  
ATOM   2705  CA  VAL A 705     198.435 172.999 260.702  1.00 66.92           C  
ATOM   2706  C   VAL A 705     198.271 173.953 261.887  1.00 66.65           C  
ATOM   2707  O   VAL A 705     199.265 174.313 262.508  1.00 70.03           O  
ATOM   2708  CB  VAL A 705     198.853 173.688 259.382  1.00 68.76           C  
ATOM   2709  CG1 VAL A 705     197.870 174.760 258.899  1.00 65.17           C  
ATOM   2710  CG2 VAL A 705     200.249 174.300 259.497  1.00 72.78           C  
ATOM   2711  N   ALA A 706     197.035 174.269 262.281  1.00 61.28           N  
ATOM   2712  CA  ALA A 706     196.725 175.208 263.359  1.00 57.83           C  
ATOM   2713  C   ALA A 706     197.317 174.858 264.727  1.00 57.46           C  
ATOM   2714  O   ALA A 706     197.418 175.741 265.572  1.00 55.15           O  
ATOM   2715  CB  ALA A 706     195.203 175.338 263.472  1.00 53.03           C  
ATOM   2716  N   TYR A 707     197.723 173.600 264.929  1.00 58.85           N  
ATOM   2717  CA  TYR A 707     198.295 173.065 266.167  1.00 51.74           C  
ATOM   2718  C   TYR A 707     199.673 172.393 265.983  1.00 58.45           C  
ATOM   2719  O   TYR A 707     200.193 171.764 266.902  1.00 63.90           O  
ATOM   2720  CB  TYR A 707     197.292 172.086 266.786  1.00 48.97           C  
ATOM   2721  CG  TYR A 707     195.849 172.549 266.807  1.00 50.84           C  
ATOM   2722  CD1 TYR A 707     194.896 171.938 265.976  1.00 49.01           C  
ATOM   2723  CD2 TYR A 707     195.448 173.549 267.707  1.00 57.84           C  
ATOM   2724  CE1 TYR A 707     193.533 172.268 266.104  1.00 58.90           C  
ATOM   2725  CE2 TYR A 707     194.089 173.892 267.834  1.00 52.38           C  
ATOM   2726  CZ  TYR A 707     193.127 173.227 267.052  1.00 58.12           C  
ATOM   2727  OH  TYR A 707     191.809 173.465 267.248  1.00 65.88           O  
ATOM   2728  N   SER A 708     200.275 172.478 264.797  1.00 60.76           N  
ATOM   2729  CA  SER A 708     201.631 171.962 264.548  1.00 59.84           C  
ATOM   2730  C   SER A 708     202.679 172.855 265.200  1.00 54.68           C  
ATOM   2731  O   SER A 708     202.520 174.076 265.246  1.00 60.42           O  
ATOM   2732  CB  SER A 708     201.886 171.845 263.043  1.00 71.81           C  
ATOM   2733  OG  SER A 708     201.887 173.107 262.393  1.00 65.86           O  
ATOM   2734  N   ASN A 709     203.751 172.302 265.751  1.00 52.58           N  
ATOM   2735  CA  ASN A 709     204.771 173.236 266.236  1.00 57.27           C  
ATOM   2736  C   ASN A 709     206.075 173.148 265.545  1.00 57.88           C  
ATOM   2737  O   ASN A 709     206.696 172.100 265.365  1.00 61.23           O  
ATOM   2738  CB  ASN A 709     204.839 173.465 267.712  1.00 61.57           C  
ATOM   2739  CG  ASN A 709     205.203 172.253 268.428  1.00 64.39           C  
ATOM   2740  OD1 ASN A 709     205.970 171.437 267.940  1.00 69.83           O  
ATOM   2741  ND2 ASN A 709     204.681 172.117 269.590  1.00 65.17           N  
ATOM   2742  N   ASN A 710     206.449 174.340 265.164  1.00 52.63           N  
ATOM   2743  CA  ASN A 710     207.612 174.583 264.312  1.00 50.62           C  
ATOM   2744  C   ASN A 710     208.422 175.765 264.860  1.00 45.27           C  
ATOM   2745  O   ASN A 710     207.897 176.638 265.551  1.00 48.09           O  
ATOM   2746  CB  ASN A 710     207.197 174.747 262.843  1.00 63.14           C  
ATOM   2747  CG  ASN A 710     206.198 175.860 262.572  1.00 61.17           C  
ATOM   2748  OD1 ASN A 710     205.580 176.455 263.433  1.00 47.30           O  
ATOM   2749  ND2 ASN A 710     206.012 176.176 261.320  1.00 60.13           N  
ATOM   2750  N   SER A 711     209.728 175.762 264.595  1.00 49.70           N  
ATOM   2751  CA  SER A 711     210.682 176.784 265.038  1.00 54.72           C  
ATOM   2752  C   SER A 711     210.461 178.103 264.288  1.00 52.87           C  
ATOM   2753  O   SER A 711     210.643 178.165 263.071  1.00 54.87           O  
ATOM   2754  CB  SER A 711     212.119 176.298 264.809  1.00 55.33           C  
ATOM   2755  OG  SER A 711     212.345 175.003 265.331  1.00 60.73           O  
ATOM   2756  N   ILE A 712     210.100 179.171 264.999  1.00 49.61           N  
ATOM   2757  CA  ILE A 712     209.845 180.503 264.447  1.00 41.87           C  
ATOM   2758  C   ILE A 712     210.824 181.507 265.024  1.00 47.83           C  
ATOM   2759  O   ILE A 712     210.965 181.598 266.238  1.00 55.47           O  
ATOM   2760  CB  ILE A 712     208.385 180.900 264.714  1.00 42.96           C  
ATOM   2761  CG1 ILE A 712     207.523 180.119 263.707  1.00 48.28           C  
ATOM   2762  CG2 ILE A 712     208.152 182.418 264.597  1.00 48.65           C  
ATOM   2763  CD1 ILE A 712     206.050 180.497 263.726  1.00 55.71           C  
ATOM   2764  N   ALA A 713     211.481 182.291 264.171  1.00 50.38           N  
ATOM   2765  CA  ALA A 713     212.333 183.380 264.621  1.00 50.98           C  
ATOM   2766  C   ALA A 713     211.485 184.502 265.223  1.00 53.44           C  
ATOM   2767  O   ALA A 713     210.526 184.988 264.615  1.00 46.97           O  
ATOM   2768  CB  ALA A 713     213.217 183.871 263.475  1.00 59.80           C  
ATOM   2769  N   ILE A 714     211.836 184.887 266.446  1.00 64.59           N  
ATOM   2770  CA  ILE A 714     211.210 185.960 267.212  1.00 56.84           C  
ATOM   2771  C   ILE A 714     212.336 186.918 267.609  1.00 57.49           C  
ATOM   2772  O   ILE A 714     213.347 186.445 268.130  1.00 59.60           O  
ATOM   2773  CB  ILE A 714     210.433 185.404 268.423  1.00 44.55           C  
ATOM   2774  CG1 ILE A 714     209.344 184.410 267.948  1.00 42.02           C  
ATOM   2775  CG2 ILE A 714     209.841 186.568 269.231  1.00 49.01           C  
ATOM   2776  CD1 ILE A 714     208.412 183.874 269.032  1.00 41.47           C  
ATOM   2777  N   PRO A 715     212.223 188.234 267.354  1.00 55.44           N  
ATOM   2778  CA  PRO A 715     213.298 189.182 267.613  1.00 55.94           C  
ATOM   2779  C   PRO A 715     213.808 189.143 269.050  1.00 59.72           C  
ATOM   2780  O   PRO A 715     213.069 189.404 270.000  1.00 59.23           O  
ATOM   2781  CB  PRO A 715     212.746 190.549 267.246  1.00 53.92           C  
ATOM   2782  CG  PRO A 715     211.750 190.208 266.142  1.00 59.63           C  
ATOM   2783  CD  PRO A 715     211.160 188.890 266.622  1.00 56.92           C  
ATOM   2784  N   THR A 716     215.084 188.807 269.214  1.00 66.00           N  
ATOM   2785  CA  THR A 716     215.736 188.748 270.519  1.00 63.11           C  
ATOM   2786  C   THR A 716     216.175 190.150 270.883  1.00 55.07           C  
ATOM   2787  O   THR A 716     215.975 190.580 272.013  1.00 51.22           O  
ATOM   2788  CB  THR A 716     216.955 187.818 270.548  1.00 66.68           C  
ATOM   2789  OG1 THR A 716     216.578 186.506 270.221  1.00 75.59           O  
ATOM   2790  CG2 THR A 716     217.602 187.731 271.923  1.00 56.73           C  
ATOM   2791  N   ASN A 717     216.722 190.875 269.906  1.00 63.38           N  
ATOM   2792  CA  ASN A 717     217.255 192.215 270.158  1.00 66.64           C  
ATOM   2793  C   ASN A 717     217.274 193.150 268.960  1.00 61.36           C  
ATOM   2794  O   ASN A 717     217.112 192.721 267.818  1.00 66.03           O  
ATOM   2795  CB  ASN A 717     218.656 192.136 270.742  1.00 64.18           C  
ATOM   2796  CG  ASN A 717     218.661 192.333 272.231  1.00 70.56           C  
ATOM   2797  OD1 ASN A 717     217.727 192.935 272.780  1.00 73.64           O  
ATOM   2798  ND2 ASN A 717     219.714 191.811 272.887  1.00 73.81           N  
ATOM   2799  N   PHE A 718     217.444 194.445 269.199  1.00 57.25           N  
ATOM   2800  CA  PHE A 718     217.389 195.393 268.088  1.00 55.87           C  
ATOM   2801  C   PHE A 718     218.620 196.240 267.820  1.00 58.46           C  
ATOM   2802  O   PHE A 718     219.285 196.706 268.740  1.00 69.75           O  
ATOM   2803  CB  PHE A 718     216.163 196.277 268.264  1.00 53.05           C  
ATOM   2804  CG  PHE A 718     214.885 195.498 268.439  1.00 48.30           C  
ATOM   2805  CD1 PHE A 718     214.344 194.763 267.378  1.00 46.48           C  
ATOM   2806  CD2 PHE A 718     214.257 195.489 269.689  1.00 49.59           C  
ATOM   2807  CE1 PHE A 718     213.165 194.036 267.560  1.00 38.54           C  
ATOM   2808  CE2 PHE A 718     213.080 194.759 269.874  1.00 52.72           C  
ATOM   2809  CZ  PHE A 718     212.538 194.031 268.812  1.00 46.50           C  
ATOM   2810  N   THR A 719     218.850 196.509 266.540  1.00 55.08           N  
ATOM   2811  CA  THR A 719     219.750 197.536 266.023  1.00 55.07           C  
ATOM   2812  C   THR A 719     218.904 198.633 265.393  1.00 55.60           C  
ATOM   2813  O   THR A 719     217.929 198.359 264.697  1.00 54.83           O  
ATOM   2814  CB  THR A 719     220.749 196.938 265.027  1.00 54.21           C  
ATOM   2815  OG1 THR A 719     221.790 196.322 265.742  1.00 72.42           O  
ATOM   2816  CG2 THR A 719     221.440 197.937 264.106  1.00 52.08           C  
ATOM   2817  N   ILE A 720     219.256 199.882 265.659  1.00 62.56           N  
ATOM   2818  CA  ILE A 720     218.663 201.035 264.989  1.00 52.08           C  
ATOM   2819  C   ILE A 720     219.220 201.187 263.568  1.00 54.22           C  
ATOM   2820  O   ILE A 720     220.384 200.911 263.293  1.00 56.62           O  
ATOM   2821  CB  ILE A 720     218.796 202.275 265.885  1.00 54.84           C  
ATOM   2822  CG1 ILE A 720     218.144 203.538 265.303  1.00 44.41           C  
ATOM   2823  CG2 ILE A 720     220.241 202.597 266.247  1.00 60.76           C  
ATOM   2824  CD1 ILE A 720     216.620 203.448 265.376  1.00 42.59           C  
ATOM   2825  N   SER A 721     218.361 201.568 262.635  1.00 61.70           N  
ATOM   2826  CA  SER A 721     218.635 201.557 261.203  1.00 54.77           C  
ATOM   2827  C   SER A 721     217.864 202.654 260.475  1.00 54.64           C  
ATOM   2828  O   SER A 721     216.887 203.185 260.997  1.00 59.30           O  
ATOM   2829  CB  SER A 721     218.293 200.188 260.635  1.00 52.15           C  
ATOM   2830  OG  SER A 721     216.925 199.920 260.738  1.00 50.81           O  
ATOM   2831  N   VAL A 722     218.293 203.014 259.269  1.00 55.19           N  
ATOM   2832  CA  VAL A 722     217.562 203.935 258.402  1.00 55.93           C  
ATOM   2833  C   VAL A 722     217.481 203.387 256.994  1.00 59.01           C  
ATOM   2834  O   VAL A 722     218.407 202.740 256.518  1.00 64.15           O  
ATOM   2835  CB  VAL A 722     218.121 205.363 258.425  1.00 51.75           C  
ATOM   2836  CG1 VAL A 722     218.169 205.909 259.847  1.00 57.84           C  
ATOM   2837  CG2 VAL A 722     219.510 205.477 257.812  1.00 56.27           C  
ATOM   2838  N   THR A 723     216.378 203.636 256.310  1.00 53.40           N  
ATOM   2839  CA  THR A 723     216.177 203.240 254.915  1.00 53.33           C  
ATOM   2840  C   THR A 723     216.077 204.488 254.053  1.00 59.18           C  
ATOM   2841  O   THR A 723     215.476 205.471 254.472  1.00 64.17           O  
ATOM   2842  CB  THR A 723     214.940 202.355 254.763  1.00 53.93           C  
ATOM   2843  OG1 THR A 723     215.106 201.211 255.570  1.00 59.82           O  
ATOM   2844  CG2 THR A 723     214.723 201.873 253.332  1.00 54.37           C  
ATOM   2845  N   THR A 724     216.654 204.460 252.860  1.00 61.29           N  
ATOM   2846  CA  THR A 724     216.309 205.388 251.782  1.00 57.50           C  
ATOM   2847  C   THR A 724     215.454 204.593 250.808  1.00 56.30           C  
ATOM   2848  O   THR A 724     215.943 203.625 250.239  1.00 59.06           O  
ATOM   2849  CB  THR A 724     217.573 205.920 251.099  1.00 65.06           C  
ATOM   2850  OG1 THR A 724     218.410 206.551 252.041  1.00 73.58           O  
ATOM   2851  CG2 THR A 724     217.279 206.964 250.029  1.00 63.50           C  
ATOM   2852  N   GLU A 725     214.181 204.933 250.644  1.00 52.35           N  
ATOM   2853  CA  GLU A 725     213.266 204.235 249.735  1.00 49.32           C  
ATOM   2854  C   GLU A 725     212.839 205.178 248.616  1.00 53.99           C  
ATOM   2855  O   GLU A 725     212.236 206.204 248.902  1.00 52.98           O  
ATOM   2856  CB  GLU A 725     212.056 203.684 250.509  1.00 48.01           C  
ATOM   2857  CG  GLU A 725     210.890 203.275 249.592  1.00 41.99           C  
ATOM   2858  CD  GLU A 725     209.924 202.198 250.118  1.00 46.83           C  
ATOM   2859  OE1 GLU A 725     209.662 202.057 251.330  1.00 43.47           O  
ATOM   2860  OE2 GLU A 725     209.305 201.504 249.283  1.00 51.68           O1-
ATOM   2861  N   ILE A 726     213.108 204.836 247.354  1.00 58.22           N  
ATOM   2862  CA  ILE A 726     212.787 205.675 246.187  1.00 50.16           C  
ATOM   2863  C   ILE A 726     211.533 205.143 245.475  1.00 50.24           C  
ATOM   2864  O   ILE A 726     211.499 203.983 245.074  1.00 54.25           O  
ATOM   2865  CB  ILE A 726     213.993 205.725 245.223  1.00 55.22           C  
ATOM   2866  CG1 ILE A 726     215.294 206.221 245.895  1.00 55.76           C  
ATOM   2867  CG2 ILE A 726     213.697 206.621 244.011  1.00 59.70           C  
ATOM   2868  CD1 ILE A 726     216.502 205.368 245.536  1.00 61.47           C  
ATOM   2869  N   LEU A 727     210.511 205.985 245.302  1.00 46.31           N  
ATOM   2870  CA  LEU A 727     209.302 205.718 244.512  1.00 46.93           C  
ATOM   2871  C   LEU A 727     209.139 206.763 243.398  1.00 53.76           C  
ATOM   2872  O   LEU A 727     209.003 207.946 243.707  1.00 54.57           O  
ATOM   2873  CB  LEU A 727     208.040 205.795 245.385  1.00 38.58           C  
ATOM   2874  CG  LEU A 727     207.640 204.523 246.122  1.00 36.16           C  
ATOM   2875  CD1 LEU A 727     208.564 204.222 247.279  1.00 41.57           C  
ATOM   2876  CD2 LEU A 727     206.253 204.716 246.720  1.00 23.45           C  
ATOM   2877  N   PRO A 728     209.035 206.379 242.118  1.00 51.52           N  
ATOM   2878  CA  PRO A 728     208.581 207.291 241.085  1.00 45.04           C  
ATOM   2879  C   PRO A 728     207.083 207.568 241.230  1.00 43.26           C  
ATOM   2880  O   PRO A 728     206.286 206.650 241.404  1.00 43.25           O  
ATOM   2881  CB  PRO A 728     208.929 206.610 239.773  1.00 49.43           C  
ATOM   2882  CG  PRO A 728     208.906 205.128 240.116  1.00 45.48           C  
ATOM   2883  CD  PRO A 728     209.348 205.076 241.564  1.00 46.10           C  
ATOM   2884  N   VAL A 729     206.700 208.840 241.158  1.00 44.81           N  
ATOM   2885  CA  VAL A 729     205.314 209.322 241.301  1.00 42.40           C  
ATOM   2886  C   VAL A 729     204.771 209.942 240.014  1.00 50.88           C  
ATOM   2887  O   VAL A 729     203.564 210.107 239.864  1.00 54.30           O  
ATOM   2888  CB  VAL A 729     205.155 210.298 242.478  1.00 49.64           C  
ATOM   2889  CG1 VAL A 729     205.679 209.685 243.777  1.00 58.81           C  
ATOM   2890  CG2 VAL A 729     205.837 211.652 242.265  1.00 50.49           C  
ATOM   2891  N   SER A 730     205.630 210.282 239.063  1.00 58.37           N  
ATOM   2892  CA  SER A 730     205.261 210.866 237.773  1.00 55.40           C  
ATOM   2893  C   SER A 730     206.158 210.337 236.661  1.00 53.12           C  
ATOM   2894  O   SER A 730     207.188 209.707 236.899  1.00 52.31           O  
ATOM   2895  CB  SER A 730     205.270 212.398 237.853  1.00 56.63           C  
ATOM   2896  OG  SER A 730     206.486 212.917 238.340  1.00 59.72           O  
ATOM   2897  N   MET A 731     205.712 210.530 235.425  1.00 53.16           N  
ATOM   2898  CA  MET A 731     206.415 210.122 234.214  1.00 50.25           C  
ATOM   2899  C   MET A 731     206.446 211.294 233.235  1.00 52.91           C  
ATOM   2900  O   MET A 731     205.397 211.852 232.909  1.00 61.50           O  
ATOM   2901  CB  MET A 731     205.687 208.896 233.650  1.00 42.60           C  
ATOM   2902  CG  MET A 731     206.268 208.336 232.361  1.00 47.58           C  
ATOM   2903  SD  MET A 731     205.665 206.679 232.027  1.00 31.03           S  
ATOM   2904  CE  MET A 731     206.559 206.268 230.526  1.00 29.86           C  
ATOM   2905  N   THR A 732     207.630 211.668 232.753  1.00 48.89           N  
ATOM   2906  CA  THR A 732     207.760 212.702 231.715  1.00 49.23           C  
ATOM   2907  C   THR A 732     207.108 212.244 230.408  1.00 56.63           C  
ATOM   2908  O   THR A 732     207.141 211.059 230.065  1.00 56.17           O  
ATOM   2909  CB  THR A 732     209.216 213.141 231.512  1.00 47.30           C  
ATOM   2910  OG1 THR A 732     209.258 214.266 230.664  1.00 54.31           O  
ATOM   2911  CG2 THR A 732     210.105 212.072 230.885  1.00 42.07           C  
ATOM   2912  N   LYS A 733     206.463 213.171 229.692  1.00 57.30           N  
ATOM   2913  CA  LYS A 733     205.610 212.867 228.539  1.00 53.08           C  
ATOM   2914  C   LYS A 733     206.444 212.642 227.283  1.00 55.73           C  
ATOM   2915  O   LYS A 733     206.775 213.568 226.544  1.00 56.24           O  
ATOM   2916  CB  LYS A 733     204.553 213.963 228.357  1.00 54.71           C  
ATOM   2917  CG  LYS A 733     203.702 214.232 229.607  1.00 60.57           C  
ATOM   2918  CD  LYS A 733     202.962 213.014 230.174  1.00 54.02           C  
ATOM   2919  CE  LYS A 733     202.194 213.360 231.459  1.00 51.92           C  
ATOM   2920  NZ  LYS A 733     201.146 214.384 231.246  1.00 52.56           N  
ATOM   2921  N   THR A 734     206.805 211.389 227.055  1.00 57.29           N  
ATOM   2922  CA  THR A 734     207.597 210.895 225.927  1.00 51.34           C  
ATOM   2923  C   THR A 734     206.814 210.897 224.610  1.00 47.66           C  
ATOM   2924  O   THR A 734     206.672 209.850 223.976  1.00 49.57           O  
ATOM   2925  CB  THR A 734     208.127 209.491 226.259  1.00 53.23           C  
ATOM   2926  OG1 THR A 734     207.060 208.656 226.655  1.00 46.99           O  
ATOM   2927  CG2 THR A 734     209.147 209.504 227.393  1.00 54.40           C  
ATOM   2928  N   SER A 735     206.287 212.050 224.189  1.00 46.20           N  
ATOM   2929  CA  SER A 735     205.639 212.228 222.883  1.00 43.52           C  
ATOM   2930  C   SER A 735     206.566 211.807 221.737  1.00 41.78           C  
ATOM   2931  O   SER A 735     207.790 211.915 221.829  1.00 41.65           O  
ATOM   2932  CB  SER A 735     205.158 213.675 222.720  1.00 45.45           C  
ATOM   2933  OG  SER A 735     206.204 214.620 222.864  1.00 47.76           O  
ATOM   2934  N   VAL A 736     206.000 211.267 220.663  1.00 43.20           N  
ATOM   2935  CA  VAL A 736     206.745 210.654 219.555  1.00 44.91           C  
ATOM   2936  C   VAL A 736     206.353 211.287 218.227  1.00 53.02           C  
ATOM   2937  O   VAL A 736     205.172 211.366 217.899  1.00 52.13           O  
ATOM   2938  CB  VAL A 736     206.600 209.118 219.595  1.00 38.58           C  
ATOM   2939  CG1 VAL A 736     205.165 208.604 219.485  1.00 33.11           C  
ATOM   2940  CG2 VAL A 736     207.425 208.429 218.519  1.00 35.44           C  
ATOM   2941  N   ASP A 737     207.357 211.662 217.445  1.00 59.28           N  
ATOM   2942  CA  ASP A 737     207.123 212.179 216.114  1.00 52.38           C  
ATOM   2943  C   ASP A 737     206.960 210.899 215.311  1.00 54.36           C  
ATOM   2944  O   ASP A 737     207.893 210.104 215.218  1.00 53.86           O  
ATOM   2945  CB  ASP A 737     208.329 212.969 215.620  1.00 49.83           C  
ATOM   2946  CG  ASP A 737     208.142 213.493 214.216  1.00 61.15           C  
ATOM   2947  OD1 ASP A 737     207.128 213.138 213.582  1.00 68.51           O  
ATOM   2948  OD2 ASP A 737     209.007 214.257 213.745  1.00 66.77           O1-
ATOM   2949  N   CYS A 738     205.867 210.737 214.618  1.00 55.65           N  
ATOM   2950  CA  CYS A 738     205.642 209.436 214.013  1.00 49.99           C  
ATOM   2951  C   CYS A 738     206.337 209.205 212.695  1.00 50.35           C  
ATOM   2952  O   CYS A 738     206.580 208.067 212.293  1.00 45.80           O  
ATOM   2953  CB  CYS A 738     204.168 209.114 214.092  1.00 45.74           C  
ATOM   2954  SG  CYS A 738     203.638 209.888 215.641  1.00 60.11           S  
ATOM   2955  N   THR A 739     206.660 210.295 212.023  1.00 55.19           N  
ATOM   2956  CA  THR A 739     207.496 210.174 210.836  1.00 54.44           C  
ATOM   2957  C   THR A 739     208.889 209.649 211.170  1.00 52.43           C  
ATOM   2958  O   THR A 739     209.307 208.610 210.662  1.00 57.70           O  
ATOM   2959  CB  THR A 739     207.627 211.514 210.091  1.00 56.53           C  
ATOM   2960  OG1 THR A 739     208.130 212.514 210.983  1.00 66.58           O  
ATOM   2961  CG2 THR A 739     206.278 211.954 209.549  1.00 49.56           C  
ATOM   2962  N   MET A 740     209.603 210.370 212.026  1.00 47.61           N  
ATOM   2963  CA  MET A 740     210.961 209.977 212.415  1.00 45.93           C  
ATOM   2964  C   MET A 740     211.024 208.579 213.043  1.00 45.43           C  
ATOM   2965  O   MET A 740     211.998 207.868 212.802  1.00 43.94           O  
ATOM   2966  CB  MET A 740     211.592 211.007 213.356  1.00 47.02           C  
ATOM   2967  CG  MET A 740     211.935 212.290 212.599  1.00 57.34           C  
ATOM   2968  SD  MET A 740     212.938 213.470 213.539  1.00 72.55           S  
ATOM   2969  CE  MET A 740     213.062 214.802 212.313  1.00 58.61           C  
ATOM   2970  N   TYR A 741     210.008 208.145 213.799  1.00 45.23           N  
ATOM   2971  CA  TYR A 741     209.987 206.781 214.341  1.00 41.16           C  
ATOM   2972  C   TYR A 741     209.898 205.721 213.239  1.00 45.14           C  
ATOM   2973  O   TYR A 741     210.767 204.862 213.141  1.00 44.80           O  
ATOM   2974  CB  TYR A 741     208.842 206.604 215.349  1.00 38.76           C  
ATOM   2975  CG  TYR A 741     209.018 205.365 216.206  1.00 34.52           C  
ATOM   2976  CD1 TYR A 741     208.701 204.089 215.702  1.00 33.03           C  
ATOM   2977  CD2 TYR A 741     209.560 205.488 217.496  1.00 33.26           C  
ATOM   2978  CE1 TYR A 741     208.958 202.934 216.463  1.00 28.87           C  
ATOM   2979  CE2 TYR A 741     209.810 204.339 218.265  1.00 34.27           C  
ATOM   2980  CZ  TYR A 741     209.530 203.061 217.742  1.00 32.23           C  
ATOM   2981  OH  TYR A 741     209.846 201.964 218.476  1.00 37.95           O  
ATOM   2982  N   ILE A 742     208.856 205.771 212.408  1.00 50.08           N  
ATOM   2983  CA  ILE A 742     208.572 204.753 211.390  1.00 39.23           C  
ATOM   2984  C   ILE A 742     209.510 204.877 210.198  1.00 43.52           C  
ATOM   2985  O   ILE A 742     210.174 203.910 209.858  1.00 40.35           O  
ATOM   2986  CB  ILE A 742     207.100 204.833 210.949  1.00 29.80           C  
ATOM   2987  CG1 ILE A 742     206.187 204.323 212.075  1.00 30.15           C  
ATOM   2988  CG2 ILE A 742     206.834 204.041 209.664  1.00 34.15           C  
ATOM   2989  CD1 ILE A 742     204.832 205.011 212.036  1.00 31.89           C  
ATOM   2990  N   CYS A 743     209.446 205.995 209.478  1.00 48.22           N  
ATOM   2991  CA  CYS A 743     210.220 206.164 208.239  1.00 36.28           C  
ATOM   2992  C   CYS A 743     211.612 206.788 208.374  1.00 40.94           C  
ATOM   2993  O   CYS A 743     212.539 206.393 207.667  1.00 49.34           O  
ATOM   2994  CB  CYS A 743     209.365 206.909 207.190  1.00 44.20           C  
ATOM   2995  SG  CYS A 743     209.995 207.028 205.488  1.00 95.19           S  
ATOM   2996  N   GLY A 744     211.765 207.754 209.273  1.00 45.96           N  
ATOM   2997  CA  GLY A 744     213.052 208.398 209.467  1.00 49.79           C  
ATOM   2998  C   GLY A 744     213.362 209.425 208.393  1.00 53.09           C  
ATOM   2999  O   GLY A 744     212.577 210.347 208.170  1.00 53.82           O  
ATOM   3000  N   ASP A 745     214.503 209.273 207.726  1.00 62.77           N  
ATOM   3001  CA  ASP A 745     214.890 210.223 206.669  1.00 65.01           C  
ATOM   3002  C   ASP A 745     214.240 209.924 205.306  1.00 60.74           C  
ATOM   3003  O   ASP A 745     214.226 210.780 204.423  1.00 61.91           O  
ATOM   3004  CB  ASP A 745     216.425 210.194 206.509  1.00 63.36           C  
ATOM   3005  CG  ASP A 745     217.023 208.829 206.125  1.00 65.42           C  
ATOM   3006  OD1 ASP A 745     218.105 208.793 205.502  1.00 67.41           O  
ATOM   3007  OD2 ASP A 745     216.452 207.768 206.457  1.00 64.83           O1-
ATOM   3008  N   SER A 746     213.758 208.701 205.093  1.00 52.64           N  
ATOM   3009  CA  SER A 746     213.451 208.186 203.761  1.00 53.49           C  
ATOM   3010  C   SER A 746     212.161 208.773 203.188  1.00 54.54           C  
ATOM   3011  O   SER A 746     211.054 208.556 203.693  1.00 52.29           O  
ATOM   3012  CB  SER A 746     213.470 206.665 203.804  1.00 53.57           C  
ATOM   3013  OG  SER A 746     213.715 206.142 202.518  1.00 60.48           O  
ATOM   3014  N   THR A 747     212.319 209.595 202.153  1.00 60.97           N  
ATOM   3015  CA  THR A 747     211.295 210.548 201.717  1.00 57.94           C  
ATOM   3016  C   THR A 747     210.104 209.884 201.037  1.00 57.15           C  
ATOM   3017  O   THR A 747     208.975 210.298 201.271  1.00 56.16           O  
ATOM   3018  CB  THR A 747     211.930 211.638 200.856  1.00 46.17           C  
ATOM   3019  OG1 THR A 747     212.771 212.412 201.685  1.00 49.51           O  
ATOM   3020  CG2 THR A 747     210.927 212.598 200.245  1.00 46.69           C  
ATOM   3021  N   GLU A 748     210.289 208.800 200.291  1.00 55.77           N  
ATOM   3022  CA  GLU A 748     209.172 208.116 199.630  1.00 55.71           C  
ATOM   3023  C   GLU A 748     208.155 207.558 200.638  1.00 59.87           C  
ATOM   3024  O   GLU A 748     206.950 207.732 200.465  1.00 57.22           O  
ATOM   3025  CB  GLU A 748     209.669 207.049 198.635  1.00 59.69           C  
ATOM   3026  CG  GLU A 748     210.293 205.767 199.213  1.00 61.62           C  
ATOM   3027  CD  GLU A 748     211.619 205.970 199.952  1.00 72.72           C  
ATOM   3028  OE1 GLU A 748     212.322 206.980 199.740  1.00 67.50           O  
ATOM   3029  OE2 GLU A 748     211.978 205.095 200.766  1.00 55.88           O1-
ATOM   3030  N   CYS A 749     208.626 206.954 201.738  1.00 57.36           N  
ATOM   3031  CA  CYS A 749     207.675 206.472 202.757  1.00 47.30           C  
ATOM   3032  C   CYS A 749     207.114 207.613 203.609  1.00 46.35           C  
ATOM   3033  O   CYS A 749     205.992 207.530 204.110  1.00 49.30           O  
ATOM   3034  CB  CYS A 749     208.152 205.266 203.620  1.00 48.51           C  
ATOM   3035  SG  CYS A 749     209.667 205.199 204.644  1.00 66.31           S  
ATOM   3036  N   SER A 750     207.899 208.674 203.766  1.00 45.82           N  
ATOM   3037  CA  SER A 750     207.460 209.832 204.531  1.00 46.31           C  
ATOM   3038  C   SER A 750     206.206 210.378 203.865  1.00 47.25           C  
ATOM   3039  O   SER A 750     205.156 210.508 204.496  1.00 48.50           O  
ATOM   3040  CB  SER A 750     208.551 210.902 204.568  1.00 49.91           C  
ATOM   3041  OG  SER A 750     209.728 210.407 205.182  1.00 49.20           O  
ATOM   3042  N   ASN A 751     206.327 210.695 202.579  1.00 50.80           N  
ATOM   3043  CA  ASN A 751     205.200 211.193 201.796  1.00 54.05           C  
ATOM   3044  C   ASN A 751     204.000 210.243 201.831  1.00 53.40           C  
ATOM   3045  O   ASN A 751     202.863 210.705 201.825  1.00 52.15           O  
ATOM   3046  CB  ASN A 751     205.669 211.443 200.357  1.00 50.59           C  
ATOM   3047  CG  ASN A 751     206.730 212.518 200.211  1.00 59.81           C  
ATOM   3048  OD1 ASN A 751     207.511 212.507 199.286  1.00 67.16           O  
ATOM   3049  ND2 ASN A 751     206.791 213.489 201.077  1.00 74.51           N  
ATOM   3050  N   LEU A 752     204.216 208.929 201.923  1.00 50.77           N  
ATOM   3051  CA  LEU A 752     203.124 207.975 202.141  1.00 46.00           C  
ATOM   3052  C   LEU A 752     202.448 208.134 203.506  1.00 43.28           C  
ATOM   3053  O   LEU A 752     201.232 208.000 203.582  1.00 43.28           O  
ATOM   3054  CB  LEU A 752     203.639 206.541 201.975  1.00 41.19           C  
ATOM   3055  CG  LEU A 752     203.870 206.160 200.511  1.00 32.48           C  
ATOM   3056  CD1 LEU A 752     204.642 204.855 200.455  1.00 32.07           C  
ATOM   3057  CD2 LEU A 752     202.554 205.926 199.792  1.00 32.04           C  
ATOM   3058  N   LEU A 753     203.195 208.458 204.564  1.00 37.68           N  
ATOM   3059  CA  LEU A 753     202.658 208.638 205.915  1.00 39.89           C  
ATOM   3060  C   LEU A 753     201.479 209.636 205.952  1.00 45.96           C  
ATOM   3061  O   LEU A 753     200.518 209.372 206.664  1.00 45.56           O  
ATOM   3062  CB  LEU A 753     203.789 209.050 206.892  1.00 41.24           C  
ATOM   3063  CG  LEU A 753     204.335 207.973 207.850  1.00 37.77           C  
ATOM   3064  CD1 LEU A 753     203.253 207.467 208.788  1.00 37.75           C  
ATOM   3065  CD2 LEU A 753     204.977 206.770 207.165  1.00 36.42           C  
ATOM   3066  N   LEU A 754     201.484 210.718 205.163  1.00 43.88           N  
ATOM   3067  CA  LEU A 754     200.377 211.697 205.140  1.00 40.99           C  
ATOM   3068  C   LEU A 754     199.020 211.059 204.806  1.00 39.51           C  
ATOM   3069  O   LEU A 754     197.997 211.446 205.362  1.00 44.54           O  
ATOM   3070  CB  LEU A 754     200.717 212.824 204.149  1.00 39.37           C  
ATOM   3071  CG  LEU A 754     201.506 213.993 204.754  1.00 36.31           C  
ATOM   3072  CD1 LEU A 754     202.688 213.584 205.619  1.00 40.68           C  
ATOM   3073  CD2 LEU A 754     202.045 214.882 203.640  1.00 43.78           C  
ATOM   3074  N   GLN A 755     198.987 210.043 203.953  1.00 35.66           N  
ATOM   3075  CA  GLN A 755     197.752 209.349 203.614  1.00 44.76           C  
ATOM   3076  C   GLN A 755     197.299 208.335 204.672  1.00 45.71           C  
ATOM   3077  O   GLN A 755     196.142 207.939 204.639  1.00 48.96           O  
ATOM   3078  CB  GLN A 755     197.897 208.715 202.230  1.00 46.31           C  
ATOM   3079  CG  GLN A 755     197.754 209.747 201.090  1.00 57.53           C  
ATOM   3080  CD  GLN A 755     196.565 209.488 200.160  1.00 59.55           C  
ATOM   3081  OE1 GLN A 755     195.460 209.158 200.562  1.00 55.14           O  
ATOM   3082  NE2 GLN A 755     196.758 209.639 198.867  1.00 58.34           N  
ATOM   3083  N   TYR A 756     198.128 207.977 205.663  1.00 42.31           N  
ATOM   3084  CA  TYR A 756     197.690 207.233 206.861  1.00 30.91           C  
ATOM   3085  C   TYR A 756     196.913 208.118 207.849  1.00 33.77           C  
ATOM   3086  O   TYR A 756     196.454 207.648 208.885  1.00 39.24           O  
ATOM   3087  CB  TYR A 756     198.870 206.537 207.556  1.00 25.77           C  
ATOM   3088  CG  TYR A 756     199.478 205.382 206.785  1.00 30.50           C  
ATOM   3089  CD1 TYR A 756     199.181 204.059 207.139  1.00 25.22           C  
ATOM   3090  CD2 TYR A 756     200.357 205.625 205.720  1.00 40.18           C  
ATOM   3091  CE1 TYR A 756     199.745 202.994 206.414  1.00 21.61           C  
ATOM   3092  CE2 TYR A 756     200.936 204.566 205.003  1.00 31.83           C  
ATOM   3093  CZ  TYR A 756     200.617 203.246 205.344  1.00 22.68           C  
ATOM   3094  OH  TYR A 756     201.113 202.236 204.603  1.00 34.61           O  
ATOM   3095  N   GLY A 757     196.729 209.400 207.531  1.00 39.30           N  
ATOM   3096  CA  GLY A 757     195.939 210.320 208.333  1.00 36.73           C  
ATOM   3097  C   GLY A 757     196.676 210.820 209.563  1.00 49.22           C  
ATOM   3098  O   GLY A 757     197.886 210.659 209.702  1.00 45.64           O  
ATOM   3099  N   SER A 758     195.941 211.446 210.478  1.00 58.93           N  
ATOM   3100  CA  SER A 758     196.545 211.999 211.692  1.00 48.79           C  
ATOM   3101  C   SER A 758     196.689 210.987 212.825  1.00 44.25           C  
ATOM   3102  O   SER A 758     196.634 211.346 214.007  1.00 50.16           O  
ATOM   3103  CB  SER A 758     195.762 213.221 212.174  1.00 50.06           C  
ATOM   3104  OG  SER A 758     195.940 214.317 211.293  1.00 60.61           O  
ATOM   3105  N   PHE A 759     197.011 209.749 212.470  1.00 43.76           N  
ATOM   3106  CA  PHE A 759     197.135 208.674 213.453  1.00 34.86           C  
ATOM   3107  C   PHE A 759     198.205 208.951 214.515  1.00 38.51           C  
ATOM   3108  O   PHE A 759     198.049 208.548 215.659  1.00 46.55           O  
ATOM   3109  CB  PHE A 759     197.282 207.291 212.790  1.00 29.30           C  
ATOM   3110  CG  PHE A 759     198.694 206.911 212.457  1.00 31.21           C  
ATOM   3111  CD1 PHE A 759     199.438 206.152 213.337  1.00 26.63           C  
ATOM   3112  CD2 PHE A 759     199.277 207.324 211.275  1.00 39.98           C  
ATOM   3113  CE1 PHE A 759     200.740 205.802 213.041  1.00 34.88           C  
ATOM   3114  CE2 PHE A 759     200.578 206.979 210.971  1.00 43.25           C  
ATOM   3115  CZ  PHE A 759     201.311 206.215 211.855  1.00 43.75           C  
ATOM   3116  N   CYS A 760     199.230 209.684 214.099  1.00 40.63           N  
ATOM   3117  CA  CYS A 760     200.338 210.084 214.945  1.00 38.57           C  
ATOM   3118  C   CYS A 760     199.844 210.918 216.119  1.00 38.47           C  
ATOM   3119  O   CYS A 760     200.279 210.740 217.256  1.00 53.05           O  
ATOM   3120  CB  CYS A 760     201.304 210.927 214.114  1.00 57.05           C  
ATOM   3121  SG  CYS A 760     202.704 211.578 215.038  1.00 71.50           S  
ATOM   3122  N   THR A 761     198.927 211.830 215.820  1.00 35.02           N  
ATOM   3123  CA  THR A 761     198.355 212.745 216.813  1.00 42.57           C  
ATOM   3124  C   THR A 761     197.612 211.909 217.847  1.00 38.87           C  
ATOM   3125  O   THR A 761     197.810 212.040 219.053  1.00 38.91           O  
ATOM   3126  CB  THR A 761     197.384 213.752 216.179  1.00 49.04           C  
ATOM   3127  OG1 THR A 761     198.086 214.564 215.231  1.00 59.52           O  
ATOM   3128  CG2 THR A 761     196.778 214.643 217.246  1.00 49.32           C  
ATOM   3129  N   GLN A 762     196.750 211.048 217.329  1.00 41.46           N  
ATOM   3130  CA  GLN A 762     195.962 210.074 218.090  1.00 36.00           C  
ATOM   3131  C   GLN A 762     196.789 209.257 219.098  1.00 35.39           C  
ATOM   3132  O   GLN A 762     196.381 209.114 220.244  1.00 39.59           O  
ATOM   3133  CB  GLN A 762     195.242 209.144 217.105  1.00 38.97           C  
ATOM   3134  CG  GLN A 762     194.344 209.879 216.109  1.00 41.49           C  
ATOM   3135  CD  GLN A 762     193.568 211.035 216.702  1.00 44.66           C  
ATOM   3136  OE1 GLN A 762     193.985 212.183 216.682  1.00 45.32           O  
ATOM   3137  NE2 GLN A 762     192.394 210.782 217.222  1.00 45.49           N  
ATOM   3138  N   LEU A 763     197.972 208.786 218.710  1.00 31.07           N  
ATOM   3139  CA  LEU A 763     198.935 208.154 219.610  1.00 29.52           C  
ATOM   3140  C   LEU A 763     199.521 209.174 220.597  1.00 29.72           C  
ATOM   3141  O   LEU A 763     199.769 208.838 221.752  1.00 39.04           O  
ATOM   3142  CB  LEU A 763     200.025 207.498 218.749  1.00 28.00           C  
ATOM   3143  CG  LEU A 763     199.682 206.080 218.258  1.00 23.47           C  
ATOM   3144  CD1 LEU A 763     198.372 205.940 217.494  1.00 24.49           C  
ATOM   3145  CD2 LEU A 763     200.803 205.592 217.350  1.00 27.35           C  
ATOM   3146  N   ASN A 764     199.705 210.429 220.193  1.00 26.12           N  
ATOM   3147  CA  ASN A 764     200.196 211.466 221.089  1.00 27.89           C  
ATOM   3148  C   ASN A 764     199.138 211.997 222.058  1.00 33.84           C  
ATOM   3149  O   ASN A 764     199.519 212.414 223.142  1.00 41.81           O  
ATOM   3150  CB  ASN A 764     200.903 212.559 220.296  1.00 25.87           C  
ATOM   3151  CG  ASN A 764     202.279 212.097 219.870  1.00 35.22           C  
ATOM   3152  OD1 ASN A 764     203.209 212.058 220.656  1.00 39.36           O  
ATOM   3153  ND2 ASN A 764     202.464 211.707 218.640  1.00 39.84           N  
ATOM   3154  N   ARG A 765     197.829 211.908 221.775  1.00 34.46           N  
ATOM   3155  CA  ARG A 765     196.777 212.141 222.788  1.00 32.93           C  
ATOM   3156  C   ARG A 765     196.962 211.190 223.955  1.00 35.65           C  
ATOM   3157  O   ARG A 765     196.854 211.608 225.101  1.00 40.38           O  
ATOM   3158  CB  ARG A 765     195.361 211.965 222.210  1.00 35.58           C  
ATOM   3159  CG  ARG A 765     194.819 213.251 221.587  1.00 37.52           C  
ATOM   3160  CD  ARG A 765     193.468 213.047 220.890  1.00 46.93           C  
ATOM   3161  NE  ARG A 765     192.362 212.672 221.798  1.00 43.56           N  
ATOM   3162  CZ  ARG A 765     191.640 213.484 222.548  1.00 47.31           C  
ATOM   3163  NH1 ARG A 765     190.601 213.051 223.191  1.00 46.66           N  
ATOM   3164  NH2 ARG A 765     191.915 214.746 222.684  1.00 52.55           N  
ATOM   3165  N   ALA A 766     197.281 209.932 223.673  1.00 32.19           N  
ATOM   3166  CA  ALA A 766     197.513 208.924 224.684  1.00 29.23           C  
ATOM   3167  C   ALA A 766     198.754 209.251 225.529  1.00 36.94           C  
ATOM   3168  O   ALA A 766     198.641 209.505 226.726  1.00 46.83           O  
ATOM   3169  CB  ALA A 766     197.591 207.571 223.971  1.00 33.66           C  
ATOM   3170  N   LEU A 767     199.931 209.319 224.900  1.00 33.57           N  
ATOM   3171  CA  LEU A 767     201.221 209.536 225.572  1.00 32.76           C  
ATOM   3172  C   LEU A 767     201.370 210.933 226.210  1.00 37.57           C  
ATOM   3173  O   LEU A 767     202.048 211.045 227.221  1.00 51.40           O  
ATOM   3174  CB  LEU A 767     202.371 209.243 224.576  1.00 29.82           C  
ATOM   3175  CG  LEU A 767     202.854 207.782 224.585  1.00 29.96           C  
ATOM   3176  CD1 LEU A 767     201.721 206.790 224.387  1.00 35.78           C  
ATOM   3177  CD2 LEU A 767     203.871 207.534 223.480  1.00 30.52           C  
ATOM   3178  N   THR A 768     200.749 211.991 225.682  1.00 35.18           N  
ATOM   3179  CA  THR A 768     200.758 213.330 226.303  1.00 42.63           C  
ATOM   3180  C   THR A 768     199.805 213.447 227.503  1.00 46.28           C  
ATOM   3181  O   THR A 768     199.992 214.290 228.382  1.00 59.20           O  
ATOM   3182  CB  THR A 768     200.476 214.426 225.259  1.00 47.06           C  
ATOM   3183  OG1 THR A 768     201.095 215.634 225.631  1.00 49.88           O  
ATOM   3184  CG2 THR A 768     198.996 214.759 225.057  1.00 55.75           C  
ATOM   3185  N   GLY A 769     198.812 212.563 227.591  1.00 38.73           N  
ATOM   3186  CA  GLY A 769     198.017 212.342 228.792  1.00 46.63           C  
ATOM   3187  C   GLY A 769     198.767 211.477 229.814  1.00 57.04           C  
ATOM   3188  O   GLY A 769     199.912 211.735 230.177  1.00 56.79           O  
ATOM   3189  N   ILE A 770     198.086 210.443 230.293  1.00 52.49           N  
ATOM   3190  CA  ILE A 770     198.602 209.292 231.036  1.00 55.19           C  
ATOM   3191  C   ILE A 770     199.625 209.668 232.121  1.00 62.97           C  
ATOM   3192  O   ILE A 770     199.381 209.457 233.309  1.00 60.48           O  
ATOM   3193  CB  ILE A 770     199.078 208.206 230.046  1.00 39.84           C  
ATOM   3194  CG1 ILE A 770     198.834 206.788 230.599  1.00 45.87           C  
ATOM   3195  CG2 ILE A 770     200.549 208.403 229.631  1.00 31.17           C  
ATOM   3196  CD1 ILE A 770     197.374 206.336 230.525  1.00 43.30           C  
ATOM   3197  N   THR A 912     193.601 191.714  81.508  1.00 73.30           N  
ATOM   3198  CA  THR A 912     194.590 191.905  82.581  1.00 73.90           C  
ATOM   3199  C   THR A 912     194.344 193.196  83.375  1.00 73.30           C  
ATOM   3200  O   THR A 912     194.411 193.199  84.607  1.00 73.30           O  
ATOM   3201  CB  THR A 912     196.028 191.847  82.019  1.00 73.30           C  
ATOM   3202  OG1 THR A 912     196.986 192.168  83.005  1.00 73.30           O  
ATOM   3203  CG2 THR A 912     196.302 192.787  80.844  1.00 73.30           C  
ATOM   3204  N   GLN A 913     193.994 194.289  82.685  1.00 71.67           N  
ATOM   3205  CA  GLN A 913     193.819 195.606  83.308  1.00 73.13           C  
ATOM   3206  C   GLN A 913     192.673 195.610  84.330  1.00 76.26           C  
ATOM   3207  O   GLN A 913     192.775 196.234  85.385  1.00 75.90           O  
ATOM   3208  CB  GLN A 913     193.613 196.659  82.204  1.00 71.67           C  
ATOM   3209  CG  GLN A 913     193.881 198.101  82.670  1.00 71.67           C  
ATOM   3210  CD  GLN A 913     195.353 198.387  82.949  1.00 73.52           C  
ATOM   3211  OE1 GLN A 913     196.222 197.533  82.853  1.00 71.67           O  
ATOM   3212  NE2 GLN A 913     195.689 199.597  83.307  1.00 71.67           N  
ATOM   3213  N   ASN A 914     191.615 194.848  84.042  1.00 76.42           N  
ATOM   3214  CA  ASN A 914     190.481 194.621  84.929  1.00 73.54           C  
ATOM   3215  C   ASN A 914     190.850 193.888  86.230  1.00 75.17           C  
ATOM   3216  O   ASN A 914     190.571 194.399  87.311  1.00 73.75           O  
ATOM   3217  CB  ASN A 914     189.350 193.912  84.155  1.00 73.54           C  
ATOM   3218  CG  ASN A 914     189.726 192.639  83.403  1.00 74.41           C  
ATOM   3219  OD1 ASN A 914     190.831 192.151  83.423  1.00 73.54           O  
ATOM   3220  ND2 ASN A 914     188.811 192.076  82.692  1.00 73.54           N  
ATOM   3221  N   VAL A 915     191.497 192.719  86.175  1.00 77.47           N  
ATOM   3222  CA  VAL A 915     191.874 191.970  87.395  1.00 75.75           C  
ATOM   3223  C   VAL A 915     192.957 192.674  88.216  1.00 73.97           C  
ATOM   3224  O   VAL A 915     192.922 192.607  89.445  1.00 73.17           O  
ATOM   3225  CB  VAL A 915     192.263 190.505  87.121  1.00 73.17           C  
ATOM   3226  CG1 VAL A 915     191.054 189.741  86.569  1.00 73.17           C  
ATOM   3227  CG2 VAL A 915     193.446 190.318  86.174  1.00 73.17           C  
ATOM   3228  N   LEU A 916     193.865 193.426  87.588  1.00 73.77           N  
ATOM   3229  CA  LEU A 916     194.846 194.239  88.315  1.00 71.58           C  
ATOM   3230  C   LEU A 916     194.170 195.389  89.088  1.00 73.83           C  
ATOM   3231  O   LEU A 916     194.585 195.711  90.201  1.00 79.24           O  
ATOM   3232  CB  LEU A 916     195.920 194.731  87.324  1.00 71.58           C  
ATOM   3233  CG  LEU A 916     197.183 195.315  87.957  1.00 71.58           C  
ATOM   3234  CD1 LEU A 916     197.936 194.316  88.805  1.00 71.58           C  
ATOM   3235  CD2 LEU A 916     198.140 195.750  86.851  1.00 71.58           C  
ATOM   3236  N   TYR A 917     193.090 195.950  88.539  1.00 72.00           N  
ATOM   3237  CA  TYR A 917     192.274 196.987  89.179  1.00 73.42           C  
ATOM   3238  C   TYR A 917     191.340 196.416  90.257  1.00 74.49           C  
ATOM   3239  O   TYR A 917     191.209 196.995  91.329  1.00 74.60           O  
ATOM   3240  CB  TYR A 917     191.501 197.744  88.091  1.00 75.90           C  
ATOM   3241  CG  TYR A 917     190.823 199.021  88.545  1.00 76.20           C  
ATOM   3242  CD1 TYR A 917     189.574 198.973  89.193  1.00 72.00           C  
ATOM   3243  CD2 TYR A 917     191.427 200.267  88.283  1.00 73.56           C  
ATOM   3244  CE1 TYR A 917     188.949 200.164  89.617  1.00 72.47           C  
ATOM   3245  CE2 TYR A 917     190.807 201.459  88.702  1.00 73.30           C  
ATOM   3246  CZ  TYR A 917     189.564 201.411  89.372  1.00 76.75           C  
ATOM   3247  OH  TYR A 917     188.962 202.562  89.770  1.00 76.41           O  
ATOM   3248  N   GLU A 918     190.732 195.249  90.049  1.00 73.35           N  
ATOM   3249  CA  GLU A 918     189.941 194.594  91.100  1.00 75.84           C  
ATOM   3250  C   GLU A 918     190.826 194.134  92.279  1.00 75.87           C  
ATOM   3251  O   GLU A 918     190.409 194.239  93.429  1.00 77.06           O  
ATOM   3252  CB  GLU A 918     189.108 193.439  90.517  1.00 74.60           C  
ATOM   3253  CG  GLU A 918     187.946 193.935  89.636  1.00 77.73           C  
ATOM   3254  CD  GLU A 918     186.968 194.849  90.381  1.00 79.57           C  
ATOM   3255  OE1 GLU A 918     186.558 194.507  91.512  1.00 73.35           O  
ATOM   3256  OE2 GLU A 918     186.584 195.900  89.828  1.00 77.58           O1-
ATOM   3257  N   ASN A 919     192.077 193.720  92.038  1.00 79.78           N  
ATOM   3258  CA  ASN A 919     193.074 193.560  93.102  1.00 74.55           C  
ATOM   3259  C   ASN A 919     193.424 194.901  93.786  1.00 72.50           C  
ATOM   3260  O   ASN A 919     193.688 194.910  94.986  1.00 72.10           O  
ATOM   3261  CB  ASN A 919     194.338 192.871  92.556  1.00 76.05           C  
ATOM   3262  CG  ASN A 919     194.208 191.360  92.520  1.00 79.24           C  
ATOM   3263  OD1 ASN A 919     194.479 190.667  93.485  1.00 78.04           O  
ATOM   3264  ND2 ASN A 919     193.815 190.800  91.408  1.00 78.51           N  
ATOM   3265  N   GLN A 920     193.375 196.031  93.068  1.00 71.43           N  
ATOM   3266  CA  GLN A 920     193.561 197.368  93.639  1.00 73.94           C  
ATOM   3267  C   GLN A 920     192.389 197.778  94.552  1.00 70.78           C  
ATOM   3268  O   GLN A 920     192.606 198.281  95.659  1.00 69.64           O  
ATOM   3269  CB  GLN A 920     193.828 198.375  92.495  1.00 71.93           C  
ATOM   3270  CG  GLN A 920     194.529 199.687  92.885  1.00 71.28           C  
ATOM   3271  CD  GLN A 920     195.994 199.483  93.249  1.00 69.64           C  
ATOM   3272  OE1 GLN A 920     196.339 198.585  93.990  1.00 69.64           O  
ATOM   3273  NE2 GLN A 920     196.928 200.261  92.769  1.00 69.64           N  
ATOM   3274  N   LYS A 921     191.146 197.471  94.149  1.00 71.28           N  
ATOM   3275  CA  LYS A 921     189.949 197.574  95.016  1.00 74.07           C  
ATOM   3276  C   LYS A 921     190.050 196.652  96.241  1.00 75.37           C  
ATOM   3277  O   LYS A 921     189.810 197.094  97.363  1.00 69.97           O  
ATOM   3278  CB  LYS A 921     188.669 197.250  94.215  1.00 72.01           C  
ATOM   3279  CG  LYS A 921     188.292 198.243  93.100  1.00 72.64           C  
ATOM   3280  CD  LYS A 921     187.927 199.658  93.584  1.00 74.04           C  
ATOM   3281  CE  LYS A 921     186.698 199.730  94.504  1.00 69.92           C  
ATOM   3282  NZ  LYS A 921     185.429 199.513  93.771  1.00 70.64           N  
ATOM   3283  N   LEU A 922     190.443 195.393  96.035  1.00 73.73           N  
ATOM   3284  CA  LEU A 922     190.591 194.371  97.076  1.00 73.06           C  
ATOM   3285  C   LEU A 922     191.544 194.822  98.185  1.00 72.65           C  
ATOM   3286  O   LEU A 922     191.133 194.902  99.342  1.00 69.65           O  
ATOM   3287  CB  LEU A 922     191.035 193.051  96.418  1.00 75.32           C  
ATOM   3288  CG  LEU A 922     191.120 191.793  97.308  1.00 75.42           C  
ATOM   3289  CD1 LEU A 922     191.334 190.569  96.416  1.00 73.63           C  
ATOM   3290  CD2 LEU A 922     192.285 191.799  98.300  1.00 69.65           C  
ATOM   3291  N   ILE A 923     192.804 195.127  97.856  1.00 76.16           N  
ATOM   3292  CA  ILE A 923     193.825 195.380  98.885  1.00 71.75           C  
ATOM   3293  C   ILE A 923     193.525 196.655  99.677  1.00 66.44           C  
ATOM   3294  O   ILE A 923     193.677 196.684 100.895  1.00 69.79           O  
ATOM   3295  CB  ILE A 923     195.248 195.376  98.282  1.00 65.37           C  
ATOM   3296  CG1 ILE A 923     196.349 195.371  99.362  1.00 65.37           C  
ATOM   3297  CG2 ILE A 923     195.517 196.579  97.368  1.00 66.03           C  
ATOM   3298  CD1 ILE A 923     196.299 194.168 100.306  1.00 65.37           C  
ATOM   3299  N   ALA A 924     192.997 197.689  99.014  1.00 66.03           N  
ATOM   3300  CA  ALA A 924     192.522 198.905  99.660  1.00 66.12           C  
ATOM   3301  C   ALA A 924     191.325 198.650 100.587  1.00 67.98           C  
ATOM   3302  O   ALA A 924     191.264 199.224 101.671  1.00 66.96           O  
ATOM   3303  CB  ALA A 924     192.180 199.923  98.569  1.00 69.28           C  
ATOM   3304  N   ASN A 925     190.385 197.776 100.205  1.00 72.01           N  
ATOM   3305  CA  ASN A 925     189.253 197.387 101.051  1.00 72.76           C  
ATOM   3306  C   ASN A 925     189.701 196.553 102.265  1.00 71.18           C  
ATOM   3307  O   ASN A 925     189.187 196.743 103.365  1.00 67.76           O  
ATOM   3308  CB  ASN A 925     188.200 196.651 100.198  1.00 76.34           C  
ATOM   3309  CG  ASN A 925     187.398 197.530  99.254  1.00 77.24           C  
ATOM   3310  OD1 ASN A 925     186.435 197.089  98.650  1.00 77.51           O  
ATOM   3311  ND2 ASN A 925     187.701 198.802  99.136  1.00 74.10           N  
ATOM   3312  N   GLN A 926     190.698 195.682 102.102  1.00 73.50           N  
ATOM   3313  CA  GLN A 926     191.322 194.972 103.221  1.00 68.24           C  
ATOM   3314  C   GLN A 926     192.054 195.931 104.178  1.00 64.08           C  
ATOM   3315  O   GLN A 926     191.899 195.808 105.395  1.00 62.36           O  
ATOM   3316  CB  GLN A 926     192.279 193.899 102.693  1.00 68.30           C  
ATOM   3317  CG  GLN A 926     191.575 192.757 101.940  1.00 69.39           C  
ATOM   3318  CD  GLN A 926     190.848 191.807 102.878  1.00 72.90           C  
ATOM   3319  OE1 GLN A 926     191.419 190.871 103.408  1.00 77.93           O  
ATOM   3320  NE2 GLN A 926     189.577 192.003 103.143  1.00 71.42           N  
ATOM   3321  N   PHE A 927     192.802 196.910 103.656  1.00 62.86           N  
ATOM   3322  CA  PHE A 927     193.519 197.909 104.457  1.00 59.52           C  
ATOM   3323  C   PHE A 927     192.598 198.891 105.189  1.00 65.32           C  
ATOM   3324  O   PHE A 927     192.717 199.062 106.400  1.00 70.46           O  
ATOM   3325  CB  PHE A 927     194.514 198.643 103.554  1.00 61.32           C  
ATOM   3326  CG  PHE A 927     195.224 199.797 104.226  1.00 63.42           C  
ATOM   3327  CD1 PHE A 927     196.319 199.543 105.066  1.00 60.21           C  
ATOM   3328  CD2 PHE A 927     194.786 201.119 104.027  1.00 64.19           C  
ATOM   3329  CE1 PHE A 927     196.994 200.604 105.686  1.00 66.99           C  
ATOM   3330  CE2 PHE A 927     195.464 202.182 104.648  1.00 61.53           C  
ATOM   3331  CZ  PHE A 927     196.578 201.925 105.466  1.00 66.79           C  
ATOM   3332  N   ASN A 928     191.636 199.487 104.484  1.00 62.09           N  
ATOM   3333  CA  ASN A 928     190.653 200.422 105.038  1.00 63.47           C  
ATOM   3334  C   ASN A 928     189.830 199.778 106.168  1.00 64.96           C  
ATOM   3335  O   ASN A 928     189.614 200.398 107.212  1.00 64.50           O  
ATOM   3336  CB  ASN A 928     189.790 200.920 103.859  1.00 67.71           C  
ATOM   3337  CG  ASN A 928     188.584 201.747 104.262  1.00 70.37           C  
ATOM   3338  OD1 ASN A 928     187.620 201.237 104.815  1.00 69.02           O  
ATOM   3339  ND2 ASN A 928     188.553 203.018 103.944  1.00 74.25           N  
ATOM   3340  N   SER A 929     189.434 198.509 106.009  1.00 67.77           N  
ATOM   3341  CA  SER A 929     188.774 197.737 107.065  1.00 64.84           C  
ATOM   3342  C   SER A 929     189.720 197.375 108.222  1.00 63.32           C  
ATOM   3343  O   SER A 929     189.314 197.446 109.385  1.00 62.86           O  
ATOM   3344  CB  SER A 929     188.156 196.488 106.437  1.00 66.05           C  
ATOM   3345  OG  SER A 929     187.507 195.683 107.407  1.00 62.68           O  
ATOM   3346  N   ALA A 930     190.998 197.072 107.946  1.00 65.00           N  
ATOM   3347  CA  ALA A 930     191.980 196.769 108.987  1.00 63.33           C  
ATOM   3348  C   ALA A 930     192.257 197.975 109.891  1.00 64.06           C  
ATOM   3349  O   ALA A 930     192.150 197.847 111.102  1.00 67.66           O  
ATOM   3350  CB  ALA A 930     193.268 196.233 108.364  1.00 63.68           C  
ATOM   3351  N   ILE A 931     192.537 199.155 109.327  1.00 62.55           N  
ATOM   3352  CA  ILE A 931     192.775 200.391 110.090  1.00 63.15           C  
ATOM   3353  C   ILE A 931     191.582 200.751 110.998  1.00 64.59           C  
ATOM   3354  O   ILE A 931     191.790 201.097 112.160  1.00 66.35           O  
ATOM   3355  CB  ILE A 931     193.161 201.558 109.153  1.00 60.42           C  
ATOM   3356  CG1 ILE A 931     194.503 201.337 108.425  1.00 62.52           C  
ATOM   3357  CG2 ILE A 931     193.203 202.884 109.923  1.00 64.68           C  
ATOM   3358  CD1 ILE A 931     195.727 201.116 109.315  1.00 60.89           C  
ATOM   3359  N   GLY A 932     190.333 200.588 110.549  1.00 69.03           N  
ATOM   3360  CA  GLY A 932     189.165 200.806 111.420  1.00 63.98           C  
ATOM   3361  C   GLY A 932     189.108 199.860 112.633  1.00 64.96           C  
ATOM   3362  O   GLY A 932     188.707 200.243 113.734  1.00 66.41           O  
ATOM   3363  N   LYS A 933     189.594 198.627 112.459  1.00 61.01           N  
ATOM   3364  CA  LYS A 933     189.778 197.638 113.527  1.00 60.62           C  
ATOM   3365  C   LYS A 933     191.011 197.942 114.389  1.00 64.90           C  
ATOM   3366  O   LYS A 933     190.994 197.666 115.588  1.00 68.74           O  
ATOM   3367  CB  LYS A 933     189.787 196.244 112.876  1.00 64.36           C  
ATOM   3368  CG  LYS A 933     189.644 195.085 113.876  1.00 64.81           C  
ATOM   3369  CD  LYS A 933     189.240 193.776 113.171  1.00 59.90           C  
ATOM   3370  CE  LYS A 933     187.733 193.760 112.844  1.00 58.41           C  
ATOM   3371  NZ  LYS A 933     187.378 192.832 111.733  1.00 62.61           N  
ATOM   3372  N   ILE A 934     192.056 198.582 113.850  1.00 63.96           N  
ATOM   3373  CA  ILE A 934     193.154 199.150 114.656  1.00 61.15           C  
ATOM   3374  C   ILE A 934     192.642 200.259 115.577  1.00 64.52           C  
ATOM   3375  O   ILE A 934     193.003 200.270 116.747  1.00 70.03           O  
ATOM   3376  CB  ILE A 934     194.324 199.676 113.788  1.00 65.15           C  
ATOM   3377  CG1 ILE A 934     194.967 198.625 112.860  1.00 64.58           C  
ATOM   3378  CG2 ILE A 934     195.422 200.282 114.668  1.00 59.42           C  
ATOM   3379  CD1 ILE A 934     195.307 197.283 113.500  1.00 62.63           C  
ATOM   3380  N   GLN A 935     191.791 201.163 115.101  1.00 63.86           N  
ATOM   3381  CA  GLN A 935     191.250 202.235 115.941  1.00 67.07           C  
ATOM   3382  C   GLN A 935     190.382 201.704 117.093  1.00 69.67           C  
ATOM   3383  O   GLN A 935     190.510 202.183 118.216  1.00 71.51           O  
ATOM   3384  CB  GLN A 935     190.495 203.240 115.063  1.00 69.77           C  
ATOM   3385  CG  GLN A 935     191.475 203.987 114.144  1.00 74.64           C  
ATOM   3386  CD  GLN A 935     190.764 204.829 113.100  1.00 83.70           C  
ATOM   3387  OE1 GLN A 935     190.234 204.338 112.113  1.00 84.98           O  
ATOM   3388  NE2 GLN A 935     190.739 206.129 113.250  1.00 82.39           N  
ATOM   3389  N   ASP A 936     189.590 200.655 116.880  1.00 68.78           N  
ATOM   3390  CA  ASP A 936     188.894 199.926 117.951  1.00 71.33           C  
ATOM   3391  C   ASP A 936     189.875 199.264 118.943  1.00 68.45           C  
ATOM   3392  O   ASP A 936     189.790 199.475 120.153  1.00 69.38           O  
ATOM   3393  CB  ASP A 936     187.968 198.880 117.301  1.00 77.07           C  
ATOM   3394  CG  ASP A 936     187.086 198.106 118.289  1.00 81.08           C  
ATOM   3395  OD1 ASP A 936     186.604 197.015 117.913  1.00 73.99           O  
ATOM   3396  OD2 ASP A 936     186.837 198.590 119.411  1.00 89.47           O1-
ATOM   3397  N   SER A 937     190.868 198.534 118.429  1.00 65.93           N  
ATOM   3398  CA  SER A 937     191.910 197.856 119.218  1.00 65.38           C  
ATOM   3399  C   SER A 937     192.713 198.807 120.123  1.00 65.41           C  
ATOM   3400  O   SER A 937     193.083 198.479 121.252  1.00 67.76           O  
ATOM   3401  CB  SER A 937     192.901 197.206 118.255  1.00 68.45           C  
ATOM   3402  OG  SER A 937     192.274 196.247 117.428  1.00 68.40           O  
ATOM   3403  N   LEU A 938     192.993 200.003 119.613  1.00 60.83           N  
ATOM   3404  CA  LEU A 938     193.797 201.009 120.280  1.00 62.95           C  
ATOM   3405  C   LEU A 938     192.966 201.873 121.237  1.00 67.70           C  
ATOM   3406  O   LEU A 938     193.392 202.125 122.359  1.00 72.76           O  
ATOM   3407  CB  LEU A 938     194.487 201.797 119.171  1.00 66.64           C  
ATOM   3408  CG  LEU A 938     195.584 202.745 119.664  1.00 67.64           C  
ATOM   3409  CD1 LEU A 938     196.616 202.901 118.560  1.00 70.11           C  
ATOM   3410  CD2 LEU A 938     195.039 204.128 119.991  1.00 72.60           C  
ATOM   3411  N   SER A 939     191.763 202.300 120.844  1.00 67.69           N  
ATOM   3412  CA  SER A 939     190.870 203.089 121.708  1.00 70.12           C  
ATOM   3413  C   SER A 939     190.421 202.299 122.946  1.00 69.35           C  
ATOM   3414  O   SER A 939     190.412 202.826 124.059  1.00 75.58           O  
ATOM   3415  CB  SER A 939     189.654 203.591 120.918  1.00 72.95           C  
ATOM   3416  OG  SER A 939     188.896 202.538 120.360  1.00 72.19           O  
ATOM   3417  N   SER A 940     190.107 201.013 122.779  1.00 69.75           N  
ATOM   3418  CA  SER A 940     189.814 200.107 123.894  1.00 67.07           C  
ATOM   3419  C   SER A 940     191.025 199.916 124.812  1.00 63.94           C  
ATOM   3420  O   SER A 940     190.882 200.075 126.018  1.00 66.40           O  
ATOM   3421  CB  SER A 940     189.291 198.769 123.385  1.00 68.92           C  
ATOM   3422  OG  SER A 940     190.201 198.203 122.465  1.00 76.30           O  
ATOM   3423  N   THR A 941     192.231 199.684 124.276  1.00 64.97           N  
ATOM   3424  CA  THR A 941     193.470 199.610 125.084  1.00 60.23           C  
ATOM   3425  C   THR A 941     193.726 200.901 125.859  1.00 60.29           C  
ATOM   3426  O   THR A 941     194.091 200.835 127.024  1.00 66.80           O  
ATOM   3427  CB  THR A 941     194.721 199.279 124.253  1.00 65.96           C  
ATOM   3428  OG1 THR A 941     194.571 198.076 123.541  1.00 73.57           O  
ATOM   3429  CG2 THR A 941     195.962 199.099 125.133  1.00 57.14           C  
ATOM   3430  N   ALA A 942     193.499 202.078 125.272  1.00 63.05           N  
ATOM   3431  CA  ALA A 942     193.600 203.345 125.996  1.00 64.63           C  
ATOM   3432  C   ALA A 942     192.569 203.463 127.138  1.00 67.68           C  
ATOM   3433  O   ALA A 942     192.915 203.833 128.256  1.00 73.83           O  
ATOM   3434  CB  ALA A 942     193.435 204.490 124.995  1.00 68.92           C  
ATOM   3435  N   SER A 943     191.308 203.115 126.876  1.00 69.61           N  
ATOM   3436  CA  SER A 943     190.235 203.103 127.879  1.00 68.50           C  
ATOM   3437  C   SER A 943     190.469 202.074 128.999  1.00 65.41           C  
ATOM   3438  O   SER A 943     190.133 202.327 130.150  1.00 63.70           O  
ATOM   3439  CB  SER A 943     188.913 202.843 127.153  1.00 69.94           C  
ATOM   3440  OG  SER A 943     187.806 203.035 128.002  1.00 73.56           O  
ATOM   3441  N   ALA A 944     191.120 200.947 128.700  1.00 61.71           N  
ATOM   3442  CA  ALA A 944     191.576 199.990 129.704  1.00 60.24           C  
ATOM   3443  C   ALA A 944     192.778 200.517 130.500  1.00 59.47           C  
ATOM   3444  O   ALA A 944     192.727 200.622 131.718  1.00 64.46           O  
ATOM   3445  CB  ALA A 944     191.941 198.667 129.015  1.00 57.73           C  
ATOM   3446  N   LEU A 945     193.876 200.873 129.838  1.00 57.15           N  
ATOM   3447  CA  LEU A 945     195.113 201.291 130.502  1.00 57.35           C  
ATOM   3448  C   LEU A 945     194.919 202.588 131.312  1.00 62.00           C  
ATOM   3449  O   LEU A 945     195.520 202.765 132.369  1.00 74.02           O  
ATOM   3450  CB  LEU A 945     196.226 201.353 129.443  1.00 65.83           C  
ATOM   3451  CG  LEU A 945     197.622 201.573 130.056  1.00 65.57           C  
ATOM   3452  CD1 LEU A 945     198.676 200.682 129.399  1.00 64.58           C  
ATOM   3453  CD2 LEU A 945     198.035 203.028 129.901  1.00 64.77           C  
ATOM   3454  N   GLY A 946     193.981 203.443 130.905  1.00 62.28           N  
ATOM   3455  CA  GLY A 946     193.524 204.595 131.687  1.00 64.96           C  
ATOM   3456  C   GLY A 946     192.654 204.263 132.910  1.00 61.23           C  
ATOM   3457  O   GLY A 946     192.651 205.042 133.860  1.00 56.55           O  
ATOM   3458  N   LYS A 947     191.964 203.111 132.952  1.00 70.03           N  
ATOM   3459  CA  LYS A 947     191.299 202.587 134.171  1.00 61.42           C  
ATOM   3460  C   LYS A 947     192.280 201.884 135.120  1.00 55.27           C  
ATOM   3461  O   LYS A 947     192.108 201.957 136.335  1.00 55.71           O  
ATOM   3462  CB  LYS A 947     190.068 201.721 133.799  1.00 61.13           C  
ATOM   3463  CG  LYS A 947     190.242 200.194 133.878  1.00 61.46           C  
ATOM   3464  CD  LYS A 947     189.041 199.449 133.286  1.00 68.27           C  
ATOM   3465  CE  LYS A 947     189.325 197.941 133.266  1.00 62.92           C  
ATOM   3466  NZ  LYS A 947     188.248 197.169 132.594  1.00 48.82           N  
ATOM   3467  N   LEU A 948     193.343 201.271 134.590  1.00 57.89           N  
ATOM   3468  CA  LEU A 948     194.433 200.684 135.385  1.00 56.95           C  
ATOM   3469  C   LEU A 948     195.265 201.769 136.080  1.00 55.18           C  
ATOM   3470  O   LEU A 948     195.515 201.670 137.274  1.00 62.64           O  
ATOM   3471  CB  LEU A 948     195.327 199.803 134.488  1.00 68.89           C  
ATOM   3472  CG  LEU A 948     194.984 198.301 134.429  1.00 64.76           C  
ATOM   3473  CD1 LEU A 948     195.301 197.590 135.743  1.00 60.78           C  
ATOM   3474  CD2 LEU A 948     193.527 198.015 134.070  1.00 61.76           C  
ATOM   3475  N   GLN A 949     195.652 202.833 135.377  1.00 57.70           N  
ATOM   3476  CA  GLN A 949     196.379 203.973 135.956  1.00 58.79           C  
ATOM   3477  C   GLN A 949     195.539 204.788 136.956  1.00 58.07           C  
ATOM   3478  O   GLN A 949     196.095 205.383 137.877  1.00 61.43           O  
ATOM   3479  CB  GLN A 949     196.923 204.821 134.796  1.00 76.38           C  
ATOM   3480  CG  GLN A 949     197.787 206.034 135.207  1.00 81.76           C  
ATOM   3481  CD  GLN A 949     197.071 207.388 135.165  1.00 76.28           C  
ATOM   3482  OE1 GLN A 949     195.861 207.514 135.097  1.00 75.61           O  
ATOM   3483  NE2 GLN A 949     197.805 208.476 135.198  1.00 69.16           N  
ATOM   3484  N   ASP A 950     194.208 204.771 136.835  1.00 55.87           N  
ATOM   3485  CA  ASP A 950     193.273 205.348 137.812  1.00 57.82           C  
ATOM   3486  C   ASP A 950     193.284 204.525 139.106  1.00 59.98           C  
ATOM   3487  O   ASP A 950     193.694 205.012 140.166  1.00 60.35           O  
ATOM   3488  CB  ASP A 950     191.872 205.403 137.174  1.00 61.27           C  
ATOM   3489  CG  ASP A 950     190.715 205.779 138.111  1.00 60.58           C  
ATOM   3490  OD1 ASP A 950     190.931 206.453 139.145  1.00 60.91           O  
ATOM   3491  OD2 ASP A 950     189.562 205.410 137.794  1.00 59.29           O1-
ATOM   3492  N   VAL A 951     192.921 203.242 139.006  1.00 59.75           N  
ATOM   3493  CA  VAL A 951     192.811 202.340 140.159  1.00 44.91           C  
ATOM   3494  C   VAL A 951     194.147 202.128 140.874  1.00 47.27           C  
ATOM   3495  O   VAL A 951     194.162 202.109 142.104  1.00 58.68           O  
ATOM   3496  CB  VAL A 951     192.119 201.027 139.746  1.00 45.23           C  
ATOM   3497  CG1 VAL A 951     192.329 199.856 140.709  1.00 47.75           C  
ATOM   3498  CG2 VAL A 951     190.609 201.273 139.669  1.00 47.81           C  
ATOM   3499  N   VAL A 952     195.284 202.031 140.179  1.00 45.96           N  
ATOM   3500  CA  VAL A 952     196.594 201.925 140.854  1.00 45.77           C  
ATOM   3501  C   VAL A 952     196.934 203.177 141.671  1.00 50.13           C  
ATOM   3502  O   VAL A 952     197.456 203.051 142.773  1.00 57.88           O  
ATOM   3503  CB  VAL A 952     197.712 201.560 139.854  1.00 45.85           C  
ATOM   3504  CG1 VAL A 952     199.136 201.700 140.406  1.00 38.70           C  
ATOM   3505  CG2 VAL A 952     197.555 200.094 139.426  1.00 53.18           C  
ATOM   3506  N   ASN A 953     196.592 204.389 141.221  1.00 53.22           N  
ATOM   3507  CA  ASN A 953     196.846 205.606 141.997  1.00 58.31           C  
ATOM   3508  C   ASN A 953     195.814 205.810 143.130  1.00 55.89           C  
ATOM   3509  O   ASN A 953     196.161 206.345 144.180  1.00 54.58           O  
ATOM   3510  CB  ASN A 953     196.954 206.803 141.038  1.00 63.73           C  
ATOM   3511  CG  ASN A 953     198.071 207.756 141.427  1.00 62.72           C  
ATOM   3512  OD1 ASN A 953     198.378 207.980 142.581  1.00 62.89           O  
ATOM   3513  ND2 ASN A 953     198.744 208.337 140.472  1.00 55.51           N  
ATOM   3514  N   GLN A 954     194.590 205.289 142.989  1.00 54.67           N  
ATOM   3515  CA  GLN A 954     193.603 205.183 144.078  1.00 52.47           C  
ATOM   3516  C   GLN A 954     194.046 204.192 145.178  1.00 51.76           C  
ATOM   3517  O   GLN A 954     193.877 204.463 146.366  1.00 55.46           O  
ATOM   3518  CB  GLN A 954     192.239 204.822 143.457  1.00 52.27           C  
ATOM   3519  CG  GLN A 954     191.039 204.974 144.405  1.00 54.44           C  
ATOM   3520  CD  GLN A 954     190.722 203.757 145.280  1.00 56.75           C  
ATOM   3521  OE1 GLN A 954     191.360 202.714 145.253  1.00 45.38           O  
ATOM   3522  NE2 GLN A 954     189.678 203.828 146.074  1.00 61.35           N  
ATOM   3523  N   ASN A 955     194.724 203.100 144.808  1.00 47.93           N  
ATOM   3524  CA  ASN A 955     195.410 202.223 145.758  1.00 49.37           C  
ATOM   3525  C   ASN A 955     196.589 202.928 146.464  1.00 52.21           C  
ATOM   3526  O   ASN A 955     196.734 202.821 147.679  1.00 53.89           O  
ATOM   3527  CB  ASN A 955     195.887 200.947 145.045  1.00 50.04           C  
ATOM   3528  CG  ASN A 955     194.815 199.890 144.924  1.00 50.61           C  
ATOM   3529  OD1 ASN A 955     194.891 198.841 145.544  1.00 48.37           O  
ATOM   3530  ND2 ASN A 955     193.790 200.109 144.141  1.00 52.52           N  
ATOM   3531  N   ALA A 956     197.413 203.688 145.745  1.00 52.04           N  
ATOM   3532  CA  ALA A 956     198.515 204.434 146.345  1.00 48.89           C  
ATOM   3533  C   ALA A 956     198.012 205.491 147.340  1.00 57.89           C  
ATOM   3534  O   ALA A 956     198.582 205.658 148.414  1.00 67.10           O  
ATOM   3535  CB  ALA A 956     199.348 205.056 145.220  1.00 59.97           C  
ATOM   3536  N   GLN A 957     196.894 206.149 147.034  1.00 62.53           N  
ATOM   3537  CA  GLN A 957     196.167 207.017 147.970  1.00 60.27           C  
ATOM   3538  C   GLN A 957     195.668 206.247 149.202  1.00 55.43           C  
ATOM   3539  O   GLN A 957     195.897 206.686 150.326  1.00 56.47           O  
ATOM   3540  CB  GLN A 957     195.036 207.730 147.204  1.00 65.71           C  
ATOM   3541  CG  GLN A 957     194.005 208.457 148.084  1.00 63.84           C  
ATOM   3542  CD  GLN A 957     192.793 207.597 148.437  1.00 66.71           C  
ATOM   3543  OE1 GLN A 957     192.077 207.101 147.581  1.00 62.58           O  
ATOM   3544  NE2 GLN A 957     192.496 207.402 149.704  1.00 70.77           N  
ATOM   3545  N   ALA A 958     195.030 205.089 149.033  1.00 55.05           N  
ATOM   3546  CA  ALA A 958     194.537 204.289 150.157  1.00 57.00           C  
ATOM   3547  C   ALA A 958     195.656 203.838 151.113  1.00 58.73           C  
ATOM   3548  O   ALA A 958     195.496 203.944 152.326  1.00 60.79           O  
ATOM   3549  CB  ALA A 958     193.731 203.102 149.628  1.00 53.72           C  
ATOM   3550  N   LEU A 959     196.815 203.417 150.606  1.00 61.25           N  
ATOM   3551  CA  LEU A 959     197.941 203.023 151.457  1.00 50.01           C  
ATOM   3552  C   LEU A 959     198.593 204.194 152.184  1.00 47.79           C  
ATOM   3553  O   LEU A 959     198.943 204.028 153.346  1.00 54.59           O  
ATOM   3554  CB  LEU A 959     198.988 202.250 150.648  1.00 59.85           C  
ATOM   3555  CG  LEU A 959     198.824 200.728 150.688  1.00 58.49           C  
ATOM   3556  CD1 LEU A 959     199.070 200.180 152.090  1.00 54.24           C  
ATOM   3557  CD2 LEU A 959     197.455 200.274 150.189  1.00 57.83           C  
ATOM   3558  N   ASN A 960     198.697 205.377 151.578  1.00 49.24           N  
ATOM   3559  CA  ASN A 960     199.156 206.552 152.325  1.00 51.69           C  
ATOM   3560  C   ASN A 960     198.119 207.011 153.370  1.00 53.99           C  
ATOM   3561  O   ASN A 960     198.508 207.498 154.428  1.00 54.86           O  
ATOM   3562  CB  ASN A 960     199.590 207.676 151.362  1.00 59.23           C  
ATOM   3563  CG  ASN A 960     201.066 207.591 151.001  1.00 55.53           C  
ATOM   3564  OD1 ASN A 960     201.619 206.531 150.744  1.00 54.78           O  
ATOM   3565  ND2 ASN A 960     201.768 208.699 151.015  1.00 54.27           N  
ATOM   3566  N   THR A 961     196.821 206.788 153.132  1.00 55.16           N  
ATOM   3567  CA  THR A 961     195.778 207.001 154.151  1.00 53.60           C  
ATOM   3568  C   THR A 961     195.939 206.016 155.315  1.00 55.36           C  
ATOM   3569  O   THR A 961     195.960 206.428 156.472  1.00 66.00           O  
ATOM   3570  CB  THR A 961     194.362 206.896 153.564  1.00 54.62           C  
ATOM   3571  OG1 THR A 961     194.224 207.640 152.372  1.00 62.17           O  
ATOM   3572  CG2 THR A 961     193.335 207.460 154.534  1.00 68.05           C  
ATOM   3573  N   LEU A 962     196.130 204.729 155.018  1.00 51.87           N  
ATOM   3574  CA  LEU A 962     196.391 203.691 156.007  1.00 39.48           C  
ATOM   3575  C   LEU A 962     197.641 204.006 156.830  1.00 37.15           C  
ATOM   3576  O   LEU A 962     197.569 203.989 158.047  1.00 46.66           O  
ATOM   3577  CB  LEU A 962     196.506 202.342 155.283  1.00 43.30           C  
ATOM   3578  CG  LEU A 962     196.363 201.139 156.226  1.00 34.77           C  
ATOM   3579  CD1 LEU A 962     194.902 200.875 156.588  1.00 39.54           C  
ATOM   3580  CD2 LEU A 962     196.938 199.870 155.606  1.00 31.07           C  
ATOM   3581  N   VAL A 963     198.774 204.350 156.218  1.00 36.96           N  
ATOM   3582  CA  VAL A 963     200.007 204.644 156.970  1.00 42.86           C  
ATOM   3583  C   VAL A 963     199.843 205.848 157.895  1.00 47.52           C  
ATOM   3584  O   VAL A 963     200.322 205.804 159.024  1.00 51.74           O  
ATOM   3585  CB  VAL A 963     201.214 204.818 156.028  1.00 58.97           C  
ATOM   3586  CG1 VAL A 963     202.419 205.464 156.720  1.00 59.55           C  
ATOM   3587  CG2 VAL A 963     201.672 203.457 155.488  1.00 62.03           C  
ATOM   3588  N   LYS A 964     199.128 206.905 157.499  1.00 47.29           N  
ATOM   3589  CA  LYS A 964     198.889 208.054 158.391  1.00 47.85           C  
ATOM   3590  C   LYS A 964     197.951 207.710 159.559  1.00 41.65           C  
ATOM   3591  O   LYS A 964     198.196 208.152 160.683  1.00 42.02           O  
ATOM   3592  CB  LYS A 964     198.379 209.261 157.589  1.00 67.43           C  
ATOM   3593  CG  LYS A 964     199.449 209.950 156.728  1.00 69.57           C  
ATOM   3594  CD  LYS A 964     200.628 210.595 157.478  1.00 68.76           C  
ATOM   3595  CE  LYS A 964     200.190 211.662 158.493  1.00 65.70           C  
ATOM   3596  NZ  LYS A 964     201.341 212.399 159.055  1.00 68.93           N  
ATOM   3597  N   GLN A 965     196.923 206.886 159.342  1.00 39.74           N  
ATOM   3598  CA  GLN A 965     196.069 206.391 160.428  1.00 45.56           C  
ATOM   3599  C   GLN A 965     196.776 205.392 161.356  1.00 40.88           C  
ATOM   3600  O   GLN A 965     196.598 205.478 162.569  1.00 44.84           O  
ATOM   3601  CB  GLN A 965     194.793 205.766 159.858  1.00 50.91           C  
ATOM   3602  CG  GLN A 965     193.834 206.827 159.286  1.00 53.43           C  
ATOM   3603  CD  GLN A 965     192.414 206.724 159.831  1.00 64.14           C  
ATOM   3604  OE1 GLN A 965     192.170 206.417 160.988  1.00 66.00           O  
ATOM   3605  NE2 GLN A 965     191.405 206.985 159.036  1.00 61.73           N  
ATOM   3606  N   LEU A 966     197.605 204.483 160.845  1.00 35.32           N  
ATOM   3607  CA  LEU A 966     198.349 203.526 161.665  1.00 29.25           C  
ATOM   3608  C   LEU A 966     199.517 204.177 162.408  1.00 34.48           C  
ATOM   3609  O   LEU A 966     199.761 203.835 163.558  1.00 40.65           O  
ATOM   3610  CB  LEU A 966     198.844 202.374 160.789  1.00 30.51           C  
ATOM   3611  CG  LEU A 966     197.869 201.201 160.692  1.00 31.70           C  
ATOM   3612  CD1 LEU A 966     196.445 201.569 160.296  1.00 31.84           C  
ATOM   3613  CD2 LEU A 966     198.437 200.232 159.671  1.00 37.95           C  
ATOM   3614  N   SER A 967     200.168 205.176 161.829  1.00 37.94           N  
ATOM   3615  CA  SER A 967     201.097 206.039 162.562  1.00 35.66           C  
ATOM   3616  C   SER A 967     200.399 206.685 163.764  1.00 39.93           C  
ATOM   3617  O   SER A 967     200.977 206.757 164.847  1.00 42.74           O  
ATOM   3618  CB  SER A 967     201.659 207.109 161.624  1.00 46.68           C  
ATOM   3619  OG  SER A 967     202.499 208.009 162.312  1.00 36.12           O  
ATOM   3620  N   SER A 968     199.123 207.062 163.621  1.00 40.03           N  
ATOM   3621  CA  SER A 968     198.331 207.524 164.762  1.00 36.88           C  
ATOM   3622  C   SER A 968     198.137 206.419 165.799  1.00 39.02           C  
ATOM   3623  O   SER A 968     198.384 206.665 166.967  1.00 46.19           O  
ATOM   3624  CB  SER A 968     197.005 208.181 164.342  1.00 45.16           C  
ATOM   3625  OG  SER A 968     195.900 207.303 164.383  1.00 41.20           O  
ATOM   3626  N   ASN A 969     197.775 205.191 165.421  1.00 37.25           N  
ATOM   3627  CA  ASN A 969     197.552 204.095 166.371  1.00 31.40           C  
ATOM   3628  C   ASN A 969     198.798 203.648 167.118  1.00 29.59           C  
ATOM   3629  O   ASN A 969     198.754 203.509 168.337  1.00 36.81           O  
ATOM   3630  CB  ASN A 969     196.896 202.891 165.680  1.00 33.89           C  
ATOM   3631  CG  ASN A 969     195.411 203.101 165.533  1.00 45.10           C  
ATOM   3632  OD1 ASN A 969     194.811 203.803 166.318  1.00 46.65           O  
ATOM   3633  ND2 ASN A 969     194.763 202.528 164.551  1.00 45.06           N  
ATOM   3634  N   PHE A 970     199.922 203.441 166.447  1.00 31.36           N  
ATOM   3635  CA  PHE A 970     201.150 203.082 167.147  1.00 35.17           C  
ATOM   3636  C   PHE A 970     201.738 204.260 167.937  1.00 35.38           C  
ATOM   3637  O   PHE A 970     202.369 204.035 168.965  1.00 37.23           O  
ATOM   3638  CB  PHE A 970     202.131 202.420 166.178  1.00 44.23           C  
ATOM   3639  CG  PHE A 970     201.529 201.217 165.472  1.00 44.68           C  
ATOM   3640  CD1 PHE A 970     201.508 201.161 164.069  1.00 43.90           C  
ATOM   3641  CD2 PHE A 970     200.943 200.176 166.216  1.00 38.79           C  
ATOM   3642  CE1 PHE A 970     200.885 200.083 163.417  1.00 44.26           C  
ATOM   3643  CE2 PHE A 970     200.321 199.098 165.566  1.00 37.26           C  
ATOM   3644  CZ  PHE A 970     200.281 199.057 164.165  1.00 40.67           C  
ATOM   3645  N   GLY A 971     201.439 205.512 167.576  1.00 38.51           N  
ATOM   3646  CA  GLY A 971     201.739 206.691 168.396  1.00 29.35           C  
ATOM   3647  C   GLY A 971     200.820 206.853 169.617  1.00 33.97           C  
ATOM   3648  O   GLY A 971     201.282 207.215 170.699  1.00 37.56           O  
ATOM   3649  N   ALA A 972     199.529 206.555 169.480  1.00 36.01           N  
ATOM   3650  CA  ALA A 972     198.558 206.603 170.569  1.00 31.22           C  
ATOM   3651  C   ALA A 972     198.861 205.496 171.581  1.00 35.22           C  
ATOM   3652  O   ALA A 972     199.063 205.773 172.761  1.00 42.05           O  
ATOM   3653  CB  ALA A 972     197.136 206.480 170.005  1.00 30.72           C  
ATOM   3654  N   ILE A 973     198.993 204.254 171.105  1.00 30.63           N  
ATOM   3655  CA  ILE A 973     199.339 203.111 171.947  1.00 23.39           C  
ATOM   3656  C   ILE A 973     200.716 203.302 172.577  1.00 29.09           C  
ATOM   3657  O   ILE A 973     200.872 202.985 173.747  1.00 34.49           O  
ATOM   3658  CB  ILE A 973     199.227 201.796 171.154  1.00 22.43           C  
ATOM   3659  CG1 ILE A 973     197.747 201.507 170.829  1.00 20.49           C  
ATOM   3660  CG2 ILE A 973     199.826 200.615 171.936  1.00 24.18           C  
ATOM   3661  CD1 ILE A 973     197.560 200.392 169.797  1.00 22.49           C  
ATOM   3662  N   SER A 974     201.690 203.896 171.884  1.00 31.21           N  
ATOM   3663  CA  SER A 974     202.975 204.266 172.504  1.00 33.15           C  
ATOM   3664  C   SER A 974     202.765 205.093 173.769  1.00 33.91           C  
ATOM   3665  O   SER A 974     203.277 204.718 174.817  1.00 38.61           O  
ATOM   3666  CB  SER A 974     203.857 205.022 171.502  1.00 49.97           C  
ATOM   3667  OG  SER A 974     204.918 205.728 172.114  1.00 46.84           O  
ATOM   3668  N   SER A 975     201.973 206.167 173.720  1.00 33.13           N  
ATOM   3669  CA  SER A 975     201.765 207.043 174.880  1.00 37.33           C  
ATOM   3670  C   SER A 975     200.889 206.419 175.981  1.00 36.65           C  
ATOM   3671  O   SER A 975     201.269 206.416 177.154  1.00 39.31           O  
ATOM   3672  CB  SER A 975     201.204 208.390 174.426  1.00 54.23           C  
ATOM   3673  OG  SER A 975     201.107 209.274 175.529  1.00 53.53           O  
ATOM   3674  N   VAL A 976     199.733 205.846 175.627  1.00 31.36           N  
ATOM   3675  CA  VAL A 976     198.792 205.254 176.598  1.00 30.55           C  
ATOM   3676  C   VAL A 976     199.366 204.015 177.292  1.00 27.60           C  
ATOM   3677  O   VAL A 976     199.157 203.831 178.486  1.00 32.65           O  
ATOM   3678  CB  VAL A 976     197.447 204.917 175.932  1.00 38.85           C  
ATOM   3679  CG1 VAL A 976     196.422 204.391 176.940  1.00 40.91           C  
ATOM   3680  CG2 VAL A 976     196.806 206.143 175.273  1.00 48.17           C  
ATOM   3681  N   LEU A 977     200.107 203.170 176.574  1.00 24.01           N  
ATOM   3682  CA  LEU A 977     200.732 201.960 177.103  1.00 25.41           C  
ATOM   3683  C   LEU A 977     202.037 202.275 177.846  1.00 35.05           C  
ATOM   3684  O   LEU A 977     202.307 201.625 178.851  1.00 39.94           O  
ATOM   3685  CB  LEU A 977     200.902 200.967 175.939  1.00 25.24           C  
ATOM   3686  CG  LEU A 977     200.841 199.485 176.307  1.00 28.53           C  
ATOM   3687  CD1 LEU A 977     200.342 198.679 175.112  1.00 37.13           C  
ATOM   3688  CD2 LEU A 977     202.203 198.927 176.677  1.00 33.67           C  
ATOM   3689  N   ASN A 978     202.795 203.310 177.465  1.00 34.26           N  
ATOM   3690  CA  ASN A 978     203.883 203.792 178.318  1.00 31.32           C  
ATOM   3691  C   ASN A 978     203.355 204.289 179.662  1.00 37.61           C  
ATOM   3692  O   ASN A 978     203.954 203.989 180.684  1.00 43.51           O  
ATOM   3693  CB  ASN A 978     204.717 204.901 177.651  1.00 38.13           C  
ATOM   3694  CG  ASN A 978     205.975 204.372 176.989  1.00 60.04           C  
ATOM   3695  OD1 ASN A 978     206.718 203.586 177.558  1.00 67.88           O  
ATOM   3696  ND2 ASN A 978     206.296 204.798 175.796  1.00 63.78           N  
ATOM   3697  N   ASP A 979     202.235 205.013 179.698  1.00 34.35           N  
ATOM   3698  CA  ASP A 979     201.646 205.457 180.966  1.00 26.38           C  
ATOM   3699  C   ASP A 979     201.162 204.295 181.829  1.00 26.22           C  
ATOM   3700  O   ASP A 979     201.540 204.240 182.992  1.00 36.32           O  
ATOM   3701  CB  ASP A 979     200.520 206.472 180.744  1.00 27.96           C  
ATOM   3702  CG  ASP A 979     201.023 207.887 180.424  1.00 56.01           C  
ATOM   3703  OD1 ASP A 979     202.204 208.206 180.693  1.00 64.69           O  
ATOM   3704  OD2 ASP A 979     200.203 208.716 179.967  1.00 67.20           O1-
ATOM   3705  N   ILE A 980     200.415 203.330 181.281  1.00 20.77           N  
ATOM   3706  CA  ILE A 980     200.066 202.080 181.985  1.00 19.01           C  
ATOM   3707  C   ILE A 980     201.317 201.386 182.552  1.00 21.63           C  
ATOM   3708  O   ILE A 980     201.290 200.957 183.695  1.00 28.98           O  
ATOM   3709  CB  ILE A 980     199.276 201.129 181.056  1.00 19.13           C  
ATOM   3710  CG1 ILE A 980     197.827 201.561 180.770  1.00 17.80           C  
ATOM   3711  CG2 ILE A 980     199.268 199.698 181.586  1.00 17.58           C  
ATOM   3712  CD1 ILE A 980     196.879 201.553 181.971  1.00 20.98           C  
ATOM   3713  N   LEU A 981     202.426 201.287 181.820  1.00 24.82           N  
ATOM   3714  CA  LEU A 981     203.677 200.695 182.311  1.00 27.05           C  
ATOM   3715  C   LEU A 981     204.296 201.521 183.449  1.00 29.36           C  
ATOM   3716  O   LEU A 981     204.658 200.989 184.492  1.00 33.34           O  
ATOM   3717  CB  LEU A 981     204.676 200.581 181.142  1.00 34.25           C  
ATOM   3718  CG  LEU A 981     204.435 199.369 180.238  1.00 37.97           C  
ATOM   3719  CD1 LEU A 981     205.184 199.528 178.916  1.00 41.76           C  
ATOM   3720  CD2 LEU A 981     204.944 198.095 180.903  1.00 31.86           C  
ATOM   3721  N   SER A 982     204.407 202.833 183.264  1.00 27.41           N  
ATOM   3722  CA  SER A 982     205.032 203.762 184.207  1.00 27.42           C  
ATOM   3723  C   SER A 982     204.251 203.911 185.515  1.00 28.59           C  
ATOM   3724  O   SER A 982     204.852 203.971 186.589  1.00 38.83           O  
ATOM   3725  CB  SER A 982     205.198 205.109 183.499  1.00 37.61           C  
ATOM   3726  OG  SER A 982     205.859 206.047 184.311  1.00 44.78           O  
ATOM   3727  N   ARG A 983     202.923 203.841 185.438  1.00 23.66           N  
ATOM   3728  CA  ARG A 983     202.090 203.939 186.636  1.00 22.96           C  
ATOM   3729  C   ARG A 983     201.950 202.575 187.349  1.00 26.14           C  
ATOM   3730  O   ARG A 983     201.870 202.532 188.572  1.00 33.87           O  
ATOM   3731  CB  ARG A 983     200.732 204.589 186.324  1.00 18.18           C  
ATOM   3732  CG  ARG A 983     199.658 203.654 185.810  1.00 20.14           C  
ATOM   3733  CD  ARG A 983     198.465 204.398 185.239  1.00 21.05           C  
ATOM   3734  NE  ARG A 983     197.460 204.681 186.257  1.00 27.55           N  
ATOM   3735  CZ  ARG A 983     196.197 204.996 185.990  1.00 34.40           C  
ATOM   3736  NH1 ARG A 983     195.779 205.069 184.736  1.00 34.93           N  
ATOM   3737  NH2 ARG A 983     195.351 205.237 186.980  1.00 43.10           N  
ATOM   3738  N   LEU A 984     201.919 201.470 186.603  1.00 21.00           N  
ATOM   3739  CA  LEU A 984     201.868 200.158 187.240  1.00 18.85           C  
ATOM   3740  C   LEU A 984     203.167 199.860 187.973  1.00 23.21           C  
ATOM   3741  O   LEU A 984     203.123 199.290 189.049  1.00 31.18           O  
ATOM   3742  CB  LEU A 984     201.501 199.083 186.211  1.00 21.79           C  
ATOM   3743  CG  LEU A 984     201.175 197.694 186.783  1.00 25.33           C  
ATOM   3744  CD1 LEU A 984     200.224 197.749 187.979  1.00 34.21           C  
ATOM   3745  CD2 LEU A 984     200.452 196.894 185.700  1.00 26.28           C  
ATOM   3746  N   ASP A 985     204.308 200.321 187.465  1.00 27.60           N  
ATOM   3747  CA  ASP A 985     205.589 200.274 188.189  1.00 28.46           C  
ATOM   3748  C   ASP A 985     205.548 201.079 189.498  1.00 28.58           C  
ATOM   3749  O   ASP A 985     206.043 200.619 190.526  1.00 32.62           O  
ATOM   3750  CB  ASP A 985     206.730 200.822 187.311  1.00 37.99           C  
ATOM   3751  CG  ASP A 985     207.165 199.969 186.117  1.00 42.90           C  
ATOM   3752  OD1 ASP A 985     206.748 198.803 185.949  1.00 34.62           O  
ATOM   3753  OD2 ASP A 985     208.016 200.463 185.348  1.00 47.43           O1-
ATOM   3754  N   LYS A 986     204.928 202.264 189.496  1.00 26.24           N  
ATOM   3755  CA  LYS A 986     204.731 203.056 190.718  1.00 24.26           C  
ATOM   3756  C   LYS A 986     203.842 202.310 191.716  1.00 26.47           C  
ATOM   3757  O   LYS A 986     204.255 202.100 192.845  1.00 31.47           O  
ATOM   3758  CB  LYS A 986     204.176 204.438 190.349  1.00 26.66           C  
ATOM   3759  CG  LYS A 986     203.897 205.375 191.532  1.00 29.03           C  
ATOM   3760  CD  LYS A 986     205.117 205.761 192.383  1.00 40.37           C  
ATOM   3761  CE  LYS A 986     206.234 206.518 191.648  1.00 39.40           C  
ATOM   3762  NZ  LYS A 986     205.810 207.853 191.161  1.00 47.07           N  
ATOM   3763  N   VAL A 987     202.660 201.842 191.322  1.00 27.56           N  
ATOM   3764  CA  VAL A 987     201.740 201.092 192.202  1.00 21.57           C  
ATOM   3765  C   VAL A 987     202.308 199.760 192.722  1.00 17.64           C  
ATOM   3766  O   VAL A 987     202.078 199.419 193.876  1.00 28.51           O  
ATOM   3767  CB  VAL A 987     200.392 200.884 191.499  1.00 30.55           C  
ATOM   3768  CG1 VAL A 987     199.411 200.038 192.317  1.00 26.05           C  
ATOM   3769  CG2 VAL A 987     199.724 202.240 191.267  1.00 31.31           C  
ATOM   3770  N   GLU A 988     203.090 199.018 191.943  1.00 21.50           N  
ATOM   3771  CA  GLU A 988     203.791 197.818 192.426  1.00 29.28           C  
ATOM   3772  C   GLU A 988     204.987 198.131 193.338  1.00 34.59           C  
ATOM   3773  O   GLU A 988     205.394 197.277 194.125  1.00 41.14           O  
ATOM   3774  CB  GLU A 988     204.197 196.936 191.230  1.00 29.83           C  
ATOM   3775  CG  GLU A 988     204.409 195.451 191.597  1.00 44.86           C  
ATOM   3776  CD  GLU A 988     205.800 195.041 192.120  1.00 48.01           C  
ATOM   3777  OE1 GLU A 988     206.820 195.644 191.732  1.00 60.87           O  
ATOM   3778  OE2 GLU A 988     205.886 194.041 192.873  1.00 40.87           O1-
ATOM   3779  N   ALA A 989     205.541 199.350 193.296  1.00 27.34           N  
ATOM   3780  CA  ALA A 989     206.500 199.823 194.299  1.00 26.32           C  
ATOM   3781  C   ALA A 989     205.803 200.235 195.592  1.00 30.11           C  
ATOM   3782  O   ALA A 989     206.177 199.776 196.669  1.00 37.90           O  
ATOM   3783  CB  ALA A 989     207.316 200.992 193.746  1.00 27.21           C  
ATOM   3784  N   GLU A 990     204.779 201.085 195.508  1.00 29.87           N  
ATOM   3785  CA  GLU A 990     204.117 201.666 196.681  1.00 23.23           C  
ATOM   3786  C   GLU A 990     203.525 200.570 197.565  1.00 24.30           C  
ATOM   3787  O   GLU A 990     203.728 200.601 198.776  1.00 35.68           O  
ATOM   3788  CB  GLU A 990     203.019 202.658 196.261  1.00 23.41           C  
ATOM   3789  CG  GLU A 990     203.482 203.850 195.405  1.00 33.65           C  
ATOM   3790  CD  GLU A 990     203.995 205.049 196.200  1.00 47.11           C  
ATOM   3791  OE1 GLU A 990     203.303 206.088 196.226  1.00 51.71           O  
ATOM   3792  OE2 GLU A 990     205.110 204.980 196.755  1.00 60.14           O1-
ATOM   3793  N   VAL A 991     202.895 199.541 196.982  1.00 25.47           N  
ATOM   3794  CA  VAL A 991     202.276 198.424 197.723  1.00 29.40           C  
ATOM   3795  C   VAL A 991     203.278 197.621 198.574  1.00 29.91           C  
ATOM   3796  O   VAL A 991     202.882 197.045 199.580  1.00 44.64           O  
ATOM   3797  CB  VAL A 991     201.436 197.544 196.769  1.00 35.75           C  
ATOM   3798  CG1 VAL A 991     202.240 196.470 196.040  1.00 38.99           C  
ATOM   3799  CG2 VAL A 991     200.270 196.867 197.479  1.00 51.87           C  
ATOM   3800  N   GLN A 992     204.577 197.632 198.248  1.00 27.74           N  
ATOM   3801  CA  GLN A 992     205.655 197.038 199.059  1.00 32.24           C  
ATOM   3802  C   GLN A 992     206.184 197.972 200.161  1.00 30.32           C  
ATOM   3803  O   GLN A 992     206.637 197.522 201.207  1.00 35.48           O  
ATOM   3804  CB  GLN A 992     206.865 196.714 198.182  1.00 37.64           C  
ATOM   3805  CG  GLN A 992     206.633 195.723 197.048  1.00 37.45           C  
ATOM   3806  CD  GLN A 992     207.897 195.648 196.201  1.00 42.44           C  
ATOM   3807  OE1 GLN A 992     208.898 195.059 196.586  1.00 49.93           O  
ATOM   3808  NE2 GLN A 992     207.926 196.306 195.069  1.00 42.67           N  
ATOM   3809  N   ILE A 993     206.160 199.285 199.946  1.00 27.99           N  
ATOM   3810  CA  ILE A 993     206.580 200.278 200.934  1.00 23.08           C  
ATOM   3811  C   ILE A 993     205.474 200.454 201.987  1.00 24.92           C  
ATOM   3812  O   ILE A 993     205.769 200.538 203.175  1.00 34.53           O  
ATOM   3813  CB  ILE A 993     206.983 201.584 200.228  1.00 27.19           C  
ATOM   3814  CG1 ILE A 993     208.251 201.346 199.387  1.00 32.94           C  
ATOM   3815  CG2 ILE A 993     207.261 202.701 201.238  1.00 32.56           C  
ATOM   3816  CD1 ILE A 993     208.559 202.466 198.399  1.00 46.22           C  
ATOM   3817  N   ASP A 994     204.200 200.417 201.590  1.00 22.75           N  
ATOM   3818  CA  ASP A 994     203.047 200.353 202.495  1.00 22.24           C  
ATOM   3819  C   ASP A 994     203.060 199.101 203.367  1.00 25.76           C  
ATOM   3820  O   ASP A 994     202.577 199.119 204.500  1.00 27.46           O  
ATOM   3821  CB  ASP A 994     201.745 200.319 201.685  1.00 25.35           C  
ATOM   3822  CG  ASP A 994     201.309 201.670 201.133  1.00 36.29           C  
ATOM   3823  OD1 ASP A 994     200.743 201.700 200.021  1.00 33.06           O  
ATOM   3824  OD2 ASP A 994     201.386 202.682 201.867  1.00 48.42           O1-
ATOM   3825  N   ARG A 995     203.615 198.017 202.850  1.00 25.69           N  
ATOM   3826  CA  ARG A 995     203.661 196.783 203.613  1.00 18.72           C  
ATOM   3827  C   ARG A 995     204.558 197.002 204.833  1.00 22.53           C  
ATOM   3828  O   ARG A 995     204.160 196.742 205.962  1.00 32.14           O  
ATOM   3829  CB  ARG A 995     204.148 195.633 202.725  1.00 30.64           C  
ATOM   3830  CG  ARG A 995     203.388 194.338 202.933  1.00 40.44           C  
ATOM   3831  CD  ARG A 995     203.860 193.255 201.978  1.00 39.73           C  
ATOM   3832  NE  ARG A 995     202.914 192.970 200.906  1.00 34.39           N  
ATOM   3833  CZ  ARG A 995     203.147 193.236 199.627  1.00 36.46           C  
ATOM   3834  NH1 ARG A 995     204.300 193.775 199.260  1.00 39.49           N  
ATOM   3835  NH2 ARG A 995     202.235 192.949 198.713  1.00 45.74           N  
ATOM   3836  N   LEU A 996     205.764 197.497 204.581  1.00 23.07           N  
ATOM   3837  CA  LEU A 996     206.734 197.776 205.623  1.00 18.86           C  
ATOM   3838  C   LEU A 996     206.303 198.915 206.535  1.00 17.28           C  
ATOM   3839  O   LEU A 996     206.524 198.811 207.728  1.00 28.32           O  
ATOM   3840  CB  LEU A 996     208.092 198.034 204.973  1.00 22.43           C  
ATOM   3841  CG  LEU A 996     209.221 198.212 205.988  1.00 24.10           C  
ATOM   3842  CD1 LEU A 996     209.423 196.970 206.842  1.00 33.75           C  
ATOM   3843  CD2 LEU A 996     210.510 198.471 205.235  1.00 33.27           C  
ATOM   3844  N   ILE A 997     205.655 199.973 206.050  1.00 17.05           N  
ATOM   3845  CA  ILE A 997     205.065 200.981 206.956  1.00 15.21           C  
ATOM   3846  C   ILE A 997     204.074 200.315 207.910  1.00 16.96           C  
ATOM   3847  O   ILE A 997     204.202 200.488 209.112  1.00 19.34           O  
ATOM   3848  CB  ILE A 997     204.420 202.158 206.199  1.00 20.18           C  
ATOM   3849  CG1 ILE A 997     205.475 203.028 205.481  1.00 24.94           C  
ATOM   3850  CG2 ILE A 997     203.626 203.051 207.163  1.00 20.58           C  
ATOM   3851  CD1 ILE A 997     204.892 203.920 204.375  1.00 29.61           C  
ATOM   3852  N   THR A 998     203.166 199.478 207.423  1.00 16.21           N  
ATOM   3853  CA  THR A 998     202.162 198.785 208.246  1.00 11.69           C  
ATOM   3854  C   THR A 998     202.736 197.810 209.286  1.00 15.40           C  
ATOM   3855  O   THR A 998     202.172 197.684 210.366  1.00 19.59           O  
ATOM   3856  CB  THR A 998     201.164 198.088 207.326  1.00 19.19           C  
ATOM   3857  OG1 THR A 998     200.634 199.027 206.417  1.00 20.52           O  
ATOM   3858  CG2 THR A 998     200.013 197.462 208.098  1.00 13.89           C  
ATOM   3859  N   GLY A 999     203.877 197.165 209.049  1.00 14.23           N  
ATOM   3860  CA  GLY A 999     204.601 196.422 210.083  1.00 13.14           C  
ATOM   3861  C   GLY A 999     205.433 197.291 211.040  1.00 15.89           C  
ATOM   3862  O   GLY A 999     205.679 196.912 212.188  1.00 25.14           O  
ATOM   3863  N   ARG A1000     205.769 198.495 210.616  1.00 14.69           N  
ATOM   3864  CA  ARG A1000     206.375 199.428 211.550  1.00  7.41           C  
ATOM   3865  C   ARG A1000     205.274 200.114 212.397  1.00 16.11           C  
ATOM   3866  O   ARG A1000     205.540 200.537 213.515  1.00 24.92           O  
ATOM   3867  CB  ARG A1000     207.274 200.403 210.846  1.00 12.34           C  
ATOM   3868  CG  ARG A1000     208.625 199.780 210.610  1.00 20.89           C  
ATOM   3869  CD  ARG A1000     209.372 200.523 209.548  1.00 17.50           C  
ATOM   3870  NE  ARG A1000     210.782 200.185 209.552  1.00 25.53           N  
ATOM   3871  CZ  ARG A1000     211.692 200.862 210.234  1.00 29.13           C  
ATOM   3872  NH1 ARG A1000     211.338 201.907 210.962  1.00 29.37           N  
ATOM   3873  NH2 ARG A1000     212.954 200.492 210.193  1.00 32.45           N  
ATOM   3874  N   LEU A1001     204.053 200.232 211.866  1.00 14.92           N  
ATOM   3875  CA  LEU A1001     202.946 200.719 212.683  1.00  8.43           C  
ATOM   3876  C   LEU A1001     202.792 199.853 213.922  1.00 15.81           C  
ATOM   3877  O   LEU A1001     202.675 200.405 214.999  1.00 16.66           O  
ATOM   3878  CB  LEU A1001     201.625 200.768 211.902  1.00 11.84           C  
ATOM   3879  CG  LEU A1001     201.529 201.780 210.759  1.00 12.92           C  
ATOM   3880  CD1 LEU A1001     200.118 201.829 210.203  1.00 12.40           C  
ATOM   3881  CD2 LEU A1001     201.896 203.179 211.205  1.00 12.26           C  
ATOM   3882  N   GLN A1002     202.888 198.527 213.810  1.00 12.71           N  
ATOM   3883  CA  GLN A1002     202.759 197.617 214.957  1.00 10.51           C  
ATOM   3884  C   GLN A1002     203.900 197.778 215.958  1.00 16.31           C  
ATOM   3885  O   GLN A1002     203.711 197.661 217.164  1.00 22.65           O  
ATOM   3886  CB  GLN A1002     202.718 196.144 214.512  1.00 10.42           C  
ATOM   3887  CG  GLN A1002     201.839 195.821 213.303  1.00 13.66           C  
ATOM   3888  CD  GLN A1002     200.474 196.487 213.320  1.00 13.36           C  
ATOM   3889  OE1 GLN A1002     199.714 196.399 214.265  1.00 13.25           O  
ATOM   3890  NE2 GLN A1002     200.112 197.184 212.273  1.00  9.90           N  
ATOM   3891  N   SER A1003     205.104 198.065 215.472  1.00 17.46           N  
ATOM   3892  CA  SER A1003     206.252 198.355 216.337  1.00 15.32           C  
ATOM   3893  C   SER A1003     206.032 199.650 217.114  1.00 14.55           C  
ATOM   3894  O   SER A1003     206.274 199.692 218.309  1.00 21.07           O  
ATOM   3895  CB  SER A1003     207.537 198.435 215.517  1.00 24.81           C  
ATOM   3896  OG  SER A1003     207.781 197.233 214.812  1.00 34.13           O  
ATOM   3897  N   LEU A1004     205.504 200.697 216.487  1.00 15.58           N  
ATOM   3898  CA  LEU A1004     205.091 201.918 217.173  1.00 15.25           C  
ATOM   3899  C   LEU A1004     203.856 201.703 218.091  1.00 16.39           C  
ATOM   3900  O   LEU A1004     203.768 202.330 219.137  1.00 23.54           O  
ATOM   3901  CB  LEU A1004     204.868 203.006 216.117  1.00 15.09           C  
ATOM   3902  CG  LEU A1004     204.349 204.324 216.696  1.00 13.43           C  
ATOM   3903  CD1 LEU A1004     205.347 205.014 217.604  1.00 18.19           C  
ATOM   3904  CD2 LEU A1004     204.025 205.295 215.580  1.00 31.45           C  
ATOM   3905  N   GLN A1005     202.925 200.799 217.777  1.00 15.39           N  
ATOM   3906  CA  GLN A1005     201.808 200.452 218.663  1.00 11.41           C  
ATOM   3907  C   GLN A1005     202.238 199.596 219.868  1.00 19.73           C  
ATOM   3908  O   GLN A1005     201.689 199.746 220.956  1.00 26.04           O  
ATOM   3909  CB  GLN A1005     200.718 199.743 217.855  1.00 13.05           C  
ATOM   3910  CG  GLN A1005     199.394 199.684 218.615  1.00 16.47           C  
ATOM   3911  CD  GLN A1005     198.817 201.058 218.905  1.00 17.58           C  
ATOM   3912  OE1 GLN A1005     198.756 201.929 218.058  1.00 25.62           O  
ATOM   3913  NE2 GLN A1005     198.369 201.313 220.110  1.00 24.11           N  
ATOM   3914  N   THR A1006     203.270 198.763 219.733  1.00 21.52           N  
ATOM   3915  CA  THR A1006     203.955 198.136 220.871  1.00 15.34           C  
ATOM   3916  C   THR A1006     204.711 199.160 221.707  1.00 16.37           C  
ATOM   3917  O   THR A1006     204.657 199.086 222.929  1.00 24.69           O  
ATOM   3918  CB  THR A1006     204.895 197.033 220.408  1.00 20.47           C  
ATOM   3919  OG1 THR A1006     204.094 196.013 219.891  1.00 30.04           O  
ATOM   3920  CG2 THR A1006     205.721 196.394 221.520  1.00 22.23           C  
ATOM   3921  N   TYR A1007     205.333 200.160 221.083  1.00 18.08           N  
ATOM   3922  CA  TYR A1007     205.912 201.280 221.799  1.00 13.56           C  
ATOM   3923  C   TYR A1007     204.854 202.005 222.606  1.00 15.96           C  
ATOM   3924  O   TYR A1007     205.013 202.119 223.811  1.00 25.37           O  
ATOM   3925  CB  TYR A1007     206.654 202.202 220.841  1.00 19.06           C  
ATOM   3926  CG  TYR A1007     207.186 203.461 221.478  1.00 16.44           C  
ATOM   3927  CD1 TYR A1007     208.440 203.455 222.102  1.00 21.22           C  
ATOM   3928  CD2 TYR A1007     206.424 204.637 221.451  1.00 17.12           C  
ATOM   3929  CE1 TYR A1007     208.932 204.622 222.704  1.00 27.07           C  
ATOM   3930  CE2 TYR A1007     206.909 205.808 222.051  1.00 23.77           C  
ATOM   3931  CZ  TYR A1007     208.172 205.807 222.668  1.00 29.64           C  
ATOM   3932  OH  TYR A1007     208.688 206.958 223.166  1.00 35.78           O  
ATOM   3933  N   VAL A1008     203.747 202.425 222.002  1.00 10.94           N  
ATOM   3934  CA  VAL A1008     202.663 203.147 222.682  1.00 11.45           C  
ATOM   3935  C   VAL A1008     202.014 202.309 223.779  1.00 18.41           C  
ATOM   3936  O   VAL A1008     201.802 202.810 224.875  1.00 25.50           O  
ATOM   3937  CB  VAL A1008     201.649 203.639 221.636  1.00 17.73           C  
ATOM   3938  CG1 VAL A1008     200.274 204.015 222.183  1.00 13.35           C  
ATOM   3939  CG2 VAL A1008     202.245 204.861 220.935  1.00 22.64           C  
ATOM   3940  N   THR A1009     201.774 201.019 223.562  1.00 18.08           N  
ATOM   3941  CA  THR A1009     201.240 200.134 224.605  1.00 12.65           C  
ATOM   3942  C   THR A1009     202.187 200.013 225.798  1.00 12.20           C  
ATOM   3943  O   THR A1009     201.758 200.288 226.905  1.00 19.32           O  
ATOM   3944  CB  THR A1009     200.904 198.740 224.068  1.00 22.36           C  
ATOM   3945  OG1 THR A1009     200.062 198.813 222.941  1.00 27.57           O  
ATOM   3946  CG2 THR A1009     200.209 197.885 225.125  1.00 16.28           C  
ATOM   3947  N   GLN A1010     203.471 199.690 225.619  1.00 16.03           N  
ATOM   3948  CA  GLN A1010     204.453 199.616 226.713  1.00 17.00           C  
ATOM   3949  C   GLN A1010     204.709 200.966 227.415  1.00 18.46           C  
ATOM   3950  O   GLN A1010     205.062 200.982 228.589  1.00 21.28           O  
ATOM   3951  CB  GLN A1010     205.760 199.030 226.169  1.00 14.52           C  
ATOM   3952  CG  GLN A1010     205.720 197.511 225.975  1.00 24.58           C  
ATOM   3953  CD  GLN A1010     207.085 196.863 225.721  1.00 32.28           C  
ATOM   3954  OE1 GLN A1010     207.442 195.850 226.299  1.00 38.41           O  
ATOM   3955  NE2 GLN A1010     207.938 197.416 224.902  1.00 28.27           N  
ATOM   3956  N   GLN A1011     204.493 202.096 226.750  1.00 15.29           N  
ATOM   3957  CA  GLN A1011     204.572 203.432 227.332  1.00  9.10           C  
ATOM   3958  C   GLN A1011     203.298 203.829 228.090  1.00 14.88           C  
ATOM   3959  O   GLN A1011     203.384 204.614 229.029  1.00 20.37           O  
ATOM   3960  CB  GLN A1011     204.905 204.438 226.217  1.00 17.79           C  
ATOM   3961  CG  GLN A1011     205.791 205.602 226.658  1.00 20.92           C  
ATOM   3962  CD  GLN A1011     207.218 205.204 227.041  1.00 27.81           C  
ATOM   3963  OE1 GLN A1011     207.691 204.093 226.856  1.00 24.50           O  
ATOM   3964  NE2 GLN A1011     207.981 206.111 227.596  1.00 41.16           N  
ATOM   3965  N   LEU A1012     202.120 203.289 227.747  1.00 16.10           N  
ATOM   3966  CA  LEU A1012     200.888 203.435 228.530  1.00 13.34           C  
ATOM   3967  C   LEU A1012     200.846 202.455 229.702  1.00 14.27           C  
ATOM   3968  O   LEU A1012     200.449 202.823 230.797  1.00 19.55           O  
ATOM   3969  CB  LEU A1012     199.655 203.209 227.649  1.00 16.91           C  
ATOM   3970  CG  LEU A1012     199.398 204.260 226.560  1.00 16.60           C  
ATOM   3971  CD1 LEU A1012     198.179 203.822 225.759  1.00  9.69           C  
ATOM   3972  CD2 LEU A1012     199.143 205.644 227.131  1.00 38.62           C  
ATOM   3973  N   ILE A1013     201.296 201.219 229.502  1.00 14.85           N  
ATOM   3974  CA  ILE A1013     201.432 200.200 230.539  1.00  8.52           C  
ATOM   3975  C   ILE A1013     202.283 200.765 231.668  1.00 13.34           C  
ATOM   3976  O   ILE A1013     201.831 200.807 232.807  1.00 20.06           O  
ATOM   3977  CB  ILE A1013     202.016 198.910 229.916  1.00 15.55           C  
ATOM   3978  CG1 ILE A1013     200.964 198.117 229.108  1.00 15.38           C  
ATOM   3979  CG2 ILE A1013     202.739 197.983 230.901  1.00 23.68           C  
ATOM   3980  CD1 ILE A1013     199.960 197.295 229.915  1.00 17.61           C  
ATOM   3981  N   ARG A1014     203.478 201.296 231.372  1.00 14.97           N  
ATOM   3982  CA  ARG A1014     204.373 201.873 232.384  1.00 11.73           C  
ATOM   3983  C   ARG A1014     203.752 203.062 233.087  1.00 11.89           C  
ATOM   3984  O   ARG A1014     203.881 203.156 234.295  1.00 25.21           O  
ATOM   3985  CB  ARG A1014     205.730 202.212 231.760  1.00 14.25           C  
ATOM   3986  CG  ARG A1014     206.693 202.815 232.788  1.00 14.43           C  
ATOM   3987  CD  ARG A1014     208.048 203.162 232.172  1.00 26.51           C  
ATOM   3988  NE  ARG A1014     208.900 203.873 233.142  1.00 38.81           N  
ATOM   3989  CZ  ARG A1014     209.640 203.325 234.079  1.00 48.11           C  
ATOM   3990  NH1 ARG A1014     210.348 204.053 234.877  1.00 52.74           N  
ATOM   3991  NH2 ARG A1014     209.673 202.044 234.243  1.00 50.52           N  
ATOM   3992  N   ALA A1015     203.035 203.927 232.390  1.00 11.74           N  
ATOM   3993  CA  ALA A1015     202.350 205.055 233.018  1.00 12.85           C  
ATOM   3994  C   ALA A1015     201.175 204.663 233.952  1.00 16.68           C  
ATOM   3995  O   ALA A1015     200.898 205.358 234.927  1.00 28.82           O  
ATOM   3996  CB  ALA A1015     201.928 205.998 231.900  1.00 20.74           C  
ATOM   3997  N   ALA A1016     200.514 203.533 233.713  1.00 14.91           N  
ATOM   3998  CA  ALA A1016     199.537 202.948 234.628  1.00 14.64           C  
ATOM   3999  C   ALA A1016     200.165 202.177 235.815  1.00 15.05           C  
ATOM   4000  O   ALA A1016     199.520 202.039 236.855  1.00 24.13           O  
ATOM   4001  CB  ALA A1016     198.588 202.065 233.824  1.00 17.43           C  
ATOM   4002  N   GLU A1017     201.424 201.722 235.732  1.00 14.72           N  
ATOM   4003  CA  GLU A1017     202.225 201.362 236.915  1.00 15.00           C  
ATOM   4004  C   GLU A1017     202.686 202.599 237.688  1.00 16.32           C  
ATOM   4005  O   GLU A1017     202.586 202.631 238.907  1.00 25.88           O  
ATOM   4006  CB  GLU A1017     203.480 200.564 236.556  1.00 17.86           C  
ATOM   4007  CG  GLU A1017     203.178 199.211 235.932  1.00 29.02           C  
ATOM   4008  CD  GLU A1017     204.472 198.447 235.645  1.00 40.13           C  
ATOM   4009  OE1 GLU A1017     204.586 197.841 234.560  1.00 35.41           O  
ATOM   4010  OE2 GLU A1017     205.368 198.342 236.516  1.00 58.43           O1-
ATOM   4011  N   ILE A1018     203.146 203.648 237.015  1.00 13.61           N  
ATOM   4012  CA  ILE A1018     203.539 204.895 237.672  1.00 13.32           C  
ATOM   4013  C   ILE A1018     202.385 205.446 238.491  1.00 18.72           C  
ATOM   4014  O   ILE A1018     202.591 205.806 239.645  1.00 32.37           O  
ATOM   4015  CB  ILE A1018     204.031 205.920 236.640  1.00 16.13           C  
ATOM   4016  CG1 ILE A1018     205.388 205.502 236.054  1.00 16.50           C  
ATOM   4017  CG2 ILE A1018     204.068 207.359 237.165  1.00 24.79           C  
ATOM   4018  CD1 ILE A1018     206.611 205.865 236.883  1.00 24.23           C  
ATOM   4019  N   ARG A1019     201.153 205.463 237.968  1.00 20.16           N  
ATOM   4020  CA  ARG A1019     199.998 205.965 238.728  1.00 19.32           C  
ATOM   4021  C   ARG A1019     199.585 205.070 239.901  1.00 20.06           C  
ATOM   4022  O   ARG A1019     199.001 205.575 240.854  1.00 29.75           O  
ATOM   4023  CB  ARG A1019     198.852 206.318 237.771  1.00 26.85           C  
ATOM   4024  CG  ARG A1019     199.159 207.646 237.054  1.00 42.99           C  
ATOM   4025  CD  ARG A1019     198.025 208.231 236.205  1.00 39.73           C  
ATOM   4026  NE  ARG A1019     197.707 207.390 235.039  1.00 34.80           N  
ATOM   4027  CZ  ARG A1019     196.831 206.405 235.012  1.00 37.66           C  
ATOM   4028  NH1 ARG A1019     196.128 206.106 236.057  1.00 39.69           N  
ATOM   4029  NH2 ARG A1019     196.625 205.694 233.948  1.00 39.68           N  
ATOM   4030  N   ALA A1020     199.970 203.796 239.935  1.00 20.02           N  
ATOM   4031  CA  ALA A1020     199.855 202.959 241.135  1.00 19.25           C  
ATOM   4032  C   ALA A1020     200.986 203.225 242.135  1.00 24.90           C  
ATOM   4033  O   ALA A1020     200.759 203.212 243.338  1.00 35.06           O  
ATOM   4034  CB  ALA A1020     199.834 201.485 240.737  1.00 20.51           C  
ATOM   4035  N   SER A1021     202.196 203.523 241.664  1.00 21.30           N  
ATOM   4036  CA  SER A1021     203.325 203.925 242.508  1.00 17.52           C  
ATOM   4037  C   SER A1021     203.131 205.313 243.131  1.00 18.96           C  
ATOM   4038  O   SER A1021     203.574 205.548 244.244  1.00 29.83           O  
ATOM   4039  CB  SER A1021     204.601 203.839 241.685  1.00 19.61           C  
ATOM   4040  OG  SER A1021     205.724 204.200 242.441  1.00 27.64           O  
ATOM   4041  N   ALA A1022     202.386 206.212 242.495  1.00 22.06           N  
ATOM   4042  CA  ALA A1022     201.886 207.443 243.099  1.00 22.53           C  
ATOM   4043  C   ALA A1022     200.751 207.231 244.131  1.00 27.22           C  
ATOM   4044  O   ALA A1022     200.660 207.981 245.102  1.00 34.85           O  
ATOM   4045  CB  ALA A1022     201.417 208.349 241.968  1.00 29.96           C  
ATOM   4046  N   ASN A1023     199.926 206.185 243.999  1.00 26.49           N  
ATOM   4047  CA  ASN A1023     199.070 205.725 245.098  1.00 22.85           C  
ATOM   4048  C   ASN A1023     199.864 205.069 246.232  1.00 23.72           C  
ATOM   4049  O   ASN A1023     199.549 205.325 247.390  1.00 31.33           O  
ATOM   4050  CB  ASN A1023     198.002 204.749 244.590  1.00 28.53           C  
ATOM   4051  CG  ASN A1023     196.791 205.415 244.009  1.00 39.78           C  
ATOM   4052  OD1 ASN A1023     196.716 206.603 243.825  1.00 39.84           O  
ATOM   4053  ND2 ASN A1023     195.772 204.656 243.722  1.00 39.87           N  
ATOM   4054  N   LEU A1024     200.907 204.285 245.948  1.00 24.49           N  
ATOM   4055  CA  LEU A1024     201.783 203.745 246.982  1.00 19.57           C  
ATOM   4056  C   LEU A1024     202.501 204.871 247.720  1.00 15.86           C  
ATOM   4057  O   LEU A1024     202.543 204.859 248.937  1.00 27.21           O  
ATOM   4058  CB  LEU A1024     202.775 202.736 246.396  1.00 22.59           C  
ATOM   4059  CG  LEU A1024     203.620 202.016 247.455  1.00 16.40           C  
ATOM   4060  CD1 LEU A1024     202.783 201.125 248.367  1.00 21.53           C  
ATOM   4061  CD2 LEU A1024     204.671 201.156 246.760  1.00 15.56           C  
ATOM   4062  N   ALA A1025     203.012 205.883 247.025  1.00 20.01           N  
ATOM   4063  CA  ALA A1025     203.582 207.070 247.629  1.00 19.59           C  
ATOM   4064  C   ALA A1025     202.567 207.839 248.469  1.00 21.59           C  
ATOM   4065  O   ALA A1025     202.979 208.460 249.433  1.00 28.98           O  
ATOM   4066  CB  ALA A1025     204.129 207.956 246.514  1.00 24.74           C  
ATOM   4067  N   ALA A1026     201.266 207.790 248.173  1.00 21.81           N  
ATOM   4068  CA  ALA A1026     200.240 208.451 248.987  1.00 21.14           C  
ATOM   4069  C   ALA A1026     199.996 207.733 250.320  1.00 25.72           C  
ATOM   4070  O   ALA A1026     200.088 208.354 251.374  1.00 33.59           O  
ATOM   4071  CB  ALA A1026     198.936 208.587 248.192  1.00 35.52           C  
ATOM   4072  N   THR A1027     199.736 206.423 250.297  1.00 25.24           N  
ATOM   4073  CA  THR A1027     199.565 205.617 251.518  1.00 22.35           C  
ATOM   4074  C   THR A1027     200.857 205.566 252.336  1.00 24.95           C  
ATOM   4075  O   THR A1027     200.828 205.819 253.535  1.00 33.87           O  
ATOM   4076  CB  THR A1027     199.006 204.225 251.205  1.00 22.29           C  
ATOM   4077  OG1 THR A1027     198.940 203.428 252.348  1.00 31.97           O  
ATOM   4078  CG2 THR A1027     199.853 203.387 250.258  1.00 35.07           C  
ATOM   4079  N   LYS A1028     202.019 205.358 251.710  1.00 23.84           N  
ATOM   4080  CA  LYS A1028     203.336 205.323 252.365  1.00 22.38           C  
ATOM   4081  C   LYS A1028     203.811 206.691 252.886  1.00 23.88           C  
ATOM   4082  O   LYS A1028     204.553 206.737 253.857  1.00 37.74           O  
ATOM   4083  CB  LYS A1028     204.332 204.699 251.379  1.00 17.92           C  
ATOM   4084  CG  LYS A1028     205.655 204.373 252.052  1.00 17.98           C  
ATOM   4085  CD  LYS A1028     206.594 203.464 251.263  1.00 20.51           C  
ATOM   4086  CE  LYS A1028     206.037 202.047 251.191  1.00 21.96           C  
ATOM   4087  NZ  LYS A1028     207.079 201.079 250.771  1.00 24.10           N  
ATOM   4088  N   MET A1029     203.371 207.811 252.315  1.00 22.44           N  
ATOM   4089  CA  MET A1029     203.510 209.134 252.930  1.00 26.68           C  
ATOM   4090  C   MET A1029     202.605 209.225 254.142  1.00 35.03           C  
ATOM   4091  O   MET A1029     203.060 209.561 255.224  1.00 47.04           O  
ATOM   4092  CB  MET A1029     203.154 210.236 251.922  1.00 28.05           C  
ATOM   4093  CG  MET A1029     202.997 211.648 252.494  1.00 35.20           C  
ATOM   4094  SD  MET A1029     204.528 212.593 252.575  1.00 65.29           S  
ATOM   4095  CE  MET A1029     203.868 214.147 253.242  1.00 73.18           C  
ATOM   4096  N   SER A1030     201.321 208.924 253.984  1.00 34.18           N  
ATOM   4097  CA  SER A1030     200.336 209.149 255.036  1.00 34.40           C  
ATOM   4098  C   SER A1030     200.637 208.353 256.296  1.00 31.90           C  
ATOM   4099  O   SER A1030     200.804 208.926 257.363  1.00 38.80           O  
ATOM   4100  CB  SER A1030     198.950 208.823 254.516  1.00 35.63           C  
ATOM   4101  OG  SER A1030     198.029 209.173 255.504  1.00 43.21           O  
ATOM   4102  N   GLU A1031     200.782 207.041 256.190  1.00 30.72           N  
ATOM   4103  CA  GLU A1031     200.884 206.147 257.346  1.00 33.27           C  
ATOM   4104  C   GLU A1031     202.194 206.241 258.115  1.00 33.45           C  
ATOM   4105  O   GLU A1031     202.317 205.636 259.178  1.00 40.28           O  
ATOM   4106  CB  GLU A1031     200.633 204.713 256.885  1.00 34.44           C  
ATOM   4107  CG  GLU A1031     199.160 204.550 256.519  1.00 33.81           C  
ATOM   4108  CD  GLU A1031     198.897 203.291 255.700  1.00 38.33           C  
ATOM   4109  OE1 GLU A1031     199.543 202.241 255.917  1.00 45.12           O  
ATOM   4110  OE2 GLU A1031     197.954 203.329 254.877  1.00 41.65           O1-
ATOM   4111  N   CYS A1032     203.181 206.978 257.603  1.00 30.65           N  
ATOM   4112  CA  CYS A1032     204.557 206.935 258.102  1.00 41.17           C  
ATOM   4113  C   CYS A1032     205.246 208.299 258.254  1.00 47.96           C  
ATOM   4114  O   CYS A1032     206.164 208.441 259.063  1.00 51.44           O  
ATOM   4115  CB  CYS A1032     205.347 206.010 257.185  1.00 30.95           C  
ATOM   4116  SG  CYS A1032     204.478 204.427 257.090  1.00 39.56           S  
ATOM   4117  N   VAL A1033     204.786 209.308 257.516  1.00 38.70           N  
ATOM   4118  CA  VAL A1033     205.105 210.711 257.759  1.00 35.42           C  
ATOM   4119  C   VAL A1033     204.064 211.344 258.672  1.00 46.04           C  
ATOM   4120  O   VAL A1033     204.448 212.061 259.592  1.00 58.53           O  
ATOM   4121  CB  VAL A1033     205.264 211.505 256.454  1.00 37.71           C  
ATOM   4122  CG1 VAL A1033     205.662 212.956 256.711  1.00 43.09           C  
ATOM   4123  CG2 VAL A1033     206.323 210.843 255.568  1.00 41.61           C  
ATOM   4124  N   LEU A1034     202.763 211.071 258.498  1.00 43.05           N  
ATOM   4125  CA  LEU A1034     201.722 211.603 259.398  1.00 36.83           C  
ATOM   4126  C   LEU A1034     201.457 210.687 260.600  1.00 37.07           C  
ATOM   4127  O   LEU A1034     200.860 211.128 261.578  1.00 40.80           O  
ATOM   4128  CB  LEU A1034     200.414 211.899 258.640  1.00 41.66           C  
ATOM   4129  CG  LEU A1034     200.572 212.749 257.367  1.00 48.79           C  
ATOM   4130  CD1 LEU A1034     199.231 212.838 256.648  1.00 43.92           C  
ATOM   4131  CD2 LEU A1034     201.040 214.168 257.686  1.00 51.95           C  
ATOM   4132  N   GLY A1035     201.907 209.436 260.537  1.00 33.19           N  
ATOM   4133  CA  GLY A1035     201.649 208.382 261.514  1.00 33.63           C  
ATOM   4134  C   GLY A1035     202.889 207.611 261.944  1.00 35.51           C  
ATOM   4135  O   GLY A1035     204.010 208.096 261.854  1.00 39.39           O  
ATOM   4136  N   GLN A1036     202.689 206.390 262.420  1.00 30.14           N  
ATOM   4137  CA  GLN A1036     203.740 205.409 262.652  1.00 33.78           C  
ATOM   4138  C   GLN A1036     203.144 204.031 262.410  1.00 33.73           C  
ATOM   4139  O   GLN A1036     202.217 203.628 263.117  1.00 34.90           O  
ATOM   4140  CB  GLN A1036     204.282 205.537 264.072  1.00 35.13           C  
ATOM   4141  CG  GLN A1036     205.262 204.423 264.460  1.00 39.71           C  
ATOM   4142  CD  GLN A1036     205.631 204.481 265.929  1.00 37.27           C  
ATOM   4143  OE1 GLN A1036     204.886 204.939 266.778  1.00 50.49           O  
ATOM   4144  NE2 GLN A1036     206.782 203.989 266.297  1.00 31.31           N  
ATOM   4145  N   SER A1037     203.643 203.326 261.403  1.00 33.38           N  
ATOM   4146  CA  SER A1037     203.055 202.063 260.984  1.00 34.75           C  
ATOM   4147  C   SER A1037     203.422 200.910 261.916  1.00 40.04           C  
ATOM   4148  O   SER A1037     204.534 200.839 262.434  1.00 42.29           O  
ATOM   4149  CB  SER A1037     203.421 201.733 259.546  1.00 38.59           C  
ATOM   4150  OG  SER A1037     202.568 200.692 259.131  1.00 36.27           O  
ATOM   4151  N   LYS A1038     202.484 199.981 262.118  1.00 41.78           N  
ATOM   4152  CA  LYS A1038     202.673 198.758 262.923  1.00 41.33           C  
ATOM   4153  C   LYS A1038     202.999 197.528 262.059  1.00 50.01           C  
ATOM   4154  O   LYS A1038     203.131 196.425 262.585  1.00 51.00           O  
ATOM   4155  CB  LYS A1038     201.447 198.583 263.838  1.00 40.48           C  
ATOM   4156  CG  LYS A1038     201.389 199.723 264.881  1.00 45.12           C  
ATOM   4157  CD  LYS A1038     199.978 200.005 265.403  1.00 47.82           C  
ATOM   4158  CE  LYS A1038     199.879 201.382 266.089  1.00 43.71           C  
ATOM   4159  NZ  LYS A1038     199.984 202.526 265.138  1.00 50.95           N  
ATOM   4160  N   ARG A1039     203.167 197.746 260.747  1.00 42.82           N  
ATOM   4161  CA  ARG A1039     203.481 196.712 259.764  1.00 36.34           C  
ATOM   4162  C   ARG A1039     204.991 196.485 259.698  1.00 35.02           C  
ATOM   4163  O   ARG A1039     205.769 197.411 259.910  1.00 34.54           O  
ATOM   4164  CB  ARG A1039     202.949 197.151 258.403  1.00 39.70           C  
ATOM   4165  CG  ARG A1039     201.432 197.226 258.342  1.00 42.34           C  
ATOM   4166  CD  ARG A1039     200.941 198.222 257.303  1.00 44.37           C  
ATOM   4167  NE  ARG A1039     201.345 197.865 255.949  1.00 49.29           N  
ATOM   4168  CZ  ARG A1039     200.745 198.325 254.857  1.00 50.50           C  
ATOM   4169  NH1 ARG A1039     199.721 199.159 254.960  1.00 51.99           N  
ATOM   4170  NH2 ARG A1039     201.169 197.950 253.661  1.00 48.81           N  
ATOM   4171  N   VAL A1040     205.406 195.257 259.398  1.00 32.92           N  
ATOM   4172  CA  VAL A1040     206.822 194.899 259.389  1.00 30.05           C  
ATOM   4173  C   VAL A1040     207.376 194.944 257.963  1.00 47.64           C  
ATOM   4174  O   VAL A1040     206.860 194.219 257.108  1.00 56.80           O  
ATOM   4175  CB  VAL A1040     207.031 193.480 259.942  1.00 30.59           C  
ATOM   4176  CG1 VAL A1040     208.507 193.116 259.925  1.00 34.19           C  
ATOM   4177  CG2 VAL A1040     206.469 193.376 261.351  1.00 46.45           C  
ATOM   4178  N   ASP A1041     208.354 195.832 257.704  1.00 45.49           N  
ATOM   4179  CA  ASP A1041     209.058 196.114 256.415  1.00 39.70           C  
ATOM   4180  C   ASP A1041     208.345 197.115 255.479  1.00 46.98           C  
ATOM   4181  O   ASP A1041     208.903 197.493 254.450  1.00 58.08           O  
ATOM   4182  CB  ASP A1041     209.622 194.894 255.648  1.00 39.61           C  
ATOM   4183  CG  ASP A1041     210.278 193.874 256.563  1.00 52.19           C  
ATOM   4184  OD1 ASP A1041     210.491 192.725 256.122  1.00 54.50           O  
ATOM   4185  OD2 ASP A1041     210.579 194.224 257.724  1.00 59.07           O1-
ATOM   4186  N   PHE A1042     207.130 197.545 255.825  1.00 46.66           N  
ATOM   4187  CA  PHE A1042     206.487 198.641 255.117  1.00 36.72           C  
ATOM   4188  C   PHE A1042     207.186 199.829 255.818  1.00 40.88           C  
ATOM   4189  O   PHE A1042     207.374 199.808 257.064  1.00 50.23           O  
ATOM   4190  CB  PHE A1042     204.985 198.674 255.344  1.00 34.88           C  
ATOM   4191  CG  PHE A1042     204.285 199.779 254.603  1.00 39.75           C  
ATOM   4192  CD1 PHE A1042     203.932 199.626 253.273  1.00 57.49           C  
ATOM   4193  CD2 PHE A1042     203.981 200.971 255.239  1.00 34.98           C  
ATOM   4194  CE1 PHE A1042     203.289 200.642 252.592  1.00 46.31           C  
ATOM   4195  CE2 PHE A1042     203.338 201.991 254.564  1.00 33.97           C  
ATOM   4196  CZ  PHE A1042     202.991 201.826 253.237  1.00 37.87           C  
ATOM   4197  N   CYS A1043     207.553 200.880 255.093  1.00 39.80           N  
ATOM   4198  CA  CYS A1043     208.280 202.028 255.686  1.00 33.13           C  
ATOM   4199  C   CYS A1043     209.672 201.588 256.300  1.00 36.06           C  
ATOM   4200  O   CYS A1043     209.939 201.825 257.478  1.00 39.83           O  
ATOM   4201  CB  CYS A1043     207.383 202.951 256.636  1.00 27.93           C  
ATOM   4202  SG  CYS A1043     205.995 203.794 255.795  1.00 33.24           S  
ATOM   4203  N   GLY A1044     210.529 200.954 255.469  1.00 40.43           N  
ATOM   4204  CA  GLY A1044     211.901 200.620 255.809  1.00 45.90           C  
ATOM   4205  C   GLY A1044     212.019 199.243 256.413  1.00 49.94           C  
ATOM   4206  O   GLY A1044     211.072 198.742 257.003  1.00 52.93           O  
ATOM   4207  N   LYS A1045     213.174 198.593 256.265  1.00 53.58           N  
ATOM   4208  CA  LYS A1045     213.379 197.257 256.840  1.00 51.93           C  
ATOM   4209  C   LYS A1045     213.150 197.289 258.361  1.00 50.17           C  
ATOM   4210  O   LYS A1045     213.558 198.243 259.023  1.00 56.36           O  
ATOM   4211  CB  LYS A1045     214.773 196.758 256.448  1.00 63.07           C  
ATOM   4212  CG  LYS A1045     214.977 195.272 256.728  1.00 65.21           C  
ATOM   4213  CD  LYS A1045     216.407 194.850 256.400  1.00 66.04           C  
ATOM   4214  CE  LYS A1045     216.553 193.346 256.637  1.00 68.87           C  
ATOM   4215  NZ  LYS A1045     217.911 192.854 256.334  1.00 51.43           N  
ATOM   4216  N   GLY A1046     212.531 196.251 258.915  1.00 46.06           N  
ATOM   4217  CA  GLY A1046     212.246 196.123 260.343  1.00 43.46           C  
ATOM   4218  C   GLY A1046     210.931 196.775 260.765  1.00 41.61           C  
ATOM   4219  O   GLY A1046     209.912 196.601 260.095  1.00 45.56           O  
ATOM   4220  N   TYR A1047     210.962 197.467 261.905  1.00 36.77           N  
ATOM   4221  CA  TYR A1047     209.818 198.074 262.590  1.00 32.42           C  
ATOM   4222  C   TYR A1047     209.959 199.592 262.642  1.00 34.83           C  
ATOM   4223  O   TYR A1047     211.043 200.120 262.855  1.00 43.87           O  
ATOM   4224  CB  TYR A1047     209.690 197.491 263.997  1.00 34.25           C  
ATOM   4225  CG  TYR A1047     209.528 195.993 264.024  1.00 33.47           C  
ATOM   4226  CD1 TYR A1047     210.661 195.159 264.070  1.00 29.73           C  
ATOM   4227  CD2 TYR A1047     208.241 195.439 263.930  1.00 34.38           C  
ATOM   4228  CE1 TYR A1047     210.510 193.769 263.953  1.00 35.69           C  
ATOM   4229  CE2 TYR A1047     208.090 194.050 263.809  1.00 41.85           C  
ATOM   4230  CZ  TYR A1047     209.223 193.215 263.792  1.00 44.22           C  
ATOM   4231  OH  TYR A1047     209.076 191.876 263.642  1.00 52.08           O  
ATOM   4232  N   HIS A1048     208.868 200.312 262.426  1.00 30.46           N  
ATOM   4233  CA  HIS A1048     208.904 201.747 262.157  1.00 34.30           C  
ATOM   4234  C   HIS A1048     208.968 202.626 263.405  1.00 41.58           C  
ATOM   4235  O   HIS A1048     208.217 202.445 264.359  1.00 49.02           O  
ATOM   4236  CB  HIS A1048     207.690 202.083 261.296  1.00 38.52           C  
ATOM   4237  CG  HIS A1048     207.621 203.506 260.839  1.00 37.55           C  
ATOM   4238  ND1 HIS A1048     206.595 204.390 261.145  1.00 36.88           N  
ATOM   4239  CD2 HIS A1048     208.488 204.116 259.994  1.00 37.08           C  
ATOM   4240  CE1 HIS A1048     206.885 205.532 260.524  1.00 39.67           C  
ATOM   4241  NE2 HIS A1048     207.995 205.382 259.806  1.00 37.92           N  
ATOM   4242  N   LEU A1049     209.826 203.637 263.375  1.00 42.90           N  
ATOM   4243  CA  LEU A1049     209.835 204.714 264.359  1.00 42.67           C  
ATOM   4244  C   LEU A1049     209.271 205.995 263.765  1.00 45.58           C  
ATOM   4245  O   LEU A1049     208.334 206.564 264.312  1.00 45.00           O  
ATOM   4246  CB  LEU A1049     211.249 204.926 264.935  1.00 45.05           C  
ATOM   4247  CG  LEU A1049     211.786 203.732 265.745  1.00 38.09           C  
ATOM   4248  CD1 LEU A1049     213.288 203.870 265.922  1.00 34.09           C  
ATOM   4249  CD2 LEU A1049     211.125 203.661 267.116  1.00 37.08           C  
ATOM   4250  N   MET A1050     209.866 206.483 262.687  1.00 43.77           N  
ATOM   4251  CA  MET A1050     209.647 207.850 262.220  1.00 46.99           C  
ATOM   4252  C   MET A1050     210.071 208.002 260.762  1.00 52.92           C  
ATOM   4253  O   MET A1050     210.868 207.203 260.279  1.00 54.89           O  
ATOM   4254  CB  MET A1050     210.481 208.758 263.122  1.00 55.72           C  
ATOM   4255  CG  MET A1050     210.071 210.221 263.108  1.00 52.00           C  
ATOM   4256  SD  MET A1050     210.939 211.138 264.386  1.00 58.48           S  
ATOM   4257  CE  MET A1050     210.089 210.564 265.866  1.00 61.03           C  
ATOM   4258  N   SER A1051     209.596 209.008 260.025  1.00 54.63           N  
ATOM   4259  CA  SER A1051     210.045 209.229 258.638  1.00 45.79           C  
ATOM   4260  C   SER A1051     210.045 210.675 258.173  1.00 46.10           C  
ATOM   4261  O   SER A1051     209.314 211.511 258.695  1.00 50.42           O  
ATOM   4262  CB  SER A1051     209.227 208.428 257.630  1.00 43.85           C  
ATOM   4263  OG  SER A1051     209.302 207.072 257.959  1.00 50.02           O  
ATOM   4264  N   PHE A1052     210.848 210.924 257.141  1.00 43.75           N  
ATOM   4265  CA  PHE A1052     211.098 212.230 256.552  1.00 48.89           C  
ATOM   4266  C   PHE A1052     211.111 212.087 255.014  1.00 52.64           C  
ATOM   4267  O   PHE A1052     211.997 211.433 254.458  1.00 52.61           O  
ATOM   4268  CB  PHE A1052     212.424 212.787 257.097  1.00 55.20           C  
ATOM   4269  CG  PHE A1052     212.641 212.559 258.583  1.00 55.18           C  
ATOM   4270  CD1 PHE A1052     211.930 213.336 259.511  1.00 53.83           C  
ATOM   4271  CD2 PHE A1052     213.487 211.526 259.032  1.00 59.92           C  
ATOM   4272  CE1 PHE A1052     212.065 213.083 260.881  1.00 48.13           C  
ATOM   4273  CE2 PHE A1052     213.622 211.281 260.408  1.00 51.30           C  
ATOM   4274  CZ  PHE A1052     212.908 212.059 261.330  1.00 50.17           C  
ATOM   4275  N   PRO A1053     210.105 212.606 254.298  1.00 48.42           N  
ATOM   4276  CA  PRO A1053     210.057 212.547 252.851  1.00 47.33           C  
ATOM   4277  C   PRO A1053     210.934 213.647 252.246  1.00 56.03           C  
ATOM   4278  O   PRO A1053     211.025 214.758 252.765  1.00 62.29           O  
ATOM   4279  CB  PRO A1053     208.582 212.732 252.496  1.00 54.18           C  
ATOM   4280  CG  PRO A1053     208.123 213.708 253.567  1.00 51.83           C  
ATOM   4281  CD  PRO A1053     208.937 213.311 254.796  1.00 55.03           C  
ATOM   4282  N   GLN A1054     211.527 213.373 251.103  1.00 55.21           N  
ATOM   4283  CA  GLN A1054     212.210 214.349 250.275  1.00 56.12           C  
ATOM   4284  C   GLN A1054     211.835 214.109 248.818  1.00 61.67           C  
ATOM   4285  O   GLN A1054     211.625 212.980 248.382  1.00 64.32           O  
ATOM   4286  CB  GLN A1054     213.721 214.308 250.540  1.00 57.72           C  
ATOM   4287  CG  GLN A1054     214.390 213.003 250.096  1.00 59.39           C  
ATOM   4288  CD  GLN A1054     215.756 212.809 250.732  1.00 55.81           C  
ATOM   4289  OE1 GLN A1054     215.933 212.851 251.934  1.00 53.59           O  
ATOM   4290  NE2 GLN A1054     216.782 212.551 249.966  1.00 57.02           N  
ATOM   4291  N   SER A1055     211.698 215.181 248.055  1.00 69.70           N  
ATOM   4292  CA  SER A1055     211.385 215.087 246.635  1.00 64.60           C  
ATOM   4293  C   SER A1055     212.595 214.647 245.809  1.00 64.72           C  
ATOM   4294  O   SER A1055     213.751 214.752 246.217  1.00 60.66           O  
ATOM   4295  CB  SER A1055     210.826 216.426 246.144  1.00 64.14           C  
ATOM   4296  OG  SER A1055     211.732 217.482 246.380  1.00 78.94           O  
ATOM   4297  N   ALA A1056     212.292 214.175 244.610  1.00 61.31           N  
ATOM   4298  CA  ALA A1056     213.180 213.933 243.482  1.00 66.41           C  
ATOM   4299  C   ALA A1056     212.433 214.404 242.208  1.00 70.11           C  
ATOM   4300  O   ALA A1056     211.232 214.682 242.297  1.00 74.83           O  
ATOM   4301  CB  ALA A1056     213.551 212.443 243.488  1.00 62.07           C  
ATOM   4302  N   PRO A1057     213.073 214.541 241.034  1.00 65.33           N  
ATOM   4303  CA  PRO A1057     212.475 215.214 239.877  1.00 62.51           C  
ATOM   4304  C   PRO A1057     211.104 214.676 239.442  1.00 66.12           C  
ATOM   4305  O   PRO A1057     210.218 215.458 239.103  1.00 69.09           O  
ATOM   4306  CB  PRO A1057     213.502 215.079 238.754  1.00 65.85           C  
ATOM   4307  CG  PRO A1057     214.830 214.917 239.487  1.00 57.76           C  
ATOM   4308  CD  PRO A1057     214.452 214.176 240.757  1.00 65.29           C  
ATOM   4309  N   HIS A1058     210.905 213.356 239.513  1.00 63.20           N  
ATOM   4310  CA  HIS A1058     209.638 212.659 239.220  1.00 61.98           C  
ATOM   4311  C   HIS A1058     209.267 211.648 240.313  1.00 60.27           C  
ATOM   4312  O   HIS A1058     208.627 210.626 240.074  1.00 58.03           O  
ATOM   4313  CB  HIS A1058     209.699 212.021 237.819  1.00 63.66           C  
ATOM   4314  CG  HIS A1058     209.476 213.009 236.709  1.00 61.82           C  
ATOM   4315  ND1 HIS A1058     208.224 213.441 236.264  1.00 57.69           N  
ATOM   4316  CD2 HIS A1058     210.443 213.666 236.016  1.00 59.83           C  
ATOM   4317  CE1 HIS A1058     208.469 214.356 235.313  1.00 56.07           C  
ATOM   4318  NE2 HIS A1058     209.792 214.506 235.144  1.00 57.08           N  
ATOM   4319  N   GLY A1059     209.711 211.882 241.541  1.00 58.85           N  
ATOM   4320  CA  GLY A1059     209.620 210.888 242.602  1.00 55.75           C  
ATOM   4321  C   GLY A1059     209.484 211.476 243.994  1.00 56.88           C  
ATOM   4322  O   GLY A1059     209.631 212.678 244.233  1.00 62.21           O  
ATOM   4323  N   VAL A1060     209.256 210.576 244.935  1.00 53.25           N  
ATOM   4324  CA  VAL A1060     209.415 210.811 246.360  1.00 51.04           C  
ATOM   4325  C   VAL A1060     210.426 209.811 246.874  1.00 50.33           C  
ATOM   4326  O   VAL A1060     210.469 208.667 246.438  1.00 54.01           O  
ATOM   4327  CB  VAL A1060     208.067 210.745 247.097  1.00 49.69           C  
ATOM   4328  CG1 VAL A1060     207.493 209.336 247.191  1.00 52.17           C  
ATOM   4329  CG2 VAL A1060     208.164 211.322 248.513  1.00 57.78           C  
ATOM   4330  N   VAL A1061     211.260 210.248 247.795  1.00 48.57           N  
ATOM   4331  CA  VAL A1061     212.216 209.415 248.497  1.00 50.57           C  
ATOM   4332  C   VAL A1061     211.915 209.544 249.972  1.00 55.24           C  
ATOM   4333  O   VAL A1061     211.732 210.647 250.477  1.00 62.04           O  
ATOM   4334  CB  VAL A1061     213.662 209.803 248.168  1.00 47.57           C  
ATOM   4335  CG1 VAL A1061     214.657 208.922 248.919  1.00 53.47           C  
ATOM   4336  CG2 VAL A1061     213.931 209.684 246.671  1.00 51.76           C  
ATOM   4337  N   PHE A1062     211.844 208.430 250.682  1.00 44.93           N  
ATOM   4338  CA  PHE A1062     211.612 208.422 252.116  1.00 42.75           C  
ATOM   4339  C   PHE A1062     212.899 208.072 252.842  1.00 48.21           C  
ATOM   4340  O   PHE A1062     213.544 207.079 252.515  1.00 57.25           O  
ATOM   4341  CB  PHE A1062     210.507 207.442 252.479  1.00 45.48           C  
ATOM   4342  CG  PHE A1062     209.193 207.724 251.789  1.00 43.20           C  
ATOM   4343  CD1 PHE A1062     208.365 208.766 252.238  1.00 38.57           C  
ATOM   4344  CD2 PHE A1062     208.820 206.974 250.664  1.00 46.09           C  
ATOM   4345  CE1 PHE A1062     207.159 209.043 251.574  1.00 38.23           C  
ATOM   4346  CE2 PHE A1062     207.607 207.243 250.013  1.00 39.83           C  
ATOM   4347  CZ  PHE A1062     206.776 208.274 250.471  1.00 35.18           C  
ATOM   4348  N   LEU A1063     213.233 208.873 253.849  1.00 45.38           N  
ATOM   4349  CA  LEU A1063     214.096 208.477 254.944  1.00 54.40           C  
ATOM   4350  C   LEU A1063     213.216 207.857 256.024  1.00 54.37           C  
ATOM   4351  O   LEU A1063     212.483 208.575 256.693  1.00 51.89           O  
ATOM   4352  CB  LEU A1063     214.817 209.711 255.493  1.00 59.58           C  
ATOM   4353  CG  LEU A1063     215.777 210.372 254.500  1.00 60.83           C  
ATOM   4354  CD1 LEU A1063     216.213 211.724 255.060  1.00 67.97           C  
ATOM   4355  CD2 LEU A1063     217.021 209.510 254.287  1.00 68.50           C  
ATOM   4356  N   HIS A1064     213.260 206.544 256.200  1.00 48.17           N  
ATOM   4357  CA  HIS A1064     212.567 205.871 257.295  1.00 45.16           C  
ATOM   4358  C   HIS A1064     213.560 205.560 258.380  1.00 59.11           C  
ATOM   4359  O   HIS A1064     214.585 204.957 258.096  1.00 64.47           O  
ATOM   4360  CB  HIS A1064     211.934 204.545 256.884  1.00 42.04           C  
ATOM   4361  CG  HIS A1064     211.177 204.577 255.603  1.00 37.46           C  
ATOM   4362  ND1 HIS A1064     211.540 203.871 254.473  1.00 44.09           N  
ATOM   4363  CD2 HIS A1064     209.988 205.184 255.384  1.00 34.40           C  
ATOM   4364  CE1 HIS A1064     210.553 204.070 253.602  1.00 41.52           C  
ATOM   4365  NE2 HIS A1064     209.618 204.865 254.112  1.00 37.01           N  
ATOM   4366  N   VAL A1065     213.240 205.900 259.621  1.00 55.77           N  
ATOM   4367  CA  VAL A1065     213.999 205.460 260.778  1.00 48.09           C  
ATOM   4368  C   VAL A1065     213.272 204.301 261.414  1.00 50.45           C  
ATOM   4369  O   VAL A1065     212.094 204.412 261.748  1.00 56.68           O  
ATOM   4370  CB  VAL A1065     214.207 206.589 261.784  1.00 44.80           C  
ATOM   4371  CG1 VAL A1065     215.184 206.101 262.847  1.00 48.52           C  
ATOM   4372  CG2 VAL A1065     214.766 207.844 261.116  1.00 47.76           C  
ATOM   4373  N   THR A1066     213.971 203.184 261.564  1.00 50.19           N  
ATOM   4374  CA  THR A1066     213.400 201.882 261.906  1.00 49.42           C  
ATOM   4375  C   THR A1066     214.370 201.080 262.771  1.00 53.93           C  
ATOM   4376  O   THR A1066     215.572 201.318 262.754  1.00 65.94           O  
ATOM   4377  CB  THR A1066     213.049 201.072 260.640  1.00 50.55           C  
ATOM   4378  OG1 THR A1066     214.176 200.715 259.893  1.00 57.85           O  
ATOM   4379  CG2 THR A1066     212.158 201.793 259.650  1.00 48.62           C  
ATOM   4380  N   TYR A1067     213.887 200.100 263.522  1.00 42.79           N  
ATOM   4381  CA  TYR A1067     214.754 199.127 264.182  1.00 37.59           C  
ATOM   4382  C   TYR A1067     214.577 197.737 263.573  1.00 46.86           C  
ATOM   4383  O   TYR A1067     213.462 197.280 263.328  1.00 49.58           O  
ATOM   4384  CB  TYR A1067     214.587 199.179 265.704  1.00 44.71           C  
ATOM   4385  CG  TYR A1067     213.196 198.967 266.261  1.00 43.17           C  
ATOM   4386  CD1 TYR A1067     212.735 197.675 266.523  1.00 42.02           C  
ATOM   4387  CD2 TYR A1067     212.368 200.066 266.530  1.00 37.87           C  
ATOM   4388  CE1 TYR A1067     211.439 197.470 267.009  1.00 34.24           C  
ATOM   4389  CE2 TYR A1067     211.062 199.871 267.005  1.00 28.32           C  
ATOM   4390  CZ  TYR A1067     210.586 198.564 267.224  1.00 28.49           C  
ATOM   4391  OH  TYR A1067     209.292 198.348 267.568  1.00 25.91           O  
ATOM   4392  N   VAL A1068     215.688 197.061 263.308  1.00 44.09           N  
ATOM   4393  CA  VAL A1068     215.736 195.675 262.829  1.00 47.97           C  
ATOM   4394  C   VAL A1068     216.241 194.775 263.953  1.00 52.00           C  
ATOM   4395  O   VAL A1068     216.967 195.255 264.820  1.00 58.14           O  
ATOM   4396  CB  VAL A1068     216.644 195.519 261.590  1.00 49.20           C  
ATOM   4397  CG1 VAL A1068     216.030 196.181 260.364  1.00 47.68           C  
ATOM   4398  CG2 VAL A1068     218.072 196.031 261.784  1.00 46.91           C  
ATOM   4399  N   PRO A1069     215.919 193.463 263.799  1.00 46.54           N  
ATOM   4400  CA  PRO A1069     216.443 192.471 264.718  1.00 49.93           C  
ATOM   4401  C   PRO A1069     217.926 192.223 264.502  1.00 51.44           C  
ATOM   4402  O   PRO A1069     218.289 191.562 263.532  1.00 53.64           O  
ATOM   4403  CB  PRO A1069     215.681 191.183 264.390  1.00 52.96           C  
ATOM   4404  CG  PRO A1069     214.863 191.448 263.202  1.00 54.12           C  
ATOM   4405  CD  PRO A1069     214.803 192.917 262.985  1.00 47.93           C  
ATOM   4406  N   ALA A1070     218.777 192.746 265.386  1.00 53.99           N  
ATOM   4407  CA  ALA A1070     220.211 192.497 265.320  1.00 57.18           C  
ATOM   4408  C   ALA A1070     220.425 191.013 265.569  1.00 62.85           C  
ATOM   4409  O   ALA A1070     221.219 190.362 264.891  1.00 65.50           O  
ATOM   4410  CB  ALA A1070     220.941 193.324 266.364  1.00 62.54           C  
ATOM   4411  N   GLN A1071     219.699 190.486 266.556  1.00 59.57           N  
ATOM   4412  CA  GLN A1071     219.737 189.082 266.878  1.00 59.04           C  
ATOM   4413  C   GLN A1071     218.286 188.577 267.036  1.00 58.09           C  
ATOM   4414  O   GLN A1071     217.391 189.343 267.385  1.00 53.66           O  
ATOM   4415  CB  GLN A1071     220.522 188.853 268.171  1.00 60.18           C  
ATOM   4416  CG  GLN A1071     221.043 187.436 268.340  1.00 64.24           C  
ATOM   4417  CD  GLN A1071     221.776 187.241 269.652  1.00 71.40           C  
ATOM   4418  OE1 GLN A1071     221.339 187.724 270.696  1.00 63.80           O  
ATOM   4419  NE2 GLN A1071     222.894 186.526 269.607  1.00 75.65           N  
ATOM   4420  N   GLU A1072     218.069 187.292 266.779  1.00 62.74           N  
ATOM   4421  CA  GLU A1072     216.774 186.642 266.920  1.00 57.73           C  
ATOM   4422  C   GLU A1072     216.981 185.149 267.174  1.00 60.17           C  
ATOM   4423  O   GLU A1072     217.968 184.559 266.728  1.00 66.94           O  
ATOM   4424  CB  GLU A1072     215.881 186.934 265.701  1.00 58.88           C  
ATOM   4425  CG  GLU A1072     216.505 186.549 264.349  1.00 62.87           C  
ATOM   4426  CD  GLU A1072     215.708 187.058 263.143  1.00 69.88           C  
ATOM   4427  OE1 GLU A1072     214.500 187.349 263.254  1.00 72.65           O  
ATOM   4428  OE2 GLU A1072     216.297 187.156 262.044  1.00 70.45           O1-
ATOM   4429  N   LYS A1073     216.042 184.533 267.885  1.00 55.86           N  
ATOM   4430  CA  LYS A1073     216.119 183.125 268.276  1.00 57.96           C  
ATOM   4431  C   LYS A1073     214.888 182.395 267.769  1.00 61.17           C  
ATOM   4432  O   LYS A1073     213.790 182.941 267.792  1.00 61.28           O  
ATOM   4433  CB  LYS A1073     216.324 183.028 269.795  1.00 58.97           C  
ATOM   4434  CG  LYS A1073     216.402 181.576 270.294  1.00 63.62           C  
ATOM   4435  CD  LYS A1073     216.790 181.485 271.777  1.00 60.23           C  
ATOM   4436  CE  LYS A1073     216.757 180.023 272.232  1.00 60.35           C  
ATOM   4437  NZ  LYS A1073     217.251 179.863 273.611  1.00 66.50           N  
ATOM   4438  N   ASN A1074     215.066 181.174 267.280  1.00 59.53           N  
ATOM   4439  CA  ASN A1074     213.961 180.299 266.919  1.00 60.92           C  
ATOM   4440  C   ASN A1074     213.399 179.650 268.184  1.00 64.33           C  
ATOM   4441  O   ASN A1074     214.053 178.804 268.797  1.00 65.62           O  
ATOM   4442  CB  ASN A1074     214.323 179.228 265.872  1.00 66.83           C  
ATOM   4443  CG  ASN A1074     215.657 179.383 265.168  1.00 79.39           C  
ATOM   4444  OD1 ASN A1074     216.699 179.322 265.812  1.00 80.17           O  
ATOM   4445  ND2 ASN A1074     215.637 179.410 263.845  1.00 85.42           N  
ATOM   4446  N   PHE A1075     212.182 180.017 268.556  1.00114.01           N  
ATOM   4447  CA  PHE A1075     211.407 179.258 269.532  1.00 56.22           C  
ATOM   4448  C   PHE A1075     210.461 178.331 268.788  1.00 50.13           C  
ATOM   4449  O   PHE A1075     209.863 178.726 267.793  1.00 58.71           O  
ATOM   4450  CB  PHE A1075     210.635 180.204 270.437  1.00 53.11           C  
ATOM   4451  CG  PHE A1075     211.531 181.194 271.133  1.00 58.45           C  
ATOM   4452  CD1 PHE A1075     212.089 180.886 272.382  1.00 60.27           C  
ATOM   4453  CD2 PHE A1075     211.840 182.408 270.504  1.00 55.24           C  
ATOM   4454  CE1 PHE A1075     212.954 181.803 273.006  1.00 63.34           C  
ATOM   4455  CE2 PHE A1075     212.703 183.321 271.126  1.00 62.52           C  
ATOM   4456  CZ  PHE A1075     213.258 183.020 272.376  1.00 57.91           C  
ATOM   4457  N   THR A1076     210.300 177.095 269.239  1.00 45.54           N  
ATOM   4458  CA  THR A1076     209.133 176.339 268.801  1.00 45.99           C  
ATOM   4459  C   THR A1076     207.882 177.044 269.305  1.00 45.78           C  
ATOM   4460  O   THR A1076     207.899 177.759 270.307  1.00 51.25           O  
ATOM   4461  CB  THR A1076     209.176 174.874 269.231  1.00 48.66           C  
ATOM   4462  OG1 THR A1076     209.293 174.744 270.623  1.00 53.48           O  
ATOM   4463  CG2 THR A1076     210.347 174.140 268.585  1.00 52.10           C  
ATOM   4464  N   THR A1077     206.806 176.905 268.554  1.00 48.08           N  
ATOM   4465  CA  THR A1077     205.535 177.588 268.769  1.00 42.12           C  
ATOM   4466  C   THR A1077     204.387 176.725 268.262  1.00 43.90           C  
ATOM   4467  O   THR A1077     204.582 175.749 267.538  1.00 51.52           O  
ATOM   4468  CB  THR A1077     205.482 178.950 268.045  1.00 43.77           C  
ATOM   4469  OG1 THR A1077     205.652 178.759 266.667  1.00 54.47           O  
ATOM   4470  CG2 THR A1077     206.514 179.982 268.476  1.00 43.03           C  
ATOM   4471  N   ALA A1078     203.176 177.118 268.626  1.00 42.32           N  
ATOM   4472  CA  ALA A1078     201.970 176.800 267.887  1.00 47.53           C  
ATOM   4473  C   ALA A1078     201.110 178.076 267.809  1.00 50.34           C  
ATOM   4474  O   ALA A1078     201.180 178.915 268.711  1.00 49.95           O  
ATOM   4475  CB  ALA A1078     201.235 175.646 268.573  1.00 48.41           C  
ATOM   4476  N   PRO A1079     200.314 178.281 266.751  1.00 53.43           N  
ATOM   4477  CA  PRO A1079     199.382 179.402 266.674  1.00 59.87           C  
ATOM   4478  C   PRO A1079     198.244 179.288 267.693  1.00 51.33           C  
ATOM   4479  O   PRO A1079     197.836 180.280 268.282  1.00 48.19           O  
ATOM   4480  CB  PRO A1079     198.814 179.383 265.261  1.00 59.35           C  
ATOM   4481  CG  PRO A1079     199.569 178.303 264.510  1.00 53.52           C  
ATOM   4482  CD  PRO A1079     200.329 177.499 265.541  1.00 52.30           C  
ATOM   4483  N   ALA A1080     197.865 178.039 267.997  1.00 47.70           N  
ATOM   4484  CA  ALA A1080     196.820 177.703 268.985  1.00 49.47           C  
ATOM   4485  C   ALA A1080     196.978 176.281 269.590  1.00 54.79           C  
ATOM   4486  O   ALA A1080     197.637 175.426 269.000  1.00 57.78           O  
ATOM   4487  CB  ALA A1080     195.438 177.872 268.372  1.00 48.83           C  
ATOM   4488  N   ILE A1081     196.371 176.041 270.761  1.00 55.62           N  
ATOM   4489  CA  ILE A1081     196.420 174.757 271.444  1.00 52.53           C  
ATOM   4490  C   ILE A1081     195.003 174.380 271.844  1.00 56.11           C  
ATOM   4491  O   ILE A1081     194.203 175.228 272.250  1.00 57.68           O  
ATOM   4492  CB  ILE A1081     197.356 174.780 272.674  1.00 49.44           C  
ATOM   4493  CG1 ILE A1081     197.038 175.972 273.580  1.00 53.15           C  
ATOM   4494  CG2 ILE A1081     198.812 174.814 272.235  1.00 48.84           C  
ATOM   4495  CD1 ILE A1081     197.914 176.045 274.816  1.00 57.18           C  
ATOM   4496  N   CYS A1082     194.695 173.093 271.721  1.00 56.45           N  
ATOM   4497  CA  CYS A1082     193.351 172.571 271.954  1.00 63.04           C  
ATOM   4498  C   CYS A1082     193.405 171.658 273.177  1.00 67.60           C  
ATOM   4499  O   CYS A1082     193.763 170.480 273.073  1.00 68.35           O  
ATOM   4500  CB  CYS A1082     192.830 171.859 270.704  1.00 64.77           C  
ATOM   4501  SG  CYS A1082     191.603 170.548 270.941  1.00 69.62           S  
ATOM   4502  N   HIS A1083     193.051 172.211 274.335  1.00 72.40           N  
ATOM   4503  CA  HIS A1083     193.076 171.479 275.595  1.00 69.55           C  
ATOM   4504  C   HIS A1083     191.745 170.765 275.786  1.00 74.66           C  
ATOM   4505  O   HIS A1083     190.687 171.406 275.781  1.00 79.14           O  
ATOM   4506  CB  HIS A1083     193.347 172.422 276.766  1.00 65.79           C  
ATOM   4507  CG  HIS A1083     194.768 172.885 276.855  1.00 62.10           C  
ATOM   4508  ND1 HIS A1083     195.122 174.099 277.408  1.00 63.04           N  
ATOM   4509  CD2 HIS A1083     195.925 172.297 276.472  1.00 61.79           C  
ATOM   4510  CE1 HIS A1083     196.434 174.239 277.356  1.00 62.49           C  
ATOM   4511  NE2 HIS A1083     196.946 173.159 276.792  1.00 61.00           N  
ATOM   4512  N   ASP A1084     191.794 169.451 275.992  1.00 73.71           N  
ATOM   4513  CA  ASP A1084     190.599 168.610 276.193  1.00 76.16           C  
ATOM   4514  C   ASP A1084     189.357 168.939 275.339  1.00 78.36           C  
ATOM   4515  O   ASP A1084     188.224 168.878 275.815  1.00 80.59           O  
ATOM   4516  CB  ASP A1084     190.241 168.451 277.684  1.00 80.51           C  
ATOM   4517  CG  ASP A1084     189.617 169.697 278.284  1.00 83.11           C  
ATOM   4518  OD1 ASP A1084     188.372 169.768 278.345  1.00 80.08           O  
ATOM   4519  OD2 ASP A1084     190.371 170.605 278.694  1.00 79.32           O1-
ATOM   4520  N   GLY A1085     189.603 169.285 274.080  1.00 76.24           N  
ATOM   4521  CA  GLY A1085     188.562 169.581 273.078  1.00 76.62           C  
ATOM   4522  C   GLY A1085     188.157 171.060 272.933  1.00 64.49           C  
ATOM   4523  O   GLY A1085     187.244 171.370 272.172  1.00 63.88           O  
ATOM   4524  N   LYS A1086     188.831 171.981 273.627  1.00 62.43           N  
ATOM   4525  CA  LYS A1086     188.683 173.435 273.477  1.00 64.36           C  
ATOM   4526  C   LYS A1086     189.979 174.040 272.917  1.00 61.28           C  
ATOM   4527  O   LYS A1086     191.055 173.766 273.442  1.00 61.38           O  
ATOM   4528  CB  LYS A1086     188.291 174.038 274.836  1.00 66.46           C  
ATOM   4529  CG  LYS A1086     186.884 173.589 275.279  1.00 70.57           C  
ATOM   4530  CD  LYS A1086     186.455 174.093 276.668  1.00 67.07           C  
ATOM   4531  CE  LYS A1086     186.367 175.620 276.819  1.00 67.49           C  
ATOM   4532  NZ  LYS A1086     185.296 176.234 275.990  1.00 53.30           N  
ATOM   4533  N   ALA A1087     189.884 174.842 271.860  1.00 58.94           N  
ATOM   4534  CA  ALA A1087     191.032 175.537 271.284  1.00 50.30           C  
ATOM   4535  C   ALA A1087     191.293 176.851 272.023  1.00 47.39           C  
ATOM   4536  O   ALA A1087     190.380 177.642 272.218  1.00 55.00           O  
ATOM   4537  CB  ALA A1087     190.816 175.730 269.782  1.00 67.05           C  
ATOM   4538  N   HIS A1088     192.528 177.082 272.443  1.00 47.46           N  
ATOM   4539  CA  HIS A1088     193.002 178.297 273.103  1.00 46.15           C  
ATOM   4540  C   HIS A1088     194.027 178.981 272.212  1.00 45.77           C  
ATOM   4541  O   HIS A1088     194.923 178.316 271.700  1.00 50.81           O  
ATOM   4542  CB  HIS A1088     193.648 177.941 274.448  1.00 58.27           C  
ATOM   4543  CG  HIS A1088     192.733 177.241 275.416  1.00 61.52           C  
ATOM   4544  ND1 HIS A1088     191.984 177.854 276.419  1.00 58.13           N  
ATOM   4545  CD2 HIS A1088     192.440 175.913 275.391  1.00 63.23           C  
ATOM   4546  CE1 HIS A1088     191.243 176.877 276.961  1.00 60.06           C  
ATOM   4547  NE2 HIS A1088     191.497 175.706 276.363  1.00 61.56           N  
ATOM   4548  N   PHE A1089     193.927 180.296 272.020  1.00 43.25           N  
ATOM   4549  CA  PHE A1089     194.848 181.049 271.161  1.00 38.23           C  
ATOM   4550  C   PHE A1089     195.095 182.477 271.655  1.00 44.33           C  
ATOM   4551  O   PHE A1089     194.251 183.029 272.352  1.00 51.66           O  
ATOM   4552  CB  PHE A1089     194.387 181.023 269.703  1.00 35.36           C  
ATOM   4553  CG  PHE A1089     192.896 181.013 269.477  1.00 33.81           C  
ATOM   4554  CD1 PHE A1089     192.234 179.783 269.336  1.00 40.53           C  
ATOM   4555  CD2 PHE A1089     192.180 182.214 269.394  1.00 33.68           C  
ATOM   4556  CE1 PHE A1089     190.856 179.751 269.098  1.00 43.82           C  
ATOM   4557  CE2 PHE A1089     190.801 182.182 269.142  1.00 31.97           C  
ATOM   4558  CZ  PHE A1089     190.143 180.951 268.991  1.00 38.70           C  
ATOM   4559  N   PRO A1090     196.249 183.093 271.347  1.00 38.16           N  
ATOM   4560  CA  PRO A1090     196.613 184.412 271.844  1.00 39.92           C  
ATOM   4561  C   PRO A1090     195.667 185.564 271.512  1.00 41.99           C  
ATOM   4562  O   PRO A1090     194.953 185.566 270.513  1.00 43.02           O  
ATOM   4563  CB  PRO A1090     197.986 184.708 271.250  1.00 36.28           C  
ATOM   4564  CG  PRO A1090     198.612 183.331 271.099  1.00 42.71           C  
ATOM   4565  CD  PRO A1090     197.407 182.493 270.691  1.00 41.40           C  
ATOM   4566  N   ARG A1091     196.007 186.665 272.190  1.00 44.25           N  
ATOM   4567  CA  ARG A1091     195.444 187.970 271.989  1.00 49.09           C  
ATOM   4568  C   ARG A1091     196.727 188.819 271.757  1.00 52.58           C  
ATOM   4569  O   ARG A1091     197.507 188.981 272.698  1.00 55.09           O  
ATOM   4570  CB  ARG A1091     194.724 188.493 273.228  1.00 58.23           C  
ATOM   4571  CG  ARG A1091     193.481 187.724 273.623  1.00 59.03           C  
ATOM   4572  CD  ARG A1091     192.388 188.655 274.122  1.00 62.89           C  
ATOM   4573  NE  ARG A1091     191.477 187.991 275.048  1.00 61.16           N  
ATOM   4574  CZ  ARG A1091     190.307 188.493 275.431  1.00 56.54           C  
ATOM   4575  NH1 ARG A1091     189.540 187.822 276.280  1.00 53.49           N  
ATOM   4576  NH2 ARG A1091     189.903 189.666 274.963  1.00 58.63           N  
ATOM   4577  N   GLU A1092     196.964 189.307 270.532  1.00 44.54           N  
ATOM   4578  CA  GLU A1092     198.109 190.182 270.220  1.00 41.48           C  
ATOM   4579  C   GLU A1092     199.490 189.571 270.572  1.00 40.69           C  
ATOM   4580  O   GLU A1092     200.310 190.195 271.240  1.00 41.65           O  
ATOM   4581  CB  GLU A1092     197.900 191.577 270.853  1.00 46.53           C  
ATOM   4582  CG  GLU A1092     196.569 192.263 270.503  1.00 46.68           C  
ATOM   4583  CD  GLU A1092     196.289 193.448 271.437  1.00 65.98           C  
ATOM   4584  OE1 GLU A1092     195.116 193.654 271.822  1.00 72.20           O  
ATOM   4585  OE2 GLU A1092     197.232 194.174 271.823  1.00 78.15           O1-
ATOM   4586  N   GLY A1093     199.765 188.331 270.161  1.00 38.06           N  
ATOM   4587  CA  GLY A1093     201.040 187.645 270.413  1.00 39.44           C  
ATOM   4588  C   GLY A1093     201.125 186.269 269.754  1.00 41.29           C  
ATOM   4589  O   GLY A1093     200.259 185.925 268.954  1.00 39.48           O  
ATOM   4590  N   VAL A1094     202.117 185.456 270.135  1.00 39.86           N  
ATOM   4591  CA  VAL A1094     202.211 184.008 269.818  1.00 43.22           C  
ATOM   4592  C   VAL A1094     202.544 183.174 271.063  1.00 49.57           C  
ATOM   4593  O   VAL A1094     203.177 183.693 271.981  1.00 55.01           O  
ATOM   4594  CB  VAL A1094     203.192 183.691 268.670  1.00 43.02           C  
ATOM   4595  CG1 VAL A1094     202.899 184.561 267.449  1.00 51.25           C  
ATOM   4596  CG2 VAL A1094     204.671 183.835 269.029  1.00 40.15           C  
ATOM   4597  N   PHE A1095     202.167 181.891 271.101  1.00 47.34           N  
ATOM   4598  CA  PHE A1095     202.639 180.964 272.137  1.00 42.62           C  
ATOM   4599  C   PHE A1095     204.127 180.608 271.960  1.00 46.05           C  
ATOM   4600  O   PHE A1095     204.475 179.592 271.363  1.00 49.97           O  
ATOM   4601  CB  PHE A1095     201.791 179.683 272.152  1.00 37.11           C  
ATOM   4602  CG  PHE A1095     200.338 179.798 272.559  1.00 38.00           C  
ATOM   4603  CD1 PHE A1095     199.955 180.563 273.674  1.00 46.67           C  
ATOM   4604  CD2 PHE A1095     199.377 179.044 271.874  1.00 43.07           C  
ATOM   4605  CE1 PHE A1095     198.612 180.617 274.070  1.00 45.27           C  
ATOM   4606  CE2 PHE A1095     198.040 179.068 272.292  1.00 42.46           C  
ATOM   4607  CZ  PHE A1095     197.651 179.856 273.385  1.00 47.34           C  
ATOM   4608  N   VAL A1096     205.029 181.427 272.493  1.00 47.57           N  
ATOM   4609  CA  VAL A1096     206.451 181.072 272.595  1.00 52.20           C  
ATOM   4610  C   VAL A1096     206.617 179.874 273.515  1.00 55.28           C  
ATOM   4611  O   VAL A1096     206.046 179.832 274.607  1.00 62.14           O  
ATOM   4612  CB  VAL A1096     207.342 182.251 273.019  1.00 56.85           C  
ATOM   4613  CG1 VAL A1096     207.256 182.709 274.472  1.00 56.36           C  
ATOM   4614  CG2 VAL A1096     208.801 181.946 272.732  1.00 58.59           C  
ATOM   4615  N   SER A1097     207.391 178.888 273.070  1.00 54.84           N  
ATOM   4616  CA  SER A1097     207.495 177.625 273.778  1.00 57.35           C  
ATOM   4617  C   SER A1097     208.793 177.412 274.511  1.00 61.69           C  
ATOM   4618  O   SER A1097     209.860 177.209 273.930  1.00 58.18           O  
ATOM   4619  CB  SER A1097     207.240 176.433 272.859  1.00 62.59           C  
ATOM   4620  OG  SER A1097     206.998 175.258 273.617  1.00 59.46           O  
ATOM   4621  N   ASN A1098     208.640 177.453 275.825  1.00 67.89           N  
ATOM   4622  CA  ASN A1098     209.685 177.197 276.792  1.00 73.43           C  
ATOM   4623  C   ASN A1098     209.728 175.652 276.978  1.00 78.54           C  
ATOM   4624  O   ASN A1098     208.785 174.948 276.582  1.00 82.06           O  
ATOM   4625  CB  ASN A1098     209.319 177.966 278.062  1.00 72.31           C  
ATOM   4626  CG  ASN A1098     210.389 177.919 279.120  1.00 76.89           C  
ATOM   4627  OD1 ASN A1098     211.569 178.167 278.872  1.00 79.45           O  
ATOM   4628  ND2 ASN A1098     209.964 177.594 280.317  1.00 80.65           N  
ATOM   4629  N   GLY A1099     210.793 175.111 277.568  1.00 79.55           N  
ATOM   4630  CA  GLY A1099     210.924 173.669 277.683  1.00 84.37           C  
ATOM   4631  C   GLY A1099     209.734 173.015 278.382  1.00 84.73           C  
ATOM   4632  O   GLY A1099     209.467 171.836 278.161  1.00 83.76           O  
ATOM   4633  N   THR A1100     209.009 173.769 279.220  1.00 82.31           N  
ATOM   4634  CA  THR A1100     208.011 173.205 280.154  1.00 79.77           C  
ATOM   4635  C   THR A1100     206.678 173.966 280.181  1.00 77.89           C  
ATOM   4636  O   THR A1100     205.675 173.428 280.650  1.00 81.85           O  
ATOM   4637  CB  THR A1100     208.632 173.082 281.559  1.00 84.48           C  
ATOM   4638  OG1 THR A1100     209.874 172.419 281.481  1.00 93.35           O  
ATOM   4639  CG2 THR A1100     207.800 172.279 282.554  1.00 81.10           C  
ATOM   4640  N   HIS A1101     206.619 175.184 279.633  1.00 70.99           N  
ATOM   4641  CA  HIS A1101     205.450 176.071 279.699  1.00 70.22           C  
ATOM   4642  C   HIS A1101     205.193 176.850 278.403  1.00 65.64           C  
ATOM   4643  O   HIS A1101     206.094 177.098 277.604  1.00 71.22           O  
ATOM   4644  CB  HIS A1101     205.610 177.044 280.880  1.00 78.44           C  
ATOM   4645  CG  HIS A1101     205.714 176.348 282.208  1.00 80.17           C  
ATOM   4646  ND1 HIS A1101     204.656 175.732 282.879  1.00 80.23           N  
ATOM   4647  CD2 HIS A1101     206.862 176.153 282.910  1.00 79.20           C  
ATOM   4648  CE1 HIS A1101     205.193 175.177 283.973  1.00 85.46           C  
ATOM   4649  NE2 HIS A1101     206.513 175.410 284.011  1.00 84.43           N  
ATOM   4650  N   TRP A1102     203.945 177.290 278.234  1.00 55.98           N  
ATOM   4651  CA  TRP A1102     203.513 178.179 277.154  1.00 52.45           C  
ATOM   4652  C   TRP A1102     203.416 179.612 277.669  1.00 48.83           C  
ATOM   4653  O   TRP A1102     202.746 179.869 278.671  1.00 53.62           O  
ATOM   4654  CB  TRP A1102     202.135 177.751 276.638  1.00 49.07           C  
ATOM   4655  CG  TRP A1102     202.038 176.447 275.914  1.00 55.35           C  
ATOM   4656  CD1 TRP A1102     201.288 175.391 276.290  1.00 58.22           C  
ATOM   4657  CD2 TRP A1102     202.578 176.103 274.604  1.00 57.56           C  
ATOM   4658  NE1 TRP A1102     201.330 174.417 275.311  1.00 63.95           N  
ATOM   4659  CE2 TRP A1102     202.074 174.821 274.233  1.00 55.36           C  
ATOM   4660  CE3 TRP A1102     203.403 176.761 273.675  1.00 47.68           C  
ATOM   4661  CZ2 TRP A1102     202.334 174.240 272.986  1.00 47.67           C  
ATOM   4662  CZ3 TRP A1102     203.656 176.199 272.415  1.00 47.85           C  
ATOM   4663  CH2 TRP A1102     203.124 174.945 272.067  1.00 52.31           C  
ATOM   4664  N   PHE A1103     204.015 180.558 276.946  1.00 47.60           N  
ATOM   4665  CA  PHE A1103     203.910 181.984 277.238  1.00 49.94           C  
ATOM   4666  C   PHE A1103     203.435 182.749 276.005  1.00 53.04           C  
ATOM   4667  O   PHE A1103     203.882 182.465 274.901  1.00 57.75           O  
ATOM   4668  CB  PHE A1103     205.268 182.512 277.697  1.00 57.40           C  
ATOM   4669  CG  PHE A1103     205.936 181.803 278.865  1.00 61.54           C  
ATOM   4670  CD1 PHE A1103     205.534 182.083 280.183  1.00 61.12           C  
ATOM   4671  CD2 PHE A1103     207.027 180.941 278.642  1.00 59.46           C  
ATOM   4672  CE1 PHE A1103     206.220 181.503 281.261  1.00 65.23           C  
ATOM   4673  CE2 PHE A1103     207.715 180.368 279.723  1.00 60.01           C  
ATOM   4674  CZ  PHE A1103     207.315 180.656 281.033  1.00 71.34           C  
ATOM   4675  N   VAL A1104     202.554 183.737 276.150  1.00 48.48           N  
ATOM   4676  CA  VAL A1104     202.146 184.606 275.045  1.00 42.02           C  
ATOM   4677  C   VAL A1104     203.170 185.728 274.891  1.00 50.91           C  
ATOM   4678  O   VAL A1104     203.060 186.779 275.526  1.00 55.06           O  
ATOM   4679  CB  VAL A1104     200.704 185.107 275.222  1.00 41.54           C  
ATOM   4680  CG1 VAL A1104     200.302 186.107 274.136  1.00 47.90           C  
ATOM   4681  CG2 VAL A1104     199.728 183.933 275.134  1.00 41.58           C  
ATOM   4682  N   THR A1105     204.200 185.503 274.074  1.00 50.73           N  
ATOM   4683  CA  THR A1105     205.128 186.574 273.685  1.00 50.20           C  
ATOM   4684  C   THR A1105     204.490 187.493 272.651  1.00 53.94           C  
ATOM   4685  O   THR A1105     203.651 187.086 271.852  1.00 55.58           O  
ATOM   4686  CB  THR A1105     206.488 186.036 273.225  1.00 49.38           C  
ATOM   4687  OG1 THR A1105     207.499 186.999 273.385  1.00 54.05           O  
ATOM   4688  CG2 THR A1105     206.578 185.598 271.777  1.00 49.09           C  
ATOM   4689  N   GLN A1106     204.886 188.758 272.653  1.00 55.72           N  
ATOM   4690  CA  GLN A1106     204.555 189.690 271.582  1.00 53.13           C  
ATOM   4691  C   GLN A1106     205.254 189.220 270.292  1.00 59.48           C  
ATOM   4692  O   GLN A1106     206.436 188.902 270.332  1.00 60.20           O  
ATOM   4693  CB  GLN A1106     205.018 191.072 272.050  1.00 50.43           C  
ATOM   4694  CG  GLN A1106     204.581 192.181 271.109  1.00 51.16           C  
ATOM   4695  CD  GLN A1106     204.968 193.580 271.588  1.00 64.65           C  
ATOM   4696  OE1 GLN A1106     205.636 193.794 272.592  1.00 61.90           O  
ATOM   4697  NE2 GLN A1106     204.536 194.606 270.900  1.00 66.54           N  
ATOM   4698  N   ARG A1107     204.548 189.082 269.170  1.00 58.74           N  
ATOM   4699  CA  ARG A1107     205.156 188.540 267.931  1.00 46.35           C  
ATOM   4700  C   ARG A1107     206.534 189.083 267.512  1.00 45.03           C  
ATOM   4701  O   ARG A1107     207.417 188.339 267.084  1.00 45.95           O  
ATOM   4702  CB  ARG A1107     204.197 188.720 266.752  1.00 41.08           C  
ATOM   4703  CG  ARG A1107     204.765 188.222 265.430  1.00 42.72           C  
ATOM   4704  CD  ARG A1107     204.889 186.707 265.422  1.00 41.66           C  
ATOM   4705  NE  ARG A1107     205.477 186.205 264.183  1.00 36.43           N  
ATOM   4706  CZ  ARG A1107     206.773 185.961 264.016  1.00 34.30           C  
ATOM   4707  NH1 ARG A1107     207.219 185.504 262.855  1.00 46.19           N  
ATOM   4708  NH2 ARG A1107     207.622 186.173 265.012  1.00 33.34           N  
ATOM   4709  N   ASN A1108     206.680 190.389 267.649  1.00 48.30           N  
ATOM   4710  CA  ASN A1108     207.888 191.124 267.278  1.00 50.14           C  
ATOM   4711  C   ASN A1108     208.967 191.245 268.370  1.00 51.99           C  
ATOM   4712  O   ASN A1108     209.888 192.034 268.181  1.00 45.67           O  
ATOM   4713  CB  ASN A1108     207.514 192.499 266.707  1.00 54.04           C  
ATOM   4714  CG  ASN A1108     206.912 193.490 267.675  1.00 57.19           C  
ATOM   4715  OD1 ASN A1108     205.871 193.283 268.243  1.00 64.28           O  
ATOM   4716  ND2 ASN A1108     207.523 194.611 267.878  1.00 46.36           N  
ATOM   4717  N   PHE A1109     208.883 190.515 269.494  1.00 59.13           N  
ATOM   4718  CA  PHE A1109     209.921 190.527 270.540  1.00 54.46           C  
ATOM   4719  C   PHE A1109     209.849 189.308 271.473  1.00 56.05           C  
ATOM   4720  O   PHE A1109     208.756 188.898 271.849  1.00 54.13           O  
ATOM   4721  CB  PHE A1109     209.779 191.811 271.366  1.00 44.26           C  
ATOM   4722  CG  PHE A1109     210.863 192.013 272.397  1.00 45.30           C  
ATOM   4723  CD1 PHE A1109     212.218 191.948 272.030  1.00 50.01           C  
ATOM   4724  CD2 PHE A1109     210.514 192.342 273.713  1.00 52.86           C  
ATOM   4725  CE1 PHE A1109     213.212 192.214 272.981  1.00 49.93           C  
ATOM   4726  CE2 PHE A1109     211.511 192.627 274.655  1.00 52.82           C  
ATOM   4727  CZ  PHE A1109     212.863 192.554 274.293  1.00 46.81           C  
ATOM   4728  N   TYR A1110     210.976 188.740 271.913  1.00 56.19           N  
ATOM   4729  CA  TYR A1110     210.983 187.733 272.985  1.00 55.45           C  
ATOM   4730  C   TYR A1110     210.863 188.353 274.391  1.00 56.09           C  
ATOM   4731  O   TYR A1110     211.827 188.863 274.958  1.00 50.93           O  
ATOM   4732  CB  TYR A1110     212.200 186.803 272.893  1.00 57.31           C  
ATOM   4733  CG  TYR A1110     212.192 185.790 274.024  1.00 64.05           C  
ATOM   4734  CD1 TYR A1110     211.144 184.850 274.111  1.00 61.38           C  
ATOM   4735  CD2 TYR A1110     213.167 185.843 275.035  1.00 66.14           C  
ATOM   4736  CE1 TYR A1110     211.082 183.953 275.196  1.00 59.83           C  
ATOM   4737  CE2 TYR A1110     213.101 184.958 276.127  1.00 68.98           C  
ATOM   4738  CZ  TYR A1110     212.067 184.005 276.206  1.00 64.75           C  
ATOM   4739  OH  TYR A1110     212.012 183.160 277.266  1.00 72.93           O  
ATOM   4740  N   GLU A1111     209.655 188.295 274.952  1.00 49.47           N  
ATOM   4741  CA  GLU A1111     209.292 188.784 276.285  1.00 51.69           C  
ATOM   4742  C   GLU A1111     208.074 187.997 276.799  1.00 58.18           C  
ATOM   4743  O   GLU A1111     206.930 188.408 276.588  1.00 57.71           O  
ATOM   4744  CB  GLU A1111     209.025 190.295 276.209  1.00 49.83           C  
ATOM   4745  CG  GLU A1111     208.634 190.922 277.549  1.00 63.58           C  
ATOM   4746  CD  GLU A1111     208.387 192.421 277.388  1.00 62.77           C  
ATOM   4747  OE1 GLU A1111     209.339 193.224 277.481  1.00 62.30           O  
ATOM   4748  OE2 GLU A1111     207.227 192.829 277.171  1.00 67.64           O1-
ATOM   4749  N   PRO A1112     208.282 186.824 277.413  1.00 56.54           N  
ATOM   4750  CA  PRO A1112     207.201 185.912 277.748  1.00 55.31           C  
ATOM   4751  C   PRO A1112     206.265 186.460 278.830  1.00 56.87           C  
ATOM   4752  O   PRO A1112     206.701 187.129 279.766  1.00 66.60           O  
ATOM   4753  CB  PRO A1112     207.884 184.614 278.169  1.00 57.80           C  
ATOM   4754  CG  PRO A1112     209.264 185.047 278.623  1.00 55.99           C  
ATOM   4755  CD  PRO A1112     209.572 186.247 277.743  1.00 58.48           C  
ATOM   4756  N   GLN A1113     204.973 186.131 278.720  1.00 55.60           N  
ATOM   4757  CA  GLN A1113     203.940 186.359 279.735  1.00 54.92           C  
ATOM   4758  C   GLN A1113     203.018 185.133 279.840  1.00 55.70           C  
ATOM   4759  O   GLN A1113     202.755 184.470 278.842  1.00 59.50           O  
ATOM   4760  CB  GLN A1113     203.140 187.636 279.435  1.00 49.63           C  
ATOM   4761  CG  GLN A1113     204.042 188.882 279.379  1.00 53.14           C  
ATOM   4762  CD  GLN A1113     203.290 190.205 279.348  1.00 63.10           C  
ATOM   4763  OE1 GLN A1113     202.087 190.307 279.549  1.00 57.77           O  
ATOM   4764  NE2 GLN A1113     203.980 191.299 279.118  1.00 67.04           N  
ATOM   4765  N   ILE A1114     202.536 184.817 281.040  1.00 56.29           N  
ATOM   4766  CA  ILE A1114     201.801 183.578 281.356  1.00 49.94           C  
ATOM   4767  C   ILE A1114     200.456 183.514 280.605  1.00 52.21           C  
ATOM   4768  O   ILE A1114     199.820 184.541 280.376  1.00 54.44           O  
ATOM   4769  CB  ILE A1114     201.672 183.467 282.901  1.00 53.35           C  
ATOM   4770  CG1 ILE A1114     202.977 182.976 283.568  1.00 52.25           C  
ATOM   4771  CG2 ILE A1114     200.554 182.521 283.369  1.00 53.79           C  
ATOM   4772  CD1 ILE A1114     204.188 183.908 283.489  1.00 45.78           C  
ATOM   4773  N   ILE A1115     199.985 182.325 280.214  1.00 47.68           N  
ATOM   4774  CA  ILE A1115     198.610 182.168 279.717  1.00 47.49           C  
ATOM   4775  C   ILE A1115     197.614 182.553 280.816  1.00 55.26           C  
ATOM   4776  O   ILE A1115     197.588 181.957 281.890  1.00 73.60           O  
ATOM   4777  CB  ILE A1115     198.336 180.737 279.202  1.00 47.04           C  
ATOM   4778  CG1 ILE A1115     199.093 180.526 277.876  1.00 60.15           C  
ATOM   4779  CG2 ILE A1115     196.826 180.473 279.007  1.00 43.51           C  
ATOM   4780  CD1 ILE A1115     198.837 179.173 277.194  1.00 51.16           C  
ATOM   4781  N   THR A1116     196.747 183.509 280.498  1.00 48.79           N  
ATOM   4782  CA  THR A1116     195.594 183.930 281.302  1.00 53.10           C  
ATOM   4783  C   THR A1116     194.414 184.189 280.366  1.00 53.72           C  
ATOM   4784  O   THR A1116     194.611 184.381 279.160  1.00 66.78           O  
ATOM   4785  CB  THR A1116     195.879 185.194 282.139  1.00 52.89           C  
ATOM   4786  OG1 THR A1116     195.874 186.352 281.338  1.00 49.03           O  
ATOM   4787  CG2 THR A1116     197.209 185.218 282.880  1.00 56.44           C  
ATOM   4788  N   THR A1117     193.186 184.257 280.887  1.00 49.86           N  
ATOM   4789  CA  THR A1117     191.998 184.604 280.068  1.00 54.32           C  
ATOM   4790  C   THR A1117     192.049 186.058 279.550  1.00 56.55           C  
ATOM   4791  O   THR A1117     191.281 186.436 278.672  1.00 55.29           O  
ATOM   4792  CB  THR A1117     190.692 184.317 280.836  1.00 58.36           C  
ATOM   4793  OG1 THR A1117     190.677 182.981 281.290  1.00 60.28           O  
ATOM   4794  CG2 THR A1117     189.419 184.436 280.000  1.00 61.80           C  
ATOM   4795  N   ASP A1118     192.998 186.879 280.018  1.00 49.37           N  
ATOM   4796  CA  ASP A1118     193.287 188.220 279.492  1.00 57.22           C  
ATOM   4797  C   ASP A1118     194.431 188.249 278.441  1.00 63.80           C  
ATOM   4798  O   ASP A1118     194.583 189.236 277.718  1.00 64.00           O  
ATOM   4799  CB  ASP A1118     193.592 189.119 280.689  1.00 59.61           C  
ATOM   4800  CG  ASP A1118     193.752 190.593 280.314  1.00 72.89           C  
ATOM   4801  OD1 ASP A1118     192.882 191.150 279.612  1.00 76.52           O  
ATOM   4802  OD2 ASP A1118     194.742 191.218 280.756  1.00 77.90           O1-
ATOM   4803  N   ASN A1119     195.236 187.184 278.326  1.00 63.24           N  
ATOM   4804  CA  ASN A1119     196.244 186.978 277.267  1.00 48.14           C  
ATOM   4805  C   ASN A1119     195.750 186.078 276.123  1.00 45.87           C  
ATOM   4806  O   ASN A1119     196.398 186.005 275.083  1.00 56.23           O  
ATOM   4807  CB  ASN A1119     197.538 186.395 277.882  1.00 47.59           C  
ATOM   4808  CG  ASN A1119     198.474 187.449 278.427  1.00 54.51           C  
ATOM   4809  OD1 ASN A1119     198.399 188.624 278.105  1.00 61.34           O  
ATOM   4810  ND2 ASN A1119     199.404 187.084 279.275  1.00 57.67           N  
ATOM   4811  N   THR A1120     194.629 185.376 276.280  1.00 41.71           N  
ATOM   4812  CA  THR A1120     194.127 184.417 275.281  1.00 42.29           C  
ATOM   4813  C   THR A1120     192.629 184.548 275.060  1.00 47.26           C  
ATOM   4814  O   THR A1120     191.901 185.071 275.903  1.00 54.47           O  
ATOM   4815  CB  THR A1120     194.466 182.969 275.652  1.00 42.03           C  
ATOM   4816  OG1 THR A1120     193.904 182.640 276.897  1.00 43.82           O  
ATOM   4817  CG2 THR A1120     195.962 182.683 275.716  1.00 47.61           C  
ATOM   4818  N   PHE A1121     192.177 184.095 273.898  1.00 48.53           N  
ATOM   4819  CA  PHE A1121     190.794 183.758 273.605  1.00 48.34           C  
ATOM   4820  C   PHE A1121     190.603 182.242 273.691  1.00 46.46           C  
ATOM   4821  O   PHE A1121     191.570 181.477 273.691  1.00 47.62           O  
ATOM   4822  CB  PHE A1121     190.428 184.277 272.209  1.00 47.97           C  
ATOM   4823  CG  PHE A1121     190.386 185.784 272.061  1.00 47.33           C  
ATOM   4824  CD1 PHE A1121     191.119 186.431 271.048  1.00 49.22           C  
ATOM   4825  CD2 PHE A1121     189.573 186.542 272.919  1.00 52.24           C  
ATOM   4826  CE1 PHE A1121     191.042 187.827 270.901  1.00 55.43           C  
ATOM   4827  CE2 PHE A1121     189.506 187.933 272.768  1.00 52.55           C  
ATOM   4828  CZ  PHE A1121     190.234 188.582 271.763  1.00 52.04           C  
ATOM   4829  N   VAL A1122     189.345 181.811 273.733  1.00 43.47           N  
ATOM   4830  CA  VAL A1122     188.952 180.411 273.902  1.00 43.93           C  
ATOM   4831  C   VAL A1122     187.803 180.070 272.956  1.00 50.47           C  
ATOM   4832  O   VAL A1122     187.023 180.941 272.582  1.00 52.15           O  
ATOM   4833  CB  VAL A1122     188.590 180.124 275.376  1.00 51.03           C  
ATOM   4834  CG1 VAL A1122     188.264 178.650 275.629  1.00 54.82           C  
ATOM   4835  CG2 VAL A1122     189.718 180.523 276.334  1.00 53.02           C  
ATOM   4836  N   SER A1123     187.703 178.806 272.566  1.00 50.51           N  
ATOM   4837  CA  SER A1123     186.775 178.299 271.554  1.00 52.59           C  
ATOM   4838  C   SER A1123     185.947 177.102 272.059  1.00 60.27           C  
ATOM   4839  O   SER A1123     185.843 176.868 273.263  1.00 65.20           O  
ATOM   4840  CB  SER A1123     187.628 177.954 270.332  1.00 56.02           C  
ATOM   4841  OG  SER A1123     186.826 177.725 269.202  1.00 64.19           O  
ATOM   4842  N   GLY A1124     185.378 176.361 271.113  1.00 62.67           N  
ATOM   4843  CA  GLY A1124     184.570 175.203 271.432  1.00 61.68           C  
ATOM   4844  C   GLY A1124     184.569 174.144 270.346  1.00 70.33           C  
ATOM   4845  O   GLY A1124     184.532 174.469 269.155  1.00 71.45           O  
ATOM   4846  N   ASN A1125     184.695 172.894 270.799  1.00 77.00           N  
ATOM   4847  CA  ASN A1125     184.679 171.639 270.018  1.00 79.85           C  
ATOM   4848  C   ASN A1125     185.948 171.218 269.262  1.00 76.00           C  
ATOM   4849  O   ASN A1125     185.949 170.158 268.647  1.00 75.98           O  
ATOM   4850  CB  ASN A1125     183.414 171.470 269.151  1.00 76.55           C  
ATOM   4851  CG  ASN A1125     182.135 171.648 269.947  1.00 78.60           C  
ATOM   4852  OD1 ASN A1125     182.170 171.923 271.145  1.00 76.61           O  
ATOM   4853  ND2 ASN A1125     180.997 171.494 269.280  1.00 79.52           N  
ATOM   4854  N   CYS A1126     187.013 172.019 269.360  1.00 70.89           N  
ATOM   4855  CA  CYS A1126     188.333 171.753 268.743  1.00 70.88           C  
ATOM   4856  C   CYS A1126     188.462 171.556 267.213  1.00 74.79           C  
ATOM   4857  O   CYS A1126     189.371 170.866 266.755  1.00 74.03           O  
ATOM   4858  CB  CYS A1126     189.018 170.585 269.469  1.00 72.83           C  
ATOM   4859  SG  CYS A1126     190.768 170.357 269.111  1.00 75.00           S  
ATOM   4860  N   ASP A1127     187.565 172.145 266.424  1.00 74.37           N  
ATOM   4861  CA  ASP A1127     187.607 172.025 264.951  1.00 67.80           C  
ATOM   4862  C   ASP A1127     188.260 173.159 264.141  1.00 66.00           C  
ATOM   4863  O   ASP A1127     188.130 174.328 264.503  1.00 62.17           O  
ATOM   4864  CB  ASP A1127     186.199 171.756 264.408  1.00 67.22           C  
ATOM   4865  CG  ASP A1127     185.607 170.464 264.937  1.00 75.59           C  
ATOM   4866  OD1 ASP A1127     186.312 169.743 265.673  1.00 84.24           O  
ATOM   4867  OD2 ASP A1127     184.436 170.172 264.617  1.00 77.21           O1-
ATOM   4868  N   VAL A1128     188.958 172.819 263.048  1.00 68.19           N  
ATOM   4869  CA  VAL A1128     189.551 173.873 262.216  1.00 62.19           C  
ATOM   4870  C   VAL A1128     188.619 174.152 261.045  1.00 63.36           C  
ATOM   4871  O   VAL A1128     188.264 173.235 260.298  1.00 65.82           O  
ATOM   4872  CB  VAL A1128     190.937 173.443 261.712  1.00 52.28           C  
ATOM   4873  CG1 VAL A1128     191.471 174.292 260.557  1.00 57.82           C  
ATOM   4874  CG2 VAL A1128     191.954 173.546 262.847  1.00 54.95           C  
ATOM   4875  N   VAL A1129     188.249 175.417 260.860  1.00 58.47           N  
ATOM   4876  CA  VAL A1129     187.636 175.873 259.608  1.00 58.71           C  
ATOM   4877  C   VAL A1129     188.724 175.955 258.535  1.00 65.30           C  
ATOM   4878  O   VAL A1129     189.766 176.547 258.785  1.00 65.88           O  
ATOM   4879  CB  VAL A1129     186.938 177.224 259.839  1.00 52.77           C  
ATOM   4880  CG1 VAL A1129     186.602 177.986 258.553  1.00 60.12           C  
ATOM   4881  CG2 VAL A1129     185.631 177.022 260.612  1.00 65.07           C  
ATOM   4882  N   ILE A1130     188.505 175.411 257.337  1.00 64.57           N  
ATOM   4883  CA  ILE A1130     189.455 175.545 256.219  1.00 54.69           C  
ATOM   4884  C   ILE A1130     188.864 176.469 255.151  1.00 55.83           C  
ATOM   4885  O   ILE A1130     187.793 176.218 254.604  1.00 58.85           O  
ATOM   4886  CB  ILE A1130     189.894 174.171 255.664  1.00 55.11           C  
ATOM   4887  CG1 ILE A1130     190.621 173.381 256.776  1.00 59.07           C  
ATOM   4888  CG2 ILE A1130     190.803 174.356 254.437  1.00 61.85           C  
ATOM   4889  CD1 ILE A1130     191.336 172.098 256.339  1.00 60.15           C  
ATOM   4890  N   GLY A1131     189.584 177.543 254.847  1.00 54.50           N  
ATOM   4891  CA  GLY A1131     189.272 178.509 253.799  1.00 57.19           C  
ATOM   4892  C   GLY A1131     190.211 178.367 252.604  1.00 62.34           C  
ATOM   4893  O   GLY A1131     191.360 177.941 252.740  1.00 60.61           O  
ATOM   4894  N   ILE A1132     189.734 178.757 251.429  1.00 65.68           N  
ATOM   4895  CA  ILE A1132     190.505 178.791 250.186  1.00 57.60           C  
ATOM   4896  C   ILE A1132     190.341 180.153 249.507  1.00 55.16           C  
ATOM   4897  O   ILE A1132     189.227 180.660 249.348  1.00 51.86           O  
ATOM   4898  CB  ILE A1132     190.123 177.584 249.294  1.00 53.84           C  
ATOM   4899  CG1 ILE A1132     190.976 177.459 248.016  1.00 57.11           C  
ATOM   4900  CG2 ILE A1132     188.639 177.574 248.878  1.00 50.88           C  
ATOM   4901  CD1 ILE A1132     192.444 177.126 248.275  1.00 57.02           C  
ATOM   4902  N   VAL A1133     191.459 180.751 249.121  1.00 53.09           N  
ATOM   4903  CA  VAL A1133     191.520 182.000 248.373  1.00 52.79           C  
ATOM   4904  C   VAL A1133     192.416 181.774 247.174  1.00 57.79           C  
ATOM   4905  O   VAL A1133     193.547 181.306 247.300  1.00 61.35           O  
ATOM   4906  CB  VAL A1133     192.023 183.158 249.247  1.00 52.96           C  
ATOM   4907  CG1 VAL A1133     192.257 184.446 248.453  1.00 50.11           C  
ATOM   4908  CG2 VAL A1133     191.018 183.477 250.356  1.00 55.54           C  
ATOM   4909  N   ASN A1134     191.926 182.138 245.999  1.00 61.83           N  
ATOM   4910  CA  ASN A1134     192.675 182.002 244.766  1.00 58.75           C  
ATOM   4911  C   ASN A1134     192.606 183.310 243.989  1.00 63.99           C  
ATOM   4912  O   ASN A1134     191.584 183.628 243.384  1.00 69.37           O  
ATOM   4913  CB  ASN A1134     192.138 180.785 244.012  1.00 68.64           C  
ATOM   4914  CG  ASN A1134     193.062 180.351 242.896  1.00 71.72           C  
ATOM   4915  OD1 ASN A1134     193.976 181.066 242.495  1.00 70.26           O  
ATOM   4916  ND2 ASN A1134     192.771 179.169 242.381  1.00 77.43           N  
ATOM   4917  N   ASN A1135     193.655 184.118 244.090  1.00 58.77           N  
ATOM   4918  CA  ASN A1135     193.715 185.419 243.448  1.00 65.32           C  
ATOM   4919  C   ASN A1135     194.069 185.270 241.966  1.00 66.78           C  
ATOM   4920  O   ASN A1135     195.196 185.518 241.545  1.00 65.58           O  
ATOM   4921  CB  ASN A1135     194.659 186.326 244.230  1.00 58.57           C  
ATOM   4922  CG  ASN A1135     194.230 186.462 245.674  1.00 52.02           C  
ATOM   4923  OD1 ASN A1135     193.238 187.085 246.004  1.00 56.57           O  
ATOM   4924  ND2 ASN A1135     194.960 185.863 246.564  1.00 52.73           N  
ATOM   4925  N   THR A1136     193.080 184.874 241.176  1.00 64.26           N  
ATOM   4926  CA  THR A1136     193.103 184.920 239.721  1.00 60.92           C  
ATOM   4927  C   THR A1136     193.224 186.381 239.285  1.00 67.65           C  
ATOM   4928  O   THR A1136     192.219 187.078 239.177  1.00 72.51           O  
ATOM   4929  CB  THR A1136     191.805 184.288 239.186  1.00 68.74           C  
ATOM   4930  OG1 THR A1136     191.687 182.955 239.609  1.00 71.33           O  
ATOM   4931  CG2 THR A1136     191.680 184.302 237.665  1.00 65.48           C  
ATOM   4932  N   VAL A1137     194.435 186.866 239.007  1.00 65.60           N  
ATOM   4933  CA  VAL A1137     194.587 188.022 238.112  1.00 56.19           C  
ATOM   4934  C   VAL A1137     193.956 187.656 236.775  1.00 45.96           C  
ATOM   4935  O   VAL A1137     193.985 186.493 236.387  1.00 46.95           O  
ATOM   4936  CB  VAL A1137     196.036 188.479 237.922  1.00 49.19           C  
ATOM   4937  CG1 VAL A1137     196.652 188.931 239.247  1.00 51.36           C  
ATOM   4938  CG2 VAL A1137     196.945 187.424 237.304  1.00 42.59           C  
ATOM   4939  N   TYR A1138     193.321 188.606 236.103  1.00 44.94           N  
ATOM   4940  CA  TYR A1138     192.378 188.286 235.035  1.00 42.19           C  
ATOM   4941  C   TYR A1138     193.071 187.600 233.857  1.00 45.26           C  
ATOM   4942  O   TYR A1138     194.076 188.091 233.350  1.00 45.02           O  
ATOM   4943  CB  TYR A1138     191.680 189.567 234.599  1.00 41.16           C  
ATOM   4944  CG  TYR A1138     190.620 189.410 233.542  1.00 43.20           C  
ATOM   4945  CD1 TYR A1138     190.859 189.870 232.235  1.00 48.90           C  
ATOM   4946  CD2 TYR A1138     189.370 188.867 233.885  1.00 50.73           C  
ATOM   4947  CE1 TYR A1138     189.856 189.751 231.258  1.00 52.10           C  
ATOM   4948  CE2 TYR A1138     188.371 188.731 232.907  1.00 56.91           C  
ATOM   4949  CZ  TYR A1138     188.626 189.144 231.586  1.00 58.05           C  
ATOM   4950  OH  TYR A1138     187.702 188.917 230.621  1.00 61.71           O  
ATOM   4951  N   ASP A1139     192.573 186.441 233.429  1.00 47.02           N  
ATOM   4952  CA  ASP A1139     193.050 185.778 232.218  1.00 44.31           C  
ATOM   4953  C   ASP A1139     192.078 186.095 231.076  1.00 47.98           C  
ATOM   4954  O   ASP A1139     190.939 185.613 231.093  1.00 47.30           O  
ATOM   4955  CB  ASP A1139     193.229 184.268 232.445  1.00 47.74           C  
ATOM   4956  CG  ASP A1139     194.224 183.633 231.471  1.00 59.63           C  
ATOM   4957  OD1 ASP A1139     194.601 184.259 230.466  1.00 61.23           O  
ATOM   4958  OD2 ASP A1139     194.658 182.494 231.727  1.00 66.21           O1-
ATOM   4959  N   PRO A1140     192.481 186.934 230.109  1.00 36.48           N  
ATOM   4960  CA  PRO A1140     191.560 187.504 229.146  1.00 36.11           C  
ATOM   4961  C   PRO A1140     191.071 186.524 228.086  1.00 39.54           C  
ATOM   4962  O   PRO A1140     191.724 185.530 227.763  1.00 42.30           O  
ATOM   4963  CB  PRO A1140     192.305 188.676 228.517  1.00 42.14           C  
ATOM   4964  CG  PRO A1140     193.778 188.354 228.705  1.00 32.30           C  
ATOM   4965  CD  PRO A1140     193.785 187.555 229.992  1.00 27.14           C  
ATOM   4966  N   LEU A1141     189.936 186.863 227.473  1.00 40.22           N  
ATOM   4967  CA  LEU A1141     189.485 186.294 226.210  1.00 41.25           C  
ATOM   4968  C   LEU A1141     190.466 186.719 225.103  1.00 39.63           C  
ATOM   4969  O   LEU A1141     190.309 187.775 224.495  1.00 41.52           O  
ATOM   4970  CB  LEU A1141     188.059 186.793 225.912  1.00 42.85           C  
ATOM   4971  CG  LEU A1141     186.933 186.137 226.719  1.00 44.75           C  
ATOM   4972  CD1 LEU A1141     186.879 186.581 228.179  1.00 51.01           C  
ATOM   4973  CD2 LEU A1141     185.594 186.505 226.077  1.00 50.21           C  
ATOM   4974  N   GLN A1142     191.510 185.930 224.845  1.00 38.32           N  
ATOM   4975  CA  GLN A1142     192.477 186.243 223.792  1.00 34.82           C  
ATOM   4976  C   GLN A1142     191.878 186.017 222.391  1.00 42.00           C  
ATOM   4977  O   GLN A1142     191.045 185.123 222.205  1.00 47.94           O  
ATOM   4978  CB  GLN A1142     193.809 185.488 223.979  1.00 31.47           C  
ATOM   4979  CG  GLN A1142     194.741 186.048 225.077  1.00 28.73           C  
ATOM   4980  CD  GLN A1142     195.323 187.430 224.770  1.00 29.70           C  
ATOM   4981  OE1 GLN A1142     194.700 188.265 224.147  1.00 33.35           O  
ATOM   4982  NE2 GLN A1142     196.518 187.758 225.178  1.00 26.55           N  
ATOM   4983  N   PRO A1143     192.241 186.834 221.390  1.00 41.21           N  
ATOM   4984  CA  PRO A1143     191.581 186.898 220.092  1.00 38.59           C  
ATOM   4985  C   PRO A1143     191.955 185.743 219.154  1.00 34.42           C  
ATOM   4986  O   PRO A1143     192.715 185.910 218.203  1.00 41.49           O  
ATOM   4987  CB  PRO A1143     191.967 188.267 219.538  1.00 32.69           C  
ATOM   4988  CG  PRO A1143     193.344 188.509 220.121  1.00 28.55           C  
ATOM   4989  CD  PRO A1143     193.232 187.888 221.493  1.00 35.63           C  
ATOM   4990  N   GLU A1144     191.389 184.565 219.393  1.00 38.51           N  
ATOM   4991  CA  GLU A1144     191.569 183.394 218.530  1.00 48.47           C  
ATOM   4992  C   GLU A1144     190.784 183.501 217.216  1.00 50.60           C  
ATOM   4993  O   GLU A1144     189.614 183.882 217.196  1.00 53.80           O  
ATOM   4994  CB  GLU A1144     191.238 182.092 219.278  1.00 53.02           C  
ATOM   4995  CG  GLU A1144     191.298 180.791 218.449  1.00 58.28           C  
ATOM   4996  CD  GLU A1144     192.675 180.455 217.842  1.00 61.98           C  
ATOM   4997  OE1 GLU A1144     193.397 181.349 217.358  1.00 57.83           O  
ATOM   4998  OE2 GLU A1144     193.042 179.264 217.838  1.00 72.81           O1-
ATOM   4999  N   LEU A1145     191.443 183.102 216.133  1.00 43.26           N  
ATOM   5000  CA  LEU A1145     191.088 183.305 214.732  1.00 40.77           C  
ATOM   5001  C   LEU A1145     190.984 181.977 213.972  1.00 46.56           C  
ATOM   5002  O   LEU A1145     191.651 181.002 214.319  1.00 55.50           O  
ATOM   5003  CB  LEU A1145     192.204 184.128 214.081  1.00 31.20           C  
ATOM   5004  CG  LEU A1145     192.313 185.586 214.524  1.00 25.34           C  
ATOM   5005  CD1 LEU A1145     193.664 186.132 214.077  1.00 20.03           C  
ATOM   5006  CD2 LEU A1145     191.226 186.417 213.860  1.00 33.26           C  
ATOM   5007  N   ASP A1146     190.213 181.943 212.887  1.00 43.80           N  
ATOM   5008  CA  ASP A1146     190.249 180.836 211.922  1.00 46.57           C  
ATOM   5009  C   ASP A1146     191.642 180.674 211.293  1.00 48.40           C  
ATOM   5010  O   ASP A1146     192.479 181.569 211.421  1.00 51.26           O  
ATOM   5011  CB  ASP A1146     189.215 181.043 210.804  1.00 44.06           C  
ATOM   5012  CG  ASP A1146     187.856 181.536 211.287  1.00 51.28           C  
ATOM   5013  OD1 ASP A1146     186.893 180.743 211.265  1.00 50.02           O  
ATOM   5014  OD2 ASP A1146     187.742 182.725 211.655  1.00 56.51           O1-
ATOM   5015  N   SER A1147     191.901 179.607 210.533  1.00 52.05           N  
ATOM   5016  CA  SER A1147     193.065 179.634 209.631  1.00 52.95           C  
ATOM   5017  C   SER A1147     192.866 180.698 208.548  1.00 49.65           C  
ATOM   5018  O   SER A1147     191.741 181.007 208.163  1.00 52.93           O  
ATOM   5019  CB  SER A1147     193.360 178.274 208.992  1.00 53.46           C  
ATOM   5020  OG  SER A1147     193.759 177.316 209.948  1.00 54.55           O  
ATOM   5021  N   PHE A1148     193.955 181.261 208.025  1.00 46.84           N  
ATOM   5022  CA  PHE A1148     193.890 182.380 207.080  1.00 42.92           C  
ATOM   5023  C   PHE A1148     193.090 182.034 205.815  1.00 46.40           C  
ATOM   5024  O   PHE A1148     192.342 182.865 205.309  1.00 49.45           O  
ATOM   5025  CB  PHE A1148     195.321 182.794 206.734  1.00 39.95           C  
ATOM   5026  CG  PHE A1148     195.460 184.114 205.999  1.00 35.78           C  
ATOM   5027  CD1 PHE A1148     195.820 185.259 206.718  1.00 38.55           C  
ATOM   5028  CD2 PHE A1148     195.290 184.206 204.610  1.00 40.19           C  
ATOM   5029  CE1 PHE A1148     195.998 186.488 206.071  1.00 32.93           C  
ATOM   5030  CE2 PHE A1148     195.476 185.435 203.960  1.00 43.00           C  
ATOM   5031  CZ  PHE A1148     195.819 186.579 204.686  1.00 29.68           C  
ATOM   5032  N   LYS A1149     193.174 180.783 205.336  1.00 54.80           N  
ATOM   5033  CA  LYS A1149     192.429 180.286 204.171  1.00 54.09           C  
ATOM   5034  C   LYS A1149     190.919 180.472 204.327  1.00 51.80           C  
ATOM   5035  O   LYS A1149     190.294 180.961 203.398  1.00 53.76           O  
ATOM   5036  CB  LYS A1149     192.763 178.810 203.893  1.00 57.41           C  
ATOM   5037  CG  LYS A1149     194.263 178.545 203.662  1.00 54.00           C  
ATOM   5038  CD  LYS A1149     194.561 177.166 203.052  1.00 59.07           C  
ATOM   5039  CE  LYS A1149     193.979 175.956 203.799  1.00 54.76           C  
ATOM   5040  NZ  LYS A1149     194.667 175.658 205.083  1.00 63.97           N  
ATOM   5041  N   GLU A1150     190.334 180.177 205.487  1.00 47.78           N  
ATOM   5042  CA  GLU A1150     188.905 180.392 205.736  1.00 48.87           C  
ATOM   5043  C   GLU A1150     188.534 181.875 205.763  1.00 47.44           C  
ATOM   5044  O   GLU A1150     187.509 182.251 205.198  1.00 49.03           O  
ATOM   5045  CB  GLU A1150     188.460 179.748 207.059  1.00 64.25           C  
ATOM   5046  CG  GLU A1150     188.501 178.219 207.055  1.00 68.39           C  
ATOM   5047  CD  GLU A1150     189.844 177.659 207.548  1.00 68.50           C  
ATOM   5048  OE1 GLU A1150     190.016 177.531 208.781  1.00 70.94           O  
ATOM   5049  OE2 GLU A1150     190.717 177.337 206.709  1.00 63.37           O1-
ATOM   5050  N   GLU A1151     189.334 182.730 206.405  1.00 41.30           N  
ATOM   5051  CA  GLU A1151     189.003 184.156 206.530  1.00 45.04           C  
ATOM   5052  C   GLU A1151     189.320 184.939 205.240  1.00 46.37           C  
ATOM   5053  O   GLU A1151     188.744 185.996 204.995  1.00 42.99           O  
ATOM   5054  CB  GLU A1151     189.698 184.728 207.776  1.00 47.12           C  
ATOM   5055  CG  GLU A1151     188.948 185.931 208.380  1.00 51.87           C  
ATOM   5056  CD  GLU A1151     189.662 186.550 209.592  1.00 46.76           C  
ATOM   5057  OE1 GLU A1151     190.889 186.372 209.719  1.00 42.27           O  
ATOM   5058  OE2 GLU A1151     189.010 187.227 210.410  1.00 52.48           O1-
ATOM   5059  N   LEU A1152     190.181 184.397 204.371  1.00 44.79           N  
ATOM   5060  CA  LEU A1152     190.443 184.875 203.014  1.00 39.49           C  
ATOM   5061  C   LEU A1152     189.317 184.474 202.058  1.00 46.63           C  
ATOM   5062  O   LEU A1152     188.638 185.333 201.499  1.00 50.56           O  
ATOM   5063  CB  LEU A1152     191.818 184.348 202.573  1.00 38.85           C  
ATOM   5064  CG  LEU A1152     192.277 184.815 201.186  1.00 37.95           C  
ATOM   5065  CD1 LEU A1152     192.591 186.309 201.170  1.00 36.73           C  
ATOM   5066  CD2 LEU A1152     193.534 184.062 200.766  1.00 40.85           C  
ATOM   5067  N   ASP A1153     189.060 183.173 201.922  1.00 44.94           N  
ATOM   5068  CA  ASP A1153     188.087 182.596 200.992  1.00 43.09           C  
ATOM   5069  C   ASP A1153     186.660 183.109 201.202  1.00 44.07           C  
ATOM   5070  O   ASP A1153     185.850 183.054 200.282  1.00 42.41           O  
ATOM   5071  CB  ASP A1153     188.094 181.065 201.113  1.00 45.36           C  
ATOM   5072  CG  ASP A1153     189.369 180.367 200.617  1.00 51.35           C  
ATOM   5073  OD1 ASP A1153     190.127 180.958 199.819  1.00 46.44           O  
ATOM   5074  OD2 ASP A1153     189.584 179.185 200.965  1.00 51.01           O1-
ATOM   5075  N   LYS A1154     186.338 183.644 202.379  1.00 47.38           N  
ATOM   5076  CA  LYS A1154     185.049 184.287 202.653  1.00 51.26           C  
ATOM   5077  C   LYS A1154     184.741 185.425 201.677  1.00 49.17           C  
ATOM   5078  O   LYS A1154     183.586 185.573 201.285  1.00 54.39           O  
ATOM   5079  CB  LYS A1154     185.048 184.769 204.111  1.00 56.45           C  
ATOM   5080  CG  LYS A1154     183.672 185.309 204.524  1.00 61.00           C  
ATOM   5081  CD  LYS A1154     183.601 185.698 206.009  1.00 65.39           C  
ATOM   5082  CE  LYS A1154     183.626 184.485 206.954  1.00 69.27           C  
ATOM   5083  NZ  LYS A1154     182.378 183.686 206.863  1.00 75.64           N  
ATOM   5084  N   TYR A1155     185.756 186.188 201.253  1.00 45.99           N  
ATOM   5085  CA  TYR A1155     185.606 187.371 200.385  1.00 50.01           C  
ATOM   5086  C   TYR A1155     186.547 187.421 199.177  1.00 50.16           C  
ATOM   5087  O   TYR A1155     186.217 188.051 198.174  1.00 50.09           O  
ATOM   5088  CB  TYR A1155     185.769 188.648 201.225  1.00 53.51           C  
ATOM   5089  CG  TYR A1155     184.608 188.866 202.170  1.00 56.79           C  
ATOM   5090  CD1 TYR A1155     184.767 188.731 203.558  1.00 53.12           C  
ATOM   5091  CD2 TYR A1155     183.339 189.135 201.625  1.00 59.55           C  
ATOM   5092  CE1 TYR A1155     183.643 188.843 204.396  1.00 56.53           C  
ATOM   5093  CE2 TYR A1155     182.212 189.233 202.457  1.00 55.54           C  
ATOM   5094  CZ  TYR A1155     182.362 189.070 203.845  1.00 50.92           C  
ATOM   5095  OH  TYR A1155     181.275 189.118 204.657  1.00 51.16           O  
ATOM   5096  N   PHE A1156     187.700 186.767 199.267  1.00 47.16           N  
ATOM   5097  CA  PHE A1156     188.693 186.787 198.188  1.00 41.14           C  
ATOM   5098  C   PHE A1156     188.251 186.207 196.836  1.00 43.48           C  
ATOM   5099  O   PHE A1156     187.655 185.132 196.774  1.00 44.17           O  
ATOM   5100  CB  PHE A1156     189.976 186.088 198.656  1.00 30.00           C  
ATOM   5101  CG  PHE A1156     191.068 186.065 197.624  1.00 30.00           C  
ATOM   5102  CD1 PHE A1156     191.866 187.177 197.414  1.00 30.00           C  
ATOM   5103  CD2 PHE A1156     191.296 184.929 196.864  1.00 30.00           C  
ATOM   5104  CE1 PHE A1156     192.871 187.158 196.466  1.00 30.00           C  
ATOM   5105  CE2 PHE A1156     192.300 184.903 195.914  1.00 30.00           C  
ATOM   5106  CZ  PHE A1156     193.088 186.020 195.714  1.00 30.00           C  
ATOM   5107  N   LYS A1157     188.554 186.935 195.760  1.00 56.11           N  
ATOM   5108  CA  LYS A1157     188.245 186.497 194.394  1.00 49.25           C  
ATOM   5109  C   LYS A1157     189.526 186.296 193.591  1.00 45.09           C  
ATOM   5110  O   LYS A1157     190.276 187.241 193.356  1.00 38.50           O  
ATOM   5111  CB  LYS A1157     187.269 187.489 193.735  1.00 43.57           C  
ATOM   5112  CG  LYS A1157     185.863 187.300 194.315  1.00 51.08           C  
ATOM   5113  CD  LYS A1157     184.802 188.147 193.606  1.00 68.28           C  
ATOM   5114  CE  LYS A1157     183.458 187.896 194.293  1.00 71.72           C  
ATOM   5115  NZ  LYS A1157     182.369 188.703 193.711  1.00 73.29           N  
ATOM   5116  N   ASN A1158     189.755 185.065 193.143  1.00 46.48           N  
ATOM   5117  CA  ASN A1158     190.964 184.640 192.431  1.00 52.76           C  
ATOM   5118  C   ASN A1158     190.819 184.857 190.913  1.00 60.48           C  
ATOM   5119  O   ASN A1158     191.043 183.963 190.102  1.00 58.43           O  
ATOM   5120  CB  ASN A1158     191.282 183.184 192.840  1.00 55.35           C  
ATOM   5121  CG  ASN A1158     192.743 182.838 192.906  1.00 61.41           C  
ATOM   5122  OD1 ASN A1158     193.595 183.685 193.146  1.00 63.07           O  
ATOM   5123  ND2 ASN A1158     193.025 181.557 192.768  1.00 64.51           N  
ATOM   5124  N   HIS A1159     190.379 186.053 190.521  1.00 64.21           N  
ATOM   5125  CA  HIS A1159     190.108 186.424 189.132  1.00 63.54           C  
ATOM   5126  C   HIS A1159     191.413 186.494 188.329  1.00 59.88           C  
ATOM   5127  O   HIS A1159     192.288 187.312 188.619  1.00 58.46           O  
ATOM   5128  CB  HIS A1159     189.353 187.759 189.119  1.00 59.54           C  
ATOM   5129  CG  HIS A1159     189.197 188.409 187.768  1.00 68.35           C  
ATOM   5130  ND1 HIS A1159     188.249 188.075 186.803  1.00 70.35           N  
ATOM   5131  CD2 HIS A1159     189.919 189.469 187.320  1.00 66.69           C  
ATOM   5132  CE1 HIS A1159     188.408 188.956 185.806  1.00 68.71           C  
ATOM   5133  NE2 HIS A1159     189.409 189.797 186.087  1.00 55.02           N  
ATOM   5134  N   THR A1160     191.539 185.644 187.311  1.00 58.53           N  
ATOM   5135  CA  THR A1160     192.655 185.686 186.361  1.00 54.99           C  
ATOM   5136  C   THR A1160     192.140 186.140 185.001  1.00 55.19           C  
ATOM   5137  O   THR A1160     191.295 185.482 184.388  1.00 58.16           O  
ATOM   5138  CB  THR A1160     193.382 184.341 186.238  1.00 48.75           C  
ATOM   5139  OG1 THR A1160     192.520 183.345 185.746  1.00 60.49           O  
ATOM   5140  CG2 THR A1160     193.943 183.850 187.570  1.00 52.83           C  
ATOM   5141  N   SER A1161     192.680 187.244 184.501  1.00 56.64           N  
ATOM   5142  CA  SER A1161     192.362 187.772 183.185  1.00 51.03           C  
ATOM   5143  C   SER A1161     192.942 186.866 182.089  1.00 54.52           C  
ATOM   5144  O   SER A1161     194.060 186.361 182.243  1.00 49.99           O  
ATOM   5145  CB  SER A1161     192.878 189.203 183.057  1.00 46.81           C  
ATOM   5146  OG  SER A1161     194.285 189.264 183.143  1.00 45.89           O  
ATOM   5147  N   PRO A1162     192.207 186.614 180.991  1.00 60.96           N  
ATOM   5148  CA  PRO A1162     192.649 185.690 179.957  1.00 66.49           C  
ATOM   5149  C   PRO A1162     193.834 186.216 179.135  1.00 59.69           C  
ATOM   5150  O   PRO A1162     193.997 187.414 178.914  1.00 57.14           O  
ATOM   5151  CB  PRO A1162     191.408 185.420 179.107  1.00 65.94           C  
ATOM   5152  CG  PRO A1162     190.566 186.681 179.277  1.00 58.20           C  
ATOM   5153  CD  PRO A1162     190.857 187.082 180.717  1.00 60.27           C  
ATOM   5154  N   ASP A1163     194.652 185.279 178.650  1.00 57.92           N  
ATOM   5155  CA  ASP A1163     195.767 185.501 177.722  1.00 58.31           C  
ATOM   5156  C   ASP A1163     195.272 186.216 176.458  1.00 69.56           C  
ATOM   5157  O   ASP A1163     194.414 185.693 175.746  1.00 69.29           O  
ATOM   5158  CB  ASP A1163     196.382 184.119 177.414  1.00 60.67           C  
ATOM   5159  CG  ASP A1163     197.541 184.092 176.410  1.00 66.22           C  
ATOM   5160  OD1 ASP A1163     197.935 185.139 175.858  1.00 69.41           O  
ATOM   5161  OD2 ASP A1163     198.077 182.989 176.170  1.00 66.36           O1-
ATOM   5162  N   VAL A1164     195.755 187.433 176.204  1.00 60.58           N  
ATOM   5163  CA  VAL A1164     195.262 188.250 175.091  1.00 62.37           C  
ATOM   5164  C   VAL A1164     195.703 187.661 173.749  1.00 63.07           C  
ATOM   5165  O   VAL A1164     196.890 187.579 173.446  1.00 61.37           O  
ATOM   5166  CB  VAL A1164     195.595 189.745 175.252  1.00 53.83           C  
ATOM   5167  CG1 VAL A1164     197.058 190.042 175.562  1.00 54.33           C  
ATOM   5168  CG2 VAL A1164     195.169 190.561 174.026  1.00 45.34           C  
ATOM   5169  N   ASP A1165     194.719 187.299 172.930  1.00 64.66           N  
ATOM   5170  CA  ASP A1165     194.876 186.960 171.521  1.00 63.73           C  
ATOM   5171  C   ASP A1165     194.188 188.017 170.661  1.00 63.37           C  
ATOM   5172  O   ASP A1165     193.102 188.492 170.989  1.00 65.42           O  
ATOM   5173  CB  ASP A1165     194.327 185.564 171.220  1.00 62.23           C  
ATOM   5174  CG  ASP A1165     195.196 184.436 171.776  1.00 67.59           C  
ATOM   5175  OD1 ASP A1165     196.435 184.567 171.824  1.00 62.13           O  
ATOM   5176  OD2 ASP A1165     194.637 183.374 172.106  1.00 76.54           O1-
ATOM   5177  N   LEU A1166     194.844 188.372 169.563  1.00 52.98           N  
ATOM   5178  CA  LEU A1166     194.412 189.348 168.567  1.00 50.83           C  
ATOM   5179  C   LEU A1166     194.805 188.872 167.153  1.00 59.32           C  
ATOM   5180  O   LEU A1166     195.545 187.896 167.006  1.00 63.09           O  
ATOM   5181  CB  LEU A1166     194.901 190.755 168.973  1.00 51.31           C  
ATOM   5182  CG  LEU A1166     196.367 191.124 168.681  1.00 46.69           C  
ATOM   5183  CD1 LEU A1166     196.614 192.567 169.115  1.00 36.58           C  
ATOM   5184  CD2 LEU A1166     197.361 190.244 169.438  1.00 48.66           C  
ATOM   5185  N   GLY A1167     194.232 189.501 166.129  1.00 58.73           N  
ATOM   5186  CA  GLY A1167     194.332 189.166 164.705  1.00 57.82           C  
ATOM   5187  C   GLY A1167     195.750 188.868 164.203  1.00 59.62           C  
ATOM   5188  O   GLY A1167     196.693 189.624 164.444  1.00 47.83           O  
ATOM   5189  N   ASP A1168     195.871 187.742 163.501  1.00 64.09           N  
ATOM   5190  CA  ASP A1168     197.099 187.085 163.056  1.00 74.11           C  
ATOM   5191  C   ASP A1168     197.307 187.262 161.541  1.00 74.31           C  
ATOM   5192  O   ASP A1168     197.105 186.351 160.734  1.00 75.98           O  
ATOM   5193  CB  ASP A1168     197.089 185.608 163.490  1.00 86.12           C  
ATOM   5194  CG  ASP A1168     195.861 184.775 163.081  1.00 83.44           C  
ATOM   5195  OD1 ASP A1168     194.772 185.324 162.798  1.00 78.38           O  
ATOM   5196  OD2 ASP A1168     195.965 183.530 163.120  1.00 81.50           O1-
ATOM   5197  N   ILE A1169     197.723 188.466 161.149  1.00 75.94           N  
ATOM   5198  CA  ILE A1169     197.765 188.919 159.753  1.00 64.14           C  
ATOM   5199  C   ILE A1169     198.707 188.118 158.832  1.00 71.69           C  
ATOM   5200  O   ILE A1169     198.625 188.262 157.617  1.00 77.17           O  
ATOM   5201  CB  ILE A1169     198.058 190.432 159.710  1.00 52.96           C  
ATOM   5202  CG1 ILE A1169     199.385 190.777 160.409  1.00 56.21           C  
ATOM   5203  CG2 ILE A1169     196.887 191.227 160.316  1.00 47.41           C  
ATOM   5204  CD1 ILE A1169     199.952 192.101 159.909  1.00 54.09           C  
ATOM   5205  N   SER A1170     199.543 187.224 159.364  1.00 67.79           N  
ATOM   5206  CA  SER A1170     200.369 186.290 158.591  1.00 78.20           C  
ATOM   5207  C   SER A1170     199.577 185.226 157.812  1.00 85.26           C  
ATOM   5208  O   SER A1170     200.140 184.565 156.942  1.00 83.28           O  
ATOM   5209  CB  SER A1170     201.361 185.612 159.538  1.00 79.42           C  
ATOM   5210  OG  SER A1170     200.689 184.959 160.600  1.00 67.05           O  
ATOM   5211  N   GLY A1171     198.276 185.049 158.072  1.00 88.70           N  
ATOM   5212  CA  GLY A1171     197.429 184.066 157.370  1.00 89.72           C  
ATOM   5213  C   GLY A1171     196.775 184.571 156.077  1.00 92.85           C  
ATOM   5214  O   GLY A1171     196.099 183.813 155.383  1.00104.08           O  
ATOM   5215  N   ILE A1172     196.949 185.841 155.735  1.00 88.95           N  
ATOM   5216  CA  ILE A1172     196.304 186.515 154.604  1.00 96.72           C  
ATOM   5217  C   ILE A1172     197.091 186.210 153.315  1.00 93.73           C  
ATOM   5218  O   ILE A1172     196.828 186.831 152.285  1.00 91.50           O  
ATOM   5219  CB  ILE A1172     196.257 188.050 154.934  1.00 87.18           C  
ATOM   5220  CG1 ILE A1172     195.479 188.312 156.253  1.00 83.27           C  
ATOM   5221  CG2 ILE A1172     195.686 188.930 153.803  1.00 82.57           C  
ATOM   5222  CD1 ILE A1172     195.523 189.762 156.762  1.00 76.12           C  
ATOM   5223  N   ASN A1173     198.037 185.276 153.342  1.00 93.95           N  
ATOM   5224  CA  ASN A1173     198.799 184.963 152.099  1.00 98.31           C  
ATOM   5225  C   ASN A1173     198.405 183.573 151.583  1.00100.31           C  
ATOM   5226  O   ASN A1173     197.629 182.894 152.287  1.00 98.78           O  
ATOM   5227  CB  ASN A1173     200.313 185.088 152.297  1.00100.04           C  
ATOM   5228  CG  ASN A1173     201.106 183.866 151.885  1.00100.11           C  
ATOM   5229  OD1 ASN A1173     200.862 182.764 152.371  1.00 97.01           O  
ATOM   5230  ND2 ASN A1173     202.068 184.064 150.997  1.00 99.37           N  
ATOM   5231  N   GLN A1180     207.134 190.860 132.377  1.00 76.76           N  
ATOM   5232  CA  GLN A1180     208.132 191.536 131.545  1.00 73.73           C  
ATOM   5233  C   GLN A1180     208.163 190.987 130.114  1.00 73.25           C  
ATOM   5234  O   GLN A1180     208.409 191.743 129.177  1.00 72.78           O  
ATOM   5235  CB  GLN A1180     209.500 191.450 132.248  1.00 77.61           C  
ATOM   5236  CG  GLN A1180     210.718 191.930 131.443  1.00 71.15           C  
ATOM   5237  CD  GLN A1180     210.701 193.399 131.021  1.00 68.80           C  
ATOM   5238  OE1 GLN A1180     209.971 194.235 131.520  1.00 72.22           O  
ATOM   5239  NE2 GLN A1180     211.550 193.794 130.105  1.00 68.30           N  
ATOM   5240  N   LYS A1181     207.861 189.697 129.915  1.00 75.84           N  
ATOM   5241  CA  LYS A1181     207.880 189.022 128.601  1.00 72.83           C  
ATOM   5242  C   LYS A1181     207.047 189.741 127.535  1.00 67.04           C  
ATOM   5243  O   LYS A1181     207.488 189.884 126.403  1.00 70.46           O  
ATOM   5244  CB  LYS A1181     207.422 187.566 128.784  1.00 73.01           C  
ATOM   5245  CG  LYS A1181     207.275 186.797 127.459  1.00 69.50           C  
ATOM   5246  CD  LYS A1181     207.131 185.276 127.652  1.00 76.23           C  
ATOM   5247  CE  LYS A1181     205.970 184.822 128.547  1.00 73.79           C  
ATOM   5248  NZ  LYS A1181     204.632 185.212 128.039  1.00 75.61           N  
ATOM   5249  N   GLU A1182     205.865 190.240 127.870  1.00 64.88           N  
ATOM   5250  CA  GLU A1182     205.058 190.998 126.916  1.00 61.74           C  
ATOM   5251  C   GLU A1182     205.680 192.361 126.581  1.00 62.90           C  
ATOM   5252  O   GLU A1182     205.617 192.781 125.432  1.00 69.31           O  
ATOM   5253  CB  GLU A1182     203.616 191.141 127.417  1.00 60.94           C  
ATOM   5254  CG  GLU A1182     202.924 189.766 127.518  1.00 64.14           C  
ATOM   5255  CD  GLU A1182     203.351 188.925 128.732  1.00 68.56           C  
ATOM   5256  OE1 GLU A1182     203.609 189.495 129.820  1.00 79.36           O  
ATOM   5257  OE2 GLU A1182     203.493 187.691 128.576  1.00 70.07           O1-
ATOM   5258  N   ILE A1183     206.355 193.027 127.526  1.00 63.56           N  
ATOM   5259  CA  ILE A1183     207.091 194.268 127.244  1.00 66.94           C  
ATOM   5260  C   ILE A1183     208.336 193.978 126.395  1.00 68.94           C  
ATOM   5261  O   ILE A1183     208.663 194.753 125.498  1.00 73.90           O  
ATOM   5262  CB  ILE A1183     207.425 195.033 128.549  1.00 74.01           C  
ATOM   5263  CG1 ILE A1183     206.147 195.317 129.379  1.00 76.99           C  
ATOM   5264  CG2 ILE A1183     208.141 196.357 128.230  1.00 64.18           C  
ATOM   5265  CD1 ILE A1183     206.035 194.414 130.618  1.00 74.45           C  
ATOM   5266  N   ASP A1184     208.997 192.834 126.591  1.00 70.19           N  
ATOM   5267  CA  ASP A1184     210.076 192.349 125.718  1.00 74.58           C  
ATOM   5268  C   ASP A1184     209.594 192.121 124.271  1.00 73.83           C  
ATOM   5269  O   ASP A1184     210.208 192.614 123.324  1.00 74.12           O  
ATOM   5270  CB  ASP A1184     210.694 191.069 126.312  1.00 81.08           C  
ATOM   5271  CG  ASP A1184     211.611 190.350 125.325  1.00 86.18           C  
ATOM   5272  OD1 ASP A1184     211.349 189.174 125.006  1.00 86.09           O  
ATOM   5273  OD2 ASP A1184     212.595 190.963 124.867  1.00 89.07           O1-
ATOM   5274  N   ARG A1185     208.443 191.467 124.124  1.00 74.04           N  
ATOM   5275  CA  ARG A1185     207.848 191.227 122.808  1.00 69.35           C  
ATOM   5276  C   ARG A1185     207.456 192.546 122.129  1.00 64.99           C  
ATOM   5277  O   ARG A1185     207.803 192.780 120.972  1.00 68.53           O  
ATOM   5278  CB  ARG A1185     206.623 190.319 122.930  1.00 67.40           C  
ATOM   5279  CG  ARG A1185     206.905 188.848 122.673  1.00 72.23           C  
ATOM   5280  CD  ARG A1185     208.111 188.353 123.455  1.00 79.32           C  
ATOM   5281  NE  ARG A1185     208.342 186.925 123.243  1.00 83.68           N  
ATOM   5282  CZ  ARG A1185     209.397 186.261 123.703  1.00 85.70           C  
ATOM   5283  NH1 ARG A1185     210.329 186.890 124.403  1.00 85.14           N  
ATOM   5284  NH2 ARG A1185     209.520 184.963 123.459  1.00 89.14           N  
ATOM   5285  N   LEU A1186     206.739 193.403 122.854  1.00 66.63           N  
ATOM   5286  CA  LEU A1186     206.342 194.703 122.300  1.00 65.25           C  
ATOM   5287  C   LEU A1186     207.557 195.579 121.904  1.00 65.01           C  
ATOM   5288  O   LEU A1186     207.496 196.258 120.886  1.00 69.89           O  
ATOM   5289  CB  LEU A1186     205.408 195.447 123.273  1.00 69.88           C  
ATOM   5290  CG  LEU A1186     203.895 195.253 123.042  1.00 71.78           C  
ATOM   5291  CD1 LEU A1186     203.390 193.835 123.269  1.00 67.98           C  
ATOM   5292  CD2 LEU A1186     203.109 196.195 123.952  1.00 66.36           C  
ATOM   5293  N   ASN A1187     208.678 195.533 122.629  1.00 66.30           N  
ATOM   5294  CA  ASN A1187     209.917 196.192 122.190  1.00 67.98           C  
ATOM   5295  C   ASN A1187     210.497 195.507 120.937  1.00 71.41           C  
ATOM   5296  O   ASN A1187     210.930 196.178 119.998  1.00 73.54           O  
ATOM   5297  CB  ASN A1187     210.944 196.213 123.338  1.00 68.96           C  
ATOM   5298  CG  ASN A1187     210.752 197.386 124.278  1.00 73.01           C  
ATOM   5299  OD1 ASN A1187     211.196 198.494 124.015  1.00 74.39           O  
ATOM   5300  ND2 ASN A1187     210.101 197.197 125.393  1.00 74.56           N  
ATOM   5301  N   GLU A1188     210.473 194.171 120.892  1.00 70.51           N  
ATOM   5302  CA  GLU A1188     210.930 193.385 119.741  1.00 66.46           C  
ATOM   5303  C   GLU A1188     210.109 193.669 118.471  1.00 70.02           C  
ATOM   5304  O   GLU A1188     210.700 193.961 117.436  1.00 76.20           O  
ATOM   5305  CB  GLU A1188     210.979 191.895 120.123  1.00 65.50           C  
ATOM   5306  CG  GLU A1188     211.312 190.934 118.968  1.00 70.51           C  
ATOM   5307  CD  GLU A1188     210.081 190.277 118.311  1.00 72.79           C  
ATOM   5308  OE1 GLU A1188     210.027 190.199 117.063  1.00 75.96           O  
ATOM   5309  OE2 GLU A1188     209.206 189.747 119.026  1.00 71.87           O1-
ATOM   5310  N   VAL A1189     208.774 193.659 118.514  1.00 68.59           N  
ATOM   5311  CA  VAL A1189     207.952 193.962 117.329  1.00 62.29           C  
ATOM   5312  C   VAL A1189     207.912 195.447 116.989  1.00 64.24           C  
ATOM   5313  O   VAL A1189     207.656 195.775 115.841  1.00 71.80           O  
ATOM   5314  CB  VAL A1189     206.531 193.391 117.402  1.00 55.19           C  
ATOM   5315  CG1 VAL A1189     206.546 191.879 117.607  1.00 57.06           C  
ATOM   5316  CG2 VAL A1189     205.700 194.074 118.475  1.00 62.67           C  
ATOM   5317  N   ALA A1190     208.235 196.366 117.902  1.00 64.03           N  
ATOM   5318  CA  ALA A1190     208.405 197.770 117.523  1.00 67.24           C  
ATOM   5319  C   ALA A1190     209.574 197.930 116.542  1.00 72.56           C  
ATOM   5320  O   ALA A1190     209.463 198.669 115.561  1.00 78.32           O  
ATOM   5321  CB  ALA A1190     208.625 198.633 118.765  1.00 70.07           C  
ATOM   5322  N   LYS A1191     210.662 197.175 116.745  1.00 75.21           N  
ATOM   5323  CA  LYS A1191     211.733 197.038 115.747  1.00 80.84           C  
ATOM   5324  C   LYS A1191     211.302 196.171 114.559  1.00 79.13           C  
ATOM   5325  O   LYS A1191     211.249 196.658 113.433  1.00 76.11           O  
ATOM   5326  CB  LYS A1191     213.046 196.551 116.388  1.00 82.55           C  
ATOM   5327  CG  LYS A1191     213.585 197.589 117.389  1.00 93.29           C  
ATOM   5328  CD  LYS A1191     215.002 197.254 117.876  1.00 99.54           C  
ATOM   5329  CE  LYS A1191     215.489 198.324 118.860  1.00107.59           C  
ATOM   5330  NZ  LYS A1191     216.910 198.139 119.237  1.00113.80           N  
ATOM   5331  N   ASN A1192     210.936 194.911 114.789  1.00 75.62           N  
ATOM   5332  CA  ASN A1192     210.641 193.934 113.739  1.00 72.66           C  
ATOM   5333  C   ASN A1192     209.393 194.220 112.883  1.00 73.14           C  
ATOM   5334  O   ASN A1192     209.168 193.524 111.898  1.00 72.54           O  
ATOM   5335  CB  ASN A1192     210.634 192.518 114.346  1.00 69.50           C  
ATOM   5336  CG  ASN A1192     212.017 192.040 114.748  1.00 72.59           C  
ATOM   5337  OD1 ASN A1192     213.039 192.633 114.442  1.00 70.66           O  
ATOM   5338  ND2 ASN A1192     212.108 190.923 115.418  1.00 74.51           N  
ATOM   5339  N   LEU A1193     208.583 195.236 113.182  1.00 67.86           N  
ATOM   5340  CA  LEU A1193     207.531 195.701 112.272  1.00 66.34           C  
ATOM   5341  C   LEU A1193     208.083 196.542 111.104  1.00 78.82           C  
ATOM   5342  O   LEU A1193     207.460 196.586 110.047  1.00 80.75           O  
ATOM   5343  CB  LEU A1193     206.426 196.391 113.089  1.00 66.44           C  
ATOM   5344  CG  LEU A1193     205.142 196.758 112.331  1.00 68.99           C  
ATOM   5345  CD1 LEU A1193     204.463 195.549 111.695  1.00 67.03           C  
ATOM   5346  CD2 LEU A1193     204.137 197.369 113.316  1.00 67.87           C  
ATOM   5347  N   ASN A1194     209.294 197.111 111.215  1.00 92.41           N  
ATOM   5348  CA  ASN A1194     209.979 197.767 110.088  1.00 82.08           C  
ATOM   5349  C   ASN A1194     210.360 196.797 108.952  1.00 77.43           C  
ATOM   5350  O   ASN A1194     210.452 197.190 107.786  1.00 73.55           O  
ATOM   5351  CB  ASN A1194     211.213 198.533 110.600  1.00 86.91           C  
ATOM   5352  CG  ASN A1194     211.136 199.993 110.214  1.00 91.62           C  
ATOM   5353  OD1 ASN A1194     210.137 200.625 110.521  1.00 91.56           O  
ATOM   5354  ND2 ASN A1194     212.206 200.585 109.710  1.00 95.03           N  
ATOM   5355  N   GLU A1195     210.488 195.508 109.272  1.00 71.93           N  
ATOM   5356  CA  GLU A1195     210.652 194.437 108.280  1.00 72.71           C  
ATOM   5357  C   GLU A1195     209.403 194.215 107.414  1.00 67.95           C  
ATOM   5358  O   GLU A1195     209.455 193.457 106.449  1.00 67.36           O  
ATOM   5359  CB  GLU A1195     211.041 193.126 108.971  1.00 69.29           C  
ATOM   5360  CG  GLU A1195     212.359 193.217 109.745  1.00 67.79           C  
ATOM   5361  CD  GLU A1195     212.852 191.818 110.117  1.00 72.62           C  
ATOM   5362  OE1 GLU A1195     212.227 191.166 110.981  1.00 75.95           O  
ATOM   5363  OE2 GLU A1195     213.860 191.351 109.542  1.00 77.77           O1-
ATOM   5364  N   SER A1196     208.290 194.889 107.723  1.00 66.17           N  
ATOM   5365  CA  SER A1196     207.067 194.886 106.916  1.00 64.94           C  
ATOM   5366  C   SER A1196     206.629 196.295 106.495  1.00 68.64           C  
ATOM   5367  O   SER A1196     205.481 196.494 106.111  1.00 76.32           O  
ATOM   5368  CB  SER A1196     205.974 194.098 107.646  1.00 67.64           C  
ATOM   5369  OG  SER A1196     205.331 193.215 106.758  1.00 65.79           O  
ATOM   5370  N   LEU A1197     207.519 197.288 106.569  1.00 68.46           N  
ATOM   5371  CA  LEU A1197     207.262 198.650 106.093  1.00 70.34           C  
ATOM   5372  C   LEU A1197     207.145 198.697 104.555  1.00 68.97           C  
ATOM   5373  O   LEU A1197     208.141 198.685 103.830  1.00 78.45           O  
ATOM   5374  CB  LEU A1197     208.361 199.572 106.650  1.00 70.64           C  
ATOM   5375  CG  LEU A1197     208.197 201.061 106.298  1.00 75.86           C  
ATOM   5376  CD1 LEU A1197     206.915 201.644 106.893  1.00 76.83           C  
ATOM   5377  CD2 LEU A1197     209.383 201.849 106.842  1.00 79.59           C  
TER    5378      LEU A1197                                                      
ATOM   5379  N   ASN B 703     226.559 208.824 262.042  1.00 77.94           N  
ATOM   5380  CA  ASN B 703     225.322 209.070 262.831  1.00 79.99           C  
ATOM   5381  C   ASN B 703     224.341 209.976 262.064  1.00 75.70           C  
ATOM   5382  O   ASN B 703     224.095 211.116 262.459  1.00 70.89           O  
ATOM   5383  CB  ASN B 703     225.653 209.634 264.239  1.00 85.22           C  
ATOM   5384  CG  ASN B 703     226.394 210.974 264.241  1.00 90.78           C  
ATOM   5385  OD1 ASN B 703     227.130 211.301 263.322  1.00 86.69           O  
ATOM   5386  ND2 ASN B 703     226.251 211.788 265.265  1.00 91.46           N  
ATOM   5387  N   SER B 704     223.775 209.509 260.946  1.00 76.06           N  
ATOM   5388  CA  SER B 704     223.212 210.411 259.919  1.00 71.63           C  
ATOM   5389  C   SER B 704     221.906 211.108 260.327  1.00 71.18           C  
ATOM   5390  O   SER B 704     221.892 212.325 260.525  1.00 74.70           O  
ATOM   5391  CB  SER B 704     223.055 209.664 258.591  1.00 74.11           C  
ATOM   5392  OG  SER B 704     222.218 208.532 258.720  1.00 72.95           O  
ATOM   5393  N   VAL B 705     220.803 210.363 260.465  1.00 65.31           N  
ATOM   5394  CA  VAL B 705     219.462 210.940 260.694  1.00 67.15           C  
ATOM   5395  C   VAL B 705     218.717 210.324 261.879  1.00 66.91           C  
ATOM   5396  O   VAL B 705     217.908 211.005 262.499  1.00 66.67           O  
ATOM   5397  CB  VAL B 705     218.656 210.957 259.373  1.00 65.81           C  
ATOM   5398  CG1 VAL B 705     218.219 209.569 258.892  1.00 65.74           C  
ATOM   5399  CG2 VAL B 705     217.428 211.861 259.487  1.00 69.59           C  
ATOM   5400  N   ALA B 706     219.061 209.096 262.274  1.00 65.85           N  
ATOM   5401  CA  ALA B 706     218.403 208.359 263.353  1.00 59.53           C  
ATOM   5402  C   ALA B 706     218.409 209.049 264.721  1.00 59.42           C  
ATOM   5403  O   ALA B 706     217.594 208.696 265.566  1.00 57.82           O  
ATOM   5404  CB  ALA B 706     219.050 206.976 263.469  1.00 56.06           C  
ATOM   5405  N   TYR B 707     219.296 210.029 264.921  1.00 59.90           N  
ATOM   5406  CA  TYR B 707     219.474 210.794 266.159  1.00 53.32           C  
ATOM   5407  C   TYR B 707     219.367 212.323 265.973  1.00 60.15           C  
ATOM   5408  O   TYR B 707     219.651 213.089 266.891  1.00 67.38           O  
ATOM   5409  CB  TYR B 707     220.822 210.415 266.779  1.00 50.43           C  
ATOM   5410  CG  TYR B 707     221.143 208.934 266.801  1.00 53.74           C  
ATOM   5411  CD1 TYR B 707     222.148 208.413 265.972  1.00 50.25           C  
ATOM   5412  CD2 TYR B 707     220.477 208.087 267.703  1.00 59.60           C  
ATOM   5413  CE1 TYR B 707     222.543 207.067 266.101  1.00 60.35           C  
ATOM   5414  CE2 TYR B 707     220.859 206.739 267.831  1.00 54.55           C  
ATOM   5415  CZ  TYR B 707     221.915 206.237 267.050  1.00 60.82           C  
ATOM   5416  OH  TYR B 707     222.368 204.977 267.248  1.00 63.64           O  
ATOM   5417  N   SER B 708     218.993 212.800 264.786  1.00 64.16           N  
ATOM   5418  CA  SER B 708     218.762 214.232 264.535  1.00 62.76           C  
ATOM   5419  C   SER B 708     217.464 214.694 265.186  1.00 57.48           C  
ATOM   5420  O   SER B 708     216.487 213.947 265.233  1.00 62.54           O  
ATOM   5421  CB  SER B 708     218.736 214.509 263.030  1.00 74.52           C  
ATOM   5422  OG  SER B 708     217.643 213.879 262.380  1.00 85.35           O  
ATOM   5423  N   ASN B 709     217.407 215.900 265.735  1.00 54.76           N  
ATOM   5424  CA  ASN B 709     216.089 216.318 266.219  1.00 61.56           C  
ATOM   5425  C   ASN B 709     215.514 217.490 265.527  1.00 59.99           C  
ATOM   5426  O   ASN B 709     216.111 218.551 265.346  1.00 61.74           O  
ATOM   5427  CB  ASN B 709     215.856 216.264 267.696  1.00 63.69           C  
ATOM   5428  CG  ASN B 709     216.724 217.186 268.411  1.00 65.75           C  
ATOM   5429  OD1 ASN B 709     217.047 218.257 267.921  1.00 70.37           O  
ATOM   5430  ND2 ASN B 709     217.103 216.803 269.573  1.00 66.27           N  
ATOM   5431  N   ASN B 710     214.294 217.218 265.147  1.00 53.28           N  
ATOM   5432  CA  ASN B 710     213.503 218.103 264.293  1.00 50.06           C  
ATOM   5433  C   ASN B 710     212.075 218.214 264.841  1.00 44.81           C  
ATOM   5434  O   ASN B 710     211.580 217.325 265.533  1.00 48.76           O  
ATOM   5435  CB  ASN B 710     213.569 217.660 262.825  1.00 63.04           C  
ATOM   5436  CG  ASN B 710     213.104 216.238 262.555  1.00 60.82           C  
ATOM   5437  OD1 ASN B 710     212.897 215.406 263.417  1.00 46.53           O  
ATOM   5438  ND2 ASN B 710     212.924 215.917 261.304  1.00 57.21           N  
ATOM   5439  N   SER B 711     211.424 219.347 264.574  1.00 47.45           N  
ATOM   5440  CA  SER B 711     210.062 219.663 265.016  1.00 53.65           C  
ATOM   5441  C   SER B 711     209.030 218.811 264.268  1.00 52.99           C  
ATOM   5442  O   SER B 711     208.886 218.936 263.050  1.00 54.46           O  
ATOM   5443  CB  SER B 711     209.765 221.150 264.785  1.00 56.13           C  
ATOM   5444  OG  SER B 711     210.773 221.994 265.307  1.00 61.50           O  
ATOM   5445  N   ILE B 712     208.286 217.967 264.979  1.00 49.82           N  
ATOM   5446  CA  ILE B 712     207.259 217.079 264.428  1.00 42.39           C  
ATOM   5447  C   ILE B 712     205.900 217.426 265.004  1.00 46.05           C  
ATOM   5448  O   ILE B 712     205.751 217.504 266.219  1.00 54.42           O  
ATOM   5449  CB  ILE B 712     207.645 215.616 264.697  1.00 42.05           C  
ATOM   5450  CG1 ILE B 712     208.752 215.258 263.691  1.00 47.08           C  
ATOM   5451  CG2 ILE B 712     206.447 214.655 264.581  1.00 47.94           C  
ATOM   5452  CD1 ILE B 712     209.161 213.794 263.712  1.00 54.75           C  
ATOM   5453  N   ALA B 713     204.893 217.602 264.151  1.00 46.09           N  
ATOM   5454  CA  ALA B 713     203.524 217.796 264.601  1.00 48.77           C  
ATOM   5455  C   ALA B 713     202.976 216.502 265.204  1.00 52.60           C  
ATOM   5456  O   ALA B 713     203.034 215.428 264.598  1.00 46.97           O  
ATOM   5457  CB  ALA B 713     202.657 218.316 263.453  1.00 58.44           C  
ATOM   5458  N   ILE B 714     202.467 216.615 266.426  1.00 61.80           N  
ATOM   5459  CA  ILE B 714     201.850 215.537 267.194  1.00 53.15           C  
ATOM   5460  C   ILE B 714     200.457 216.035 267.590  1.00 54.84           C  
ATOM   5461  O   ILE B 714     200.361 217.148 268.110  1.00 57.38           O  
ATOM   5462  CB  ILE B 714     202.719 215.144 268.406  1.00 39.91           C  
ATOM   5463  CG1 ILE B 714     204.125 214.697 267.932  1.00 40.24           C  
ATOM   5464  CG2 ILE B 714     202.007 214.051 269.214  1.00 44.76           C  
ATOM   5465  CD1 ILE B 714     205.054 214.159 269.016  1.00 36.80           C  
ATOM   5466  N   PRO B 715     199.373 215.279 267.336  1.00 52.85           N  
ATOM   5467  CA  PRO B 715     198.015 215.737 267.594  1.00 53.49           C  
ATOM   5468  C   PRO B 715     197.794 216.200 269.030  1.00 58.13           C  
ATOM   5469  O   PRO B 715     197.937 215.430 269.981  1.00 57.64           O  
ATOM   5470  CB  PRO B 715     197.108 214.575 267.228  1.00 52.43           C  
ATOM   5471  CG  PRO B 715     197.900 213.881 266.125  1.00 57.12           C  
ATOM   5472  CD  PRO B 715     199.337 214.029 266.605  1.00 53.28           C  
ATOM   5473  N   THR B 716     197.447 217.473 269.193  1.00 64.47           N  
ATOM   5474  CA  THR B 716     197.173 218.069 270.496  1.00 62.49           C  
ATOM   5475  C   THR B 716     195.738 217.749 270.861  1.00 54.79           C  
ATOM   5476  O   THR B 716     195.465 217.362 271.992  1.00 49.99           O  
ATOM   5477  CB  THR B 716     197.369 219.589 270.524  1.00 65.83           C  
ATOM   5478  OG1 THR B 716     198.694 219.918 270.197  1.00 75.31           O  
ATOM   5479  CG2 THR B 716     197.120 220.195 271.898  1.00 55.53           C  
ATOM   5480  N   ASN B 717     194.837 217.860 269.884  1.00 62.84           N  
ATOM   5481  CA  ASN B 717     193.410 217.652 270.135  1.00 66.69           C  
ATOM   5482  C   ASN B 717     192.591 217.200 268.937  1.00 60.02           C  
ATOM   5483  O   ASN B 717     193.044 217.272 267.796  1.00 66.17           O  
ATOM   5484  CB  ASN B 717     192.778 218.905 270.718  1.00 67.17           C  
ATOM   5485  CG  ASN B 717     192.605 218.813 272.206  1.00 71.36           C  
ATOM   5486  OD1 ASN B 717     192.550 217.705 272.757  1.00 69.40           O  
ATOM   5487  ND2 ASN B 717     192.531 219.987 272.862  1.00 72.64           N  
ATOM   5488  N   PHE B 718     191.385 216.700 269.177  1.00 55.84           N  
ATOM   5489  CA  PHE B 718     190.591 216.176 268.067  1.00 55.95           C  
ATOM   5490  C   PHE B 718     189.242 216.819 267.798  1.00 59.19           C  
ATOM   5491  O   PHE B 718     188.506 217.164 268.717  1.00 67.45           O  
ATOM   5492  CB  PHE B 718     190.438 214.674 268.245  1.00 52.78           C  
ATOM   5493  CG  PHE B 718     191.751 213.957 268.421  1.00 48.70           C  
ATOM   5494  CD1 PHE B 718     192.659 213.853 267.360  1.00 46.52           C  
ATOM   5495  CD2 PHE B 718     192.073 213.418 269.671  1.00 50.18           C  
ATOM   5496  CE1 PHE B 718     193.878 213.195 267.544  1.00 38.53           C  
ATOM   5497  CE2 PHE B 718     193.293 212.764 269.858  1.00 50.97           C  
ATOM   5498  CZ  PHE B 718     194.195 212.657 268.796  1.00 45.28           C  
ATOM   5499  N   THR B 719     188.895 216.882 266.517  1.00 53.98           N  
ATOM   5500  CA  THR B 719     187.555 217.148 266.000  1.00 55.66           C  
ATOM   5501  C   THR B 719     187.028 215.867 265.372  1.00 54.17           C  
ATOM   5502  O   THR B 719     187.753 215.158 264.676  1.00 54.47           O  
ATOM   5503  CB  THR B 719     187.574 218.312 265.002  1.00 55.37           C  
ATOM   5504  OG1 THR B 719     187.588 219.522 265.716  1.00 73.23           O  
ATOM   5505  CG2 THR B 719     186.364 218.409 264.081  1.00 52.87           C  
ATOM   5506  N   ILE B 720     185.770 215.548 265.638  1.00 63.22           N  
ATOM   5507  CA  ILE B 720     185.068 214.457 264.968  1.00 51.42           C  
ATOM   5508  C   ILE B 720     184.658 214.862 263.548  1.00 54.12           C  
ATOM   5509  O   ILE B 720     184.316 216.007 263.271  1.00 57.27           O  
ATOM   5510  CB  ILE B 720     183.928 213.954 265.865  1.00 54.55           C  
ATOM   5511  CG1 ILE B 720     183.160 212.757 265.284  1.00 43.80           C  
ATOM   5512  CG2 ILE B 720     182.926 215.045 266.226  1.00 60.24           C  
ATOM   5513  CD1 ILE B 720     183.999 211.482 265.359  1.00 41.78           C  
ATOM   5514  N   SER B 721     184.758 213.926 262.615  1.00 59.29           N  
ATOM   5515  CA  SER B 721     184.630 214.167 261.183  1.00 54.18           C  
ATOM   5516  C   SER B 721     184.066 212.950 260.456  1.00 53.29           C  
ATOM   5517  O   SER B 721     184.094 211.840 260.980  1.00 58.87           O  
ATOM   5518  CB  SER B 721     185.988 214.555 260.614  1.00 52.79           C  
ATOM   5519  OG  SER B 721     186.904 213.503 260.719  1.00 52.06           O  
ATOM   5520  N   VAL B 722     183.540 213.141 259.251  1.00 57.00           N  
ATOM   5521  CA  VAL B 722     183.107 212.045 258.385  1.00 57.39           C  
ATOM   5522  C   VAL B 722     183.623 212.248 256.976  1.00 58.94           C  
ATOM   5523  O   VAL B 722     183.721 213.372 256.499  1.00 63.31           O  
ATOM   5524  CB  VAL B 722     181.591 211.816 258.407  1.00 52.70           C  
ATOM   5525  CG1 VAL B 722     181.094 211.587 259.830  1.00 58.30           C  
ATOM   5526  CG2 VAL B 722     180.798 212.962 257.792  1.00 58.03           C  
ATOM   5527  N   THR B 723     183.959 211.166 256.294  1.00 54.39           N  
ATOM   5528  CA  THR B 723     184.402 211.189 254.899  1.00 53.12           C  
ATOM   5529  C   THR B 723     183.372 210.477 254.038  1.00 58.43           C  
ATOM   5530  O   THR B 723     182.821 209.467 254.458  1.00 63.76           O  
ATOM   5531  CB  THR B 723     185.787 210.560 254.748  1.00 52.86           C  
ATOM   5532  OG1 THR B 723     186.695 211.276 255.554  1.00 61.34           O  
ATOM   5533  CG2 THR B 723     186.313 210.611 253.317  1.00 56.46           C  
ATOM   5534  N   THR B 724     183.108 210.990 252.844  1.00 58.88           N  
ATOM   5535  CA  THR B 724     182.477 210.226 251.767  1.00 56.83           C  
ATOM   5536  C   THR B 724     183.593 209.881 250.794  1.00 56.59           C  
ATOM   5537  O   THR B 724     184.187 210.788 250.224  1.00 59.51           O  
ATOM   5538  CB  THR B 724     181.384 211.054 251.082  1.00 65.91           C  
ATOM   5539  OG1 THR B 724     180.419 211.465 252.024  1.00 75.17           O  
ATOM   5540  CG2 THR B 724     180.627 210.276 250.013  1.00 63.43           C  
ATOM   5541  N   GLU B 725     183.934 208.609 250.631  1.00 51.09           N  
ATOM   5542  CA  GLU B 725     184.996 208.164 249.723  1.00 50.30           C  
ATOM   5543  C   GLU B 725     184.394 207.321 248.605  1.00 53.78           C  
ATOM   5544  O   GLU B 725     183.806 206.286 248.892  1.00 52.97           O  
ATOM   5545  CB  GLU B 725     186.078 207.392 250.498  1.00 49.07           C  
ATOM   5546  CG  GLU B 725     187.016 206.585 249.583  1.00 42.40           C  
ATOM   5547  CD  GLU B 725     188.430 206.287 250.109  1.00 45.03           C  
ATOM   5548  OE1 GLU B 725     188.684 206.132 251.321  1.00 42.84           O  
ATOM   5549  OE2 GLU B 725     189.341 206.097 249.275  1.00 48.77           O1-
ATOM   5550  N   ILE B 726     184.555 207.723 247.342  1.00 57.63           N  
ATOM   5551  CA  ILE B 726     183.990 207.024 246.176  1.00 50.07           C  
ATOM   5552  C   ILE B 726     185.077 206.203 245.466  1.00 50.82           C  
ATOM   5553  O   ILE B 726     186.099 206.753 245.064  1.00 54.87           O  
ATOM   5554  CB  ILE B 726     183.344 208.043 245.211  1.00 56.14           C  
ATOM   5555  CG1 ILE B 726     182.264 208.922 245.882  1.00 56.05           C  
ATOM   5556  CG2 ILE B 726     182.716 207.338 243.999  1.00 58.28           C  
ATOM   5557  CD1 ILE B 726     182.399 210.395 245.521  1.00 60.31           C  
ATOM   5558  N   LEU B 727     184.858 204.897 245.294  1.00 44.83           N  
ATOM   5559  CA  LEU B 727     185.694 203.983 244.506  1.00 45.45           C  
ATOM   5560  C   LEU B 727     184.870 203.317 243.392  1.00 50.80           C  
ATOM   5561  O   LEU B 727     183.913 202.609 243.702  1.00 54.60           O  
ATOM   5562  CB  LEU B 727     186.257 202.852 245.380  1.00 36.93           C  
ATOM   5563  CG  LEU B 727     187.559 203.142 246.117  1.00 34.74           C  
ATOM   5564  CD1 LEU B 727     187.358 204.094 247.273  1.00 39.37           C  
ATOM   5565  CD2 LEU B 727     188.085 201.845 246.717  1.00 21.72           C  
ATOM   5566  N   PRO B 728     185.255 203.417 242.112  1.00 47.18           N  
ATOM   5567  CA  PRO B 728     184.692 202.567 241.080  1.00 42.11           C  
ATOM   5568  C   PRO B 728     185.201 201.132 241.227  1.00 40.73           C  
ATOM   5569  O   PRO B 728     186.395 200.900 241.402  1.00 40.16           O  
ATOM   5570  CB  PRO B 728     185.109 203.207 239.768  1.00 45.36           C  
ATOM   5571  CG  PRO B 728     186.403 203.928 240.110  1.00 42.79           C  
ATOM   5572  CD  PRO B 728     186.227 204.339 241.557  1.00 43.91           C  
ATOM   5573  N   VAL B 729     184.291 200.164 241.156  1.00 42.32           N  
ATOM   5574  CA  VAL B 729     184.566 198.723 241.301  1.00 40.22           C  
ATOM   5575  C   VAL B 729     184.300 197.941 240.015  1.00 49.12           C  
ATOM   5576  O   VAL B 729     184.761 196.813 239.866  1.00 52.58           O  
ATOM   5577  CB  VAL B 729     183.800 198.099 242.478  1.00 48.59           C  
ATOM   5578  CG1 VAL B 729     184.068 198.861 243.776  1.00 57.16           C  
ATOM   5579  CG2 VAL B 729     182.286 198.013 242.266  1.00 48.38           C  
ATOM   5580  N   SER B 730     183.577 198.514 239.063  1.00 55.73           N  
ATOM   5581  CA  SER B 730     183.256 197.900 237.774  1.00 50.33           C  
ATOM   5582  C   SER B 730     183.266 198.940 236.660  1.00 49.57           C  
ATOM   5583  O   SER B 730     183.296 200.148 236.897  1.00 49.52           O  
ATOM   5584  CB  SER B 730     181.924 197.143 237.855  1.00 54.07           C  
ATOM   5585  OG  SER B 730     180.867 197.937 238.340  1.00 57.11           O  
ATOM   5586  N   MET B 731     183.321 198.456 235.425  1.00 49.49           N  
ATOM   5587  CA  MET B 731     183.324 199.267 234.213  1.00 48.29           C  
ATOM   5588  C   MET B 731     182.293 198.707 233.234  1.00 51.38           C  
ATOM   5589  O   MET B 731     182.335 197.520 232.910  1.00 60.69           O  
ATOM   5590  CB  MET B 731     184.750 199.249 233.650  1.00 42.88           C  
ATOM   5591  CG  MET B 731     184.945 200.030 232.360  1.00 47.16           C  
ATOM   5592  SD  MET B 731     186.681 200.336 232.025  1.00 30.36           S  
ATOM   5593  CE  MET B 731     186.591 201.314 230.523  1.00 29.40           C  
ATOM   5594  N   THR B 732     181.378 199.545 232.752  1.00 47.60           N  
ATOM   5595  CA  THR B 732     180.418 199.141 231.714  1.00 46.51           C  
ATOM   5596  C   THR B 732     181.140 198.802 230.407  1.00 53.24           C  
ATOM   5597  O   THR B 732     182.151 199.422 230.064  1.00 51.55           O  
ATOM   5598  CB  THR B 732     179.310 200.181 231.509  1.00 44.13           C  
ATOM   5599  OG1 THR B 732     178.314 199.654 230.661  1.00 51.54           O  
ATOM   5600  CG2 THR B 732     179.792 201.485 230.881  1.00 41.42           C  
ATOM   5601  N   LYS B 733     180.660 197.780 229.692  1.00 52.01           N  
ATOM   5602  CA  LYS B 733     181.350 197.191 228.540  1.00 48.27           C  
ATOM   5603  C   LYS B 733     181.128 198.024 227.283  1.00 53.30           C  
ATOM   5604  O   LYS B 733     180.161 197.847 226.544  1.00 53.17           O  
ATOM   5605  CB  LYS B 733     180.928 195.728 228.360  1.00 51.94           C  
ATOM   5606  CG  LYS B 733     181.120 194.857 229.611  1.00 56.29           C  
ATOM   5607  CD  LYS B 733     182.546 194.826 230.179  1.00 52.87           C  
ATOM   5608  CE  LYS B 733     182.629 193.989 231.465  1.00 50.14           C  
ATOM   5609  NZ  LYS B 733     182.266 192.570 231.253  1.00 50.81           N  
ATOM   5610  N   THR B 734     182.033 198.963 227.054  1.00 54.16           N  
ATOM   5611  CA  THR B 734     182.065 199.894 225.925  1.00 48.42           C  
ATOM   5612  C   THR B 734     182.455 199.213 224.609  1.00 47.83           C  
ATOM   5613  O   THR B 734     183.434 199.613 223.975  1.00 49.04           O  
ATOM   5614  CB  THR B 734     183.016 201.055 226.256  1.00 51.32           C  
ATOM   5615  OG1 THR B 734     184.273 200.549 226.652  1.00 47.96           O  
ATOM   5616  CG2 THR B 734     182.495 201.934 227.388  1.00 53.08           C  
ATOM   5617  N   SER B 735     181.720 198.180 224.189  1.00 45.43           N  
ATOM   5618  CA  SER B 735     181.890 197.529 222.884  1.00 43.82           C  
ATOM   5619  C   SER B 735     181.792 198.540 221.737  1.00 42.70           C  
ATOM   5620  O   SER B 735     181.086 199.546 221.827  1.00 45.19           O  
ATOM   5621  CB  SER B 735     180.877 196.388 222.722  1.00 45.64           C  
ATOM   5622  OG  SER B 735     179.535 196.823 222.865  1.00 51.30           O  
ATOM   5623  N   VAL B 736     182.543 198.318 220.663  1.00 43.80           N  
ATOM   5624  CA  VAL B 736     182.702 199.269 219.554  1.00 45.92           C  
ATOM   5625  C   VAL B 736     182.349 198.611 218.226  1.00 53.29           C  
ATOM   5626  O   VAL B 736     182.871 197.548 217.900  1.00 51.89           O  
ATOM   5627  CB  VAL B 736     184.104 199.911 219.594  1.00 38.26           C  
ATOM   5628  CG1 VAL B 736     185.267 198.924 219.485  1.00 32.82           C  
ATOM   5629  CG2 VAL B 736     184.289 200.968 218.516  1.00 34.58           C  
ATOM   5630  N   ASP B 737     181.522 199.292 217.444  1.00 57.63           N  
ATOM   5631  CA  ASP B 737     181.193 198.829 216.113  1.00 50.40           C  
ATOM   5632  C   ASP B 737     182.383 199.327 215.310  1.00 52.80           C  
ATOM   5633  O   ASP B 737     182.605 200.532 215.215  1.00 51.38           O  
ATOM   5634  CB  ASP B 737     179.905 199.478 215.618  1.00 47.62           C  
ATOM   5635  CG  ASP B 737     179.546 199.053 214.215  1.00 59.62           C  
ATOM   5636  OD1 ASP B 737     180.360 198.351 213.581  1.00 63.58           O  
ATOM   5637  OD2 ASP B 737     178.451 199.420 213.742  1.00 63.77           O1-
ATOM   5638  N   CYS B 738     183.069 198.460 214.618  1.00 55.65           N  
ATOM   5639  CA  CYS B 738     184.309 198.915 214.012  1.00 46.57           C  
ATOM   5640  C   CYS B 738     184.162 199.631 212.694  1.00 48.58           C  
ATOM   5641  O   CYS B 738     185.026 200.409 212.291  1.00 43.71           O  
ATOM   5642  CB  CYS B 738     185.324 197.799 214.093  1.00 43.79           C  
ATOM   5643  SG  CYS B 738     184.918 196.955 215.643  1.00 56.17           S  
ATOM   5644  N   THR B 739     183.056 199.365 212.022  1.00 53.00           N  
ATOM   5645  CA  THR B 739     182.744 200.148 210.834  1.00 52.56           C  
ATOM   5646  C   THR B 739     182.502 201.617 211.166  1.00 50.33           C  
ATOM   5647  O   THR B 739     183.193 202.497 210.657  1.00 56.48           O  
ATOM   5648  CB  THR B 739     181.518 199.591 210.089  1.00 56.29           C  
ATOM   5649  OG1 THR B 739     180.400 199.528 210.982  1.00 64.62           O  
ATOM   5650  CG2 THR B 739     181.810 198.202 209.549  1.00 47.77           C  
ATOM   5651  N   MET B 740     181.520 201.876 212.021  1.00 46.18           N  
ATOM   5652  CA  MET B 740     181.183 203.249 212.408  1.00 44.70           C  
ATOM   5653  C   MET B 740     182.361 204.003 213.036  1.00 42.60           C  
ATOM   5654  O   MET B 740     182.491 205.202 212.793  1.00 43.82           O  
ATOM   5655  CB  MET B 740     179.975 203.283 213.350  1.00 46.27           C  
ATOM   5656  CG  MET B 740     178.692 202.938 212.592  1.00 55.77           C  
ATOM   5657  SD  MET B 740     177.169 203.218 213.531  1.00 72.09           S  
ATOM   5658  CE  MET B 740     175.953 202.659 212.306  1.00 55.92           C  
ATOM   5659  N   TYR B 741     183.245 203.341 213.792  1.00 46.07           N  
ATOM   5660  CA  TYR B 741     184.437 204.005 214.334  1.00 40.58           C  
ATOM   5661  C   TYR B 741     185.400 204.457 213.232  1.00 44.42           C  
ATOM   5662  O   TYR B 741     185.709 205.638 213.132  1.00 45.98           O  
ATOM   5663  CB  TYR B 741     185.162 203.103 215.344  1.00 37.40           C  
ATOM   5664  CG  TYR B 741     186.147 203.877 216.199  1.00 32.48           C  
ATOM   5665  CD1 TYR B 741     187.411 204.239 215.696  1.00 32.84           C  
ATOM   5666  CD2 TYR B 741     185.770 204.286 217.489  1.00 31.07           C  
ATOM   5667  CE1 TYR B 741     188.283 205.039 216.455  1.00 27.69           C  
ATOM   5668  CE2 TYR B 741     186.639 205.077 218.257  1.00 31.28           C  
ATOM   5669  CZ  TYR B 741     187.887 205.473 217.733  1.00 29.81           C  
ATOM   5670  OH  TYR B 741     188.679 206.296 218.467  1.00 35.70           O  
ATOM   5671  N   ILE B 742     185.877 203.528 212.402  1.00 47.72           N  
ATOM   5672  CA  ILE B 742     186.901 203.790 211.384  1.00 38.72           C  
ATOM   5673  C   ILE B 742     186.326 204.538 210.191  1.00 42.48           C  
ATOM   5674  O   ILE B 742     186.831 205.597 209.849  1.00 39.70           O  
ATOM   5675  CB  ILE B 742     187.567 202.474 210.945  1.00 29.39           C  
ATOM   5676  CG1 ILE B 742     188.465 201.940 212.071  1.00 30.31           C  
ATOM   5677  CG2 ILE B 742     188.387 202.638 209.660  1.00 34.77           C  
ATOM   5678  CD1 ILE B 742     188.547 200.422 212.034  1.00 33.01           C  
ATOM   5679  N   CYS B 743     185.389 203.923 209.472  1.00 47.22           N  
ATOM   5680  CA  CYS B 743     184.856 204.507 208.232  1.00 35.36           C  
ATOM   5681  C   CYS B 743     183.620 205.402 208.366  1.00 39.54           C  
ATOM   5682  O   CYS B 743     183.499 206.401 207.657  1.00 47.32           O  
ATOM   5683  CB  CYS B 743     184.638 203.393 207.184  1.00 41.19           C  
ATOM   5684  SG  CYS B 743     184.220 203.878 205.481  1.00 94.65           S  
ATOM   5685  N   GLY B 744     182.707 205.052 209.265  1.00 45.64           N  
ATOM   5686  CA  GLY B 744     181.505 205.846 209.457  1.00 47.15           C  
ATOM   5687  C   GLY B 744     180.461 205.600 208.384  1.00 54.04           C  
ATOM   5688  O   GLY B 744     180.055 204.459 208.162  1.00 53.73           O  
ATOM   5689  N   ASP B 745     180.023 206.663 207.715  1.00 64.33           N  
ATOM   5690  CA  ASP B 745     179.007 206.523 206.657  1.00 67.57           C  
ATOM   5691  C   ASP B 745     179.591 206.107 205.295  1.00 61.94           C  
ATOM   5692  O   ASP B 745     178.857 205.666 204.413  1.00 62.18           O  
ATOM   5693  CB  ASP B 745     178.265 207.866 206.496  1.00 66.27           C  
ATOM   5694  CG  ASP B 745     179.149 209.066 206.111  1.00 61.11           C  
ATOM   5695  OD1 ASP B 745     178.639 210.021 205.486  1.00 68.85           O  
ATOM   5696  OD2 ASP B 745     180.353 209.101 206.442  1.00 65.94           O1-
ATOM   5697  N   SER B 746     180.891 206.301 205.083  1.00 54.53           N  
ATOM   5698  CA  SER B 746     181.491 206.291 203.750  1.00 52.15           C  
ATOM   5699  C   SER B 746     181.628 204.878 203.180  1.00 52.88           C  
ATOM   5700  O   SER B 746     182.368 204.029 203.686  1.00 49.64           O  
ATOM   5701  CB  SER B 746     182.799 207.067 203.792  1.00 51.04           C  
ATOM   5702  OG  SER B 746     183.130 207.539 202.507  1.00 55.87           O  
ATOM   5703  N   THR B 747     180.837 204.604 202.145  1.00 58.69           N  
ATOM   5704  CA  THR B 747     180.523 203.239 201.710  1.00 56.62           C  
ATOM   5705  C   THR B 747     181.693 202.539 201.031  1.00 53.58           C  
ATOM   5706  O   THR B 747     181.899 201.355 201.267  1.00 52.38           O  
ATOM   5707  CB  THR B 747     179.262 203.244 200.849  1.00 48.16           C  
ATOM   5708  OG1 THR B 747     178.171 203.587 201.677  1.00 50.38           O  
ATOM   5709  CG2 THR B 747     178.931 201.895 200.239  1.00 44.32           C  
ATOM   5710  N   GLU B 748     182.540 203.240 200.285  1.00 52.52           N  
ATOM   5711  CA  GLU B 748     183.691 202.614 199.624  1.00 51.05           C  
ATOM   5712  C   GLU B 748     184.683 202.013 200.634  1.00 57.08           C  
ATOM   5713  O   GLU B 748     185.133 200.882 200.462  1.00 57.23           O  
ATOM   5714  CB  GLU B 748     184.367 203.575 198.629  1.00 54.79           C  
ATOM   5715  CG  GLU B 748     185.166 204.757 199.206  1.00 54.85           C  
ATOM   5716  CD  GLU B 748     184.326 205.806 199.943  1.00 62.26           C  
ATOM   5717  OE1 GLU B 748     183.100 205.910 199.731  1.00 66.81           O  
ATOM   5718  OE2 GLU B 748     184.905 206.555 200.756  1.00 61.60           O1-
ATOM   5719  N   CYS B 749     184.970 202.724 201.733  1.00 51.30           N  
ATOM   5720  CA  CYS B 749     185.863 202.142 202.753  1.00 44.26           C  
ATOM   5721  C   CYS B 749     185.154 201.087 203.606  1.00 44.64           C  
ATOM   5722  O   CYS B 749     185.787 200.158 204.108  1.00 45.44           O  
ATOM   5723  CB  CYS B 749     186.669 203.160 203.615  1.00 47.31           C  
ATOM   5724  SG  CYS B 749     185.969 204.507 204.637  1.00 68.67           S  
ATOM   5725  N   SER B 750     183.843 201.237 203.762  1.00 42.92           N  
ATOM   5726  CA  SER B 750     183.059 200.279 204.529  1.00 43.00           C  
ATOM   5727  C   SER B 750     183.213 198.919 203.864  1.00 40.48           C  
ATOM   5728  O   SER B 750     183.625 197.946 204.496  1.00 44.01           O  
ATOM   5729  CB  SER B 750     181.587 200.689 204.565  1.00 47.00           C  
ATOM   5730  OG  SER B 750     181.428 201.958 205.177  1.00 45.91           O  
ATOM   5731  N   ASN B 751     182.878 198.864 202.579  1.00 46.84           N  
ATOM   5732  CA  ASN B 751     183.010 197.638 201.797  1.00 48.54           C  
ATOM   5733  C   ASN B 751     184.433 197.074 201.833  1.00 50.79           C  
ATOM   5734  O   ASN B 751     184.600 195.857 201.829  1.00 50.79           O  
ATOM   5735  CB  ASN B 751     182.560 197.917 200.358  1.00 44.51           C  
ATOM   5736  CG  ASN B 751     181.098 198.299 200.211  1.00 54.55           C  
ATOM   5737  OD1 ASN B 751     180.718 198.980 199.285  1.00 61.87           O  
ATOM   5738  ND2 ASN B 751     180.226 197.868 201.077  1.00 54.10           N  
ATOM   5739  N   LEU B 752     185.463 197.917 201.924  1.00 51.00           N  
ATOM   5740  CA  LEU B 752     186.835 197.448 202.143  1.00 46.30           C  
ATOM   5741  C   LEU B 752     187.035 196.785 203.509  1.00 41.00           C  
ATOM   5742  O   LEU B 752     187.758 195.798 203.586  1.00 40.89           O  
ATOM   5743  CB  LEU B 752     187.820 198.611 201.976  1.00 41.11           C  
ATOM   5744  CG  LEU B 752     188.035 199.000 200.512  1.00 34.00           C  
ATOM   5745  CD1 LEU B 752     188.779 200.320 200.454  1.00 38.17           C  
ATOM   5746  CD2 LEU B 752     188.895 197.976 199.793  1.00 32.03           C  
ATOM   5747  N   LEU B 753     186.381 197.272 204.566  1.00 34.64           N  
ATOM   5748  CA  LEU B 753     186.493 196.719 205.918  1.00 36.62           C  
ATOM   5749  C   LEU B 753     186.217 195.199 205.957  1.00 42.04           C  
ATOM   5750  O   LEU B 753     186.927 194.499 206.670  1.00 43.79           O  
ATOM   5751  CB  LEU B 753     185.570 197.493 206.894  1.00 37.56           C  
ATOM   5752  CG  LEU B 753     186.231 198.506 207.851  1.00 35.12           C  
ATOM   5753  CD1 LEU B 753     187.209 197.822 208.790  1.00 32.54           C  
ATOM   5754  CD2 LEU B 753     186.952 199.662 207.164  1.00 34.72           C  
ATOM   5755  N   LEU B 754     185.278 194.661 205.168  1.00 40.42           N  
ATOM   5756  CA  LEU B 754     184.983 193.213 205.147  1.00 37.45           C  
ATOM   5757  C   LEU B 754     186.214 192.356 204.815  1.00 37.55           C  
ATOM   5758  O   LEU B 754     186.390 191.277 205.372  1.00 42.70           O  
ATOM   5759  CB  LEU B 754     183.837 192.943 204.157  1.00 37.06           C  
ATOM   5760  CG  LEU B 754     182.430 193.043 204.761  1.00 34.59           C  
ATOM   5761  CD1 LEU B 754     182.194 194.273 205.624  1.00 37.41           C  
ATOM   5762  CD2 LEU B 754     181.391 193.064 203.647  1.00 40.70           C  
ATOM   5763  N   GLN B 755     187.111 192.834 203.961  1.00 34.13           N  
ATOM   5764  CA  GLN B 755     188.329 192.111 203.623  1.00 40.91           C  
ATOM   5765  C   GLN B 755     189.433 192.227 204.682  1.00 42.51           C  
ATOM   5766  O   GLN B 755     190.355 191.423 204.649  1.00 47.99           O  
ATOM   5767  CB  GLN B 755     188.806 192.552 202.239  1.00 46.98           C  
ATOM   5768  CG  GLN B 755     187.984 191.910 201.099  1.00 51.05           C  
ATOM   5769  CD  GLN B 755     188.802 191.009 200.171  1.00 58.89           C  
ATOM   5770  OE1 GLN B 755     189.640 190.217 200.574  1.00 54.75           O  
ATOM   5771  NE2 GLN B 755     188.575 191.098 198.877  1.00 59.49           N  
ATOM   5772  N   TYR B 756     189.330 193.124 205.671  1.00 39.45           N  
ATOM   5773  CA  TYR B 756     190.192 193.118 206.869  1.00 28.02           C  
ATOM   5774  C   TYR B 756     189.814 192.005 207.858  1.00 31.57           C  
ATOM   5775  O   TYR B 756     190.450 191.843 208.895  1.00 36.56           O  
ATOM   5776  CB  TYR B 756     190.205 194.489 207.562  1.00 22.63           C  
ATOM   5777  CG  TYR B 756     190.901 195.592 206.790  1.00 26.43           C  
ATOM   5778  CD1 TYR B 756     192.196 195.996 207.145  1.00 21.39           C  
ATOM   5779  CD2 TYR B 756     190.252 196.231 205.724  1.00 35.53           C  
ATOM   5780  CE1 TYR B 756     192.838 197.016 206.418  1.00 18.14           C  
ATOM   5781  CE2 TYR B 756     190.881 197.261 205.006  1.00 27.27           C  
ATOM   5782  CZ  TYR B 756     192.183 197.644 205.346  1.00 20.36           C  
ATOM   5783  OH  TYR B 756     192.811 198.578 204.605  1.00 35.22           O  
ATOM   5784  N   GLY B 757     188.795 191.205 207.542  1.00 37.70           N  
ATOM   5785  CA  GLY B 757     188.393 190.061 208.345  1.00 34.71           C  
ATOM   5786  C   GLY B 757     187.591 190.451 209.575  1.00 44.88           C  
ATOM   5787  O   GLY B 757     187.126 191.580 209.711  1.00 43.92           O  
ATOM   5788  N   SER B 758     187.416 189.503 210.490  1.00 53.28           N  
ATOM   5789  CA  SER B 758     186.636 189.751 211.704  1.00 43.71           C  
ATOM   5790  C   SER B 758     187.439 190.383 212.837  1.00 41.96           C  
ATOM   5791  O   SER B 758     187.155 190.158 214.018  1.00 45.76           O  
ATOM   5792  CB  SER B 758     185.968 188.462 212.187  1.00 44.33           C  
ATOM   5793  OG  SER B 758     184.930 188.068 211.307  1.00 56.93           O  
ATOM   5794  N   PHE B 759     188.351 191.280 212.480  1.00 41.26           N  
ATOM   5795  CA  PHE B 759     189.220 191.926 213.463  1.00 32.77           C  
ATOM   5796  C   PHE B 759     188.445 192.715 214.523  1.00 37.64           C  
ATOM   5797  O   PHE B 759     188.872 192.784 215.668  1.00 45.80           O  
ATOM   5798  CB  PHE B 759     190.345 192.744 212.798  1.00 29.37           C  
ATOM   5799  CG  PHE B 759     189.969 194.156 212.464  1.00 27.37           C  
ATOM   5800  CD1 PHE B 759     190.254 195.182 213.343  1.00 23.69           C  
ATOM   5801  CD2 PHE B 759     189.320 194.453 211.281  1.00 34.44           C  
ATOM   5802  CE1 PHE B 759     189.906 196.483 213.045  1.00 30.87           C  
ATOM   5803  CE2 PHE B 759     188.968 195.752 210.976  1.00 35.24           C  
ATOM   5804  CZ  PHE B 759     189.263 196.770 211.859  1.00 37.29           C  
ATOM   5805  N   CYS B 760     187.298 193.237 214.107  1.00 39.33           N  
ATOM   5806  CA  CYS B 760     186.398 193.998 214.951  1.00 36.44           C  
ATOM   5807  C   CYS B 760     185.922 193.155 216.126  1.00 37.93           C  
ATOM   5808  O   CYS B 760     185.858 193.622 217.263  1.00 52.48           O  
ATOM   5809  CB  CYS B 760     185.185 194.412 214.119  1.00 56.98           C  
ATOM   5810  SG  CYS B 760     183.921 195.301 215.042  1.00 71.72           S  
ATOM   5811  N   THR B 761     185.590 191.904 215.828  1.00 36.00           N  
ATOM   5812  CA  THR B 761     185.083 190.952 216.823  1.00 41.13           C  
ATOM   5813  C   THR B 761     186.178 190.728 217.858  1.00 40.65           C  
ATOM   5814  O   THR B 761     185.966 190.835 219.064  1.00 40.05           O  
ATOM   5815  CB  THR B 761     184.697 189.608 216.191  1.00 47.99           C  
ATOM   5816  OG1 THR B 761     183.643 189.809 215.243  1.00 57.89           O  
ATOM   5817  CG2 THR B 761     184.228 188.639 217.259  1.00 46.54           C  
ATOM   5818  N   GLN B 762     187.355 190.412 217.340  1.00 41.58           N  
ATOM   5819  CA  GLN B 762     188.592 190.216 218.102  1.00 37.65           C  
ATOM   5820  C   GLN B 762     188.887 191.342 219.109  1.00 36.59           C  
ATOM   5821  O   GLN B 762     189.214 191.062 220.255  1.00 40.67           O  
ATOM   5822  CB  GLN B 762     189.759 190.056 217.117  1.00 41.10           C  
ATOM   5823  CG  GLN B 762     189.571 188.910 216.123  1.00 43.56           C  
ATOM   5824  CD  GLN B 762     188.957 187.660 216.717  1.00 44.67           C  
ATOM   5825  OE1 GLN B 762     187.754 187.448 216.697  1.00 46.13           O  
ATOM   5826  NE2 GLN B 762     189.762 186.771 217.239  1.00 45.09           N  
ATOM   5827  N   LEU B 763     188.703 192.602 218.719  1.00 32.55           N  
ATOM   5828  CA  LEU B 763     188.769 193.753 219.617  1.00 30.66           C  
ATOM   5829  C   LEU B 763     187.593 193.753 220.604  1.00 30.45           C  
ATOM   5830  O   LEU B 763     187.760 194.137 221.759  1.00 41.18           O  
ATOM   5831  CB  LEU B 763     188.794 195.024 218.754  1.00 27.72           C  
ATOM   5832  CG  LEU B 763     190.193 195.435 218.264  1.00 22.88           C  
ATOM   5833  CD1 LEU B 763     190.969 194.369 217.501  1.00 25.22           C  
ATOM   5834  CD2 LEU B 763     190.056 196.649 217.354  1.00 25.64           C  
ATOM   5835  N   ASN B 764     186.414 193.284 220.201  1.00 29.24           N  
ATOM   5836  CA  ASN B 764     185.271 193.192 221.096  1.00 26.30           C  
ATOM   5837  C   ASN B 764     185.339 192.012 222.067  1.00 34.60           C  
ATOM   5838  O   ASN B 764     184.787 192.134 223.150  1.00 44.26           O  
ATOM   5839  CB  ASN B 764     183.971 193.258 220.303  1.00 27.90           C  
ATOM   5840  CG  ASN B 764     183.683 194.679 219.875  1.00 37.35           C  
ATOM   5841  OD1 ASN B 764     183.251 195.506 220.659  1.00 41.47           O  
ATOM   5842  ND2 ASN B 764     183.929 195.033 218.645  1.00 39.52           N  
ATOM   5843  N   ARG B 765     186.071 190.922 221.786  1.00 35.25           N  
ATOM   5844  CA  ARG B 765     186.394 189.896 222.800  1.00 33.59           C  
ATOM   5845  C   ARG B 765     187.125 190.533 223.966  1.00 36.30           C  
ATOM   5846  O   ARG B 765     186.817 190.231 225.112  1.00 40.16           O  
ATOM   5847  CB  ARG B 765     187.254 188.756 222.223  1.00 35.56           C  
ATOM   5848  CG  ARG B 765     186.411 187.643 221.601  1.00 35.58           C  
ATOM   5849  CD  ARG B 765     187.263 186.574 220.906  1.00 44.27           C  
ATOM   5850  NE  ARG B 765     188.141 185.805 221.815  1.00 41.86           N  
ATOM   5851  CZ  ARG B 765     187.798 184.774 222.567  1.00 46.47           C  
ATOM   5852  NH1 ARG B 765     188.692 184.092 223.211  1.00 44.83           N  
ATOM   5853  NH2 ARG B 765     186.567 184.383 222.702  1.00 52.69           N  
ATOM   5854  N   ALA B 766     188.055 191.437 223.683  1.00 33.19           N  
ATOM   5855  CA  ALA B 766     188.813 192.143 224.693  1.00 31.53           C  
ATOM   5856  C   ALA B 766     187.909 193.056 225.537  1.00 38.56           C  
ATOM   5857  O   ALA B 766     187.745 192.833 226.734  1.00 48.77           O  
ATOM   5858  CB  ALA B 766     189.945 192.885 223.980  1.00 33.49           C  
ATOM   5859  N   LEU B 767     187.262 194.040 224.906  1.00 34.64           N  
ATOM   5860  CA  LEU B 767     186.429 195.050 225.577  1.00 34.49           C  
ATOM   5861  C   LEU B 767     185.145 194.482 226.215  1.00 39.98           C  
ATOM   5862  O   LEU B 767     184.708 195.015 227.225  1.00 52.94           O  
ATOM   5863  CB  LEU B 767     186.108 196.192 224.579  1.00 30.27           C  
ATOM   5864  CG  LEU B 767     187.132 197.340 224.588  1.00 30.97           C  
ATOM   5865  CD1 LEU B 767     188.558 196.853 224.390  1.00 37.39           C  
ATOM   5866  CD2 LEU B 767     186.840 198.343 223.481  1.00 30.42           C  
ATOM   5867  N   THR B 768     184.538 193.415 225.689  1.00 37.09           N  
ATOM   5868  CA  THR B 768     183.374 192.754 226.310  1.00 44.01           C  
ATOM   5869  C   THR B 768     183.749 191.872 227.511  1.00 47.99           C  
ATOM   5870  O   THR B 768     182.925 191.614 228.391  1.00 59.86           O  
ATOM   5871  CB  THR B 768     182.565 191.961 225.267  1.00 50.61           C  
ATOM   5872  OG1 THR B 768     181.210 191.893 225.639  1.00 52.81           O  
ATOM   5873  CG2 THR B 768     183.017 190.512 225.067  1.00 62.47           C  
ATOM   5874  N   GLY B 769     185.011 191.453 227.600  1.00 40.28           N  
ATOM   5875  CA  GLY B 769     185.599 190.877 228.802  1.00 48.75           C  
ATOM   5876  C   GLY B 769     185.974 191.960 229.823  1.00 55.23           C  
ATOM   5877  O   GLY B 769     185.177 192.823 230.184  1.00 57.16           O  
ATOM   5878  N   ILE B 770     187.209 191.888 230.302  1.00 53.12           N  
ATOM   5879  CA  ILE B 770     187.948 192.910 231.045  1.00 57.67           C  
ATOM   5880  C   ILE B 770     187.111 193.610 232.128  1.00 59.88           C  
ATOM   5881  O   ILE B 770     187.415 193.506 233.317  1.00 61.42           O  
ATOM   5882  CB  ILE B 770     188.651 193.864 230.053  1.00 41.03           C  
ATOM   5883  CG1 ILE B 770     190.001 194.363 230.606  1.00 49.43           C  
ATOM   5884  CG2 ILE B 770     187.746 195.039 229.636  1.00 33.13           C  
ATOM   5885  CD1 ILE B 770     191.123 193.323 230.533  1.00 45.72           C  
ATOM   5886  N   THR B 912     205.704 197.171  81.514  1.00 73.30           N  
ATOM   5887  CA  THR B 912     205.043 197.934  82.586  1.00 74.66           C  
ATOM   5888  C   THR B 912     204.048 197.076  83.381  1.00 73.30           C  
ATOM   5889  O   THR B 912     204.011 197.134  84.612  1.00 73.30           O  
ATOM   5890  CB  THR B 912     204.375 199.208  82.023  1.00 74.15           C  
ATOM   5891  OG1 THR B 912     203.619 199.878  83.007  1.00 73.30           O  
ATOM   5892  CG2 THR B 912     203.424 198.973  80.848  1.00 73.30           C  
ATOM   5893  N   GLN B 913     203.277 196.226  82.692  1.00 71.67           N  
ATOM   5894  CA  GLN B 913     202.223 195.417  83.315  1.00 71.95           C  
ATOM   5895  C   GLN B 913     202.792 194.424  84.339  1.00 75.35           C  
ATOM   5896  O   GLN B 913     202.201 194.202  85.394  1.00 75.90           O  
ATOM   5897  CB  GLN B 913     201.414 194.711  82.212  1.00 71.67           C  
ATOM   5898  CG  GLN B 913     200.031 194.223  82.679  1.00 71.67           C  
ATOM   5899  CD  GLN B 913     199.048 195.356  82.956  1.00 72.73           C  
ATOM   5900  OE1 GLN B 913     199.353 196.535  82.858  1.00 71.77           O  
ATOM   5901  NE2 GLN B 913     197.832 195.042  83.315  1.00 71.67           N  
ATOM   5902  N   ASN B 914     203.981 193.888  84.052  1.00 73.54           N  
ATOM   5903  CA  ASN B 914     204.744 193.020  84.940  1.00 73.54           C  
ATOM   5904  C   ASN B 914     205.194 193.708  86.241  1.00 75.17           C  
ATOM   5905  O   ASN B 914     204.891 193.212  87.322  1.00 73.54           O  
ATOM   5906  CB  ASN B 914     205.924 192.394  84.168  1.00 73.54           C  
ATOM   5907  CG  ASN B 914     206.838 193.354  83.414  1.00 75.15           C  
ATOM   5908  OD1 ASN B 914     206.709 194.555  83.432  1.00 73.54           O  
ATOM   5909  ND2 ASN B 914     207.783 192.843  82.705  1.00 73.54           N  
ATOM   5910  N   VAL B 915     205.883 194.853  86.184  1.00 77.47           N  
ATOM   5911  CA  VAL B 915     206.343 195.555  87.403  1.00 77.46           C  
ATOM   5912  C   VAL B 915     205.192 196.141  88.223  1.00 73.17           C  
ATOM   5913  O   VAL B 915     205.267 196.147  89.453  1.00 73.17           O  
ATOM   5914  CB  VAL B 915     207.418 196.623  87.128  1.00 73.17           C  
ATOM   5915  CG1 VAL B 915     208.684 195.957  86.578  1.00 73.17           C  
ATOM   5916  CG2 VAL B 915     206.989 197.740  86.180  1.00 73.17           C  
ATOM   5917  N   LEU B 916     204.087 196.551  87.595  1.00 73.77           N  
ATOM   5918  CA  LEU B 916     202.893 196.997  88.321  1.00 71.58           C  
ATOM   5919  C   LEU B 916     202.234 195.837  89.095  1.00 72.56           C  
ATOM   5920  O   LEU B 916     201.748 196.037  90.208  1.00 75.84           O  
ATOM   5921  CB  LEU B 916     201.930 197.679  87.329  1.00 71.58           C  
ATOM   5922  CG  LEU B 916     200.793 198.483  87.961  1.00 71.58           C  
ATOM   5923  CD1 LEU B 916     201.282 199.635  88.807  1.00 71.58           C  
ATOM   5924  CD2 LEU B 916     199.939 199.092  86.853  1.00 71.58           C  
ATOM   5925  N   TYR B 917     202.288 194.620  88.548  1.00 73.60           N  
ATOM   5926  CA  TYR B 917     201.797 193.396  89.189  1.00 74.76           C  
ATOM   5927  C   TYR B 917     202.759 192.874  90.268  1.00 72.65           C  
ATOM   5928  O   TYR B 917     202.322 192.473  91.340  1.00 74.60           O  
ATOM   5929  CB  TYR B 917     201.529 192.347  88.103  1.00 75.34           C  
ATOM   5930  CG  TYR B 917     200.761 191.122  88.558  1.00 75.54           C  
ATOM   5931  CD1 TYR B 917     201.427 190.065  89.207  1.00 72.00           C  
ATOM   5932  CD2 TYR B 917     199.380 191.023  88.296  1.00 73.83           C  
ATOM   5933  CE1 TYR B 917     200.708 188.929  89.633  1.00 72.04           C  
ATOM   5934  CE2 TYR B 917     198.658 189.890  88.716  1.00 73.98           C  
ATOM   5935  CZ  TYR B 917     199.320 188.838  89.387  1.00 76.51           C  
ATOM   5936  OH  TYR B 917     198.623 187.742  89.787  1.00 73.92           O  
ATOM   5937  N   GLU B 918     204.073 192.930  90.060  1.00 73.35           N  
ATOM   5938  CA  GLU B 918     205.036 192.574  91.112  1.00 75.84           C  
ATOM   5939  C   GLU B 918     204.992 193.572  92.290  1.00 76.99           C  
ATOM   5940  O   GLU B 918     205.109 193.159  93.440  1.00 76.58           O  
ATOM   5941  CB  GLU B 918     206.453 192.429  90.529  1.00 74.60           C  
ATOM   5942  CG  GLU B 918     206.604 191.173  89.650  1.00 79.31           C  
ATOM   5943  CD  GLU B 918     206.301 189.870  90.397  1.00 80.16           C  
ATOM   5944  OE1 GLU B 918     206.802 189.687  91.528  1.00 76.51           O  
ATOM   5945  OE2 GLU B 918     205.583 189.011  89.844  1.00 79.63           O1-
ATOM   5946  N   ASN B 919     204.725 194.861  92.047  1.00 79.78           N  
ATOM   5947  CA  ASN B 919     204.365 195.807  93.110  1.00 77.84           C  
ATOM   5948  C   ASN B 919     203.028 195.441  93.793  1.00 72.97           C  
ATOM   5949  O   ASN B 919     202.889 195.667  94.993  1.00 72.10           O  
ATOM   5950  CB  ASN B 919     204.331 197.245  92.562  1.00 77.31           C  
ATOM   5951  CG  ASN B 919     205.705 197.888  92.525  1.00 79.99           C  
ATOM   5952  OD1 ASN B 919     206.169 198.469  93.489  1.00 82.79           O  
ATOM   5953  ND2 ASN B 919     206.387 197.826  91.414  1.00 80.38           N  
ATOM   5954  N   GLN B 920     202.075 194.833  93.077  1.00 70.37           N  
ATOM   5955  CA  GLN B 920     200.824 194.326  93.648  1.00 73.95           C  
ATOM   5956  C   GLN B 920     201.054 193.107  94.563  1.00 69.64           C  
ATOM   5957  O   GLN B 920     200.510 193.046  95.669  1.00 69.64           O  
ATOM   5958  CB  GLN B 920     199.818 194.053  92.504  1.00 71.93           C  
ATOM   5959  CG  GLN B 920     198.331 194.004  92.894  1.00 72.05           C  
ATOM   5960  CD  GLN B 920     197.776 195.376  93.256  1.00 69.64           C  
ATOM   5961  OE1 GLN B 920     198.381 196.125  93.996  1.00 69.64           O  
ATOM   5962  NE2 GLN B 920     196.635 195.796  92.775  1.00 69.64           N  
ATOM   5963  N   LYS B 921     201.941 192.184  94.161  1.00 71.28           N  
ATOM   5964  CA  LYS B 921     202.450 191.097  95.030  1.00 71.80           C  
ATOM   5965  C   LYS B 921     203.198 191.646  96.254  1.00 75.59           C  
ATOM   5966  O   LYS B 921     202.934 191.219  97.376  1.00 69.92           O  
ATOM   5967  CB  LYS B 921     203.370 190.149  94.230  1.00 71.62           C  
ATOM   5968  CG  LYS B 921     202.699 189.324  93.116  1.00 71.85           C  
ATOM   5969  CD  LYS B 921     201.656 188.301  93.600  1.00 72.70           C  
ATOM   5970  CE  LYS B 921     202.207 187.203  94.523  1.00 69.92           C  
ATOM   5971  NZ  LYS B 921     203.029 186.210  93.790  1.00 74.77           N  
ATOM   5972  N   LEU B 922     204.092 192.615  96.046  1.00 73.73           N  
ATOM   5973  CA  LEU B 922     204.903 193.256  97.087  1.00 73.06           C  
ATOM   5974  C   LEU B 922     204.036 193.857  98.196  1.00 71.74           C  
ATOM   5975  O   LEU B 922     204.171 193.463  99.353  1.00 69.65           O  
ATOM   5976  CB  LEU B 922     205.825 194.300  96.428  1.00 75.47           C  
ATOM   5977  CG  LEU B 922     206.872 195.003  97.317  1.00 75.39           C  
ATOM   5978  CD1 LEU B 922     207.825 195.799  96.425  1.00 74.92           C  
ATOM   5979  CD2 LEU B 922     206.284 196.010  98.308  1.00 69.65           C  
ATOM   5980  N   ILE B 923     203.142 194.797  97.865  1.00 76.16           N  
ATOM   5981  CA  ILE B 923     202.413 195.556  98.893  1.00 70.68           C  
ATOM   5982  C   ILE B 923     201.458 194.659  99.685  1.00 66.10           C  
ATOM   5983  O   ILE B 923     201.357 194.778 100.904  1.00 69.79           O  
ATOM   5984  CB  ILE B 923     201.705 196.789  98.288  1.00 65.37           C  
ATOM   5985  CG1 ILE B 923     201.159 197.746  99.367  1.00 65.37           C  
ATOM   5986  CG2 ILE B 923     200.528 196.420  97.374  1.00 65.99           C  
ATOM   5987  CD1 ILE B 923     202.226 198.306 100.310  1.00 65.37           C  
ATOM   5988  N   ALA B 924     200.826 193.685  99.024  1.00 66.03           N  
ATOM   5989  CA  ALA B 924     200.010 192.666  99.671  1.00 66.12           C  
ATOM   5990  C   ALA B 924     200.829 191.758 100.599  1.00 68.09           C  
ATOM   5991  O   ALA B 924     200.362 191.420 101.684  1.00 66.96           O  
ATOM   5992  CB  ALA B 924     199.300 191.860  98.580  1.00 69.30           C  
ATOM   5993  N   ASN B 925     202.056 191.380 100.218  1.00 71.73           N  
ATOM   5994  CA  ASN B 925     202.959 190.595 101.065  1.00 70.68           C  
ATOM   5995  C   ASN B 925     203.457 191.401 102.278  1.00 70.63           C  
ATOM   5996  O   ASN B 925     203.549 190.863 103.379  1.00 66.33           O  
ATOM   5997  CB  ASN B 925     204.122 190.050 100.213  1.00 75.95           C  
ATOM   5998  CG  ASN B 925     203.762 188.914  99.270  1.00 76.79           C  
ATOM   5999  OD1 ASN B 925     204.626 188.300  98.668  1.00 78.42           O  
ATOM   6000  ND2 ASN B 925     202.509 188.541  99.152  1.00 73.03           N  
ATOM   6001  N   GLN B 926     203.713 192.700 102.114  1.00 73.50           N  
ATOM   6002  CA  GLN B 926     204.015 193.597 103.232  1.00 68.63           C  
ATOM   6003  C   GLN B 926     202.819 193.753 104.188  1.00 64.29           C  
ATOM   6004  O   GLN B 926     203.003 193.681 105.406  1.00 64.39           O  
ATOM   6005  CB  GLN B 926     204.467 194.961 102.701  1.00 68.02           C  
ATOM   6006  CG  GLN B 926     205.809 194.921 101.949  1.00 66.65           C  
ATOM   6007  CD  GLN B 926     206.994 194.768 102.887  1.00 73.83           C  
ATOM   6008  OE1 GLN B 926     207.520 195.730 103.416  1.00 77.78           O  
ATOM   6009  NE2 GLN B 926     207.459 193.569 103.154  1.00 73.10           N  
ATOM   6010  N   PHE B 927     201.597 193.911 103.666  1.00 62.86           N  
ATOM   6011  CA  PHE B 927     200.374 194.033 104.466  1.00 60.62           C  
ATOM   6012  C   PHE B 927     199.983 192.746 105.200  1.00 65.22           C  
ATOM   6013  O   PHE B 927     199.775 192.765 106.410  1.00 71.10           O  
ATOM   6014  CB  PHE B 927     199.241 194.527 103.563  1.00 63.84           C  
ATOM   6015  CG  PHE B 927     197.887 194.567 104.234  1.00 63.40           C  
ATOM   6016  CD1 PHE B 927     197.559 195.643 105.073  1.00 60.80           C  
ATOM   6017  CD2 PHE B 927     196.960 193.526 104.037  1.00 63.12           C  
ATOM   6018  CE1 PHE B 927     196.303 195.699 105.692  1.00 67.41           C  
ATOM   6019  CE2 PHE B 927     195.700 193.583 104.657  1.00 59.23           C  
ATOM   6020  CZ  PHE B 927     195.366 194.678 105.473  1.00 66.47           C  
ATOM   6021  N   ASN B 928     199.948 191.614 104.496  1.00 63.16           N  
ATOM   6022  CA  ASN B 928     199.629 190.296 105.052  1.00 63.28           C  
ATOM   6023  C   ASN B 928     200.598 189.906 106.182  1.00 64.91           C  
ATOM   6024  O   ASN B 928     200.169 189.410 107.227  1.00 65.86           O  
ATOM   6025  CB  ASN B 928     199.630 189.298 103.874  1.00 70.21           C  
ATOM   6026  CG  ASN B 928     199.516 187.841 104.279  1.00 71.39           C  
ATOM   6027  OD1 ASN B 928     200.439 187.261 104.833  1.00 69.40           O  
ATOM   6028  ND2 ASN B 928     198.430 187.179 103.961  1.00 77.16           N  
ATOM   6029  N   SER B 929     201.894 190.197 106.023  1.00 67.77           N  
ATOM   6030  CA  SER B 929     202.893 190.013 107.080  1.00 64.88           C  
ATOM   6031  C   SER B 929     202.734 191.014 108.236  1.00 66.82           C  
ATOM   6032  O   SER B 929     202.876 190.629 109.399  1.00 61.65           O  
ATOM   6033  CB  SER B 929     204.284 190.100 106.452  1.00 68.60           C  
ATOM   6034  OG  SER B 929     205.305 189.942 107.423  1.00 66.29           O  
ATOM   6035  N   ALA B 930     202.358 192.273 107.958  1.00 65.62           N  
ATOM   6036  CA  ALA B 930     202.129 193.276 108.998  1.00 63.77           C  
ATOM   6037  C   ALA B 930     200.946 192.915 109.902  1.00 65.29           C  
ATOM   6038  O   ALA B 930     201.110 192.887 111.113  1.00 67.41           O  
ATOM   6039  CB  ALA B 930     201.950 194.659 108.373  1.00 62.80           C  
ATOM   6040  N   ILE B 931     199.785 192.567 109.337  1.00 62.69           N  
ATOM   6041  CA  ILE B 931     198.594 192.156 110.101  1.00 62.27           C  
ATOM   6042  C   ILE B 931     198.878 190.944 111.010  1.00 65.57           C  
ATOM   6043  O   ILE B 931     198.475 190.953 112.173  1.00 66.22           O  
ATOM   6044  CB  ILE B 931     197.392 191.906 109.164  1.00 60.02           C  
ATOM   6045  CG1 ILE B 931     196.912 193.178 108.435  1.00 62.88           C  
ATOM   6046  CG2 ILE B 931     196.222 191.281 109.935  1.00 64.13           C  
ATOM   6047  CD1 ILE B 931     196.492 194.349 109.322  1.00 58.77           C  
ATOM   6048  N   GLY B 932     199.644 189.943 110.563  1.00 68.90           N  
ATOM   6049  CA  GLY B 932     200.039 188.824 111.436  1.00 64.61           C  
ATOM   6050  C   GLY B 932     200.886 189.248 112.649  1.00 65.58           C  
ATOM   6051  O   GLY B 932     200.755 188.711 113.750  1.00 68.27           O  
ATOM   6052  N   LYS B 933     201.712 190.285 112.473  1.00 63.11           N  
ATOM   6053  CA  LYS B 933     202.476 190.940 113.541  1.00 61.60           C  
ATOM   6054  C   LYS B 933     201.596 191.858 114.401  1.00 64.10           C  
ATOM   6055  O   LYS B 933     201.844 191.982 115.600  1.00 70.23           O  
ATOM   6056  CB  LYS B 933     203.679 191.644 112.889  1.00 65.46           C  
ATOM   6057  CG  LYS B 933     204.755 192.101 113.889  1.00 64.53           C  
ATOM   6058  CD  LYS B 933     206.091 192.404 113.183  1.00 60.88           C  
ATOM   6059  CE  LYS B 933     206.857 191.106 112.859  1.00 61.06           C  
ATOM   6060  NZ  LYS B 933     207.838 191.261 111.748  1.00 60.34           N  
ATOM   6061  N   ILE B 934     200.520 192.442 113.861  1.00 64.65           N  
ATOM   6062  CA  ILE B 934     199.480 193.111 114.666  1.00 62.74           C  
ATOM   6063  C   ILE B 934     198.774 192.114 115.589  1.00 63.69           C  
ATOM   6064  O   ILE B 934     198.584 192.422 116.758  1.00 68.86           O  
ATOM   6065  CB  ILE B 934     198.439 193.860 113.797  1.00 66.26           C  
ATOM   6066  CG1 ILE B 934     199.028 194.941 112.868  1.00 65.28           C  
ATOM   6067  CG2 ILE B 934     197.365 194.509 114.676  1.00 58.79           C  
ATOM   6068  CD1 ILE B 934     200.020 195.906 113.507  1.00 64.03           C  
ATOM   6069  N   GLN B 935     198.416 190.924 115.114  1.00 64.17           N  
ATOM   6070  CA  GLN B 935     197.758 189.921 115.955  1.00 67.19           C  
ATOM   6071  C   GLN B 935     198.652 189.437 117.108  1.00 69.96           C  
ATOM   6072  O   GLN B 935     198.172 189.309 118.231  1.00 71.33           O  
ATOM   6073  CB  GLN B 935     197.265 188.764 115.078  1.00 69.41           C  
ATOM   6074  CG  GLN B 935     196.129 189.238 114.158  1.00 75.63           C  
ATOM   6075  CD  GLN B 935     195.755 188.200 113.116  1.00 82.78           C  
ATOM   6076  OE1 GLN B 935     196.445 187.985 112.130  1.00 84.56           O  
ATOM   6077  NE2 GLN B 935     194.641 187.529 113.267  1.00 78.71           N  
ATOM   6078  N   ASP B 936     199.956 189.274 116.895  1.00 67.79           N  
ATOM   6079  CA  ASP B 936     200.935 189.037 117.967  1.00 70.83           C  
ATOM   6080  C   ASP B 936     201.019 190.219 118.957  1.00 67.52           C  
ATOM   6081  O   ASP B 936     200.878 190.041 120.167  1.00 69.18           O  
ATOM   6082  CB  ASP B 936     202.304 188.757 117.317  1.00 73.50           C  
ATOM   6083  CG  ASP B 936     203.415 188.380 118.306  1.00 76.45           C  
ATOM   6084  OD1 ASP B 936     204.600 188.508 117.930  1.00 70.22           O  
ATOM   6085  OD2 ASP B 936     203.120 187.925 119.428  1.00 85.04           O1-
ATOM   6086  N   SER B 937     201.154 191.443 118.442  1.00 66.24           N  
ATOM   6087  CA  SER B 937     201.221 192.685 119.229  1.00 65.06           C  
ATOM   6088  C   SER B 937     199.995 192.906 120.134  1.00 64.68           C  
ATOM   6089  O   SER B 937     200.095 193.393 121.262  1.00 67.16           O  
ATOM   6090  CB  SER B 937     201.289 193.867 118.264  1.00 67.62           C  
ATOM   6091  OG  SER B 937     202.433 193.803 117.438  1.00 67.84           O  
ATOM   6092  N   LEU B 938     198.820 192.551 119.623  1.00 60.43           N  
ATOM   6093  CA  LEU B 938     197.546 192.746 120.290  1.00 60.99           C  
ATOM   6094  C   LEU B 938     197.213 191.595 121.249  1.00 65.80           C  
ATOM   6095  O   LEU B 938     196.781 191.840 122.370  1.00 71.96           O  
ATOM   6096  CB  LEU B 938     196.519 192.948 119.180  1.00 65.57           C  
ATOM   6097  CG  LEU B 938     195.150 193.425 119.673  1.00 65.61           C  
ATOM   6098  CD1 LEU B 938     194.499 194.240 118.567  1.00 66.94           C  
ATOM   6099  CD2 LEU B 938     194.224 192.262 120.001  1.00 69.59           C  
ATOM   6100  N   SER B 939     197.444 190.340 120.857  1.00 65.63           N  
ATOM   6101  CA  SER B 939     197.208 189.173 121.723  1.00 68.08           C  
ATOM   6102  C   SER B 939     198.116 189.180 122.961  1.00 68.52           C  
ATOM   6103  O   SER B 939     197.664 188.911 124.074  1.00 72.74           O  
ATOM   6104  CB  SER B 939     197.380 187.867 120.935  1.00 70.74           C  
ATOM   6105  OG  SER B 939     198.671 187.736 120.377  1.00 70.75           O  
ATOM   6106  N   SER B 940     199.386 189.551 122.794  1.00 68.53           N  
ATOM   6107  CA  SER B 940     200.318 189.751 123.909  1.00 65.21           C  
ATOM   6108  C   SER B 940     199.877 190.897 124.825  1.00 62.74           C  
ATOM   6109  O   SER B 940     199.811 190.695 126.032  1.00 64.89           O  
ATOM   6110  CB  SER B 940     201.738 189.966 123.399  1.00 68.39           C  
ATOM   6111  OG  SER B 940     201.773 191.036 122.479  1.00 75.13           O  
ATOM   6112  N   THR B 941     199.475 192.056 124.287  1.00 62.43           N  
ATOM   6113  CA  THR B 941     198.920 193.167 125.094  1.00 59.12           C  
ATOM   6114  C   THR B 941     197.675 192.745 125.869  1.00 58.23           C  
ATOM   6115  O   THR B 941     197.549 193.096 127.034  1.00 64.71           O  
ATOM   6116  CB  THR B 941     198.583 194.415 124.261  1.00 63.24           C  
ATOM   6117  OG1 THR B 941     199.700 194.886 123.549  1.00 71.42           O  
ATOM   6118  CG2 THR B 941     198.118 195.581 125.140  1.00 54.93           C  
ATOM   6119  N   ALA B 942     196.769 191.960 125.283  1.00 61.06           N  
ATOM   6120  CA  ALA B 942     195.620 191.415 126.007  1.00 62.67           C  
ATOM   6121  C   ALA B 942     196.033 190.464 127.150  1.00 67.11           C  
ATOM   6122  O   ALA B 942     195.539 190.581 128.269  1.00 68.34           O  
ATOM   6123  CB  ALA B 942     194.711 190.698 125.008  1.00 67.51           C  
ATOM   6124  N   SER B 943     196.965 189.546 126.890  1.00 70.03           N  
ATOM   6125  CA  SER B 943     197.511 188.623 127.894  1.00 68.73           C  
ATOM   6126  C   SER B 943     198.285 189.342 129.014  1.00 66.09           C  
ATOM   6127  O   SER B 943     198.233 188.926 130.165  1.00 68.01           O  
ATOM   6128  CB  SER B 943     198.397 187.608 127.170  1.00 68.66           C  
ATOM   6129  OG  SER B 943     198.784 186.553 128.020  1.00 73.59           O  
ATOM   6130  N   ALA B 944     198.936 190.468 128.714  1.00 63.87           N  
ATOM   6131  CA  ALA B 944     199.537 191.343 129.716  1.00 60.76           C  
ATOM   6132  C   ALA B 944     198.479 192.122 130.511  1.00 59.77           C  
ATOM   6133  O   ALA B 944     198.414 192.027 131.729  1.00 64.37           O  
ATOM   6134  CB  ALA B 944     200.501 192.319 129.026  1.00 56.71           C  
ATOM   6135  N   LEU B 945     197.623 192.894 129.848  1.00 58.58           N  
ATOM   6136  CA  LEU B 945     196.642 193.757 130.511  1.00 57.83           C  
ATOM   6137  C   LEU B 945     195.615 192.942 131.321  1.00 61.98           C  
ATOM   6138  O   LEU B 945     195.162 193.376 132.378  1.00 73.15           O  
ATOM   6139  CB  LEU B 945     196.033 194.690 129.451  1.00 65.59           C  
ATOM   6140  CG  LEU B 945     195.145 195.790 130.062  1.00 67.24           C  
ATOM   6141  CD1 LEU B 945     195.389 197.147 129.403  1.00 65.02           C  
ATOM   6142  CD2 LEU B 945     193.678 195.420 129.907  1.00 64.59           C  
ATOM   6143  N   GLY B 946     195.344 191.702 130.916  1.00 63.00           N  
ATOM   6144  CA  GLY B 946     194.574 190.732 131.700  1.00 65.73           C  
ATOM   6145  C   GLY B 946     195.296 190.146 132.923  1.00 62.43           C  
ATOM   6146  O   GLY B 946     194.623 189.755 133.873  1.00 57.08           O  
ATOM   6147  N   LYS B 947     196.639 190.124 132.965  1.00 67.18           N  
ATOM   6148  CA  LYS B 947     197.425 189.811 134.184  1.00 62.01           C  
ATOM   6149  C   LYS B 947     197.544 191.014 135.133  1.00 55.76           C  
ATOM   6150  O   LYS B 947     197.566 190.830 136.348  1.00 55.49           O  
ATOM   6151  CB  LYS B 947     198.790 189.177 133.814  1.00 63.35           C  
ATOM   6152  CG  LYS B 947     200.026 190.091 133.892  1.00 61.90           C  
ATOM   6153  CD  LYS B 947     201.272 189.422 133.301  1.00 66.71           C  
ATOM   6154  CE  LYS B 947     202.436 190.422 133.280  1.00 59.82           C  
ATOM   6155  NZ  LYS B 947     203.643 189.874 132.609  1.00 47.54           N  
ATOM   6156  N   LEU B 948     197.544 192.240 134.601  1.00 59.03           N  
ATOM   6157  CA  LEU B 948     197.507 193.478 135.394  1.00 57.89           C  
ATOM   6158  C   LEU B 948     196.151 193.657 136.089  1.00 55.45           C  
ATOM   6159  O   LEU B 948     196.112 193.926 137.282  1.00 62.05           O  
ATOM   6160  CB  LEU B 948     197.824 194.692 134.496  1.00 65.70           C  
ATOM   6161  CG  LEU B 948     199.296 195.145 134.436  1.00 63.71           C  
ATOM   6162  CD1 LEU B 948     199.753 195.777 135.749  1.00 59.58           C  
ATOM   6163  CD2 LEU B 948     200.272 194.026 134.079  1.00 61.51           C  
ATOM   6164  N   GLN B 949     195.036 193.460 135.385  1.00 58.01           N  
ATOM   6165  CA  GLN B 949     193.685 193.521 135.965  1.00 58.17           C  
ATOM   6166  C   GLN B 949     193.399 192.387 136.966  1.00 57.25           C  
ATOM   6167  O   GLN B 949     192.605 192.573 137.886  1.00 60.97           O  
ATOM   6168  CB  GLN B 949     192.679 193.567 134.805  1.00 75.97           C  
ATOM   6169  CG  GLN B 949     191.197 193.709 135.215  1.00 82.02           C  
ATOM   6170  CD  GLN B 949     190.381 192.413 135.175  1.00 75.56           C  
ATOM   6171  OE1 GLN B 949     190.877 191.301 135.108  1.00 75.90           O  
ATOM   6172  NE2 GLN B 949     189.073 192.505 135.207  1.00 68.19           N  
ATOM   6173  N   ASP B 950     194.079 191.242 136.847  1.00 58.41           N  
ATOM   6174  CA  ASP B 950     194.047 190.146 137.825  1.00 57.66           C  
ATOM   6175  C   ASP B 950     194.753 190.568 139.119  1.00 59.04           C  
ATOM   6176  O   ASP B 950     194.127 190.682 140.178  1.00 59.00           O  
ATOM   6177  CB  ASP B 950     194.699 188.904 137.189  1.00 60.85           C  
ATOM   6178  CG  ASP B 950     194.951 187.715 138.127  1.00 59.13           C  
ATOM   6179  OD1 ASP B 950     194.259 187.567 139.161  1.00 60.58           O  
ATOM   6180  OD2 ASP B 950     195.847 186.900 137.812  1.00 58.48           O1-
ATOM   6181  N   VAL B 951     196.046 190.895 139.018  1.00 59.27           N  
ATOM   6182  CA  VAL B 951     196.882 191.252 140.171  1.00 44.98           C  
ATOM   6183  C   VAL B 951     196.398 192.516 140.885  1.00 47.95           C  
ATOM   6184  O   VAL B 951     196.407 192.540 142.115  1.00 59.45           O  
ATOM   6185  CB  VAL B 951     198.366 191.308 139.759  1.00 46.70           C  
ATOM   6186  CG1 VAL B 951     199.274 192.076 140.720  1.00 49.82           C  
ATOM   6187  CG2 VAL B 951     198.907 189.877 139.683  1.00 47.16           C  
ATOM   6188  N   VAL B 952     195.914 193.548 140.188  1.00 46.53           N  
ATOM   6189  CA  VAL B 952     195.351 194.737 140.861  1.00 45.92           C  
ATOM   6190  C   VAL B 952     194.096 194.407 141.679  1.00 50.22           C  
ATOM   6191  O   VAL B 952     193.945 194.924 142.780  1.00 56.21           O  
ATOM   6192  CB  VAL B 952     195.108 195.886 139.860  1.00 44.84           C  
ATOM   6193  CG1 VAL B 952     194.276 197.050 140.410  1.00 38.67           C  
ATOM   6194  CG2 VAL B 952     196.457 196.482 139.431  1.00 53.02           C  
ATOM   6195  N   ASN B 953     193.218 193.504 141.229  1.00 52.46           N  
ATOM   6196  CA  ASN B 953     192.036 193.117 142.006  1.00 57.28           C  
ATOM   6197  C   ASN B 953     192.375 192.122 143.140  1.00 55.60           C  
ATOM   6198  O   ASN B 953     191.738 192.157 144.189  1.00 55.22           O  
ATOM   6199  CB  ASN B 953     190.945 192.611 141.047  1.00 62.39           C  
ATOM   6200  CG  ASN B 953     189.562 193.103 141.435  1.00 60.82           C  
ATOM   6201  OD1 ASN B 953     189.215 193.258 142.589  1.00 58.80           O  
ATOM   6202  ND2 ASN B 953     188.723 193.395 140.480  1.00 52.95           N  
ATOM   6203  N   GLN B 954     193.438 191.322 143.000  1.00 56.26           N  
ATOM   6204  CA  GLN B 954     194.023 190.522 144.090  1.00 54.51           C  
ATOM   6205  C   GLN B 954     194.660 191.403 145.189  1.00 52.65           C  
ATOM   6206  O   GLN B 954     194.509 191.122 146.377  1.00 54.44           O  
ATOM   6207  CB  GLN B 954     195.017 189.520 143.471  1.00 56.49           C  
ATOM   6208  CG  GLN B 954     195.485 188.406 144.420  1.00 59.34           C  
ATOM   6209  CD  GLN B 954     196.698 188.741 145.295  1.00 61.01           C  
ATOM   6210  OE1 GLN B 954     197.282 189.815 145.267  1.00 47.20           O  
ATOM   6211  NE2 GLN B 954     197.158 187.803 146.090  1.00 68.25           N  
ATOM   6212  N   ASN B 955     195.267 192.535 144.818  1.00 49.02           N  
ATOM   6213  CA  ASN B 955     195.683 193.569 145.767  1.00 50.04           C  
ATOM   6214  C   ASN B 955     194.484 194.239 146.471  1.00 52.01           C  
ATOM   6215  O   ASN B 955     194.504 194.419 147.686  1.00 55.05           O  
ATOM   6216  CB  ASN B 955     196.550 194.618 145.052  1.00 49.43           C  
ATOM   6217  CG  ASN B 955     198.002 194.218 144.932  1.00 50.49           C  
ATOM   6218  OD1 ASN B 955     198.873 194.809 145.552  1.00 49.33           O  
ATOM   6219  ND2 ASN B 955     198.325 193.220 144.150  1.00 52.79           N  
ATOM   6220  N   ALA B 956     193.413 194.571 145.752  1.00 50.39           N  
ATOM   6221  CA  ALA B 956     192.217 195.154 146.351  1.00 47.32           C  
ATOM   6222  C   ALA B 956     191.552 194.191 147.347  1.00 57.02           C  
ATOM   6223  O   ALA B 956     191.122 194.603 148.420  1.00 64.00           O  
ATOM   6224  CB  ALA B 956     191.262 195.563 145.226  1.00 56.35           C  
ATOM   6225  N   GLN B 957     191.541 192.893 147.043  1.00 60.93           N  
ATOM   6226  CA  GLN B 957     191.152 191.832 147.980  1.00 59.54           C  
ATOM   6227  C   GLN B 957     192.068 191.786 149.212  1.00 55.90           C  
ATOM   6228  O   GLN B 957     191.574 191.766 150.336  1.00 58.78           O  
ATOM   6229  CB  GLN B 957     191.100 190.495 147.216  1.00 65.18           C  
ATOM   6230  CG  GLN B 957     190.986 189.240 148.097  1.00 64.83           C  
ATOM   6231  CD  GLN B 957     192.336 188.620 148.451  1.00 63.33           C  
ATOM   6232  OE1 GLN B 957     193.124 188.247 147.596  1.00 59.51           O  
ATOM   6233  NE2 GLN B 957     192.653 188.462 149.719  1.00 69.68           N  
ATOM   6234  N   ALA B 958     193.390 191.812 149.044  1.00 54.23           N  
ATOM   6235  CA  ALA B 958     194.329 191.786 150.168  1.00 57.40           C  
ATOM   6236  C   ALA B 958     194.161 192.982 151.123  1.00 59.01           C  
ATOM   6237  O   ALA B 958     194.149 192.791 152.336  1.00 63.59           O  
ATOM   6238  CB  ALA B 958     195.760 191.680 149.639  1.00 54.07           C  
ATOM   6239  N   LEU B 959     193.947 194.195 150.614  1.00 58.95           N  
ATOM   6240  CA  LEU B 959     193.725 195.368 151.463  1.00 52.33           C  
ATOM   6241  C   LEU B 959     192.385 195.349 152.190  1.00 49.34           C  
ATOM   6242  O   LEU B 959     192.353 195.737 153.352  1.00 58.25           O  
ATOM   6243  CB  LEU B 959     193.871 196.661 150.652  1.00 63.43           C  
ATOM   6244  CG  LEU B 959     195.271 197.279 150.692  1.00 58.43           C  
ATOM   6245  CD1 LEU B 959     195.623 197.768 152.093  1.00 53.82           C  
ATOM   6246  CD2 LEU B 959     196.349 196.320 150.194  1.00 58.52           C  
ATOM   6247  N   ASN B 960     191.308 194.847 151.584  1.00 48.25           N  
ATOM   6248  CA  ASN B 960     190.060 194.658 152.331  1.00 52.04           C  
ATOM   6249  C   ASN B 960     190.181 193.532 153.378  1.00 55.74           C  
ATOM   6250  O   ASN B 960     189.565 193.628 154.436  1.00 56.15           O  
ATOM   6251  CB  ASN B 960     188.870 194.472 151.369  1.00 58.16           C  
ATOM   6252  CG  ASN B 960     188.207 195.792 151.005  1.00 55.08           C  
ATOM   6253  OD1 ASN B 960     188.848 196.800 150.747  1.00 50.00           O  
ATOM   6254  ND2 ASN B 960     186.896 195.846 151.019  1.00 52.97           N  
ATOM   6255  N   THR B 961     191.022 192.519 153.141  1.00 56.52           N  
ATOM   6256  CA  THR B 961     191.359 191.511 154.161  1.00 54.14           C  
ATOM   6257  C   THR B 961     192.131 192.144 155.325  1.00 55.16           C  
ATOM   6258  O   THR B 961     191.764 191.957 156.483  1.00 65.59           O  
ATOM   6259  CB  THR B 961     192.158 190.336 153.576  1.00 56.05           C  
ATOM   6260  OG1 THR B 961     191.583 189.843 152.385  1.00 64.11           O  
ATOM   6261  CG2 THR B 961     192.182 189.166 154.548  1.00 67.62           C  
ATOM   6262  N   LEU B 962     193.151 192.952 155.028  1.00 52.11           N  
ATOM   6263  CA  LEU B 962     193.919 193.698 156.015  1.00 39.01           C  
ATOM   6264  C   LEU B 962     193.022 194.625 156.837  1.00 36.60           C  
ATOM   6265  O   LEU B 962     193.073 194.572 158.054  1.00 49.65           O  
ATOM   6266  CB  LEU B 962     195.031 194.470 155.291  1.00 44.67           C  
ATOM   6267  CG  LEU B 962     196.144 194.949 156.233  1.00 33.99           C  
ATOM   6268  CD1 LEU B 962     197.103 193.817 156.597  1.00 40.20           C  
ATOM   6269  CD2 LEU B 962     196.956 196.080 155.612  1.00 30.56           C  
ATOM   6270  N   VAL B 963     192.158 195.433 156.224  1.00 36.88           N  
ATOM   6271  CA  VAL B 963     191.287 196.355 156.974  1.00 43.03           C  
ATOM   6272  C   VAL B 963     190.326 195.613 157.901  1.00 47.11           C  
ATOM   6273  O   VAL B 963     190.124 196.051 159.028  1.00 52.95           O  
ATOM   6274  CB  VAL B 963     190.533 197.313 156.031  1.00 58.80           C  
ATOM   6275  CG1 VAL B 963     189.371 198.034 156.722  1.00 59.58           C  
ATOM   6276  CG2 VAL B 963     191.484 198.389 155.490  1.00 63.68           C  
ATOM   6277  N   LYS B 964     189.768 194.464 157.506  1.00 48.15           N  
ATOM   6278  CA  LYS B 964     188.892 193.685 158.398  1.00 49.69           C  
ATOM   6279  C   LYS B 964     189.658 193.045 159.567  1.00 43.48           C  
ATOM   6280  O   LYS B 964     189.153 193.039 160.691  1.00 43.67           O  
ATOM   6281  CB  LYS B 964     188.101 192.639 157.598  1.00 68.61           C  
ATOM   6282  CG  LYS B 964     186.970 193.220 156.735  1.00 70.45           C  
ATOM   6283  CD  LYS B 964     185.822 193.920 157.484  1.00 68.84           C  
ATOM   6284  CE  LYS B 964     185.117 193.008 158.500  1.00 68.06           C  
ATOM   6285  NZ  LYS B 964     183.903 193.638 159.061  1.00 72.32           N  
ATOM   6286  N   GLN B 965     190.886 192.567 159.351  1.00 42.45           N  
ATOM   6287  CA  GLN B 965     191.741 192.075 160.437  1.00 42.13           C  
ATOM   6288  C   GLN B 965     192.253 193.189 161.364  1.00 39.84           C  
ATOM   6289  O   GLN B 965     192.267 192.993 162.577  1.00 43.81           O  
ATOM   6290  CB  GLN B 965     192.920 191.282 159.869  1.00 48.42           C  
ATOM   6291  CG  GLN B 965     192.480 189.920 159.299  1.00 55.43           C  
ATOM   6292  CD  GLN B 965     193.279 188.742 159.845  1.00 65.32           C  
ATOM   6293  OE1 GLN B 965     193.666 188.686 161.003  1.00 64.62           O  
ATOM   6294  NE2 GLN B 965     193.558 187.738 159.052  1.00 62.67           N  
ATOM   6295  N   LEU B 966     192.626 194.360 160.852  1.00 36.67           N  
ATOM   6296  CA  LEU B 966     193.083 195.484 161.671  1.00 29.68           C  
ATOM   6297  C   LEU B 966     191.935 196.171 162.413  1.00 33.81           C  
ATOM   6298  O   LEU B 966     192.109 196.555 163.562  1.00 42.53           O  
ATOM   6299  CB  LEU B 966     193.834 196.487 160.794  1.00 29.57           C  
ATOM   6300  CG  LEU B 966     195.337 196.228 160.697  1.00 30.79           C  
ATOM   6301  CD1 LEU B 966     195.730 194.811 160.303  1.00 31.30           C  
ATOM   6302  CD2 LEU B 966     195.893 197.203 159.675  1.00 31.84           C  
ATOM   6303  N   SER B 967     190.744 196.235 161.834  1.00 37.35           N  
ATOM   6304  CA  SER B 967     189.532 196.610 162.566  1.00 39.11           C  
ATOM   6305  C   SER B 967     189.322 195.683 163.768  1.00 43.56           C  
ATOM   6306  O   SER B 967     188.970 196.150 164.852  1.00 46.87           O  
ATOM   6307  CB  SER B 967     188.325 196.560 161.628  1.00 49.32           C  
ATOM   6308  OG  SER B 967     187.125 196.839 162.315  1.00 38.55           O  
ATOM   6309  N   SER B 968     189.633 194.389 163.628  1.00 46.43           N  
ATOM   6310  CA  SER B 968     189.629 193.474 164.770  1.00 38.49           C  
ATOM   6311  C   SER B 968     190.682 193.860 165.806  1.00 39.94           C  
ATOM   6312  O   SER B 968     190.345 193.952 166.975  1.00 45.59           O  
ATOM   6313  CB  SER B 968     189.722 191.997 164.351  1.00 46.12           C  
ATOM   6314  OG  SER B 968     191.035 191.478 164.394  1.00 41.08           O  
ATOM   6315  N   ASN B 969     191.927 194.159 165.428  1.00 35.51           N  
ATOM   6316  CA  ASN B 969     192.987 194.515 166.378  1.00 29.31           C  
ATOM   6317  C   ASN B 969     192.752 195.819 167.123  1.00 29.30           C  
ATOM   6318  O   ASN B 969     192.894 195.852 168.342  1.00 34.91           O  
ATOM   6319  CB  ASN B 969     194.358 194.547 165.687  1.00 34.37           C  
ATOM   6320  CG  ASN B 969     194.919 193.156 165.542  1.00 41.88           C  
ATOM   6321  OD1 ASN B 969     194.610 192.287 166.329  1.00 46.07           O  
ATOM   6322  ND2 ASN B 969     195.739 192.881 164.561  1.00 40.97           N  
ATOM   6323  N   PHE B 970     192.369 196.895 166.451  1.00 31.87           N  
ATOM   6324  CA  PHE B 970     192.066 198.139 167.149  1.00 34.86           C  
ATOM   6325  C   PHE B 970     190.753 198.061 167.939  1.00 37.93           C  
ATOM   6326  O   PHE B 970     190.632 198.721 168.966  1.00 38.76           O  
ATOM   6327  CB  PHE B 970     192.150 199.318 166.178  1.00 44.10           C  
ATOM   6328  CG  PHE B 970     193.493 199.396 165.473  1.00 43.30           C  
ATOM   6329  CD1 PHE B 970     193.552 199.405 164.070  1.00 41.88           C  
ATOM   6330  CD2 PHE B 970     194.688 199.410 166.217  1.00 39.30           C  
ATOM   6331  CE1 PHE B 970     194.798 199.403 163.418  1.00 46.12           C  
ATOM   6332  CE2 PHE B 970     195.932 199.410 165.568  1.00 36.62           C  
ATOM   6333  CZ  PHE B 970     195.988 199.393 164.167  1.00 43.09           C  
ATOM   6334  N   GLY B 971     189.817 197.175 167.579  1.00 38.27           N  
ATOM   6335  CA  GLY B 971     188.646 196.847 168.399  1.00 34.48           C  
ATOM   6336  C   GLY B 971     188.964 195.972 169.622  1.00 36.53           C  
ATOM   6337  O   GLY B 971     188.420 196.192 170.703  1.00 38.25           O  
ATOM   6338  N   ALA B 972     189.868 195.003 169.485  1.00 33.58           N  
ATOM   6339  CA  ALA B 972     190.311 194.139 170.576  1.00 29.77           C  
ATOM   6340  C   ALA B 972     191.118 194.956 171.587  1.00 34.06           C  
ATOM   6341  O   ALA B 972     190.778 194.994 172.767  1.00 39.48           O  
ATOM   6342  CB  ALA B 972     191.128 192.968 170.013  1.00 30.54           C  
ATOM   6343  N   ILE B 973     192.129 195.690 171.111  1.00 28.55           N  
ATOM   6344  CA  ILE B 973     192.946 196.561 171.951  1.00 22.65           C  
ATOM   6345  C   ILE B 973     192.091 197.660 172.580  1.00 26.34           C  
ATOM   6346  O   ILE B 973     192.289 197.955 173.749  1.00 35.18           O  
ATOM   6347  CB  ILE B 973     194.141 197.121 171.158  1.00 22.08           C  
ATOM   6348  CG1 ILE B 973     195.130 195.983 170.835  1.00 21.58           C  
ATOM   6349  CG2 ILE B 973     194.864 198.231 171.938  1.00 24.06           C  
ATOM   6350  CD1 ILE B 973     196.190 196.377 169.802  1.00 27.39           C  
ATOM   6351  N   SER B 974     191.091 198.206 171.886  1.00 31.01           N  
ATOM   6352  CA  SER B 974     190.128 199.135 172.504  1.00 31.71           C  
ATOM   6353  C   SER B 974     189.517 198.542 173.770  1.00 29.82           C  
ATOM   6354  O   SER B 974     189.585 199.174 174.817  1.00 37.33           O  
ATOM   6355  CB  SER B 974     189.033 199.519 171.502  1.00 46.76           C  
ATOM   6356  OG  SER B 974     187.891 200.087 172.113  1.00 43.76           O  
ATOM   6357  N   SER B 975     188.982 197.318 173.723  1.00 30.88           N  
ATOM   6358  CA  SER B 975     188.327 196.702 174.884  1.00 33.96           C  
ATOM   6359  C   SER B 975     189.305 196.257 175.985  1.00 34.01           C  
ATOM   6360  O   SER B 975     189.117 196.589 177.158  1.00 37.39           O  
ATOM   6361  CB  SER B 975     187.441 195.543 174.430  1.00 46.72           C  
ATOM   6362  OG  SER B 975     186.723 195.018 175.534  1.00 49.27           O  
ATOM   6363  N   VAL B 976     190.379 195.541 175.633  1.00 28.38           N  
ATOM   6364  CA  VAL B 976     191.362 195.023 176.604  1.00 26.86           C  
ATOM   6365  C   VAL B 976     192.148 196.140 177.296  1.00 23.77           C  
ATOM   6366  O   VAL B 976     192.411 196.053 178.491  1.00 32.89           O  
ATOM   6367  CB  VAL B 976     192.326 194.026 175.940  1.00 32.49           C  
ATOM   6368  CG1 VAL B 976     193.294 193.402 176.948  1.00 28.41           C  
ATOM   6369  CG2 VAL B 976     191.585 192.857 175.282  1.00 51.36           C  
ATOM   6370  N   LEU B 977     192.510 197.204 176.577  1.00 23.79           N  
ATOM   6371  CA  LEU B 977     193.245 198.350 177.105  1.00 24.90           C  
ATOM   6372  C   LEU B 977     192.321 199.324 177.847  1.00 34.48           C  
ATOM   6373  O   LEU B 977     192.748 199.884 178.851  1.00 40.11           O  
ATOM   6374  CB  LEU B 977     194.021 198.992 175.941  1.00 24.94           C  
ATOM   6375  CG  LEU B 977     195.335 199.681 176.308  1.00 30.84           C  
ATOM   6376  CD1 LEU B 977     196.283 199.649 175.113  1.00 37.16           C  
ATOM   6377  CD2 LEU B 977     195.137 201.140 176.676  1.00 36.89           C  
ATOM   6378  N   ASN B 978     191.045 199.463 177.465  1.00 33.49           N  
ATOM   6379  CA  ASN B 978     190.083 200.166 178.317  1.00 31.59           C  
ATOM   6380  C   ASN B 978     189.917 199.461 179.662  1.00 38.71           C  
ATOM   6381  O   ASN B 978     189.877 200.132 180.683  1.00 45.89           O  
ATOM   6382  CB  ASN B 978     188.706 200.333 177.650  1.00 36.39           C  
ATOM   6383  CG  ASN B 978     188.536 201.686 176.986  1.00 58.75           C  
ATOM   6384  OD1 ASN B 978     188.845 202.723 177.553  1.00 67.57           O  
ATOM   6385  ND2 ASN B 978     188.007 201.750 175.793  1.00 61.58           N  
ATOM   6386  N   ASP B 979     189.850 198.130 179.699  1.00 35.06           N  
ATOM   6387  CA  ASP B 979     189.759 197.400 180.969  1.00 28.04           C  
ATOM   6388  C   ASP B 979     191.007 197.562 181.832  1.00 28.96           C  
ATOM   6389  O   ASP B 979     190.865 197.918 182.995  1.00 36.42           O  
ATOM   6390  CB  ASP B 979     189.442 195.917 180.748  1.00 35.04           C  
ATOM   6391  CG  ASP B 979     187.966 195.645 180.429  1.00 55.14           C  
ATOM   6392  OD1 ASP B 979     187.098 196.509 180.696  1.00 58.72           O  
ATOM   6393  OD2 ASP B 979     187.657 194.520 179.973  1.00 65.74           O1-
ATOM   6394  N   ILE B 980     192.217 197.396 181.285  1.00 22.61           N  
ATOM   6395  CA  ILE B 980     193.473 197.719 181.988  1.00 21.01           C  
ATOM   6396  C   ILE B 980     193.450 199.151 182.553  1.00 22.55           C  
ATOM   6397  O   ILE B 980     193.834 199.343 183.696  1.00 31.36           O  
ATOM   6398  CB  ILE B 980     194.692 197.510 181.059  1.00 20.53           C  
ATOM   6399  CG1 ILE B 980     195.042 196.038 180.776  1.00 17.39           C  
ATOM   6400  CG2 ILE B 980     195.935 198.218 181.588  1.00 20.44           C  
ATOM   6401  CD1 ILE B 980     195.522 195.223 181.978  1.00 20.01           C  
ATOM   6402  N   LEU B 981     192.981 200.160 181.820  1.00 26.91           N  
ATOM   6403  CA  LEU B 981     192.868 201.540 182.309  1.00 30.91           C  
ATOM   6404  C   LEU B 981     191.843 201.665 183.446  1.00 31.82           C  
ATOM   6405  O   LEU B 981     192.123 202.246 184.489  1.00 34.63           O  
ATOM   6406  CB  LEU B 981     192.468 202.461 181.139  1.00 35.77           C  
ATOM   6407  CG  LEU B 981     193.638 202.856 180.235  1.00 38.95           C  
ATOM   6408  CD1 LEU B 981     193.126 203.424 178.912  1.00 41.97           C  
ATOM   6409  CD2 LEU B 981     194.487 203.935 180.898  1.00 33.84           C  
ATOM   6410  N   SER B 982     190.652 201.105 183.262  1.00 29.71           N  
ATOM   6411  CA  SER B 982     189.534 201.183 184.205  1.00 29.91           C  
ATOM   6412  C   SER B 982     189.795 200.434 185.514  1.00 29.92           C  
ATOM   6413  O   SER B 982     189.442 200.926 186.587  1.00 39.00           O  
ATOM   6414  CB  SER B 982     188.285 200.653 183.497  1.00 38.82           C  
ATOM   6415  OG  SER B 982     187.142 200.759 184.309  1.00 44.85           O  
ATOM   6416  N   ARG B 983     190.520 199.319 185.438  1.00 24.82           N  
ATOM   6417  CA  ARG B 983     190.850 198.550 186.637  1.00 22.85           C  
ATOM   6418  C   ARG B 983     192.102 199.111 187.350  1.00 25.88           C  
ATOM   6419  O   ARG B 983     192.179 199.065 188.574  1.00 33.14           O  
ATOM   6420  CB  ARG B 983     190.966 197.048 186.327  1.00 19.06           C  
ATOM   6421  CG  ARG B 983     192.313 196.584 185.814  1.00 20.98           C  
ATOM   6422  CD  ARG B 983     192.265 195.178 185.245  1.00 21.45           C  
ATOM   6423  NE  ARG B 983     192.522 194.168 186.264  1.00 27.16           N  
ATOM   6424  CZ  ARG B 983     192.880 192.916 185.999  1.00 32.98           C  
ATOM   6425  NH1 ARG B 983     193.026 192.517 184.746  1.00 34.29           N  
ATOM   6426  NH2 ARG B 983     193.094 192.064 186.990  1.00 42.91           N  
ATOM   6427  N   LEU B 984     193.075 199.636 186.603  1.00 22.07           N  
ATOM   6428  CA  LEU B 984     194.237 200.248 187.240  1.00 19.85           C  
ATOM   6429  C   LEU B 984     193.846 201.523 187.971  1.00 25.10           C  
ATOM   6430  O   LEU B 984     194.361 201.771 189.047  1.00 32.93           O  
ATOM   6431  CB  LEU B 984     195.351 200.465 186.211  1.00 23.52           C  
ATOM   6432  CG  LEU B 984     196.717 200.878 186.783  1.00 28.08           C  
ATOM   6433  CD1 LEU B 984     197.144 200.029 187.980  1.00 37.07           C  
ATOM   6434  CD2 LEU B 984     197.772 200.650 185.700  1.00 29.16           C  
ATOM   6435  N   ASP B 985     192.876 202.280 187.462  1.00 30.33           N  
ATOM   6436  CA  ASP B 985     192.276 203.414 188.185  1.00 29.87           C  
ATOM   6437  C   ASP B 985     191.599 202.978 189.494  1.00 29.31           C  
ATOM   6438  O   ASP B 985     191.750 203.638 190.521  1.00 31.53           O  
ATOM   6439  CB  ASP B 985     191.231 204.128 187.305  1.00 39.09           C  
ATOM   6440  CG  ASP B 985     191.753 204.929 186.110  1.00 46.89           C  
ATOM   6441  OD1 ASP B 985     192.972 205.150 185.943  1.00 38.19           O  
ATOM   6442  OD2 ASP B 985     190.900 205.418 185.341  1.00 48.36           O1-
ATOM   6443  N   LYS B 986     190.883 201.849 189.493  1.00 26.23           N  
ATOM   6444  CA  LYS B 986     190.295 201.284 190.716  1.00 24.23           C  
ATOM   6445  C   LYS B 986     191.386 200.888 191.714  1.00 27.26           C  
ATOM   6446  O   LYS B 986     191.360 201.352 192.843  1.00 33.66           O  
ATOM   6447  CB  LYS B 986     189.375 200.112 190.349  1.00 25.29           C  
ATOM   6448  CG  LYS B 986     188.703 199.404 191.532  1.00 25.09           C  
ATOM   6449  CD  LYS B 986     187.759 200.268 192.382  1.00 43.14           C  
ATOM   6450  CE  LYS B 986     186.545 200.857 191.646  1.00 40.66           C  
ATOM   6451  NZ  LYS B 986     185.601 199.822 191.159  1.00 68.72           N  
ATOM   6452  N   VAL B 987     192.381 200.098 191.322  1.00 28.31           N  
ATOM   6453  CA  VAL B 987     193.490 199.677 192.203  1.00 22.67           C  
ATOM   6454  C   VAL B 987     194.360 200.835 192.721  1.00 20.77           C  
ATOM   6455  O   VAL B 987     194.770 200.807 193.875  1.00 28.03           O  
ATOM   6456  CB  VAL B 987     194.344 198.612 191.501  1.00 32.16           C  
ATOM   6457  CG1 VAL B 987     195.567 198.186 192.320  1.00 26.38           C  
ATOM   6458  CG2 VAL B 987     193.503 197.355 191.270  1.00 34.63           C  
ATOM   6459  N   GLU B 988     194.612 201.882 191.941  1.00 23.39           N  
ATOM   6460  CA  GLU B 988     195.301 203.089 192.423  1.00 32.67           C  
ATOM   6461  C   GLU B 988     194.432 203.970 193.333  1.00 37.94           C  
ATOM   6462  O   GLU B 988     194.969 204.751 194.119  1.00 42.43           O  
ATOM   6463  CB  GLU B 988     195.863 203.880 191.226  1.00 31.59           C  
ATOM   6464  CG  GLU B 988     197.042 204.807 191.592  1.00 51.63           C  
ATOM   6465  CD  GLU B 988     196.703 206.217 192.113  1.00 57.83           C  
ATOM   6466  OE1 GLU B 988     195.671 206.799 191.724  1.00 68.83           O  
ATOM   6467  OE2 GLU B 988     197.525 206.792 192.865  1.00 53.83           O1-
ATOM   6468  N   ALA B 989     193.099 203.841 193.292  1.00 29.83           N  
ATOM   6469  CA  ALA B 989     192.210 204.437 194.293  1.00 29.52           C  
ATOM   6470  C   ALA B 989     192.202 203.629 195.588  1.00 33.30           C  
ATOM   6471  O   ALA B 989     192.412 204.183 196.664  1.00 41.32           O  
ATOM   6472  CB  ALA B 989     190.790 204.559 193.739  1.00 30.74           C  
ATOM   6473  N   GLU B 990     191.977 202.317 195.505  1.00 33.40           N  
ATOM   6474  CA  GLU B 990     191.805 201.454 196.679  1.00 24.92           C  
ATOM   6475  C   GLU B 990     193.049 201.490 197.563  1.00 27.48           C  
ATOM   6476  O   GLU B 990     192.921 201.652 198.774  1.00 39.43           O  
ATOM   6477  CB  GLU B 990     191.494 200.007 196.261  1.00 27.17           C  
ATOM   6478  CG  GLU B 990     190.230 199.811 195.405  1.00 36.83           C  
ATOM   6479  CD  GLU B 990     188.936 199.658 196.199  1.00 56.54           C  
ATOM   6480  OE1 GLU B 990     188.382 198.539 196.227  1.00 54.81           O  
ATOM   6481  OE2 GLU B 990     188.438 200.658 196.753  1.00 61.97           O1-
ATOM   6482  N   VAL B 991     194.256 201.458 196.980  1.00 28.15           N  
ATOM   6483  CA  VAL B 991     195.533 201.481 197.722  1.00 33.12           C  
ATOM   6484  C   VAL B 991     195.727 202.751 198.571  1.00 32.96           C  
ATOM   6485  O   VAL B 991     196.424 202.697 199.577  1.00 46.53           O  
ATOM   6486  CB  VAL B 991     196.714 201.192 196.768  1.00 38.29           C  
ATOM   6487  CG1 VAL B 991     197.243 202.425 196.038  1.00 42.88           C  
ATOM   6488  CG2 VAL B 991     197.884 200.521 197.479  1.00 54.54           C  
ATOM   6489  N   GLN B 992     195.069 203.871 198.244  1.00 29.95           N  
ATOM   6490  CA  GLN B 992     195.044 205.103 199.053  1.00 32.43           C  
ATOM   6491  C   GLN B 992     193.970 205.095 200.155  1.00 30.21           C  
ATOM   6492  O   GLN B 992     194.134 205.714 201.200  1.00 34.77           O  
ATOM   6493  CB  GLN B 992     194.720 206.312 198.174  1.00 39.67           C  
ATOM   6494  CG  GLN B 992     195.695 206.604 197.040  1.00 38.29           C  
ATOM   6495  CD  GLN B 992     195.128 207.735 196.191  1.00 41.30           C  
ATOM   6496  OE1 GLN B 992     195.138 208.898 196.575  1.00 49.85           O  
ATOM   6497  NE2 GLN B 992     194.544 207.430 195.060  1.00 43.75           N  
ATOM   6498  N   ILE B 993     192.845 204.418 199.940  1.00 29.64           N  
ATOM   6499  CA  ILE B 993     191.776 204.287 200.929  1.00 25.07           C  
ATOM   6500  C   ILE B 993     192.175 203.243 201.983  1.00 27.36           C  
ATOM   6501  O   ILE B 993     191.954 203.458 203.170  1.00 38.48           O  
ATOM   6502  CB  ILE B 993     190.442 203.982 200.222  1.00 28.79           C  
ATOM   6503  CG1 ILE B 993     190.015 205.199 199.380  1.00 35.75           C  
ATOM   6504  CG2 ILE B 993     189.336 203.667 201.232  1.00 28.80           C  
ATOM   6505  CD1 ILE B 993     188.892 204.904 198.392  1.00 50.04           C  
ATOM   6506  N   ASP B 994     192.844 202.157 201.587  1.00 24.43           N  
ATOM   6507  CA  ASP B 994     193.475 201.191 202.494  1.00 23.96           C  
ATOM   6508  C   ASP B 994     194.553 201.829 203.365  1.00 27.72           C  
ATOM   6509  O   ASP B 994     194.779 201.403 204.499  1.00 27.44           O  
ATOM   6510  CB  ASP B 994     194.156 200.080 201.685  1.00 27.61           C  
ATOM   6511  CG  ASP B 994     193.203 199.025 201.135  1.00 38.49           C  
ATOM   6512  OD1 ASP B 994     193.460 198.519 200.023  1.00 34.55           O  
ATOM   6513  OD2 ASP B 994     192.288 198.587 201.869  1.00 50.42           O1-
ATOM   6514  N   ARG B 995     195.215 202.851 202.847  1.00 27.34           N  
ATOM   6515  CA  ARG B 995     196.260 203.509 203.609  1.00 21.34           C  
ATOM   6516  C   ARG B 995     195.623 204.178 204.828  1.00 24.30           C  
ATOM   6517  O   ARG B 995     196.046 203.965 205.958  1.00 32.64           O  
ATOM   6518  CB  ARG B 995     197.013 204.504 202.720  1.00 33.14           C  
ATOM   6519  CG  ARG B 995     198.515 204.493 202.928  1.00 42.73           C  
ATOM   6520  CD  ARG B 995     199.217 205.442 201.973  1.00 43.11           C  
ATOM   6521  NE  ARG B 995     199.938 204.763 200.901  1.00 36.64           N  
ATOM   6522  CZ  ARG B 995     199.591 204.831 199.622  1.00 38.51           C  
ATOM   6523  NH1 ARG B 995     198.548 205.559 199.254  1.00 39.64           N  
ATOM   6524  NH2 ARG B 995     200.295 204.183 198.709  1.00 48.70           N  
ATOM   6525  N   LEU B 996     194.591 204.974 204.575  1.00 24.49           N  
ATOM   6526  CA  LEU B 996     193.864 205.677 205.616  1.00 19.19           C  
ATOM   6527  C   LEU B 996     193.093 204.736 206.529  1.00 15.74           C  
ATOM   6528  O   LEU B 996     193.073 204.980 207.722  1.00 26.13           O  
ATOM   6529  CB  LEU B 996     192.963 206.724 204.965  1.00 23.09           C  
ATOM   6530  CG  LEU B 996     192.244 207.614 205.978  1.00 24.43           C  
ATOM   6531  CD1 LEU B 996     193.218 208.410 206.832  1.00 34.72           C  
ATOM   6532  CD2 LEU B 996     191.375 208.600 205.224  1.00 34.42           C  
ATOM   6533  N   ILE B 997     192.500 203.645 206.045  1.00 18.08           N  
ATOM   6534  CA  ILE B 997     191.922 202.631 206.952  1.00 15.66           C  
ATOM   6535  C   ILE B 997     192.994 202.107 207.908  1.00 14.62           C  
ATOM   6536  O   ILE B 997     192.780 202.133 209.109  1.00 19.16           O  
ATOM   6537  CB  ILE B 997     191.225 201.483 206.197  1.00 20.04           C  
ATOM   6538  CG1 ILE B 997     189.945 201.961 205.478  1.00 25.48           C  
ATOM   6539  CG2 ILE B 997     190.848 200.350 207.162  1.00 20.37           C  
ATOM   6540  CD1 ILE B 997     189.463 201.010 204.373  1.00 29.47           C  
ATOM   6541  N   THR B 998     194.173 201.738 207.421  1.00 15.98           N  
ATOM   6542  CA  THR B 998     195.274 201.215 208.245  1.00 14.76           C  
ATOM   6543  C   THR B 998     195.832 202.202 209.284  1.00 16.08           C  
ATOM   6544  O   THR B 998     196.223 201.777 210.365  1.00 18.80           O  
ATOM   6545  CB  THR B 998     196.378 200.698 207.325  1.00 22.17           C  
ATOM   6546  OG1 THR B 998     195.829 199.769 206.418  1.00 22.51           O  
ATOM   6547  CG2 THR B 998     197.495 200.015 208.099  1.00 15.28           C  
ATOM   6548  N   GLY B 999     195.821 203.512 209.045  1.00 14.37           N  
ATOM   6549  CA  GLY B 999     196.103 204.511 210.078  1.00 14.82           C  
ATOM   6550  C   GLY B 999     194.934 204.799 211.034  1.00 15.91           C  
ATOM   6551  O   GLY B 999     195.138 205.203 212.182  1.00 24.68           O  
ATOM   6552  N   ARG B1000     193.723 204.488 210.611  1.00 14.44           N  
ATOM   6553  CA  ARG B1000     192.612 204.548 211.545  1.00  9.09           C  
ATOM   6554  C   ARG B1000     192.567 203.252 212.392  1.00 18.36           C  
ATOM   6555  O   ARG B1000     192.067 203.273 213.511  1.00 27.33           O  
ATOM   6556  CB  ARG B1000     191.318 204.839 210.840  1.00 10.98           C  
ATOM   6557  CG  ARG B1000     191.182 206.320 210.602  1.00 19.62           C  
ATOM   6558  CD  ARG B1000     190.165 206.594 209.539  1.00 17.09           C  
ATOM   6559  NE  ARG B1000     189.754 207.984 209.541  1.00 24.66           N  
ATOM   6560  CZ  ARG B1000     188.712 208.435 210.223  1.00 27.57           C  
ATOM   6561  NH1 ARG B1000     187.984 207.607 210.951  1.00 27.89           N  
ATOM   6562  NH2 ARG B1000     188.402 209.713 210.179  1.00 31.73           N  
ATOM   6563  N   LEU B1001     193.076 202.135 211.864  1.00 18.64           N  
ATOM   6564  CA  LEU B1001     193.206 200.934 212.682  1.00 12.14           C  
ATOM   6565  C   LEU B1001     194.033 201.235 213.920  1.00 16.20           C  
ATOM   6566  O   LEU B1001     193.614 200.859 214.998  1.00 20.80           O  
ATOM   6567  CB  LEU B1001     193.825 199.765 211.903  1.00 13.80           C  
ATOM   6568  CG  LEU B1001     192.996 199.174 210.760  1.00 13.66           C  
ATOM   6569  CD1 LEU B1001     193.659 197.926 210.206  1.00 12.59           C  
ATOM   6570  CD2 LEU B1001     191.600 198.793 211.206  1.00 11.51           C  
ATOM   6571  N   GLN B1002     195.134 201.981 213.808  1.00  0.00           N  
ATOM   6572  CA  GLN B1002     195.986 202.325 214.955  1.00 20.84           C  
ATOM   6573  C   GLN B1002     195.277 203.234 215.954  1.00 20.66           C  
ATOM   6574  O   GLN B1002     195.472 203.131 217.161  1.00 23.91           O  
ATOM   6575  CB  GLN B1002     197.283 203.025 214.509  1.00 12.77           C  
ATOM   6576  CG  GLN B1002     198.002 202.424 213.301  1.00 14.48           C  
ATOM   6577  CD  GLN B1002     198.107 200.909 213.320  1.00 12.77           C  
ATOM   6578  OE1 GLN B1002     198.564 200.296 214.266  1.00 12.97           O  
ATOM   6579  NE2 GLN B1002     197.685 200.245 212.273  1.00 11.61           N  
ATOM   6580  N   SER B1003     194.427 204.133 215.467  1.00 17.84           N  
ATOM   6581  CA  SER B1003     193.601 204.983 216.330  1.00 15.48           C  
ATOM   6582  C   SER B1003     192.590 204.147 217.109  1.00 14.73           C  
ATOM   6583  O   SER B1003     192.432 204.337 218.303  1.00 21.53           O  
ATOM   6584  CB  SER B1003     192.890 206.056 215.509  1.00 25.85           C  
ATOM   6585  OG  SER B1003     193.810 206.867 214.803  1.00 36.68           O  
ATOM   6586  N   LEU B1004     191.947 203.166 216.483  1.00 15.97           N  
ATOM   6587  CA  LEU B1004     191.096 202.199 217.170  1.00 14.77           C  
ATOM   6588  C   LEU B1004     191.899 201.238 218.089  1.00 17.13           C  
ATOM   6589  O   LEU B1004     191.399 200.849 219.136  1.00 24.12           O  
ATOM   6590  CB  LEU B1004     190.265 201.460 216.115  1.00 14.76           C  
ATOM   6591  CG  LEU B1004     189.382 200.353 216.694  1.00 14.20           C  
ATOM   6592  CD1 LEU B1004     188.285 200.874 217.602  1.00 18.55           C  
ATOM   6593  CD2 LEU B1004     188.703 199.586 215.580  1.00 33.30           C  
ATOM   6594  N   GLN B1005     193.147 200.883 217.776  1.00 15.08           N  
ATOM   6595  CA  GLN B1005     194.006 200.089 218.663  1.00 10.52           C  
ATOM   6596  C   GLN B1005     194.531 200.891 219.867  1.00 19.24           C  
ATOM   6597  O   GLN B1005     194.676 200.342 220.956  1.00 25.76           O  
ATOM   6598  CB  GLN B1005     195.165 199.498 217.856  1.00 13.15           C  
ATOM   6599  CG  GLN B1005     195.876 198.382 218.617  1.00 15.58           C  
ATOM   6600  CD  GLN B1005     194.975 197.196 218.909  1.00 16.16           C  
ATOM   6601  OE1 GLN B1005     194.252 196.707 218.062  1.00 23.35           O  
ATOM   6602  NE2 GLN B1005     194.978 196.682 220.114  1.00 22.38           N  
ATOM   6603  N   THR B1006     194.738 202.201 219.731  1.00 21.51           N  
ATOM   6604  CA  THR B1006     194.938 203.110 220.867  1.00 15.55           C  
ATOM   6605  C   THR B1006     193.674 203.254 221.703  1.00 15.97           C  
ATOM   6606  O   THR B1006     193.764 203.245 222.925  1.00 24.19           O  
ATOM   6607  CB  THR B1006     195.424 204.474 220.403  1.00 20.78           C  
ATOM   6608  OG1 THR B1006     196.707 204.289 219.886  1.00 31.68           O  
ATOM   6609  CG2 THR B1006     195.565 205.511 221.513  1.00 23.29           C  
ATOM   6610  N   TYR B1007     192.496 203.292 221.078  1.00 18.42           N  
ATOM   6611  CA  TYR B1007     191.237 203.234 221.795  1.00 12.48           C  
ATOM   6612  C   TYR B1007     191.137 201.957 222.603  1.00 15.45           C  
ATOM   6613  O   TYR B1007     190.959 202.039 223.808  1.00 25.04           O  
ATOM   6614  CB  TYR B1007     190.067 203.415 220.836  1.00 19.86           C  
ATOM   6615  CG  TYR B1007     188.711 203.247 221.473  1.00 17.02           C  
ATOM   6616  CD1 TYR B1007     188.090 204.338 222.095  1.00 22.77           C  
ATOM   6617  CD2 TYR B1007     188.073 201.999 221.448  1.00 17.49           C  
ATOM   6618  CE1 TYR B1007     186.832 204.181 222.697  1.00 27.65           C  
ATOM   6619  CE2 TYR B1007     186.816 201.835 222.048  1.00 23.96           C  
ATOM   6620  CZ  TYR B1007     186.186 202.930 222.663  1.00 28.62           C  
ATOM   6621  OH  TYR B1007     184.931 202.803 223.161  1.00 34.36           O  
ATOM   6622  N   VAL B1008     191.327 200.787 222.000  1.00 12.41           N  
ATOM   6623  CA  VAL B1008     191.243 199.488 222.682  1.00 11.27           C  
ATOM   6624  C   VAL B1008     192.293 199.347 223.780  1.00 17.15           C  
ATOM   6625  O   VAL B1008     191.964 198.914 224.876  1.00 24.12           O  
ATOM   6626  CB  VAL B1008     191.324 198.363 221.638  1.00 17.30           C  
ATOM   6627  CG1 VAL B1008     191.685 196.985 222.186  1.00 12.28           C  
ATOM   6628  CG2 VAL B1008     189.967 198.267 220.936  1.00 22.73           C  
ATOM   6629  N   THR B1009     193.530 199.783 223.563  1.00 18.45           N  
ATOM   6630  CA  THR B1009     194.563 199.764 224.606  1.00 10.23           C  
ATOM   6631  C   THR B1009     194.195 200.646 225.798  1.00 12.79           C  
ATOM   6632  O   THR B1009     194.171 200.138 226.905  1.00 14.88           O  
ATOM   6633  CB  THR B1009     195.939 200.169 224.068  1.00 20.39           C  
ATOM   6634  OG1 THR B1009     196.297 199.401 222.942  1.00 25.98           O  
ATOM   6635  CG2 THR B1009     197.027 199.995 225.126  1.00 15.51           C  
ATOM   6636  N   GLN B1010     193.833 201.919 225.617  1.00 14.37           N  
ATOM   6637  CA  GLN B1010     193.406 202.809 226.710  1.00 13.54           C  
ATOM   6638  C   GLN B1010     192.108 202.356 227.411  1.00 15.70           C  
ATOM   6639  O   GLN B1010     191.918 202.656 228.585  1.00 18.87           O  
ATOM   6640  CB  GLN B1010     193.261 204.233 226.164  1.00 13.77           C  
ATOM   6641  CG  GLN B1010     194.597 204.957 225.969  1.00 24.24           C  
ATOM   6642  CD  GLN B1010     194.476 206.463 225.714  1.00 33.77           C  
ATOM   6643  OE1 GLN B1010     195.175 207.279 226.290  1.00 39.97           O  
ATOM   6644  NE2 GLN B1010     193.571 206.924 224.893  1.00 28.81           N  
ATOM   6645  N   GLN B1011     191.238 201.604 226.748  1.00 13.58           N  
ATOM   6646  CA  GLN B1011     190.041 201.006 227.330  1.00  9.75           C  
ATOM   6647  C   GLN B1011     190.334 199.704 228.090  1.00 13.52           C  
ATOM   6648  O   GLN B1011     189.611 199.388 229.029  1.00 18.61           O  
ATOM   6649  CB  GLN B1011     189.004 200.789 226.215  1.00 16.17           C  
ATOM   6650  CG  GLN B1011     187.552 200.976 226.656  1.00 20.71           C  
ATOM   6651  CD  GLN B1011     187.184 202.412 227.037  1.00 27.32           C  
ATOM   6652  OE1 GLN B1011     187.910 203.376 226.851  1.00 24.78           O  
ATOM   6653  NE2 GLN B1011     186.017 202.620 227.591  1.00 40.44           N  
ATOM   6654  N   LEU B1012     191.390 198.953 227.748  1.00 14.81           N  
ATOM   6655  CA  LEU B1012     191.879 197.815 228.533  1.00 11.81           C  
ATOM   6656  C   LEU B1012     192.749 198.270 229.704  1.00 13.16           C  
ATOM   6657  O   LEU B1012     192.628 197.743 230.800  1.00 17.64           O  
ATOM   6658  CB  LEU B1012     192.692 196.858 227.653  1.00 15.28           C  
ATOM   6659  CG  LEU B1012     191.909 196.109 226.565  1.00 15.59           C  
ATOM   6660  CD1 LEU B1012     192.898 195.271 225.765  1.00  8.73           C  
ATOM   6661  CD2 LEU B1012     190.839 195.197 227.136  1.00 38.47           C  
ATOM   6662  N   ILE B1013     193.595 199.277 229.503  1.00 13.58           N  
ATOM   6663  CA  ILE B1013     194.409 199.905 230.540  1.00  6.92           C  
ATOM   6664  C   ILE B1013     193.494 200.361 231.667  1.00 12.61           C  
ATOM   6665  O   ILE B1013     193.684 199.950 232.808  1.00 18.38           O  
ATOM   6666  CB  ILE B1013     195.235 201.055 229.915  1.00 12.68           C  
ATOM   6667  CG1 ILE B1013     196.448 200.539 229.108  1.00 13.73           C  
ATOM   6668  CG2 ILE B1013     195.677 202.145 230.899  1.00 21.33           C  
ATOM   6669  CD1 ILE B1013     197.661 200.081 229.916  1.00 17.51           C  
ATOM   6670  N   ARG B1014     192.437 201.130 231.371  1.00 13.09           N  
ATOM   6671  CA  ARG B1014     191.489 201.619 232.382  1.00 10.88           C  
ATOM   6672  C   ARG B1014     190.770 200.488 233.086  1.00 10.27           C  
ATOM   6673  O   ARG B1014     190.624 200.554 234.294  1.00 23.84           O  
ATOM   6674  CB  ARG B1014     190.518 202.624 231.756  1.00 12.62           C  
ATOM   6675  CG  ARG B1014     189.515 203.158 232.783  1.00 13.08           C  
ATOM   6676  CD  ARG B1014     188.537 204.157 232.166  1.00 25.93           C  
ATOM   6677  NE  ARG B1014     187.495 204.541 233.135  1.00 39.32           N  
ATOM   6678  CZ  ARG B1014     187.600 205.457 234.071  1.00 46.93           C  
ATOM   6679  NH1 ARG B1014     186.615 205.708 234.869  1.00 54.90           N  
ATOM   6680  NH2 ARG B1014     188.693 206.126 234.234  1.00 48.95           N  
ATOM   6681  N   ALA B1015     190.380 199.433 232.390  1.00 10.43           N  
ATOM   6682  CA  ALA B1015     189.744 198.277 233.019  1.00 11.48           C  
ATOM   6683  C   ALA B1015     190.671 197.456 233.955  1.00 16.31           C  
ATOM   6684  O   ALA B1015     190.207 196.870 234.931  1.00 27.04           O  
ATOM   6685  CB  ALA B1015     189.139 197.439 231.903  1.00 19.35           C  
ATOM   6686  N   ALA B1016     191.980 197.448 233.716  1.00 13.49           N  
ATOM   6687  CA  ALA B1016     192.975 196.896 234.632  1.00 13.58           C  
ATOM   6688  C   ALA B1016     193.329 197.826 235.818  1.00 13.98           C  
ATOM   6689  O   ALA B1016     193.771 197.338 236.859  1.00 23.00           O  
ATOM   6690  CB  ALA B1016     194.214 196.513 233.829  1.00 15.99           C  
ATOM   6691  N   GLU B1017     193.094 199.144 235.734  1.00 14.01           N  
ATOM   6692  CA  GLU B1017     193.005 200.020 236.915  1.00 14.91           C  
ATOM   6693  C   GLU B1017     191.703 199.802 237.689  1.00 17.61           C  
ATOM   6694  O   GLU B1017     191.725 199.701 238.908  1.00 27.09           O  
ATOM   6695  CB  GLU B1017     193.069 201.504 236.554  1.00 17.66           C  
ATOM   6696  CG  GLU B1017     194.393 201.918 235.930  1.00 28.91           C  
ATOM   6697  CD  GLU B1017     194.408 203.421 235.641  1.00 40.77           C  
ATOM   6698  OE1 GLU B1017     194.876 203.820 234.556  1.00 32.11           O  
ATOM   6699  OE2 GLU B1017     194.050 204.250 236.510  1.00 60.54           O1-
ATOM   6700  N   ILE B1018     190.564 199.675 237.015  1.00 12.74           N  
ATOM   6701  CA  ILE B1018     189.288 199.393 237.672  1.00 15.27           C  
ATOM   6702  C   ILE B1018     189.387 198.119 238.493  1.00 19.06           C  
ATOM   6703  O   ILE B1018     188.972 198.119 239.646  1.00 31.52           O  
ATOM   6704  CB  ILE B1018     188.155 199.306 236.640  1.00 16.84           C  
ATOM   6705  CG1 ILE B1018     187.838 200.689 236.052  1.00 17.09           C  
ATOM   6706  CG2 ILE B1018     186.890 198.619 237.166  1.00 24.91           C  
ATOM   6707  CD1 ILE B1018     186.913 201.568 236.880  1.00 24.10           C  
ATOM   6708  N   ARG B1019     189.989 197.042 237.971  1.00 21.13           N  
ATOM   6709  CA  ARG B1019     190.131 195.792 238.733  1.00 19.99           C  
ATOM   6710  C   ARG B1019     191.112 195.883 239.906  1.00 20.44           C  
ATOM   6711  O   ARG B1019     190.966 195.127 240.860  1.00 30.33           O  
ATOM   6712  CB  ARG B1019     190.398 194.622 237.777  1.00 27.91           C  
ATOM   6713  CG  ARG B1019     189.094 194.224 237.061  1.00 41.03           C  
ATOM   6714  CD  ARG B1019     189.154 192.948 236.213  1.00 40.75           C  
ATOM   6715  NE  ARG B1019     190.042 193.091 235.047  1.00 33.44           N  
ATOM   6716  CZ  ARG B1019     191.333 192.825 235.021  1.00 36.80           C  
ATOM   6717  NH1 ARG B1019     191.943 192.366 236.067  1.00 37.81           N  
ATOM   6718  NH2 ARG B1019     192.052 193.000 233.957  1.00 39.54           N  
ATOM   6719  N   ALA B1020     192.023 196.854 239.939  1.00 20.38           N  
ATOM   6720  CA  ALA B1020     192.805 197.174 241.139  1.00 21.25           C  
ATOM   6721  C   ALA B1020     192.010 198.021 242.137  1.00 25.54           C  
ATOM   6722  O   ALA B1020     192.134 197.833 243.340  1.00 36.58           O  
ATOM   6723  CB  ALA B1020     194.092 197.892 240.740  1.00 20.87           C  
ATOM   6724  N   SER B1021     191.147 198.920 241.665  1.00 22.37           N  
ATOM   6725  CA  SER B1021     190.234 199.698 242.508  1.00 17.95           C  
ATOM   6726  C   SER B1021     189.129 198.838 243.132  1.00 19.23           C  
ATOM   6727  O   SER B1021     188.704 199.105 244.244  1.00 29.64           O  
ATOM   6728  CB  SER B1021     189.671 200.846 241.684  1.00 20.44           C  
ATOM   6729  OG  SER B1021     188.797 201.639 242.438  1.00 27.07           O  
ATOM   6730  N   ALA B1022     188.723 197.742 242.497  1.00 21.73           N  
ATOM   6731  CA  ALA B1022     187.906 196.694 243.102  1.00 22.99           C  
ATOM   6732  C   ALA B1022     188.657 195.819 244.136  1.00 28.95           C  
ATOM   6733  O   ALA B1022     188.053 195.366 245.107  1.00 36.92           O  
ATOM   6734  CB  ALA B1022     187.356 195.834 241.972  1.00 31.38           C  
ATOM   6735  N   ASN B1023     189.974 195.627 244.004  1.00 28.39           N  
ATOM   6736  CA  ASN B1023     190.801 195.117 245.104  1.00 23.98           C  
ATOM   6737  C   ASN B1023     190.972 196.133 246.237  1.00 24.85           C  
ATOM   6738  O   ASN B1023     190.908 195.735 247.395  1.00 31.45           O  
ATOM   6739  CB  ASN B1023     192.180 194.679 244.596  1.00 30.39           C  
ATOM   6740  CG  ASN B1023     192.208 193.296 244.017  1.00 39.48           C  
ATOM   6741  OD1 ASN B1023     191.217 192.637 243.835  1.00 39.65           O  
ATOM   6742  ND2 ASN B1023     193.375 192.792 243.731  1.00 40.09           N  
ATOM   6743  N   LEU B1024     191.130 197.428 245.951  1.00 25.80           N  
ATOM   6744  CA  LEU B1024     191.160 198.458 246.984  1.00 20.09           C  
ATOM   6745  C   LEU B1024     189.826 198.519 247.721  1.00 19.16           C  
ATOM   6746  O   LEU B1024     189.814 198.563 248.938  1.00 26.32           O  
ATOM   6747  CB  LEU B1024     191.538 199.821 246.396  1.00 22.84           C  
ATOM   6748  CG  LEU B1024     191.739 200.915 247.454  1.00 16.40           C  
ATOM   6749  CD1 LEU B1024     192.929 200.636 248.366  1.00 22.68           C  
ATOM   6750  CD2 LEU B1024     191.959 202.254 246.757  1.00 15.64           C  
ATOM   6751  N   ALA B1025     188.694 198.455 247.026  1.00 18.10           N  
ATOM   6752  CA  ALA B1025     187.380 198.356 247.630  1.00 19.38           C  
ATOM   6753  C   ALA B1025     187.222 197.093 248.472  1.00 21.14           C  
ATOM   6754  O   ALA B1025     186.478 197.141 249.435  1.00 28.42           O  
ATOM   6755  CB  ALA B1025     186.340 198.385 246.515  1.00 25.56           C  
ATOM   6756  N   ALA B1026     187.914 195.991 248.178  1.00 21.97           N  
ATOM   6757  CA  ALA B1026     187.854 194.773 248.992  1.00 20.74           C  
ATOM   6758  C   ALA B1026     188.598 194.922 250.326  1.00 25.75           C  
ATOM   6759  O   ALA B1026     188.013 194.693 251.380  1.00 33.82           O  
ATOM   6760  CB  ALA B1026     188.388 193.575 248.200  1.00 35.65           C  
ATOM   6761  N   THR B1027     189.863 195.352 250.302  1.00 25.16           N  
ATOM   6762  CA  THR B1027     190.646 195.608 251.523  1.00 21.68           C  
ATOM   6763  C   THR B1027     190.045 196.753 252.340  1.00 24.49           C  
ATOM   6764  O   THR B1027     189.839 196.603 253.538  1.00 35.67           O  
ATOM   6765  CB  THR B1027     192.131 195.819 251.211  1.00 22.82           C  
ATOM   6766  OG1 THR B1027     192.854 196.161 252.353  1.00 32.59           O  
ATOM   6767  CG2 THR B1027     192.434 196.969 250.262  1.00 36.50           C  
ATOM   6768  N   LYS B1028     189.644 197.863 251.712  1.00 24.42           N  
ATOM   6769  CA  LYS B1028     189.015 199.022 252.366  1.00 21.72           C  
ATOM   6770  C   LYS B1028     187.594 198.750 252.886  1.00 23.23           C  
ATOM   6771  O   LYS B1028     187.183 199.372 253.857  1.00 36.30           O  
ATOM   6772  CB  LYS B1028     189.059 200.195 251.378  1.00 17.76           C  
ATOM   6773  CG  LYS B1028     188.680 201.505 252.049  1.00 17.79           C  
ATOM   6774  CD  LYS B1028     188.998 202.771 251.259  1.00 20.33           C  
ATOM   6775  CE  LYS B1028     190.504 202.997 251.187  1.00 21.47           C  
ATOM   6776  NZ  LYS B1028     190.822 204.383 250.765  1.00 22.38           N  
ATOM   6777  N   MET B1029     186.844 197.809 252.316  1.00 21.37           N  
ATOM   6778  CA  MET B1029     185.628 197.269 252.932  1.00 24.02           C  
ATOM   6779  C   MET B1029     186.001 196.441 254.145  1.00 33.66           C  
ATOM   6780  O   MET B1029     185.482 196.669 255.227  1.00 47.21           O  
ATOM   6781  CB  MET B1029     184.851 196.408 251.925  1.00 24.16           C  
ATOM   6782  CG  MET B1029     183.706 195.568 252.498  1.00 29.61           C  
ATOM   6783  SD  MET B1029     182.123 196.422 252.578  1.00 61.68           S  
ATOM   6784  CE  MET B1029     181.107 195.075 253.246  1.00 48.20           C  
ATOM   6785  N   SER B1030     186.904 195.479 253.989  1.00 34.15           N  
ATOM   6786  CA  SER B1030     187.200 194.515 255.042  1.00 33.94           C  
ATOM   6787  C   SER B1030     187.739 195.175 256.301  1.00 31.64           C  
ATOM   6788  O   SER B1030     187.159 195.035 257.368  1.00 37.38           O  
ATOM   6789  CB  SER B1030     188.175 193.477 254.523  1.00 38.08           C  
ATOM   6790  OG  SER B1030     188.333 192.505 255.512  1.00 42.70           O  
ATOM   6791  N   GLU B1031     188.803 195.956 256.195  1.00 30.45           N  
ATOM   6792  CA  GLU B1031     189.526 196.492 257.350  1.00 32.82           C  
ATOM   6793  C   GLU B1031     188.790 197.582 258.118  1.00 33.23           C  
ATOM   6794  O   GLU B1031     189.252 197.992 259.180  1.00 39.82           O  
ATOM   6795  CB  GLU B1031     190.894 196.992 256.888  1.00 34.25           C  
ATOM   6796  CG  GLU B1031     191.772 195.796 256.524  1.00 34.01           C  
ATOM   6797  CD  GLU B1031     192.994 196.197 255.705  1.00 38.99           C  
ATOM   6798  OE1 GLU B1031     193.580 197.282 255.920  1.00 45.24           O  
ATOM   6799  OE2 GLU B1031     193.432 195.360 254.883  1.00 42.49           O1-
ATOM   6800  N   CYS B1032     187.659 198.067 257.605  1.00 30.49           N  
ATOM   6801  CA  CYS B1032     187.008 199.282 258.101  1.00 39.97           C  
ATOM   6802  C   CYS B1032     185.482 199.197 258.254  1.00 47.87           C  
ATOM   6803  O   CYS B1032     184.900 199.921 259.062  1.00 51.72           O  
ATOM   6804  CB  CYS B1032     187.415 200.427 257.183  1.00 30.27           C  
ATOM   6805  SG  CYS B1032     189.220 200.465 257.088  1.00 41.15           S  
ATOM   6806  N   VAL B1033     184.839 198.293 257.517  1.00 38.09           N  
ATOM   6807  CA  VAL B1033     183.463 197.869 257.760  1.00 34.83           C  
ATOM   6808  C   VAL B1033     183.435 196.652 258.674  1.00 45.37           C  
ATOM   6809  O   VAL B1033     182.622 196.627 259.594  1.00 59.65           O  
ATOM   6810  CB  VAL B1033     182.697 197.608 256.455  1.00 37.17           C  
ATOM   6811  CG1 VAL B1033     181.241 197.228 256.712  1.00 43.16           C  
ATOM   6812  CG2 VAL B1033     182.741 198.855 255.568  1.00 40.56           C  
ATOM   6813  N   LEU B1034     184.322 195.661 258.502  1.00 43.01           N  
ATOM   6814  CA  LEU B1034     184.381 194.495 259.403  1.00 37.14           C  
ATOM   6815  C   LEU B1034     185.307 194.724 260.605  1.00 35.44           C  
ATOM   6816  O   LEU B1034     185.223 193.989 261.585  1.00 39.45           O  
ATOM   6817  CB  LEU B1034     184.778 193.213 258.647  1.00 41.73           C  
ATOM   6818  CG  LEU B1034     183.964 192.923 257.374  1.00 48.30           C  
ATOM   6819  CD1 LEU B1034     184.557 191.716 256.657  1.00 47.31           C  
ATOM   6820  CD2 LEU B1034     182.501 192.620 257.693  1.00 52.65           C  
ATOM   6821  N   GLY B1035     186.166 195.739 260.541  1.00 32.28           N  
ATOM   6822  CA  GLY B1035     187.207 196.044 261.518  1.00 32.02           C  
ATOM   6823  C   GLY B1035     187.256 197.504 261.946  1.00 35.80           C  
ATOM   6824  O   GLY B1035     186.276 198.232 261.855  1.00 41.24           O  
ATOM   6825  N   GLN B1036     188.412 197.942 262.422  1.00 30.07           N  
ATOM   6826  CA  GLN B1036     188.738 199.342 262.652  1.00 33.98           C  
ATOM   6827  C   GLN B1036     190.229 199.514 262.410  1.00 34.77           C  
ATOM   6828  O   GLN B1036     191.041 198.913 263.118  1.00 34.93           O  
ATOM   6829  CB  GLN B1036     188.355 199.750 264.072  1.00 35.45           C  
ATOM   6830  CG  GLN B1036     188.831 201.156 264.457  1.00 38.62           C  
ATOM   6831  CD  GLN B1036     188.595 201.448 265.926  1.00 38.07           C  
ATOM   6832  OE1 GLN B1036     188.570 200.575 266.776  1.00 50.31           O  
ATOM   6833  NE2 GLN B1036     188.446 202.692 266.293  1.00 34.76           N  
ATOM   6834  N   SER B1037     190.590 200.298 261.402  1.00 34.00           N  
ATOM   6835  CA  SER B1037     191.978 200.418 260.983  1.00 35.63           C  
ATOM   6836  C   SER B1037     192.793 201.314 261.914  1.00 39.85           C  
ATOM   6837  O   SER B1037     192.299 202.314 262.431  1.00 42.58           O  
ATOM   6838  CB  SER B1037     192.082 200.899 259.544  1.00 37.31           C  
ATOM   6839  OG  SER B1037     193.410 200.680 259.130  1.00 37.18           O  
ATOM   6840  N   LYS B1038     194.066 200.966 262.118  1.00 39.55           N  
ATOM   6841  CA  LYS B1038     195.031 201.742 262.921  1.00 41.22           C  
ATOM   6842  C   LYS B1038     195.934 202.639 262.057  1.00 50.12           C  
ATOM   6843  O   LYS B1038     196.823 203.304 262.581  1.00 51.58           O  
ATOM   6844  CB  LYS B1038     195.796 200.768 263.838  1.00 39.63           C  
ATOM   6845  CG  LYS B1038     194.837 200.150 264.881  1.00 46.40           C  
ATOM   6846  CD  LYS B1038     195.297 198.788 265.405  1.00 48.46           C  
ATOM   6847  CE  LYS B1038     194.154 198.014 266.092  1.00 38.67           C  
ATOM   6848  NZ  LYS B1038     193.111 197.533 265.142  1.00 48.79           N  
ATOM   6849  N   ARG B1039     195.661 202.672 260.744  1.00 42.82           N  
ATOM   6850  CA  ARG B1039     196.400 203.461 259.761  1.00 36.80           C  
ATOM   6851  C   ARG B1039     195.843 204.881 259.692  1.00 35.68           C  
ATOM   6852  O   ARG B1039     194.652 205.093 259.904  1.00 36.27           O  
ATOM   6853  CB  ARG B1039     196.286 202.779 258.400  1.00 40.55           C  
ATOM   6854  CG  ARG B1039     196.980 201.427 258.341  1.00 42.05           C  
ATOM   6855  CD  ARG B1039     196.362 200.502 257.304  1.00 45.98           C  
ATOM   6856  NE  ARG B1039     196.470 201.029 255.948  1.00 48.94           N  
ATOM   6857  CZ  ARG B1039     196.372 200.278 254.858  1.00 51.83           C  
ATOM   6858  NH1 ARG B1039     196.161 198.974 254.962  1.00 54.71           N  
ATOM   6859  NH2 ARG B1039     196.485 200.831 253.660  1.00 52.91           N  
ATOM   6860  N   VAL B1040     196.699 205.854 259.392  1.00 34.18           N  
ATOM   6861  CA  VAL B1040     196.301 207.260 259.380  1.00 32.37           C  
ATOM   6862  C   VAL B1040     195.986 207.715 257.953  1.00 48.41           C  
ATOM   6863  O   VAL B1040     196.872 207.630 257.099  1.00 57.64           O  
ATOM   6864  CB  VAL B1040     197.426 208.151 259.933  1.00 30.53           C  
ATOM   6865  CG1 VAL B1040     197.004 209.611 259.913  1.00 34.01           C  
ATOM   6866  CG2 VAL B1040     197.796 207.718 261.343  1.00 43.42           C  
ATOM   6867  N   ASP B1041     194.728 208.119 257.694  1.00 45.38           N  
ATOM   6868  CA  ASP B1041     194.132 208.586 256.405  1.00 40.25           C  
ATOM   6869  C   ASP B1041     193.622 207.466 255.470  1.00 47.59           C  
ATOM   6870  O   ASP B1041     193.015 207.759 254.440  1.00 55.52           O  
ATOM   6871  CB  ASP B1041     194.907 209.683 255.636  1.00 38.97           C  
ATOM   6872  CG  ASP B1041     195.462 210.762 256.550  1.00 51.88           C  
ATOM   6873  OD1 ASP B1041     196.351 211.519 256.107  1.00 51.32           O  
ATOM   6874  OD2 ASP B1041     195.009 210.850 257.710  1.00 59.02           O1-
ATOM   6875  N   PHE B1042     193.856 206.200 255.817  1.00 47.29           N  
ATOM   6876  CA  PHE B1042     193.228 205.094 255.111  1.00 37.22           C  
ATOM   6877  C   PHE B1042     191.849 205.107 255.811  1.00 41.28           C  
ATOM   6878  O   PHE B1042     191.774 205.282 257.057  1.00 49.76           O  
ATOM   6879  CB  PHE B1042     193.950 203.776 255.340  1.00 34.56           C  
ATOM   6880  CG  PHE B1042     193.343 202.618 254.600  1.00 41.34           C  
ATOM   6881  CD1 PHE B1042     193.652 202.386 253.270  1.00 60.76           C  
ATOM   6882  CD2 PHE B1042     192.462 201.759 255.237  1.00 37.23           C  
ATOM   6883  CE1 PHE B1042     193.094 201.321 252.590  1.00 48.53           C  
ATOM   6884  CE2 PHE B1042     191.901 200.692 254.563  1.00 35.21           C  
ATOM   6885  CZ  PHE B1042     192.217 200.472 253.237  1.00 41.28           C  
ATOM   6886  N   CYS B1043     190.756 204.899 255.086  1.00 40.85           N  
ATOM   6887  CA  CYS B1043     189.399 204.955 255.679  1.00 33.56           C  
ATOM   6888  C   CYS B1043     189.084 206.382 256.291  1.00 37.48           C  
ATOM   6889  O   CYS B1043     188.745 206.496 257.469  1.00 45.37           O  
ATOM   6890  CB  CYS B1043     189.048 203.718 256.631  1.00 27.91           C  
ATOM   6891  SG  CYS B1043     189.011 202.093 255.792  1.00 33.36           S  
ATOM   6892  N   GLY B1044     189.205 207.440 255.459  1.00 41.86           N  
ATOM   6893  CA  GLY B1044     188.808 208.795 255.796  1.00 47.00           C  
ATOM   6894  C   GLY B1044     189.942 209.587 256.400  1.00 50.11           C  
ATOM   6895  O   GLY B1044     190.849 209.018 256.991  1.00 54.00           O  
ATOM   6896  N   LYS B1045     189.928 210.912 256.250  1.00 52.14           N  
ATOM   6897  CA  LYS B1045     190.983 211.758 256.824  1.00 53.03           C  
ATOM   6898  C   LYS B1045     191.069 211.545 258.346  1.00 52.11           C  
ATOM   6899  O   LYS B1045     190.039 211.423 259.008  1.00 57.14           O  
ATOM   6900  CB  LYS B1045     190.718 213.214 256.431  1.00 65.16           C  
ATOM   6901  CG  LYS B1045     191.904 214.133 256.710  1.00 65.68           C  
ATOM   6902  CD  LYS B1045     191.555 215.583 256.379  1.00 66.58           C  
ATOM   6903  CE  LYS B1045     192.784 216.461 256.616  1.00 63.79           C  
ATOM   6904  NZ  LYS B1045     192.532 217.883 256.311  1.00 54.98           N  
ATOM   6905  N   GLY B1046     192.277 211.528 258.900  1.00 48.41           N  
ATOM   6906  CA  GLY B1046     192.531 211.347 260.328  1.00 45.21           C  
ATOM   6907  C   GLY B1046     192.623 209.883 260.752  1.00 43.18           C  
ATOM   6908  O   GLY B1046     193.283 209.086 260.083  1.00 44.71           O  
ATOM   6909  N   TYR B1047     192.007 209.565 261.893  1.00 40.57           N  
ATOM   6910  CA  TYR B1047     192.053 208.272 262.580  1.00 35.38           C  
ATOM   6911  C   TYR B1047     190.668 207.636 262.631  1.00 37.54           C  
ATOM   6912  O   TYR B1047     189.668 208.311 262.844  1.00 46.78           O  
ATOM   6913  CB  TYR B1047     192.622 208.454 263.986  1.00 36.70           C  
ATOM   6914  CG  TYR B1047     194.001 209.063 264.012  1.00 35.01           C  
ATOM   6915  CD1 TYR B1047     194.156 210.461 264.057  1.00 31.18           C  
ATOM   6916  CD2 TYR B1047     195.124 208.225 263.920  1.00 36.18           C  
ATOM   6917  CE1 TYR B1047     195.436 211.024 263.940  1.00 36.34           C  
ATOM   6918  CE2 TYR B1047     196.402 208.788 263.798  1.00 42.84           C  
ATOM   6919  CZ  TYR B1047     196.559 210.187 263.780  1.00 44.56           C  
ATOM   6920  OH  TYR B1047     197.793 210.728 263.630  1.00 52.67           O  
ATOM   6921  N   HIS B1048     190.590 206.331 262.417  1.00 32.33           N  
ATOM   6922  CA  HIS B1048     189.328 205.645 262.149  1.00 36.67           C  
ATOM   6923  C   HIS B1048     188.536 205.262 263.397  1.00 44.20           C  
ATOM   6924  O   HIS B1048     189.067 204.703 264.352  1.00 49.26           O  
ATOM   6925  CB  HIS B1048     189.645 204.424 261.290  1.00 41.54           C  
ATOM   6926  CG  HIS B1048     188.447 203.653 260.833  1.00 38.51           C  
ATOM   6927  ND1 HIS B1048     188.194 202.322 261.141  1.00 36.58           N  
ATOM   6928  CD2 HIS B1048     187.485 204.098 259.988  1.00 37.38           C  
ATOM   6929  CE1 HIS B1048     187.060 202.002 260.521  1.00 38.58           C  
ATOM   6930  NE2 HIS B1048     186.635 203.037 259.801  1.00 37.10           N  
ATOM   6931  N   LEU B1049     187.231 205.500 263.367  1.00 47.51           N  
ATOM   6932  CA  LEU B1049     186.293 204.971 264.351  1.00 45.29           C  
ATOM   6933  C   LEU B1049     185.465 203.841 263.759  1.00 47.05           C  
ATOM   6934  O   LEU B1049     185.440 202.746 264.307  1.00 47.01           O  
ATOM   6935  CB  LEU B1049     185.402 206.091 264.925  1.00 48.34           C  
ATOM   6936  CG  LEU B1049     186.169 207.153 265.734  1.00 39.76           C  
ATOM   6937  CD1 LEU B1049     185.298 208.386 265.910  1.00 35.61           C  
ATOM   6938  CD2 LEU B1049     186.560 206.618 267.106  1.00 39.11           C  
ATOM   6939  N   MET B1050     184.746 204.112 262.680  1.00 43.37           N  
ATOM   6940  CA  MET B1050     183.671 203.238 262.214  1.00 49.59           C  
ATOM   6941  C   MET B1050     183.328 203.528 260.755  1.00 53.10           C  
ATOM   6942  O   MET B1050     183.622 204.616 260.271  1.00 53.14           O  
ATOM   6943  CB  MET B1050     182.468 203.509 263.115  1.00 55.93           C  
ATOM   6944  CG  MET B1050     181.406 202.422 263.103  1.00 53.51           C  
ATOM   6945  SD  MET B1050     180.177 202.717 264.380  1.00 61.64           S  
ATOM   6946  CE  MET B1050     181.099 202.270 265.861  1.00 58.99           C  
ATOM   6947  N   SER B1051     182.695 202.613 260.019  1.00 53.04           N  
ATOM   6948  CA  SER B1051     182.278 202.890 258.633  1.00 42.77           C  
ATOM   6949  C   SER B1051     181.026 202.167 258.168  1.00 45.37           C  
ATOM   6950  O   SER B1051     180.667 201.115 258.691  1.00 50.61           O  
ATOM   6951  CB  SER B1051     183.381 202.580 257.625  1.00 39.87           C  
ATOM   6952  OG  SER B1051     184.519 203.323 257.953  1.00 46.16           O  
ATOM   6953  N   PHE B1052     180.409 202.736 257.135  1.00 43.07           N  
ATOM   6954  CA  PHE B1052     179.154 202.299 256.546  1.00 49.41           C  
ATOM   6955  C   PHE B1052     179.271 202.380 255.008  1.00 51.99           C  
ATOM   6956  O   PHE B1052     179.395 203.474 254.451  1.00 52.51           O  
ATOM   6957  CB  PHE B1052     178.008 203.170 257.089  1.00 56.20           C  
ATOM   6958  CG  PHE B1052     178.097 203.474 258.575  1.00 56.36           C  
ATOM   6959  CD1 PHE B1052     177.779 202.471 259.505  1.00 54.11           C  
ATOM   6960  CD2 PHE B1052     178.569 204.724 259.023  1.00 61.71           C  
ATOM   6961  CE1 PHE B1052     177.930 202.716 260.875  1.00 47.36           C  
ATOM   6962  CE2 PHE B1052     178.714 204.964 260.399  1.00 51.44           C  
ATOM   6963  CZ  PHE B1052     178.396 203.958 261.322  1.00 50.35           C  
ATOM   6964  N   PRO B1053     179.325 201.248 254.293  1.00 47.79           N  
ATOM   6965  CA  PRO B1053     179.399 201.234 252.846  1.00 45.71           C  
ATOM   6966  C   PRO B1053     178.009 201.444 252.242  1.00 54.34           C  
ATOM   6967  O   PRO B1053     177.001 200.968 252.761  1.00 62.18           O  
ATOM   6968  CB  PRO B1053     179.977 199.864 252.494  1.00 51.18           C  
ATOM   6969  CG  PRO B1053     179.360 198.980 253.566  1.00 50.04           C  
ATOM   6970  CD  PRO B1053     179.297 199.885 254.793  1.00 54.51           C  
ATOM   6971  N   GLN B1054     177.950 202.093 251.097  1.00 53.31           N  
ATOM   6972  CA  GLN B1054     176.764 202.195 250.269  1.00 54.54           C  
ATOM   6973  C   GLN B1054     177.159 201.988 248.812  1.00 58.72           C  
ATOM   6974  O   GLN B1054     178.242 202.370 248.376  1.00 62.07           O  
ATOM   6975  CB  GLN B1054     176.044 203.525 250.532  1.00 58.54           C  
ATOM   6976  CG  GLN B1054     176.840 204.756 250.087  1.00 58.55           C  
ATOM   6977  CD  GLN B1054     176.325 206.037 250.721  1.00 55.09           C  
ATOM   6978  OE1 GLN B1054     176.200 206.171 251.922  1.00 52.42           O  
ATOM   6979  NE2 GLN B1054     176.036 207.053 249.954  1.00 57.41           N  
ATOM   6980  N   SER B1055     176.300 201.333 248.050  1.00 67.45           N  
ATOM   6981  CA  SER B1055     176.537 201.107 246.630  1.00 62.02           C  
ATOM   6982  C   SER B1055     176.314 202.374 245.803  1.00 61.46           C  
ATOM   6983  O   SER B1055     175.645 203.323 246.210  1.00 60.69           O  
ATOM   6984  CB  SER B1055     175.657 199.954 246.141  1.00 63.88           C  
ATOM   6985  OG  SER B1055     174.289 200.211 246.376  1.00 80.35           O  
ATOM   6986  N   ALA B1056     176.875 202.346 244.604  1.00 60.24           N  
ATOM   6987  CA  ALA B1056     176.640 203.234 243.475  1.00 66.63           C  
ATOM   6988  C   ALA B1056     176.606 202.350 242.201  1.00 70.36           C  
ATOM   6989  O   ALA B1056     176.965 201.171 242.293  1.00 75.45           O  
ATOM   6990  CB  ALA B1056     177.746 204.301 243.479  1.00 61.37           C  
ATOM   6991  N   PRO B1057     176.168 202.835 241.027  1.00 67.00           N  
ATOM   6992  CA  PRO B1057     175.884 201.980 239.871  1.00 63.97           C  
ATOM   6993  C   PRO B1057     177.035 201.060 239.438  1.00 64.17           C  
ATOM   6994  O   PRO B1057     176.800 199.902 239.100  1.00 69.35           O  
ATOM   6995  CB  PRO B1057     175.488 202.935 238.747  1.00 68.24           C  
ATOM   6996  CG  PRO B1057     174.964 204.167 239.478  1.00 61.59           C  
ATOM   6997  CD  PRO B1057     175.795 204.211 240.748  1.00 68.16           C  
ATOM   6998  N   HIS B1058     178.278 201.548 239.508  1.00 63.29           N  
ATOM   6999  CA  HIS B1058     179.515 200.797 239.217  1.00 60.67           C  
ATOM   7000  C   HIS B1058     180.576 200.983 240.309  1.00 58.76           C  
ATOM   7001  O   HIS B1058     181.781 200.939 240.070  1.00 57.23           O  
ATOM   7002  CB  HIS B1058     180.038 201.167 237.815  1.00 62.45           C  
ATOM   7003  CG  HIS B1058     179.294 200.479 236.706  1.00 60.59           C  
ATOM   7004  ND1 HIS B1058     179.545 199.179 236.263  1.00 55.68           N  
ATOM   7005  CD2 HIS B1058     178.241 200.988 236.012  1.00 58.88           C  
ATOM   7006  CE1 HIS B1058     178.630 198.932 235.312  1.00 54.17           C  
ATOM   7007  NE2 HIS B1058     177.839 200.002 235.141  1.00 55.93           N  
ATOM   7008  N   GLY B1059     180.151 201.252 241.537  1.00 62.38           N  
ATOM   7009  CA  GLY B1059     181.057 201.671 242.598  1.00 53.88           C  
ATOM   7010  C   GLY B1059     180.615 201.261 243.990  1.00 55.67           C  
ATOM   7011  O   GLY B1059     179.501 200.789 244.230  1.00 60.02           O  
ATOM   7012  N   VAL B1060     181.508 201.515 244.931  1.00 51.84           N  
ATOM   7013  CA  VAL B1060     181.226 201.537 246.355  1.00 48.52           C  
ATOM   7014  C   VAL B1060     181.586 202.914 246.868  1.00 48.02           C  
ATOM   7015  O   VAL B1060     182.556 203.522 246.432  1.00 51.94           O  
ATOM   7016  CB  VAL B1060     181.956 200.403 247.094  1.00 46.65           C  
ATOM   7017  CG1 VAL B1060     183.463 200.611 247.188  1.00 49.89           C  
ATOM   7018  CG2 VAL B1060     181.408 200.201 248.510  1.00 54.52           C  
ATOM   7019  N   VAL B1061     180.791 203.419 247.789  1.00 46.69           N  
ATOM   7020  CA  VAL B1061     181.035 204.664 248.489  1.00 47.80           C  
ATOM   7021  C   VAL B1061     181.072 204.341 249.964  1.00 53.17           C  
ATOM   7022  O   VAL B1061     180.209 203.631 250.470  1.00 58.80           O  
ATOM   7023  CB  VAL B1061     179.976 205.722 248.158  1.00 45.97           C  
ATOM   7024  CG1 VAL B1061     180.242 207.025 248.908  1.00 52.85           C  
ATOM   7025  CG2 VAL B1061     179.945 206.012 246.661  1.00 51.21           C  
ATOM   7026  N   PHE B1062     182.073 204.837 250.673  1.00 42.78           N  
ATOM   7027  CA  PHE B1062     182.195 204.642 252.108  1.00 41.57           C  
ATOM   7028  C   PHE B1062     181.856 205.932 252.832  1.00 48.52           C  
ATOM   7029  O   PHE B1062     182.393 206.987 252.504  1.00 58.74           O  
ATOM   7030  CB  PHE B1062     183.597 204.174 252.471  1.00 44.00           C  
ATOM   7031  CG  PHE B1062     184.009 202.895 251.784  1.00 40.30           C  
ATOM   7032  CD1 PHE B1062     183.520 201.657 252.234  1.00 36.15           C  
ATOM   7033  CD2 PHE B1062     184.846 202.944 250.659  1.00 46.46           C  
ATOM   7034  CE1 PHE B1062     183.883 200.474 251.572  1.00 36.04           C  
ATOM   7035  CE2 PHE B1062     185.219 201.759 250.009  1.00 37.43           C  
ATOM   7036  CZ  PHE B1062     184.741 200.525 250.469  1.00 31.89           C  
ATOM   7037  N   LEU B1063     180.994 205.823 253.839  1.00 46.82           N  
ATOM   7038  CA  LEU B1063     180.906 206.769 254.933  1.00 55.32           C  
ATOM   7039  C   LEU B1063     181.883 206.318 256.014  1.00 54.47           C  
ATOM   7040  O   LEU B1063     181.627 205.325 256.684  1.00 50.99           O  
ATOM   7041  CB  LEU B1063     179.476 206.778 255.482  1.00 59.87           C  
ATOM   7042  CG  LEU B1063     178.425 207.277 254.487  1.00 60.99           C  
ATOM   7043  CD1 LEU B1063     177.036 206.981 255.048  1.00 68.06           C  
ATOM   7044  CD2 LEU B1063     178.549 208.786 254.273  1.00 65.80           C  
ATOM   7045  N   HIS B1064     182.998 207.013 256.189  1.00 46.70           N  
ATOM   7046  CA  HIS B1064     183.927 206.751 257.284  1.00 43.91           C  
ATOM   7047  C   HIS B1064     183.700 207.767 258.368  1.00 59.51           C  
ATOM   7048  O   HIS B1064     183.710 208.956 258.082  1.00 67.13           O  
ATOM   7049  CB  HIS B1064     185.392 206.865 256.874  1.00 41.29           C  
ATOM   7050  CG  HIS B1064     185.743 206.190 255.594  1.00 37.37           C  
ATOM   7051  ND1 HIS B1064     186.173 206.856 254.463  1.00 42.52           N  
ATOM   7052  CD2 HIS B1064     185.812 204.858 255.376  1.00 33.96           C  
ATOM   7053  CE1 HIS B1064     186.495 205.901 253.594  1.00 42.22           C  
ATOM   7054  NE2 HIS B1064     186.272 204.695 254.105  1.00 37.08           N  
ATOM   7055  N   VAL B1065     183.566 207.321 259.609  1.00 55.03           N  
ATOM   7056  CA  VAL B1065     183.566 208.201 260.766  1.00 48.47           C  
ATOM   7057  C   VAL B1065     184.934 208.151 261.402  1.00 52.83           C  
ATOM   7058  O   VAL B1065     185.427 207.075 261.738  1.00 58.36           O  
ATOM   7059  CB  VAL B1065     182.485 207.818 261.772  1.00 45.29           C  
ATOM   7060  CG1 VAL B1065     182.419 208.909 262.834  1.00 48.53           C  
ATOM   7061  CG2 VAL B1065     181.118 207.674 261.104  1.00 47.87           C  
ATOM   7062  N   THR B1066     185.552 209.315 261.550  1.00 52.84           N  
ATOM   7063  CA  THR B1066     186.965 209.471 261.893  1.00 51.92           C  
ATOM   7064  C   THR B1066     187.175 210.713 262.756  1.00 55.80           C  
ATOM   7065  O   THR B1066     186.368 211.635 262.738  1.00 66.63           O  
ATOM   7066  CB  THR B1066     187.842 209.570 260.627  1.00 52.69           C  
ATOM   7067  OG1 THR B1066     187.588 210.723 259.878  1.00 57.87           O  
ATOM   7068  CG2 THR B1066     187.663 208.437 259.638  1.00 50.21           C  
ATOM   7069  N   TYR B1067     188.265 210.786 263.508  1.00 44.38           N  
ATOM   7070  CA  TYR B1067     188.674 212.023 264.166  1.00 39.76           C  
ATOM   7071  C   TYR B1067     189.966 212.564 263.556  1.00 48.18           C  
ATOM   7072  O   TYR B1067     190.919 211.826 263.313  1.00 48.87           O  
ATOM   7073  CB  TYR B1067     188.712 211.855 265.688  1.00 46.05           C  
ATOM   7074  CG  TYR B1067     189.591 210.757 266.246  1.00 44.10           C  
ATOM   7075  CD1 TYR B1067     190.941 211.004 266.509  1.00 42.04           C  
ATOM   7076  CD2 TYR B1067     189.052 209.491 266.517  1.00 38.38           C  
ATOM   7077  CE1 TYR B1067     191.766 209.984 266.996  1.00 35.68           C  
ATOM   7078  CE2 TYR B1067     189.874 208.457 266.994  1.00 29.90           C  
ATOM   7079  CZ  TYR B1067     191.244 208.699 267.212  1.00 29.39           C  
ATOM   7080  OH  TYR B1067     192.078 207.686 267.558  1.00 29.89           O  
ATOM   7081  N   VAL B1068     189.997 213.864 263.290  1.00 44.46           N  
ATOM   7082  CA  VAL B1068     191.174 214.597 262.809  1.00 50.11           C  
ATOM   7083  C   VAL B1068     191.701 215.487 263.933  1.00 53.22           C  
ATOM   7084  O   VAL B1068     190.922 215.876 264.799  1.00 57.95           O  
ATOM   7085  CB  VAL B1068     190.856 215.460 261.570  1.00 49.19           C  
ATOM   7086  CG1 VAL B1068     190.589 214.596 260.345  1.00 49.61           C  
ATOM   7087  CG2 VAL B1068     189.698 216.442 261.763  1.00 47.85           C  
ATOM   7088  N   PRO B1069     192.999 215.862 263.779  1.00 49.41           N  
ATOM   7089  CA  PRO B1069     193.595 216.813 264.697  1.00 51.42           C  
ATOM   7090  C   PRO B1069     193.069 218.222 264.478  1.00 53.93           C  
ATOM   7091  O   PRO B1069     193.460 218.866 263.507  1.00 56.15           O  
ATOM   7092  CB  PRO B1069     195.092 216.797 264.369  1.00 52.00           C  
ATOM   7093  CG  PRO B1069     195.271 215.954 263.182  1.00 53.31           C  
ATOM   7094  CD  PRO B1069     194.029 215.168 262.965  1.00 49.13           C  
ATOM   7095  N   ALA B1070     192.191 218.699 265.362  1.00 53.96           N  
ATOM   7096  CA  ALA B1070     191.689 220.065 265.294  1.00 57.50           C  
ATOM   7097  C   ALA B1070     192.868 220.993 265.542  1.00 61.83           C  
ATOM   7098  O   ALA B1070     193.035 222.005 264.863  1.00 64.29           O  
ATOM   7099  CB  ALA B1070     190.609 220.285 266.337  1.00 61.17           C  
ATOM   7100  N   GLN B1071     193.687 220.628 266.530  1.00 59.85           N  
ATOM   7101  CA  GLN B1071     194.884 221.363 266.851  1.00 57.91           C  
ATOM   7102  C   GLN B1071     196.047 220.359 267.010  1.00 56.60           C  
ATOM   7103  O   GLN B1071     195.831 219.201 267.361  1.00 51.82           O  
ATOM   7104  CB  GLN B1071     194.690 222.158 268.143  1.00 58.19           C  
ATOM   7105  CG  GLN B1071     195.657 223.319 268.310  1.00 62.11           C  
ATOM   7106  CD  GLN B1071     195.459 224.052 269.621  1.00 65.75           C  
ATOM   7107  OE1 GLN B1071     195.259 223.434 270.667  1.00 61.13           O  
ATOM   7108  NE2 GLN B1071     195.520 225.378 269.575  1.00 69.88           N  
ATOM   7109  N   GLU B1072     197.268 220.812 266.754  1.00 60.09           N  
ATOM   7110  CA  GLU B1072     198.479 220.016 266.896  1.00 56.12           C  
ATOM   7111  C   GLU B1072     199.668 220.941 267.148  1.00 58.77           C  
ATOM   7112  O   GLU B1072     199.687 222.091 266.701  1.00 65.80           O  
ATOM   7113  CB  GLU B1072     198.672 219.095 265.677  1.00 56.17           C  
ATOM   7114  CG  GLU B1072     198.694 219.826 264.325  1.00 61.80           C  
ATOM   7115  CD  GLU B1072     198.651 218.880 263.120  1.00 68.60           C  
ATOM   7116  OE1 GLU B1072     199.003 217.689 263.233  1.00 71.10           O  
ATOM   7117  OE2 GLU B1072     198.273 219.339 262.021  1.00 65.68           O1-
ATOM   7118  N   LYS B1073     200.670 220.437 267.861  1.00 54.87           N  
ATOM   7119  CA  LYS B1073     201.852 221.208 268.251  1.00 56.15           C  
ATOM   7120  C   LYS B1073     203.100 220.505 267.745  1.00 59.61           C  
ATOM   7121  O   LYS B1073     203.175 219.282 267.770  1.00 59.27           O  
ATOM   7122  CB  LYS B1073     201.833 221.435 269.770  1.00 58.18           C  
ATOM   7123  CG  LYS B1073     203.052 222.230 270.267  1.00 63.40           C  
ATOM   7124  CD  LYS B1073     202.936 222.613 271.750  1.00 59.76           C  
ATOM   7125  CE  LYS B1073     204.219 223.316 272.204  1.00 62.61           C  
ATOM   7126  NZ  LYS B1073     204.111 223.825 273.583  1.00 68.48           N  
ATOM   7127  N   ASN B1074     204.069 221.269 267.255  1.00 57.81           N  
ATOM   7128  CA  ASN B1074     205.379 220.749 266.895  1.00 59.87           C  
ATOM   7129  C   ASN B1074     206.221 220.589 268.160  1.00 63.62           C  
ATOM   7130  O   ASN B1074     206.627 221.578 268.772  1.00 63.56           O  
ATOM   7131  CB  ASN B1074     206.125 221.597 265.847  1.00 63.72           C  
ATOM   7132  CG  ASN B1074     205.325 222.673 265.142  1.00 77.10           C  
ATOM   7133  OD1 ASN B1074     204.856 223.608 265.785  1.00 77.28           O  
ATOM   7134  ND2 ASN B1074     205.311 222.641 263.819  1.00 82.42           N  
ATOM   7135  N   PHE B1075     206.511 219.351 268.534  1.00114.01           N  
ATOM   7136  CA  PHE B1075     207.555 219.061 269.511  1.00 56.58           C  
ATOM   7137  C   PHE B1075     208.832 218.703 268.767  1.00 49.94           C  
ATOM   7138  O   PHE B1075     208.789 217.986 267.773  1.00 59.24           O  
ATOM   7139  CB  PHE B1075     207.123 217.920 270.417  1.00 52.86           C  
ATOM   7140  CG  PHE B1075     205.817 218.202 271.112  1.00 58.55           C  
ATOM   7141  CD1 PHE B1075     205.804 218.841 272.361  1.00 60.11           C  
ATOM   7142  CD2 PHE B1075     204.611 217.863 270.483  1.00 55.32           C  
ATOM   7143  CE1 PHE B1075     204.578 219.133 272.984  1.00 63.34           C  
ATOM   7144  CE2 PHE B1075     203.388 218.155 271.104  1.00 62.52           C  
ATOM   7145  CZ  PHE B1075     203.372 218.788 272.354  1.00 58.04           C  
ATOM   7146  N   THR B1076     209.982 219.182 269.217  1.00 45.37           N  
ATOM   7147  CA  THR B1076     211.221 218.549 268.781  1.00 45.43           C  
ATOM   7148  C   THR B1076     211.235 217.113 269.287  1.00 47.59           C  
ATOM   7149  O   THR B1076     210.607 216.772 270.289  1.00 53.76           O  
ATOM   7150  CB  THR B1076     212.468 219.318 269.210  1.00 48.82           C  
ATOM   7151  OG1 THR B1076     212.522 219.487 270.602  1.00 55.19           O  
ATOM   7152  CG2 THR B1076     212.518 220.699 268.562  1.00 53.85           C  
ATOM   7153  N   THR B1077     211.894 216.250 268.537  1.00 47.72           N  
ATOM   7154  CA  THR B1077     211.937 214.808 268.754  1.00 42.61           C  
ATOM   7155  C   THR B1077     213.258 214.244 268.247  1.00 44.57           C  
ATOM   7156  O   THR B1077     214.006 214.900 267.523  1.00 50.28           O  
ATOM   7157  CB  THR B1077     210.784 214.080 268.031  1.00 43.31           C  
ATOM   7158  OG1 THR B1077     210.865 214.321 266.653  1.00 54.51           O  
ATOM   7159  CG2 THR B1077     209.374 214.459 268.461  1.00 45.25           C  
ATOM   7160  N   ALA B1078     213.523 212.999 268.614  1.00 43.60           N  
ATOM   7161  CA  ALA B1078     214.401 212.113 267.876  1.00 48.49           C  
ATOM   7162  C   ALA B1078     213.726 210.730 267.799  1.00 50.90           C  
ATOM   7163  O   ALA B1078     212.964 210.373 268.702  1.00 50.47           O  
ATOM   7164  CB  ALA B1078     215.768 212.053 268.562  1.00 49.55           C  
ATOM   7165  N   PRO B1079     213.946 209.937 266.743  1.00 54.31           N  
ATOM   7166  CA  PRO B1079     213.441 208.569 266.667  1.00 60.56           C  
ATOM   7167  C   PRO B1079     214.108 207.642 267.688  1.00 54.22           C  
ATOM   7168  O   PRO B1079     213.453 206.794 268.277  1.00 53.30           O  
ATOM   7169  CB  PRO B1079     213.741 208.084 265.255  1.00 60.83           C  
ATOM   7170  CG  PRO B1079     214.300 209.278 264.503  1.00 55.22           C  
ATOM   7171  CD  PRO B1079     214.616 210.339 265.533  1.00 54.10           C  
ATOM   7172  N   ALA B1080     215.380 207.938 267.991  1.00 51.55           N  
ATOM   7173  CA  ALA B1080     216.192 207.202 268.980  1.00 52.37           C  
ATOM   7174  C   ALA B1080     217.345 208.050 269.585  1.00 58.48           C  
ATOM   7175  O   ALA B1080     217.757 209.048 268.994  1.00 63.66           O  
ATOM   7176  CB  ALA B1080     216.737 205.920 268.370  1.00 48.16           C  
ATOM   7177  N   ILE B1081     217.856 207.645 270.756  1.00 59.23           N  
ATOM   7178  CA  ILE B1081     218.943 208.331 271.439  1.00 54.98           C  
ATOM   7179  C   ILE B1081     219.978 207.293 271.841  1.00 57.15           C  
ATOM   7180  O   ILE B1081     219.643 206.176 272.248  1.00 62.37           O  
ATOM   7181  CB  ILE B1081     218.455 209.132 272.668  1.00 51.96           C  
ATOM   7182  CG1 ILE B1081     217.582 208.262 273.574  1.00 55.40           C  
ATOM   7183  CG2 ILE B1081     217.699 210.375 272.227  1.00 51.00           C  
ATOM   7184  CD1 ILE B1081     217.080 208.985 274.809  1.00 61.29           C  
ATOM   7185  N   CYS B1082     221.247 207.668 271.717  1.00 58.20           N  
ATOM   7186  CA  CYS B1082     222.371 206.765 271.952  1.00 65.77           C  
ATOM   7187  C   CYS B1082     223.134 207.270 273.173  1.00 69.75           C  
ATOM   7188  O   CYS B1082     223.975 208.169 273.069  1.00 69.80           O  
ATOM   7189  CB  CYS B1082     223.248 206.668 270.702  1.00 65.26           C  
ATOM   7190  SG  CYS B1082     224.997 206.261 270.939  1.00 71.06           S  
ATOM   7191  N   HIS B1083     222.832 206.689 274.332  1.00 72.08           N  
ATOM   7192  CA  HIS B1083     223.453 207.078 275.592  1.00 72.00           C  
ATOM   7193  C   HIS B1083     224.737 206.282 275.785  1.00 77.85           C  
ATOM   7194  O   HIS B1083     224.710 205.046 275.781  1.00 81.22           O  
ATOM   7195  CB  HIS B1083     222.501 206.843 276.763  1.00 67.66           C  
ATOM   7196  CG  HIS B1083     221.389 207.842 276.851  1.00 64.59           C  
ATOM   7197  ND1 HIS B1083     220.161 207.543 277.404  1.00 63.62           N  
ATOM   7198  CD2 HIS B1083     221.321 209.138 276.466  1.00 63.57           C  
ATOM   7199  CE1 HIS B1083     219.385 208.610 277.350  1.00 64.12           C  
ATOM   7200  NE2 HIS B1083     220.064 209.592 276.785  1.00 63.67           N  
ATOM   7201  N   ASP B1084     225.851 206.981 275.990  1.00 75.84           N  
ATOM   7202  CA  ASP B1084     227.176 206.367 276.192  1.00 77.78           C  
ATOM   7203  C   ASP B1084     227.512 205.126 275.340  1.00 79.72           C  
ATOM   7204  O   ASP B1084     228.131 204.175 275.817  1.00 81.32           O  
ATOM   7205  CB  ASP B1084     227.492 206.138 277.683  1.00 79.23           C  
ATOM   7206  CG  ASP B1084     226.725 204.976 278.284  1.00 82.65           C  
ATOM   7207  OD1 ASP B1084     227.285 203.862 278.347  1.00 80.01           O  
ATOM   7208  OD2 ASP B1084     225.561 205.176 278.695  1.00 85.50           O1-
ATOM   7209  N   GLY B1085     227.089 205.164 274.080  1.00 77.21           N  
ATOM   7210  CA  GLY B1085     227.354 204.113 273.079  1.00 78.81           C  
ATOM   7211  C   GLY B1085     226.275 203.023 272.936  1.00 69.75           C  
ATOM   7212  O   GLY B1085     226.463 202.076 272.177  1.00 70.41           O  
ATOM   7213  N   LYS B1086     225.140 203.147 273.629  1.00 66.01           N  
ATOM   7214  CA  LYS B1086     223.954 202.292 273.481  1.00 66.41           C  
ATOM   7215  C   LYS B1086     222.783 203.112 272.920  1.00 63.58           C  
ATOM   7216  O   LYS B1086     222.483 204.181 273.443  1.00 62.65           O  
ATOM   7217  CB  LYS B1086     223.628 201.654 274.841  1.00 66.87           C  
ATOM   7218  CG  LYS B1086     224.720 200.660 275.285  1.00 70.81           C  
ATOM   7219  CD  LYS B1086     224.498 200.038 276.675  1.00 65.06           C  
ATOM   7220  CE  LYS B1086     223.219 199.199 276.827  1.00 65.95           C  
ATOM   7221  NZ  LYS B1086     223.222 197.964 275.998  1.00 57.23           N  
ATOM   7222  N   ALA B1087     222.136 202.628 271.862  1.00 59.12           N  
ATOM   7223  CA  ALA B1087     220.960 203.274 271.285  1.00 50.13           C  
ATOM   7224  C   ALA B1087     219.692 202.844 272.025  1.00 46.67           C  
ATOM   7225  O   ALA B1087     219.463 201.659 272.222  1.00 54.86           O  
ATOM   7226  CB  ALA B1087     220.902 202.988 269.784  1.00 64.54           C  
ATOM   7227  N   HIS B1088     218.874 203.799 272.444  1.00 46.77           N  
ATOM   7228  CA  HIS B1088     217.585 203.603 273.103  1.00 48.37           C  
ATOM   7229  C   HIS B1088     216.481 204.148 272.212  1.00 48.04           C  
ATOM   7230  O   HIS B1088     216.609 205.256 271.698  1.00 53.35           O  
ATOM   7231  CB  HIS B1088     217.570 204.342 274.448  1.00 58.36           C  
ATOM   7232  CG  HIS B1088     218.634 203.901 275.416  1.00 59.91           C  
ATOM   7233  ND1 HIS B1088     218.477 202.947 276.421  1.00 54.34           N  
ATOM   7234  CD2 HIS B1088     219.930 204.311 275.391  1.00 62.18           C  
ATOM   7235  CE1 HIS B1088     219.694 202.794 276.963  1.00 57.38           C  
ATOM   7236  NE2 HIS B1088     220.580 203.599 276.364  1.00 60.83           N  
ATOM   7237  N   PHE B1089     215.392 203.404 272.020  1.00 45.82           N  
ATOM   7238  CA  PHE B1089     214.279 203.825 271.160  1.00 40.67           C  
ATOM   7239  C   PHE B1089     212.919 203.326 271.655  1.00 46.53           C  
ATOM   7240  O   PHE B1089     212.863 202.319 272.354  1.00 55.46           O  
ATOM   7241  CB  PHE B1089     214.533 203.436 269.703  1.00 36.60           C  
ATOM   7242  CG  PHE B1089     215.286 202.150 269.479  1.00 35.39           C  
ATOM   7243  CD1 PHE B1089     216.682 202.190 269.338  1.00 40.43           C  
ATOM   7244  CD2 PHE B1089     214.604 200.929 269.398  1.00 35.29           C  
ATOM   7245  CE1 PHE B1089     217.399 201.013 269.102  1.00 43.04           C  
ATOM   7246  CE2 PHE B1089     215.320 199.750 269.147  1.00 32.58           C  
ATOM   7247  CZ  PHE B1089     216.715 199.795 268.996  1.00 38.25           C  
ATOM   7248  N   PRO B1090     211.809 204.016 271.345  1.00 38.33           N  
ATOM   7249  CA  PRO B1090     210.484 203.674 271.843  1.00 41.62           C  
ATOM   7250  C   PRO B1090     209.960 202.278 271.512  1.00 42.49           C  
ATOM   7251  O   PRO B1090     210.315 201.658 270.514  1.00 44.24           O  
ATOM   7252  CB  PRO B1090     209.541 204.714 271.247  1.00 39.18           C  
ATOM   7253  CG  PRO B1090     210.422 205.944 271.095  1.00 44.38           C  
ATOM   7254  CD  PRO B1090     211.750 205.318 270.688  1.00 44.05           C  
ATOM   7255  N   ARG B1091     208.835 202.024 272.191  1.00 41.16           N  
ATOM   7256  CA  ARG B1091     207.986 200.883 271.991  1.00 49.65           C  
ATOM   7257  C   ARG B1091     206.610 201.570 271.758  1.00 52.29           C  
ATOM   7258  O   ARG B1091     206.079 202.166 272.698  1.00 53.28           O  
ATOM   7259  CB  ARG B1091     207.893 200.000 273.231  1.00 53.59           C  
ATOM   7260  CG  ARG B1091     209.181 199.308 273.627  1.00 58.55           C  
ATOM   7261  CD  ARG B1091     208.920 197.896 274.128  1.00 55.28           C  
ATOM   7262  NE  ARG B1091     209.951 197.440 275.055  1.00 59.31           N  
ATOM   7263  CZ  ARG B1091     210.100 196.177 275.439  1.00 54.66           C  
ATOM   7264  NH1 ARG B1091     211.064 195.849 276.289  1.00 49.26           N  
ATOM   7265  NH2 ARG B1091     209.286 195.240 274.973  1.00 56.73           N  
ATOM   7266  N   GLU B1092     206.070 201.530 270.533  1.00 46.35           N  
ATOM   7267  CA  GLU B1092     204.739 202.084 270.220  1.00 42.41           C  
ATOM   7268  C   GLU B1092     204.579 203.586 270.570  1.00 41.88           C  
ATOM   7269  O   GLU B1092     203.628 203.985 271.237  1.00 42.38           O  
ATOM   7270  CB  GLU B1092     203.635 201.207 270.854  1.00 47.01           C  
ATOM   7271  CG  GLU B1092     203.706 199.710 270.506  1.00 44.73           C  
ATOM   7272  CD  GLU B1092     202.819 198.877 271.440  1.00 67.66           C  
ATOM   7273  OE1 GLU B1092     203.227 197.758 271.827  1.00 73.24           O  
ATOM   7274  OE2 GLU B1092     201.720 199.331 271.826  1.00 80.11           O1-
ATOM   7275  N   GLY B1093     205.515 204.443 270.158  1.00 38.28           N  
ATOM   7276  CA  GLY B1093     205.472 205.891 270.408  1.00 40.42           C  
ATOM   7277  C   GLY B1093     206.622 206.651 269.749  1.00 39.11           C  
ATOM   7278  O   GLY B1093     207.352 206.072 268.949  1.00 39.78           O  
ATOM   7279  N   VAL B1094     206.830 207.917 270.128  1.00 37.08           N  
ATOM   7280  CA  VAL B1094     208.037 208.722 269.810  1.00 40.89           C  
ATOM   7281  C   VAL B1094     208.593 209.429 271.054  1.00 48.37           C  
ATOM   7282  O   VAL B1094     207.827 209.719 271.972  1.00 55.43           O  
ATOM   7283  CB  VAL B1094     207.821 209.728 268.661  1.00 40.85           C  
ATOM   7284  CG1 VAL B1094     207.215 209.038 267.441  1.00 49.11           C  
ATOM   7285  CG2 VAL B1094     206.957 210.938 269.018  1.00 38.19           C  
ATOM   7286  N   PHE B1095     209.893 209.743 271.092  1.00 46.33           N  
ATOM   7287  CA  PHE B1095     210.459 210.617 272.127  1.00 43.94           C  
ATOM   7288  C   PHE B1095     210.024 212.083 271.948  1.00 46.69           C  
ATOM   7289  O   PHE B1095     210.730 212.892 271.350  1.00 49.14           O  
ATOM   7290  CB  PHE B1095     211.992 210.522 272.142  1.00 38.53           C  
ATOM   7291  CG  PHE B1095     212.619 209.207 272.551  1.00 41.12           C  
ATOM   7292  CD1 PHE B1095     212.148 208.494 273.667  1.00 49.76           C  
ATOM   7293  CD2 PHE B1095     213.752 208.750 271.867  1.00 46.27           C  
ATOM   7294  CE1 PHE B1095     212.772 207.304 274.064  1.00 49.99           C  
ATOM   7295  CE2 PHE B1095     214.399 207.581 272.287  1.00 47.14           C  
ATOM   7296  CZ  PHE B1095     213.911 206.851 273.381  1.00 48.20           C  
ATOM   7297  N   VAL B1096     208.864 212.456 272.480  1.00 48.27           N  
ATOM   7298  CA  VAL B1096     208.461 213.865 272.580  1.00 52.69           C  
ATOM   7299  C   VAL B1096     209.415 214.609 273.500  1.00 54.53           C  
ATOM   7300  O   VAL B1096     209.737 214.137 274.592  1.00 62.01           O  
ATOM   7301  CB  VAL B1096     206.994 214.048 273.004  1.00 54.97           C  
ATOM   7302  CG1 VAL B1096     206.640 213.747 274.457  1.00 55.39           C  
ATOM   7303  CG2 VAL B1096     206.529 215.464 272.715  1.00 57.32           C  
ATOM   7304  N   SER B1097     209.883 215.772 273.054  1.00 53.08           N  
ATOM   7305  CA  SER B1097     210.925 216.493 273.760  1.00 57.69           C  
ATOM   7306  C   SER B1097     210.460 217.725 274.492  1.00 60.91           C  
ATOM   7307  O   SER B1097     210.103 218.750 273.910  1.00 57.11           O  
ATOM   7308  CB  SER B1097     212.085 216.867 272.841  1.00 62.46           C  
ATOM   7309  OG  SER B1097     213.223 217.246 273.599  1.00 59.77           O  
ATOM   7310  N   ASN B1098     210.501 217.574 275.806  1.00 66.96           N  
ATOM   7311  CA  ASN B1098     210.201 218.608 276.772  1.00 71.97           C  
ATOM   7312  C   ASN B1098     211.517 219.418 276.957  1.00 76.61           C  
ATOM   7313  O   ASN B1098     212.598 218.952 276.562  1.00 81.59           O  
ATOM   7314  CB  ASN B1098     209.717 217.908 278.042  1.00 70.80           C  
ATOM   7315  CG  ASN B1098     209.222 218.860 279.099  1.00 72.99           C  
ATOM   7316  OD1 ASN B1098     208.418 219.759 278.850  1.00 76.09           O  
ATOM   7317  ND2 ASN B1098     209.716 218.656 280.297  1.00 78.22           N  
ATOM   7318  N   GLY B1099     211.453 220.611 277.545  1.00 78.06           N  
ATOM   7319  CA  GLY B1099     212.636 221.446 277.659  1.00 82.36           C  
ATOM   7320  C   GLY B1099     213.797 220.743 278.360  1.00 84.60           C  
ATOM   7321  O   GLY B1099     214.953 221.100 278.138  1.00 84.22           O  
ATOM   7322  N   THR B1100     213.507 219.739 279.199  1.00 81.84           N  
ATOM   7323  CA  THR B1100     214.494 219.157 280.134  1.00 79.96           C  
ATOM   7324  C   THR B1100     214.501 217.622 280.163  1.00 78.73           C  
ATOM   7325  O   THR B1100     215.468 217.023 280.633  1.00 80.20           O  
ATOM   7326  CB  THR B1100     214.289 219.759 281.538  1.00 83.79           C  
ATOM   7327  OG1 THR B1100     214.243 221.166 281.458  1.00 88.89           O  
ATOM   7328  CG2 THR B1100     215.401 219.441 282.534  1.00 79.58           C  
ATOM   7329  N   HIS B1101     213.476 216.962 279.615  1.00 71.60           N  
ATOM   7330  CA  HIS B1101     213.291 215.506 279.684  1.00 70.01           C  
ATOM   7331  C   HIS B1101     212.745 214.892 278.388  1.00 66.78           C  
ATOM   7332  O   HIS B1101     212.080 215.549 277.588  1.00 70.81           O  
ATOM   7333  CB  HIS B1101     212.368 215.160 280.865  1.00 78.06           C  
ATOM   7334  CG  HIS B1101     212.919 215.599 282.192  1.00 80.93           C  
ATOM   7335  ND1 HIS B1101     213.982 214.992 282.864  1.00 81.83           N  
ATOM   7336  CD2 HIS B1101     212.514 216.693 282.893  1.00 78.32           C  
ATOM   7337  CE1 HIS B1101     214.193 215.736 283.958  1.00 85.15           C  
ATOM   7338  NE2 HIS B1101     213.332 216.762 283.994  1.00 84.40           N  
ATOM   7339  N   TRP B1102     212.988 213.591 278.221  1.00 59.86           N  
ATOM   7340  CA  TRP B1102     212.434 212.772 277.141  1.00 53.71           C  
ATOM   7341  C   TRP B1102     211.241 211.972 277.658  1.00 50.49           C  
ATOM   7342  O   TRP B1102     211.353 211.265 278.660  1.00 54.22           O  
ATOM   7343  CB  TRP B1102     213.494 211.792 276.627  1.00 52.65           C  
ATOM   7344  CG  TRP B1102     214.671 212.358 275.902  1.00 58.67           C  
ATOM   7345  CD1 TRP B1102     215.960 212.237 276.279  1.00 58.93           C  
ATOM   7346  CD2 TRP B1102     214.700 212.996 274.592  1.00 59.51           C  
ATOM   7347  NE1 TRP B1102     216.783 212.758 275.299  1.00 58.97           N  
ATOM   7348  CE2 TRP B1102     216.062 213.200 274.220  1.00 56.82           C  
ATOM   7349  CE3 TRP B1102     213.717 213.381 273.663  1.00 49.47           C  
ATOM   7350  CZ2 TRP B1102     216.436 213.714 272.974  1.00 49.38           C  
ATOM   7351  CZ3 TRP B1102     214.078 213.879 272.402  1.00 46.95           C  
ATOM   7352  CH2 TRP B1102     215.430 214.045 272.053  1.00 53.62           C  
ATOM   7353  N   PHE B1103     210.122 212.018 276.934  1.00 46.19           N  
ATOM   7354  CA  PHE B1103     208.940 211.214 277.227  1.00 51.62           C  
ATOM   7355  C   PHE B1103     208.514 210.419 275.994  1.00 53.06           C  
ATOM   7356  O   PHE B1103     208.537 210.946 274.890  1.00 57.26           O  
ATOM   7357  CB  PHE B1103     207.804 212.128 277.684  1.00 58.83           C  
ATOM   7358  CG  PHE B1103     208.083 213.062 278.851  1.00 61.69           C  
ATOM   7359  CD1 PHE B1103     208.042 212.576 280.170  1.00 59.85           C  
ATOM   7360  CD2 PHE B1103     208.285 214.437 278.627  1.00 57.12           C  
ATOM   7361  CE1 PHE B1103     208.201 213.460 281.247  1.00 64.19           C  
ATOM   7362  CE2 PHE B1103     208.438 215.321 279.706  1.00 57.39           C  
ATOM   7363  CZ  PHE B1103     208.388 214.832 281.017  1.00 69.12           C  
ATOM   7364  N   VAL B1104     208.099 209.163 276.142  1.00 47.42           N  
ATOM   7365  CA  VAL B1104     207.550 208.373 275.038  1.00 42.76           C  
ATOM   7366  C   VAL B1104     206.067 208.699 274.883  1.00 48.93           C  
ATOM   7367  O   VAL B1104     205.211 208.080 275.518  1.00 50.19           O  
ATOM   7368  CB  VAL B1104     207.838 206.874 275.216  1.00 38.27           C  
ATOM   7369  CG1 VAL B1104     207.173 206.025 274.132  1.00 44.54           C  
ATOM   7370  CG2 VAL B1104     209.341 206.615 275.129  1.00 45.40           C  
ATOM   7371  N   THR B1105     205.748 209.703 274.065  1.00 47.44           N  
ATOM   7372  CA  THR B1105     204.356 209.971 273.675  1.00 49.47           C  
ATOM   7373  C   THR B1105     203.879 208.958 272.642  1.00 53.60           C  
ATOM   7374  O   THR B1105     204.651 208.434 271.843  1.00 54.34           O  
ATOM   7375  CB  THR B1105     204.142 211.418 273.213  1.00 48.05           C  
ATOM   7376  OG1 THR B1105     202.803 211.812 273.372  1.00 50.54           O  
ATOM   7377  CG2 THR B1105     204.477 211.713 271.765  1.00 48.03           C  
ATOM   7378  N   GLN B1106     202.585 208.669 272.644  1.00 53.36           N  
ATOM   7379  CA  GLN B1106     201.944 207.914 271.573  1.00 51.90           C  
ATOM   7380  C   GLN B1106     202.002 208.754 270.283  1.00 53.25           C  
ATOM   7381  O   GLN B1106     201.686 209.937 270.321  1.00 58.94           O  
ATOM   7382  CB  GLN B1106     200.515 207.626 272.042  1.00 50.37           C  
ATOM   7383  CG  GLN B1106     199.773 206.692 271.102  1.00 49.19           C  
ATOM   7384  CD  GLN B1106     198.368 206.329 271.581  1.00 62.56           C  
ATOM   7385  OE1 GLN B1106     197.848 206.802 272.584  1.00 62.12           O  
ATOM   7386  NE2 GLN B1106     197.695 205.440 270.894  1.00 67.11           N  
ATOM   7387  N   ARG B1107     202.474 208.210 269.162  1.00 56.16           N  
ATOM   7388  CA  ARG B1107     202.640 209.006 267.921  1.00 45.22           C  
ATOM   7389  C   ARG B1107     201.481 209.927 267.501  1.00 43.81           C  
ATOM   7390  O   ARG B1107     201.684 211.063 267.072  1.00 43.61           O  
ATOM   7391  CB  ARG B1107     202.964 208.083 266.743  1.00 39.70           C  
ATOM   7392  CG  ARG B1107     203.112 208.822 265.421  1.00 40.59           C  
ATOM   7393  CD  ARG B1107     204.362 209.687 265.412  1.00 39.74           C  
ATOM   7394  NE  ARG B1107     204.503 210.446 264.172  1.00 34.43           N  
ATOM   7395  CZ  ARG B1107     204.067 211.690 264.003  1.00 32.66           C  
ATOM   7396  NH1 ARG B1107     204.240 212.303 262.841  1.00 43.77           N  
ATOM   7397  NH2 ARG B1107     203.459 212.321 264.998  1.00 28.12           N  
ATOM   7398  N   ASN B1108     200.277 209.401 267.638  1.00 47.80           N  
ATOM   7399  CA  ASN B1108     199.036 210.080 267.267  1.00 49.79           C  
ATOM   7400  C   ASN B1108     198.392 210.956 268.357  1.00 52.54           C  
ATOM   7401  O   ASN B1108     197.249 211.359 268.168  1.00 46.86           O  
ATOM   7402  CB  ASN B1108     198.033 209.068 266.696  1.00 54.59           C  
ATOM   7403  CG  ASN B1108     197.475 208.053 267.666  1.00 57.34           C  
ATOM   7404  OD1 ASN B1108     198.174 207.255 268.234  1.00 65.46           O  
ATOM   7405  ND2 ASN B1108     196.198 208.022 267.869  1.00 47.56           N  
ATOM   7406  N   PHE B1109     199.067 211.249 269.481  1.00 60.05           N  
ATOM   7407  CA  PHE B1109     198.537 212.143 270.526  1.00 53.47           C  
ATOM   7408  C   PHE B1109     199.629 212.691 271.459  1.00 54.83           C  
ATOM   7409  O   PHE B1109     200.530 211.949 271.835  1.00 53.65           O  
ATOM   7410  CB  PHE B1109     197.495 211.380 271.352  1.00 45.72           C  
ATOM   7411  CG  PHE B1109     196.779 212.219 272.383  1.00 47.53           C  
ATOM   7412  CD1 PHE B1109     196.158 213.424 272.013  1.00 50.90           C  
ATOM   7413  CD2 PHE B1109     196.669 211.754 273.699  1.00 54.46           C  
ATOM   7414  CE1 PHE B1109     195.431 214.154 272.964  1.00 48.65           C  
ATOM   7415  CE2 PHE B1109     195.922 212.476 274.639  1.00 53.81           C  
ATOM   7416  CZ  PHE B1109     195.311 213.683 274.276  1.00 42.98           C  
ATOM   7417  N   TYR B1110     199.557 213.951 271.897  1.00 57.05           N  
ATOM   7418  CA  TYR B1110     200.427 214.462 272.968  1.00 55.50           C  
ATOM   7419  C   TYR B1110     199.949 214.050 274.374  1.00 56.80           C  
ATOM   7420  O   TYR B1110     199.025 214.631 274.941  1.00 51.37           O  
ATOM   7421  CB  TYR B1110     200.624 215.981 272.874  1.00 58.14           C  
ATOM   7422  CG  TYR B1110     201.505 216.482 274.004  1.00 64.20           C  
ATOM   7423  CD1 TYR B1110     202.842 216.044 274.092  1.00 61.98           C  
ATOM   7424  CD2 TYR B1110     200.972 217.302 275.014  1.00 67.03           C  
ATOM   7425  CE1 TYR B1110     203.650 216.440 275.177  1.00 60.73           C  
ATOM   7426  CE2 TYR B1110     201.771 217.688 276.106  1.00 68.83           C  
ATOM   7427  CZ  TYR B1110     203.113 217.268 276.186  1.00 64.74           C  
ATOM   7428  OH  TYR B1110     203.872 217.644 277.245  1.00 73.64           O  
ATOM   7429  N   GLU B1111     200.603 213.034 274.936  1.00 52.37           N  
ATOM   7430  CA  GLU B1111     200.360 212.477 276.271  1.00 52.63           C  
ATOM   7431  C   GLU B1111     201.651 211.815 276.785  1.00 58.74           C  
ATOM   7432  O   GLU B1111     201.866 210.619 276.577  1.00 58.06           O  
ATOM   7433  CB  GLU B1111     199.185 211.490 276.196  1.00 51.56           C  
ATOM   7434  CG  GLU B1111     198.837 210.840 277.537  1.00 65.60           C  
ATOM   7435  CD  GLU B1111     197.662 209.877 277.376  1.00 65.93           C  
ATOM   7436  OE1 GLU B1111     196.490 210.300 277.468  1.00 63.75           O  
ATOM   7437  OE2 GLU B1111     197.888 208.668 277.161  1.00 70.34           O1-
ATOM   7438  N   PRO B1112     202.562 212.583 277.399  1.00 56.92           N  
ATOM   7439  CA  PRO B1112     203.893 212.103 277.735  1.00 54.98           C  
ATOM   7440  C   PRO B1112     203.885 211.019 278.819  1.00 57.69           C  
ATOM   7441  O   PRO B1112     203.088 211.064 279.754  1.00 65.57           O  
ATOM   7442  CB  PRO B1112     204.675 213.344 278.154  1.00 57.56           C  
ATOM   7443  CG  PRO B1112     203.611 214.324 278.607  1.00 56.48           C  
ATOM   7444  CD  PRO B1112     202.417 213.989 277.727  1.00 59.13           C  
ATOM   7445  N   GLN B1113     204.816 210.065 278.709  1.00 54.70           N  
ATOM   7446  CA  GLN B1113     205.135 209.058 279.726  1.00 54.08           C  
ATOM   7447  C   GLN B1113     206.657 208.871 279.831  1.00 54.51           C  
ATOM   7448  O   GLN B1113     207.363 208.974 278.833  1.00 55.68           O  
ATOM   7449  CB  GLN B1113     204.428 207.725 279.427  1.00 48.75           C  
ATOM   7450  CG  GLN B1113     202.898 207.884 279.370  1.00 54.77           C  
ATOM   7451  CD  GLN B1113     202.128 206.571 279.341  1.00 63.88           C  
ATOM   7452  OE1 GLN B1113     202.641 205.479 279.544  1.00 56.98           O  
ATOM   7453  NE2 GLN B1113     200.836 206.623 279.111  1.00 68.90           N  
ATOM   7454  N   ILE B1114     207.172 208.613 281.032  1.00 55.06           N  
ATOM   7455  CA  ILE B1114     208.612 208.596 281.349  1.00 48.91           C  
ATOM   7456  C   ILE B1114     209.339 207.462 280.599  1.00 50.80           C  
ATOM   7457  O   ILE B1114     208.768 206.398 280.371  1.00 52.51           O  
ATOM   7458  CB  ILE B1114     208.772 208.542 282.893  1.00 52.49           C  
ATOM   7459  CG1 ILE B1114     208.545 209.919 283.559  1.00 50.48           C  
ATOM   7460  CG2 ILE B1114     210.150 208.047 283.362  1.00 51.61           C  
ATOM   7461  CD1 ILE B1114     207.133 210.501 283.479  1.00 44.35           C  
ATOM   7462  N   ILE B1115     210.605 207.648 280.208  1.00 48.19           N  
ATOM   7463  CA  ILE B1115     211.428 206.534 279.712  1.00 46.63           C  
ATOM   7464  C   ILE B1115     211.593 205.481 280.813  1.00 55.18           C  
ATOM   7465  O   ILE B1115     212.121 205.758 281.887  1.00 73.39           O  
ATOM   7466  CB  ILE B1115     212.805 207.012 279.198  1.00 44.55           C  
ATOM   7467  CG1 ILE B1115     212.610 207.772 277.870  1.00 60.93           C  
ATOM   7468  CG2 ILE B1115     213.789 205.835 279.003  1.00 42.15           C  
ATOM   7469  CD1 ILE B1115     213.909 208.225 277.188  1.00 58.22           C  
ATOM   7470  N   THR B1116     211.198 204.252 280.496  1.00 46.72           N  
ATOM   7471  CA  THR B1116     211.409 203.044 281.301  1.00 52.08           C  
ATOM   7472  C   THR B1116     211.775 201.891 280.368  1.00 54.84           C  
ATOM   7473  O   THR B1116     211.510 201.964 279.161  1.00 63.14           O  
ATOM   7474  CB  THR B1116     210.171 202.660 282.139  1.00 56.26           C  
ATOM   7475  OG1 THR B1116     209.171 202.076 281.339  1.00 49.33           O  
ATOM   7476  CG2 THR B1116     209.486 203.801 282.879  1.00 57.60           C  
ATOM   7477  N   THR B1117     212.329 200.794 280.890  1.00 52.67           N  
ATOM   7478  CA  THR B1117     212.623 199.590 280.073  1.00 55.80           C  
ATOM   7479  C   THR B1117     211.337 198.908 279.555  1.00 57.22           C  
ATOM   7480  O   THR B1117     211.394 198.053 278.679  1.00 55.41           O  
ATOM   7481  CB  THR B1117     213.524 198.604 280.842  1.00 58.57           C  
ATOM   7482  OG1 THR B1117     214.688 199.259 281.296  1.00 59.55           O  
ATOM   7483  CG2 THR B1117     214.056 197.441 280.008  1.00 58.20           C  
ATOM   7484  N   ASP B1118     210.152 199.320 280.022  1.00 52.14           N  
ATOM   7485  CA  ASP B1118     208.846 198.899 279.497  1.00 57.56           C  
ATOM   7486  C   ASP B1118     208.250 199.875 278.445  1.00 63.32           C  
ATOM   7487  O   ASP B1118     207.319 199.512 277.722  1.00 60.61           O  
ATOM   7488  CB  ASP B1118     207.915 198.716 280.694  1.00 61.99           C  
ATOM   7489  CG  ASP B1118     206.558 198.118 280.319  1.00 75.43           C  
ATOM   7490  OD1 ASP B1118     206.511 197.084 279.619  1.00 76.61           O  
ATOM   7491  OD2 ASP B1118     205.522 198.664 280.760  1.00 73.26           O1-
ATOM   7492  N   ASN B1119     208.770 201.104 278.328  1.00 58.43           N  
ATOM   7493  CA  ASN B1119     208.445 202.079 277.268  1.00 48.25           C  
ATOM   7494  C   ASN B1119     209.472 202.099 276.124  1.00 47.49           C  
ATOM   7495  O   ASN B1119     209.212 202.696 275.083  1.00 59.99           O  
ATOM   7496  CB  ASN B1119     208.303 203.492 277.881  1.00 44.65           C  
ATOM   7497  CG  ASN B1119     206.922 203.776 278.425  1.00 46.22           C  
ATOM   7498  OD1 ASN B1119     205.942 203.123 278.104  1.00 52.57           O  
ATOM   7499  ND2 ASN B1119     206.774 204.765 279.272  1.00 49.53           N  
ATOM   7500  N   THR B1120     210.640 201.479 276.282  1.00 42.88           N  
ATOM   7501  CA  THR B1120     211.722 201.522 275.283  1.00 44.50           C  
ATOM   7502  C   THR B1120     212.357 200.159 275.063  1.00 48.17           C  
ATOM   7503  O   THR B1120     212.268 199.268 275.908  1.00 54.59           O  
ATOM   7504  CB  THR B1120     212.806 202.540 275.652  1.00 43.42           C  
ATOM   7505  OG1 THR B1120     213.372 202.219 276.898  1.00 44.87           O  
ATOM   7506  CG2 THR B1120     212.306 203.979 275.715  1.00 49.74           C  
ATOM   7507  N   PHE B1121     212.975 199.993 273.902  1.00 50.18           N  
ATOM   7508  CA  PHE B1121     213.958 198.962 273.611  1.00 51.04           C  
ATOM   7509  C   PHE B1121     215.367 199.555 273.696  1.00 46.74           C  
ATOM   7510  O   PHE B1121     215.546 200.774 273.695  1.00 48.28           O  
ATOM   7511  CB  PHE B1121     213.692 198.384 272.215  1.00 48.61           C  
ATOM   7512  CG  PHE B1121     212.407 197.594 272.068  1.00 47.30           C  
ATOM   7513  CD1 PHE B1121     211.481 197.905 271.055  1.00 48.40           C  
ATOM   7514  CD2 PHE B1121     212.157 196.513 272.927  1.00 52.32           C  
ATOM   7515  CE1 PHE B1121     210.310 197.140 270.908  1.00 54.37           C  
ATOM   7516  CE2 PHE B1121     210.985 195.759 272.778  1.00 52.36           C  
ATOM   7517  CZ  PHE B1121     210.060 196.064 271.771  1.00 51.33           C  
ATOM   7518  N   VAL B1122     216.369 198.680 273.740  1.00 43.00           N  
ATOM   7519  CA  VAL B1122     217.778 199.040 273.908  1.00 43.37           C  
ATOM   7520  C   VAL B1122     218.648 198.214 272.964  1.00 49.41           C  
ATOM   7521  O   VAL B1122     218.283 197.103 272.591  1.00 51.42           O  
ATOM   7522  CB  VAL B1122     218.207 198.871 275.383  1.00 50.99           C  
ATOM   7523  CG1 VAL B1122     219.646 199.326 275.635  1.00 53.70           C  
ATOM   7524  CG2 VAL B1122     217.297 199.651 276.340  1.00 53.58           C  
ATOM   7525  N   SER B1123     219.792 198.758 272.573  1.00 47.15           N  
ATOM   7526  CA  SER B1123     220.695 198.206 271.562  1.00 49.56           C  
ATOM   7527  C   SER B1123     222.146 198.088 272.067  1.00 58.03           C  
ATOM   7528  O   SER B1123     222.401 198.117 273.271  1.00 63.89           O  
ATOM   7529  CB  SER B1123     220.568 199.117 270.339  1.00 53.56           C  
ATOM   7530  OG  SER B1123     221.168 198.534 269.210  1.00 60.68           O  
ATOM   7531  N   GLY B1124     223.072 197.965 271.122  1.00 59.08           N  
ATOM   7532  CA  GLY B1124     224.480 197.844 271.441  1.00 61.16           C  
ATOM   7533  C   GLY B1124     225.397 198.371 270.355  1.00 70.70           C  
ATOM   7534  O   GLY B1124     225.135 198.175 269.164  1.00 71.78           O  
ATOM   7535  N   ASN B1125     226.417 199.105 270.807  1.00 80.48           N  
ATOM   7536  CA  ASN B1125     227.511 199.717 270.025  1.00 82.25           C  
ATOM   7537  C   ASN B1125     227.242 201.026 269.268  1.00 77.44           C  
ATOM   7538  O   ASN B1125     228.160 201.555 268.652  1.00 75.03           O  
ATOM   7539  CB  ASN B1125     228.291 198.705 269.160  1.00 78.43           C  
ATOM   7540  CG  ASN B1125     228.775 197.509 269.957  1.00 79.52           C  
ATOM   7541  OD1 ASN B1125     228.520 197.404 271.156  1.00 78.98           O  
ATOM   7542  ND2 ASN B1125     229.478 196.600 269.292  1.00 80.26           N  
ATOM   7543  N   CYS B1126     226.017 201.548 269.364  1.00 72.25           N  
ATOM   7544  CA  CYS B1126     225.588 202.823 268.746  1.00 70.86           C  
ATOM   7545  C   CYS B1126     225.694 203.032 267.216  1.00 73.89           C  
ATOM   7546  O   CYS B1126     225.838 204.164 266.757  1.00 74.10           O  
ATOM   7547  CB  CYS B1126     226.257 204.001 269.471  1.00 73.26           C  
ATOM   7548  SG  CYS B1126     225.580 205.631 269.110  1.00 75.42           S  
ATOM   7549  N   ASP B1127     225.632 201.960 266.429  1.00 73.81           N  
ATOM   7550  CA  ASP B1127     225.716 202.054 264.955  1.00 64.38           C  
ATOM   7551  C   ASP B1127     224.407 202.052 264.145  1.00 65.32           C  
ATOM   7552  O   ASP B1127     223.459 201.356 264.508  1.00 62.96           O  
ATOM   7553  CB  ASP B1127     226.652 200.968 264.414  1.00 65.03           C  
ATOM   7554  CG  ASP B1127     228.067 201.101 264.943  1.00 75.23           C  
ATOM   7555  OD1 ASP B1127     228.339 202.073 265.678  1.00 85.98           O  
ATOM   7556  OD2 ASP B1127     228.906 200.233 264.624  1.00 76.35           O1-
ATOM   7557  N   VAL B1128     224.353 202.825 263.051  1.00 66.61           N  
ATOM   7558  CA  VAL B1128     223.144 202.811 262.218  1.00 61.74           C  
ATOM   7559  C   VAL B1128     223.368 201.863 261.049  1.00 63.20           C  
ATOM   7560  O   VAL B1128     224.340 202.012 260.302  1.00 66.58           O  
ATOM   7561  CB  VAL B1128     222.824 204.226 261.713  1.00 51.33           C  
ATOM   7562  CG1 VAL B1128     221.822 204.263 260.558  1.00 55.26           C  
ATOM   7563  CG2 VAL B1128     222.227 205.056 262.847  1.00 54.93           C  
ATOM   7564  N   VAL B1129     222.457 200.910 260.865  1.00 58.69           N  
ATOM   7565  CA  VAL B1129     222.369 200.149 259.614  1.00 57.66           C  
ATOM   7566  C   VAL B1129     221.755 201.049 258.540  1.00 63.95           C  
ATOM   7567  O   VAL B1129     220.721 201.656 258.788  1.00 66.12           O  
ATOM   7568  CB  VAL B1129     221.548 198.870 259.846  1.00 51.39           C  
ATOM   7569  CG1 VAL B1129     221.056 198.196 258.561  1.00 57.83           C  
ATOM   7570  CG2 VAL B1129     222.376 197.840 260.621  1.00 66.04           C  
ATOM   7571  N   ILE B1130     222.336 201.130 257.341  1.00 64.71           N  
ATOM   7572  CA  ILE B1130     221.745 201.884 256.222  1.00 56.25           C  
ATOM   7573  C   ILE B1130     221.240 200.910 255.155  1.00 55.94           C  
ATOM   7574  O   ILE B1130     221.993 200.106 254.610  1.00 59.85           O  
ATOM   7575  CB  ILE B1130     222.716 202.951 255.667  1.00 56.37           C  
ATOM   7576  CG1 ILE B1130     223.037 203.977 256.777  1.00 60.61           C  
ATOM   7577  CG2 ILE B1130     222.102 203.644 254.439  1.00 64.38           C  
ATOM   7578  CD1 ILE B1130     223.791 205.236 256.338  1.00 65.57           C  
ATOM   7579  N   GLY B1131     219.950 200.996 254.852  1.00 54.97           N  
ATOM   7580  CA  GLY B1131     219.270 200.242 253.804  1.00 57.28           C  
ATOM   7581  C   GLY B1131     218.924 201.124 252.608  1.00 63.29           C  
ATOM   7582  O   GLY B1131     218.718 202.333 252.742  1.00 62.32           O  
ATOM   7583  N   ILE B1132     218.824 200.514 251.434  1.00 65.81           N  
ATOM   7584  CA  ILE B1132     218.410 201.164 250.190  1.00 60.31           C  
ATOM   7585  C   ILE B1132     217.313 200.340 249.512  1.00 56.00           C  
ATOM   7586  O   ILE B1132     217.430 199.122 249.354  1.00 51.49           O  
ATOM   7587  CB  ILE B1132     219.646 201.435 249.298  1.00 55.93           C  
ATOM   7588  CG1 ILE B1132     219.329 202.234 248.018  1.00 58.70           C  
ATOM   7589  CG2 ILE B1132     220.397 200.154 248.884  1.00 51.45           C  
ATOM   7590  CD1 ILE B1132     218.884 203.673 248.276  1.00 57.22           C  
ATOM   7591  N   VAL B1133     216.236 201.010 249.124  1.00 54.99           N  
ATOM   7592  CA  VAL B1133     215.124 200.437 248.377  1.00 53.89           C  
ATOM   7593  C   VAL B1133     214.872 201.325 247.177  1.00 58.97           C  
ATOM   7594  O   VAL B1133     214.712 202.538 247.302  1.00 61.80           O  
ATOM   7595  CB  VAL B1133     213.869 200.295 249.251  1.00 52.49           C  
ATOM   7596  CG1 VAL B1133     212.636 199.854 248.457  1.00 47.52           C  
ATOM   7597  CG2 VAL B1133     214.094 199.267 250.361  1.00 56.55           C  
ATOM   7598  N   ASN B1134     214.801 200.717 246.003  1.00 62.03           N  
ATOM   7599  CA  ASN B1134     214.545 201.432 244.769  1.00 58.74           C  
ATOM   7600  C   ASN B1134     213.447 200.717 243.992  1.00 64.78           C  
ATOM   7601  O   ASN B1134     213.682 199.672 243.388  1.00 70.92           O  
ATOM   7602  CB  ASN B1134     215.868 201.574 244.015  1.00 69.71           C  
ATOM   7603  CG  ASN B1134     215.783 202.590 242.898  1.00 74.29           C  
ATOM   7604  OD1 ASN B1134     214.706 203.024 242.495  1.00 72.25           O  
ATOM   7605  ND2 ASN B1134     216.952 202.928 242.382  1.00 82.15           N  
ATOM   7606  N   ASN B1135     212.223 201.223 244.093  1.00 59.91           N  
ATOM   7607  CA  ASN B1135     211.066 200.623 243.451  1.00 65.02           C  
ATOM   7608  C   ASN B1135     211.019 201.003 241.968  1.00 66.04           C  
ATOM   7609  O   ASN B1135     210.241 201.855 241.546  1.00 65.47           O  
ATOM   7610  CB  ASN B1135     209.808 200.989 244.232  1.00 57.43           C  
ATOM   7611  CG  ASN B1135     209.905 200.551 245.677  1.00 53.26           C  
ATOM   7612  OD1 ASN B1135     209.861 199.381 246.008  1.00 56.99           O  
ATOM   7613  ND2 ASN B1135     210.058 201.484 246.566  1.00 53.69           N  
ATOM   7614  N   THR B1136     211.856 200.343 241.180  1.00 62.66           N  
ATOM   7615  CA  THR B1136     211.805 200.338 239.725  1.00 62.22           C  
ATOM   7616  C   THR B1136     210.479 199.712 239.289  1.00 64.89           C  
ATOM   7617  O   THR B1136     210.377 198.493 239.182  1.00 69.54           O  
ATOM   7618  CB  THR B1136     213.001 199.529 239.191  1.00 68.83           C  
ATOM   7619  OG1 THR B1136     214.215 200.093 239.614  1.00 71.87           O  
ATOM   7620  CG2 THR B1136     213.051 199.412 237.670  1.00 66.09           C  
ATOM   7621  N   VAL B1137     209.453 200.519 239.010  1.00 62.18           N  
ATOM   7622  CA  VAL B1137     208.376 200.071 238.115  1.00 56.10           C  
ATOM   7623  C   VAL B1137     209.009 199.706 236.779  1.00 46.66           C  
ATOM   7624  O   VAL B1137     210.003 200.311 236.391  1.00 46.86           O  
ATOM   7625  CB  VAL B1137     207.257 201.097 237.924  1.00 49.00           C  
ATOM   7626  CG1 VAL B1137     206.557 201.407 239.248  1.00 50.40           C  
ATOM   7627  CG2 VAL B1137     207.717 202.411 237.304  1.00 43.28           C  
ATOM   7628  N   TYR B1138     208.503 198.680 236.108  1.00 44.09           N  
ATOM   7629  CA  TYR B1138     209.252 198.022 235.041  1.00 43.23           C  
ATOM   7630  C   TYR B1138     209.501 198.964 233.862  1.00 44.46           C  
ATOM   7631  O   TYR B1138     208.573 199.588 233.353  1.00 46.09           O  
ATOM   7632  CB  TYR B1138     208.492 196.777 234.606  1.00 42.93           C  
ATOM   7633  CG  TYR B1138     209.158 195.935 233.550  1.00 43.09           C  
ATOM   7634  CD1 TYR B1138     208.640 195.911 232.244  1.00 49.29           C  
ATOM   7635  CD2 TYR B1138     210.253 195.125 233.895  1.00 51.58           C  
ATOM   7636  CE1 TYR B1138     209.244 195.100 231.268  1.00 53.18           C  
ATOM   7637  CE2 TYR B1138     210.870 194.327 232.918  1.00 58.65           C  
ATOM   7638  CZ  TYR B1138     210.385 194.340 231.597  1.00 59.33           C  
ATOM   7639  OH  TYR B1138     211.043 193.651 230.633  1.00 61.72           O  
ATOM   7640  N   ASP B1139     210.753 199.111 233.434  1.00 43.57           N  
ATOM   7641  CA  ASP B1139     211.090 199.854 232.222  1.00 41.74           C  
ATOM   7642  C   ASP B1139     211.301 198.852 231.081  1.00 44.88           C  
ATOM   7643  O   ASP B1139     212.288 198.107 231.100  1.00 44.74           O  
ATOM   7644  CB  ASP B1139     212.308 200.763 232.448  1.00 47.26           C  
ATOM   7645  CG  ASP B1139     212.361 201.941 231.472  1.00 57.55           C  
ATOM   7646  OD1 ASP B1139     211.631 201.954 230.467  1.00 58.08           O  
ATOM   7647  OD2 ASP B1139     213.131 202.887 231.728  1.00 64.67           O1-
ATOM   7648  N   PRO B1140     210.374 198.780 230.114  1.00 36.17           N  
ATOM   7649  CA  PRO B1140     210.340 197.696 229.153  1.00 33.66           C  
ATOM   7650  C   PRO B1140     211.433 197.762 228.093  1.00 36.90           C  
ATOM   7651  O   PRO B1140     211.968 198.823 227.769  1.00 38.82           O  
ATOM   7652  CB  PRO B1140     208.952 197.755 228.523  1.00 38.56           C  
ATOM   7653  CG  PRO B1140     208.495 199.192 228.709  1.00 30.70           C  
ATOM   7654  CD  PRO B1140     209.184 199.600 229.996  1.00 26.50           C  
ATOM   7655  N   LEU B1141     211.707 196.609 227.481  1.00 36.60           N  
ATOM   7656  CA  LEU B1141     212.426 196.500 226.219  1.00 36.10           C  
ATOM   7657  C   LEU B1141     211.567 197.136 225.110  1.00 34.75           C  
ATOM   7658  O   LEU B1141     210.731 196.472 224.503  1.00 39.03           O  
ATOM   7659  CB  LEU B1141     212.706 195.015 225.922  1.00 39.08           C  
ATOM   7660  CG  LEU B1141     213.837 194.369 226.731  1.00 42.77           C  
ATOM   7661  CD1 LEU B1141     213.479 194.102 228.191  1.00 50.44           C  
ATOM   7662  CD2 LEU B1141     214.187 193.025 226.090  1.00 48.59           C  
ATOM   7663  N   GLN B1142     211.729 198.435 224.851  1.00 34.20           N  
ATOM   7664  CA  GLN B1142     210.975 199.114 223.796  1.00 32.05           C  
ATOM   7665  C   GLN B1142     211.471 198.707 222.396  1.00 40.49           C  
ATOM   7666  O   GLN B1142     212.661 198.432 222.211  1.00 48.67           O  
ATOM   7667  CB  GLN B1142     210.963 200.645 223.981  1.00 30.75           C  
ATOM   7668  CG  GLN B1142     210.012 201.174 225.079  1.00 27.99           C  
ATOM   7669  CD  GLN B1142     208.524 200.988 224.772  1.00 29.79           C  
ATOM   7670  OE1 GLN B1142     208.112 200.030 224.150  1.00 33.07           O  
ATOM   7671  NE2 GLN B1142     207.643 201.859 225.179  1.00 26.92           N  
ATOM   7672  N   PRO B1143     210.581 198.611 221.395  1.00 42.39           N  
ATOM   7673  CA  PRO B1143     210.856 198.006 220.098  1.00 39.06           C  
ATOM   7674  C   PRO B1143     211.670 198.906 219.159  1.00 35.28           C  
ATOM   7675  O   PRO B1143     211.145 199.480 218.207  1.00 42.59           O  
ATOM   7676  CB  PRO B1143     209.478 197.656 219.545  1.00 32.89           C  
ATOM   7677  CG  PRO B1143     208.580 198.728 220.126  1.00 28.39           C  
ATOM   7678  CD  PRO B1143     209.173 198.943 221.497  1.00 35.82           C  
ATOM   7679  N   GLU B1144     212.974 199.005 219.399  1.00 39.52           N  
ATOM   7680  CA  GLU B1144     213.897 199.745 218.534  1.00 48.36           C  
ATOM   7681  C   GLU B1144     214.198 199.010 217.221  1.00 51.69           C  
ATOM   7682  O   GLU B1144     214.452 197.805 217.203  1.00 53.78           O  
ATOM   7683  CB  GLU B1144     215.191 200.110 219.283  1.00 53.67           C  
ATOM   7684  CG  GLU B1144     216.288 200.810 218.453  1.00 58.86           C  
ATOM   7685  CD  GLU B1144     215.891 202.171 217.844  1.00 64.00           C  
ATOM   7686  OE1 GLU B1144     214.756 202.349 217.360  1.00 59.31           O  
ATOM   7687  OE2 GLU B1144     216.739 203.084 217.839  1.00 74.51           O1-
ATOM   7688  N   LEU B1145     214.214 199.779 216.138  1.00 43.91           N  
ATOM   7689  CA  LEU B1145     214.215 199.368 214.737  1.00 42.30           C  
ATOM   7690  C   LEU B1145     215.418 199.940 213.977  1.00 48.04           C  
ATOM   7691  O   LEU B1145     215.929 201.006 214.322  1.00 55.91           O  
ATOM   7692  CB  LEU B1145     212.946 199.923 214.085  1.00 31.50           C  
ATOM   7693  CG  LEU B1145     211.628 199.288 214.529  1.00 24.84           C  
ATOM   7694  CD1 LEU B1145     210.480 200.186 214.080  1.00 20.99           C  
ATOM   7695  CD2 LEU B1145     211.451 197.931 213.867  1.00 31.01           C  
ATOM   7696  N   ASP B1146     215.832 199.288 212.893  1.00 45.42           N  
ATOM   7697  CA  ASP B1146     216.774 199.872 211.927  1.00 45.60           C  
ATOM   7698  C   ASP B1146     216.218 201.158 211.296  1.00 48.82           C  
ATOM   7699  O   ASP B1146     215.026 201.436 211.424  1.00 51.85           O  
ATOM   7700  CB  ASP B1146     217.112 198.871 210.811  1.00 47.85           C  
ATOM   7701  CG  ASP B1146     217.364 197.448 211.295  1.00 49.63           C  
ATOM   7702  OD1 ASP B1146     218.532 197.009 211.275  1.00 50.40           O  
ATOM   7703  OD2 ASP B1146     216.391 196.755 211.664  1.00 54.87           O1-
ATOM   7704  N   SER B1147     217.014 201.914 210.536  1.00 53.31           N  
ATOM   7705  CA  SER B1147     216.408 202.908 209.632  1.00 54.23           C  
ATOM   7706  C   SER B1147     215.587 202.203 208.550  1.00 50.92           C  
ATOM   7707  O   SER B1147     215.881 201.074 208.166  1.00 51.32           O  
ATOM   7708  CB  SER B1147     217.439 203.843 208.992  1.00 52.78           C  
ATOM   7709  OG  SER B1147     218.070 204.668 209.947  1.00 54.99           O  
ATOM   7710  N   PHE B1148     214.555 202.864 208.026  1.00 49.66           N  
ATOM   7711  CA  PHE B1148     213.618 202.247 207.081  1.00 44.83           C  
ATOM   7712  C   PHE B1148     214.318 201.725 205.818  1.00 49.34           C  
ATOM   7713  O   PHE B1148     213.972 200.662 205.313  1.00 49.89           O  
ATOM   7714  CB  PHE B1148     212.544 203.280 206.734  1.00 42.05           C  
ATOM   7715  CG  PHE B1148     211.332 202.739 206.000  1.00 38.30           C  
ATOM   7716  CD1 PHE B1148     210.160 202.479 206.718  1.00 40.52           C  
ATOM   7717  CD2 PHE B1148     211.337 202.544 204.611  1.00 43.11           C  
ATOM   7718  CE1 PHE B1148     209.007 202.018 206.071  1.00 32.70           C  
ATOM   7719  CE2 PHE B1148     210.180 202.090 203.961  1.00 40.84           C  
ATOM   7720  CZ  PHE B1148     209.018 201.817 204.687  1.00 29.25           C  
ATOM   7721  N   LYS B1149     215.360 202.423 205.337  1.00 56.58           N  
ATOM   7722  CA  LYS B1149     216.163 202.024 204.174  1.00 54.26           C  
ATOM   7723  C   LYS B1149     216.757 200.623 204.331  1.00 51.79           C  
ATOM   7724  O   LYS B1149     216.645 199.837 203.404  1.00 53.31           O  
ATOM   7725  CB  LYS B1149     217.275 203.051 203.894  1.00 58.04           C  
ATOM   7726  CG  LYS B1149     216.754 204.482 203.661  1.00 55.70           C  
ATOM   7727  CD  LYS B1149     217.800 205.429 203.050  1.00 62.13           C  
ATOM   7728  CE  LYS B1149     219.139 205.530 203.797  1.00 59.14           C  
ATOM   7729  NZ  LYS B1149     219.053 206.277 205.080  1.00 68.92           N  
ATOM   7730  N   GLU B1150     217.304 200.266 205.492  1.00 47.84           N  
ATOM   7731  CA  GLU B1150     217.832 198.921 205.743  1.00 48.11           C  
ATOM   7732  C   GLU B1150     216.733 197.858 205.771  1.00 45.75           C  
ATOM   7733  O   GLU B1150     216.919 196.782 205.207  1.00 47.78           O  
ATOM   7734  CB  GLU B1150     218.612 198.859 207.065  1.00 62.05           C  
ATOM   7735  CG  GLU B1150     219.916 199.659 207.061  1.00 69.32           C  
ATOM   7736  CD  GLU B1150     219.729 201.102 207.552  1.00 69.91           C  
ATOM   7737  OE1 GLU B1150     219.754 201.317 208.785  1.00 71.70           O  
ATOM   7738  OE2 GLU B1150     219.572 202.018 206.712  1.00 64.37           O1-
ATOM   7739  N   GLU B1151     215.592 198.125 206.412  1.00 39.94           N  
ATOM   7740  CA  GLU B1151     214.522 197.126 206.538  1.00 43.87           C  
ATOM   7741  C   GLU B1151     213.686 197.008 205.248  1.00 46.11           C  
ATOM   7742  O   GLU B1151     213.058 195.980 205.004  1.00 42.40           O  
ATOM   7743  CB  GLU B1151     213.679 197.443 207.784  1.00 46.80           C  
ATOM   7744  CG  GLU B1151     213.012 196.194 208.389  1.00 51.33           C  
ATOM   7745  CD  GLU B1151     212.119 196.504 209.600  1.00 48.54           C  
ATOM   7746  OE1 GLU B1151     211.659 197.656 209.726  1.00 43.64           O  
ATOM   7747  OE2 GLU B1151     211.857 195.602 210.420  1.00 50.65           O1-
ATOM   7748  N   LEU B1152     213.726 198.023 204.378  1.00 44.76           N  
ATOM   7749  CA  LEU B1152     213.181 198.009 203.021  1.00 39.65           C  
ATOM   7750  C   LEU B1152     214.091 197.233 202.066  1.00 45.87           C  
ATOM   7751  O   LEU B1152     213.686 196.215 201.508  1.00 48.41           O  
ATOM   7752  CB  LEU B1152     212.950 199.463 202.577  1.00 39.67           C  
ATOM   7753  CG  LEU B1152     212.316 199.626 201.191  1.00 37.20           C  
ATOM   7754  CD1 LEU B1152     210.866 199.151 201.175  1.00 33.60           C  
ATOM   7755  CD2 LEU B1152     212.341 201.090 200.769  1.00 38.74           C  
ATOM   7756  N   ASP B1153     215.346 197.661 201.929  1.00 50.03           N  
ATOM   7757  CA  ASP B1153     216.332 197.105 201.001  1.00 43.23           C  
ATOM   7758  C   ASP B1153     216.601 195.613 201.212  1.00 43.47           C  
ATOM   7759  O   ASP B1153     217.054 194.937 200.293  1.00 42.09           O  
ATOM   7760  CB  ASP B1153     217.654 197.876 201.121  1.00 45.16           C  
ATOM   7761  CG  ASP B1153     217.622 199.329 200.623  1.00 50.83           C  
ATOM   7762  OD1 ASP B1153     216.731 199.689 199.825  1.00 46.90           O  
ATOM   7763  OD2 ASP B1153     218.539 200.106 200.971  1.00 50.03           O1-
ATOM   7764  N   LYS B1154     216.298 195.068 202.390  1.00 46.31           N  
ATOM   7765  CA  LYS B1154     216.385 193.631 202.666  1.00 50.35           C  
ATOM   7766  C   LYS B1154     215.554 192.794 201.691  1.00 47.52           C  
ATOM   7767  O   LYS B1154     216.003 191.719 201.300  1.00 54.51           O  
ATOM   7768  CB  LYS B1154     215.968 193.391 204.124  1.00 58.36           C  
ATOM   7769  CG  LYS B1154     216.188 191.929 204.539  1.00 60.45           C  
ATOM   7770  CD  LYS B1154     215.886 191.675 206.025  1.00 63.49           C  
ATOM   7771  CE  LYS B1154     216.924 192.305 206.969  1.00 64.07           C  
ATOM   7772  NZ  LYS B1154     218.240 191.623 206.879  1.00 70.23           N  
ATOM   7773  N   TYR B1155     214.386 193.291 201.266  1.00 46.16           N  
ATOM   7774  CA  TYR B1155     213.436 192.569 200.398  1.00 48.45           C  
ATOM   7775  C   TYR B1155     212.923 193.357 199.189  1.00 50.45           C  
ATOM   7776  O   TYR B1155     212.543 192.755 198.187  1.00 50.31           O  
ATOM   7777  CB  TYR B1155     212.248 192.073 201.239  1.00 53.49           C  
ATOM   7778  CG  TYR B1155     212.640 190.959 202.186  1.00 56.86           C  
ATOM   7779  CD1 TYR B1155     212.677 191.167 203.573  1.00 54.66           C  
ATOM   7780  CD2 TYR B1155     213.041 189.725 201.643  1.00 60.68           C  
ATOM   7781  CE1 TYR B1155     213.142 190.138 204.413  1.00 56.49           C  
ATOM   7782  CE2 TYR B1155     213.519 188.701 202.476  1.00 53.04           C  
ATOM   7783  CZ  TYR B1155     213.585 188.914 203.864  1.00 52.78           C  
ATOM   7784  OH  TYR B1155     214.087 187.950 204.677  1.00 50.53           O  
ATOM   7785  N   PHE B1156     212.912 194.682 199.278  1.00 45.70           N  
ATOM   7786  CA  PHE B1156     212.399 195.532 198.198  1.00 39.01           C  
ATOM   7787  C   PHE B1156     213.122 195.438 196.846  1.00 43.69           C  
ATOM   7788  O   PHE B1156     214.352 195.460 196.785  1.00 43.66           O  
ATOM   7789  CB  PHE B1156     212.362 196.993 198.664  1.00 30.00           C  
ATOM   7790  CG  PHE B1156     211.839 197.949 197.630  1.00 30.00           C  
ATOM   7791  CD1 PHE B1156     210.477 198.085 197.419  1.00 30.00           C  
ATOM   7792  CD2 PHE B1156     212.710 198.712 196.870  1.00 30.00           C  
ATOM   7793  CE1 PHE B1156     209.992 198.965 196.469  1.00 30.00           C  
ATOM   7794  CE2 PHE B1156     212.232 199.593 195.918  1.00 30.00           C  
ATOM   7795  CZ  PHE B1156     210.871 199.720 195.717  1.00 30.00           C  
ATOM   7796  N   LYS B1157     212.341 195.334 195.770  1.00 53.89           N  
ATOM   7797  CA  LYS B1157     212.875 195.284 194.404  1.00 48.07           C  
ATOM   7798  C   LYS B1157     212.410 196.493 193.600  1.00 41.82           C  
ATOM   7799  O   LYS B1157     211.217 196.670 193.364  1.00 33.09           O  
ATOM   7800  CB  LYS B1157     212.504 193.942 193.746  1.00 40.85           C  
ATOM   7801  CG  LYS B1157     213.371 192.820 194.328  1.00 50.49           C  
ATOM   7802  CD  LYS B1157     213.167 191.476 193.621  1.00 65.87           C  
ATOM   7803  CE  LYS B1157     214.057 190.438 194.310  1.00 72.00           C  
ATOM   7804  NZ  LYS B1157     213.902 189.091 193.729  1.00 74.31           N  
ATOM   7805  N   ASN B1158     213.362 197.306 193.150  1.00 46.73           N  
ATOM   7806  CA  ASN B1158     213.126 198.564 192.437  1.00 51.34           C  
ATOM   7807  C   ASN B1158     213.011 198.328 190.919  1.00 60.09           C  
ATOM   7808  O   ASN B1158     213.673 198.968 190.108  1.00 57.18           O  
ATOM   7809  CB  ASN B1158     214.228 199.568 192.845  1.00 55.88           C  
ATOM   7810  CG  ASN B1158     213.797 201.007 192.909  1.00 63.04           C  
ATOM   7811  OD1 ASN B1158     212.639 201.322 193.148  1.00 66.13           O  
ATOM   7812  ND2 ASN B1158     214.766 201.891 192.770  1.00 69.79           N  
ATOM   7813  N   HIS B1159     212.195 197.349 190.528  1.00 59.38           N  
ATOM   7814  CA  HIS B1159     212.009 196.928 189.140  1.00 53.02           C  
ATOM   7815  C   HIS B1159     211.297 198.022 188.335  1.00 58.08           C  
ATOM   7816  O   HIS B1159     210.150 198.371 188.625  1.00 57.64           O  
ATOM   7817  CB  HIS B1159     211.230 195.606 189.128  1.00 57.56           C  
ATOM   7818  CG  HIS B1159     210.746 195.144 187.778  1.00 63.55           C  
ATOM   7819  ND1 HIS B1159     211.508 194.488 186.814  1.00 65.27           N  
ATOM   7820  CD2 HIS B1159     209.467 195.239 187.329  1.00 61.69           C  
ATOM   7821  CE1 HIS B1159     210.666 194.185 185.817  1.00 65.00           C  
ATOM   7822  NE2 HIS B1159     209.437 194.633 186.097  1.00 59.53           N  
ATOM   7823  N   THR B1160     211.970 198.554 187.317  1.00 58.22           N  
ATOM   7824  CA  THR B1160     211.376 199.499 186.366  1.00 57.08           C  
ATOM   7825  C   THR B1160     211.240 198.824 185.006  1.00 62.20           C  
ATOM   7826  O   THR B1160     212.233 198.420 184.394  1.00 62.95           O  
ATOM   7827  CB  THR B1160     212.178 200.801 186.241  1.00 51.08           C  
ATOM   7828  OG1 THR B1160     213.471 200.551 185.749  1.00 61.17           O  
ATOM   7829  CG2 THR B1160     212.322 201.533 187.572  1.00 54.11           C  
ATOM   7830  N   SER B1161     210.015 198.740 184.507  1.00 62.97           N  
ATOM   7831  CA  SER B1161     209.716 198.198 183.191  1.00 56.52           C  
ATOM   7832  C   SER B1161     210.212 199.152 182.093  1.00 56.02           C  
ATOM   7833  O   SER B1161     210.090 200.373 182.246  1.00 55.27           O  
ATOM   7834  CB  SER B1161     208.219 197.931 183.063  1.00 51.56           C  
ATOM   7835  OG  SER B1161     207.463 199.118 183.147  1.00 47.11           O  
ATOM   7836  N   PRO B1162     210.798 198.640 180.996  1.00 60.95           N  
ATOM   7837  CA  PRO B1162     211.377 199.484 179.962  1.00 68.32           C  
ATOM   7838  C   PRO B1162     210.330 200.246 179.138  1.00 63.01           C  
ATOM   7839  O   PRO B1162     209.210 199.788 178.918  1.00 58.75           O  
ATOM   7840  CB  PRO B1162     212.231 198.542 179.113  1.00 68.00           C  
ATOM   7841  CG  PRO B1162     211.559 197.183 179.284  1.00 59.69           C  
ATOM   7842  CD  PRO B1162     211.067 197.237 180.725  1.00 62.34           C  
ATOM   7843  N   ASP B1163     210.733 201.422 178.652  1.00 59.33           N  
ATOM   7844  CA  ASP B1163     209.983 202.275 177.722  1.00 61.71           C  
ATOM   7845  C   ASP B1163     209.612 201.488 176.459  1.00 66.88           C  
ATOM   7846  O   ASP B1163     210.493 201.005 175.749  1.00 72.77           O  
ATOM   7847  CB  ASP B1163     210.873 203.499 177.413  1.00 63.26           C  
ATOM   7848  CG  ASP B1163     210.317 204.514 176.408  1.00 67.84           C  
ATOM   7849  OD1 ASP B1163     209.214 204.332 175.856  1.00 68.97           O  
ATOM   7850  OD2 ASP B1163     211.004 205.530 176.166  1.00 66.97           O1-
ATOM   7851  N   VAL B1164     208.316 201.298 176.206  1.00 61.40           N  
ATOM   7852  CA  VAL B1164     207.855 200.462 175.094  1.00 64.48           C  
ATOM   7853  C   VAL B1164     208.145 201.136 173.751  1.00 65.85           C  
ATOM   7854  O   VAL B1164     207.623 202.205 173.447  1.00 63.19           O  
ATOM   7855  CB  VAL B1164     206.393 200.002 175.254  1.00 56.57           C  
ATOM   7856  CG1 VAL B1164     205.405 201.122 175.563  1.00 56.80           C  
ATOM   7857  CG2 VAL B1164     205.899 199.224 174.029  1.00 48.54           C  
ATOM   7858  N   ASP B1165     208.950 200.464 172.933  1.00 69.22           N  
ATOM   7859  CA  ASP B1165     209.165 200.767 171.523  1.00 60.83           C  
ATOM   7860  C   ASP B1165     208.595 199.641 170.664  1.00 65.06           C  
ATOM   7861  O   ASP B1165     208.725 198.463 170.994  1.00 68.37           O  
ATOM   7862  CB  ASP B1165     210.649 200.989 171.223  1.00 63.17           C  
ATOM   7863  CG  ASP B1165     211.192 202.306 171.777  1.00 70.20           C  
ATOM   7864  OD1 ASP B1165     210.460 203.314 171.823  1.00 65.21           O  
ATOM   7865  OD2 ASP B1165     212.392 202.353 172.107  1.00 77.48           O1-
ATOM   7866  N   LEU B1166     207.959 200.031 169.566  1.00 58.27           N  
ATOM   7867  CA  LEU B1166     207.330 199.168 168.571  1.00 54.08           C  
ATOM   7868  C   LEU B1166     207.545 199.744 167.156  1.00 60.96           C  
ATOM   7869  O   LEU B1166     208.021 200.873 167.008  1.00 68.14           O  
ATOM   7870  CB  LEU B1166     205.867 198.889 168.978  1.00 53.57           C  
ATOM   7871  CG  LEU B1166     204.815 199.973 168.684  1.00 48.43           C  
ATOM   7872  CD1 LEU B1166     203.441 199.467 169.117  1.00 37.01           C  
ATOM   7873  CD2 LEU B1166     205.079 201.275 169.439  1.00 50.08           C  
ATOM   7874  N   GLY B1167     207.288 198.933 166.133  1.00 58.37           N  
ATOM   7875  CA  GLY B1167     207.528 199.184 164.709  1.00 57.16           C  
ATOM   7876  C   GLY B1167     207.078 200.560 164.205  1.00 58.63           C  
ATOM   7877  O   GLY B1167     205.951 201.000 164.445  1.00 47.38           O  
ATOM   7878  N   ASP B1168     207.993 201.227 163.503  1.00 65.11           N  
ATOM   7879  CA  ASP B1168     207.948 202.619 163.056  1.00 70.54           C  
ATOM   7880  C   ASP B1168     207.691 202.708 161.540  1.00 71.96           C  
ATOM   7881  O   ASP B1168     208.581 202.988 160.733  1.00 74.36           O  
ATOM   7882  CB  ASP B1168     209.232 203.349 163.489  1.00 79.58           C  
ATOM   7883  CG  ASP B1168     210.568 202.701 163.082  1.00 80.54           C  
ATOM   7884  OD1 ASP B1168     210.636 201.483 162.799  1.00 76.13           O  
ATOM   7885  OD2 ASP B1168     211.595 203.413 163.119  1.00 81.00           O1-
ATOM   7886  N   ILE B1169     206.441 202.467 161.149  1.00 72.98           N  
ATOM   7887  CA  ILE B1169     206.027 202.275 159.753  1.00 63.56           C  
ATOM   7888  C   ILE B1169     206.251 203.490 158.830  1.00 70.34           C  
ATOM   7889  O   ILE B1169     206.167 203.345 157.615  1.00 77.08           O  
ATOM   7890  CB  ILE B1169     204.571 201.772 159.710  1.00 53.38           C  
ATOM   7891  CG1 ILE B1169     203.609 202.751 160.407  1.00 55.23           C  
ATOM   7892  CG2 ILE B1169     204.467 200.361 160.318  1.00 49.93           C  
ATOM   7893  CD1 ILE B1169     202.179 202.579 159.908  1.00 55.38           C  
ATOM   7894  N   SER B1170     206.607 204.661 159.361  1.00 73.93           N  
ATOM   7895  CA  SER B1170     207.004 205.843 158.586  1.00 78.04           C  
ATOM   7896  C   SER B1170     208.321 205.687 157.808  1.00 83.66           C  
ATOM   7897  O   SER B1170     208.613 206.505 156.937  1.00 81.66           O  
ATOM   7898  CB  SER B1170     207.095 207.042 159.532  1.00 74.84           C  
ATOM   7899  OG  SER B1170     207.996 206.788 160.594  1.00 64.16           O  
ATOM   7900  N   GLY B1171     209.125 204.650 158.070  1.00 87.13           N  
ATOM   7901  CA  GLY B1171     210.400 204.406 157.368  1.00 88.86           C  
ATOM   7902  C   GLY B1171     210.290 203.585 156.076  1.00 89.91           C  
ATOM   7903  O   GLY B1171     211.284 203.378 155.382  1.00102.19           O  
ATOM   7904  N   ILE B1172     209.102 203.101 155.735  1.00 88.06           N  
ATOM   7905  CA  ILE B1172     208.841 202.205 154.605  1.00 93.46           C  
ATOM   7906  C   ILE B1172     208.712 203.036 153.314  1.00 93.88           C  
ATOM   7907  O   ILE B1172     208.305 202.497 152.285  1.00 92.24           O  
ATOM   7908  CB  ILE B1172     207.535 201.397 154.935  1.00 84.02           C  
ATOM   7909  CG1 ILE B1172     207.697 200.594 156.256  1.00 84.62           C  
ATOM   7910  CG2 ILE B1172     207.058 200.461 153.805  1.00 82.71           C  
ATOM   7911  CD1 ILE B1172     206.418 199.908 156.765  1.00 81.97           C  
ATOM   7912  N   ASN B1173     209.049 204.323 153.340  1.00 94.38           N  
ATOM   7913  CA  ASN B1173     208.939 205.138 152.096  1.00 99.76           C  
ATOM   7914  C   ASN B1173     210.340 205.490 151.580  1.00100.32           C  
ATOM   7915  O   ASN B1173     211.316 205.158 152.284  1.00 98.11           O  
ATOM   7916  CB  ASN B1173     208.074 206.387 152.292  1.00100.24           C  
ATOM   7917  CG  ASN B1173     208.736 207.684 151.878  1.00100.90           C  
ATOM   7918  OD1 ASN B1173     209.812 208.024 152.364  1.00 99.22           O  
ATOM   7919  ND2 ASN B1173     208.084 208.417 150.989  1.00 99.88           N  
ATOM   7920  N   GLN B1180     199.670 209.385 132.367  1.00 76.81           N  
ATOM   7921  CA  GLN B1180     198.586 209.910 131.533  1.00 75.48           C  
ATOM   7922  C   GLN B1180     199.046 210.210 130.102  1.00 75.41           C  
ATOM   7923  O   GLN B1180     198.268 210.044 129.166  1.00 75.32           O  
ATOM   7924  CB  GLN B1180     197.976 211.139 132.235  1.00 80.16           C  
ATOM   7925  CG  GLN B1180     196.952 211.954 131.429  1.00 73.75           C  
ATOM   7926  CD  GLN B1180     195.688 211.204 131.007  1.00 69.43           C  
ATOM   7927  OE1 GLN B1180     195.329 210.154 131.507  1.00 72.50           O  
ATOM   7928  NE2 GLN B1180     194.922 211.741 130.091  1.00 69.54           N  
ATOM   7929  N   LYS B1181     200.314 210.593 129.903  1.00 76.47           N  
ATOM   7930  CA  LYS B1181     200.890 210.945 128.588  1.00 74.36           C  
ATOM   7931  C   LYS B1181     200.684 209.863 127.523  1.00 69.62           C  
ATOM   7932  O   LYS B1181     200.340 210.172 126.392  1.00 71.51           O  
ATOM   7933  CB  LYS B1181     202.380 211.276 128.772  1.00 74.26           C  
ATOM   7934  CG  LYS B1181     203.119 211.531 127.446  1.00 69.90           C  
ATOM   7935  CD  LYS B1181     204.509 212.167 127.638  1.00 74.80           C  
ATOM   7936  CE  LYS B1181     205.482 211.389 128.535  1.00 72.38           C  
ATOM   7937  NZ  LYS B1181     205.813 210.035 128.028  1.00 75.87           N  
ATOM   7938  N   GLU B1182     200.842 208.590 127.860  1.00 66.71           N  
ATOM   7939  CA  GLU B1182     200.589 207.510 126.908  1.00 63.65           C  
ATOM   7940  C   GLU B1182     199.097 207.368 126.573  1.00 64.14           C  
ATOM   7941  O   GLU B1182     198.766 207.102 125.424  1.00 70.38           O  
ATOM   7942  CB  GLU B1182     201.186 206.191 127.410  1.00 62.41           C  
ATOM   7943  CG  GLU B1182     202.722 206.279 127.512  1.00 65.09           C  
ATOM   7944  CD  GLU B1182     203.237 207.070 128.725  1.00 69.88           C  
ATOM   7945  OE1 GLU B1182     202.614 207.011 129.813  1.00 81.80           O  
ATOM   7946  OE2 GLU B1182     204.235 207.810 128.568  1.00 69.98           O1-
ATOM   7947  N   ILE B1183     198.183 207.621 127.517  1.00 64.46           N  
ATOM   7948  CA  ILE B1183     196.740 207.638 127.235  1.00 67.73           C  
ATOM   7949  C   ILE B1183     196.369 208.860 126.384  1.00 71.83           C  
ATOM   7950  O   ILE B1183     195.535 208.755 125.487  1.00 75.13           O  
ATOM   7951  CB  ILE B1183     195.911 207.547 128.539  1.00 75.38           C  
ATOM   7952  CG1 ILE B1183     196.303 206.299 129.372  1.00 79.55           C  
ATOM   7953  CG2 ILE B1183     194.406 207.505 128.221  1.00 64.67           C  
ATOM   7954  CD1 ILE B1183     197.141 206.655 130.610  1.00 75.79           C  
ATOM   7955  N   ASP B1184     197.030 210.004 126.579  1.00 70.65           N  
ATOM   7956  CA  ASP B1184     196.911 211.181 125.704  1.00 74.54           C  
ATOM   7957  C   ASP B1184     197.350 210.875 124.258  1.00 74.26           C  
ATOM   7958  O   ASP B1184     196.616 211.160 123.310  1.00 74.18           O  
ATOM   7959  CB  ASP B1184     197.711 212.357 126.297  1.00 79.65           C  
ATOM   7960  CG  ASP B1184     197.876 213.508 125.309  1.00 84.85           C  
ATOM   7961  OD1 ASP B1184     199.025 213.869 124.989  1.00 85.28           O  
ATOM   7962  OD2 ASP B1184     196.853 214.053 124.849  1.00 87.74           O1-
ATOM   7963  N   ARG B1185     198.491 210.205 124.112  1.00 74.23           N  
ATOM   7964  CA  ARG B1185     198.997 209.808 122.797  1.00 69.21           C  
ATOM   7965  C   ARG B1185     198.051 208.808 122.119  1.00 65.38           C  
ATOM   7966  O   ARG B1185     197.675 208.990 120.962  1.00 68.83           O  
ATOM   7967  CB  ARG B1185     200.395 209.200 122.920  1.00 68.15           C  
ATOM   7968  CG  ARG B1185     201.529 210.180 122.661  1.00 72.51           C  
ATOM   7969  CD  ARG B1185     201.356 211.472 123.442  1.00 78.39           C  
ATOM   7970  NE  ARG B1185     202.476 212.386 123.229  1.00 79.69           N  
ATOM   7971  CZ  ARG B1185     202.525 213.632 123.687  1.00 83.88           C  
ATOM   7972  NH1 ARG B1185     201.514 214.126 124.387  1.00 87.40           N  
ATOM   7973  NH2 ARG B1185     203.588 214.387 123.443  1.00 87.58           N  
ATOM   7974  N   LEU B1186     197.667 207.760 122.845  1.00 66.31           N  
ATOM   7975  CA  LEU B1186     196.739 206.766 122.292  1.00 67.20           C  
ATOM   7976  C   LEU B1186     195.374 207.380 121.895  1.00 65.21           C  
ATOM   7977  O   LEU B1186     194.815 206.986 120.877  1.00 69.04           O  
ATOM   7978  CB  LEU B1186     196.561 205.586 123.266  1.00 69.69           C  
ATOM   7979  CG  LEU B1186     197.486 204.372 123.037  1.00 68.87           C  
ATOM   7980  CD1 LEU B1186     198.966 204.644 123.264  1.00 67.07           C  
ATOM   7981  CD2 LEU B1186     197.062 203.222 123.948  1.00 63.66           C  
ATOM   7982  N   ASN B1187     194.853 208.374 122.619  1.00 67.08           N  
ATOM   7983  CA  ASN B1187     193.663 209.118 122.179  1.00 68.89           C  
ATOM   7984  C   ASN B1187     193.966 209.961 120.925  1.00 73.39           C  
ATOM   7985  O   ASN B1187     193.169 209.999 119.986  1.00 74.41           O  
ATOM   7986  CB  ASN B1187     193.131 209.999 123.326  1.00 70.48           C  
ATOM   7987  CG  ASN B1187     192.210 209.247 124.266  1.00 73.87           C  
ATOM   7988  OD1 ASN B1187     191.029 209.078 124.003  1.00 74.85           O  
ATOM   7989  ND2 ASN B1187     192.699 208.779 125.382  1.00 76.34           N  
ATOM   7990  N   GLU B1188     195.136 210.608 120.879  1.00 71.89           N  
ATOM   7991  CA  GLU B1188     195.588 211.395 119.727  1.00 67.96           C  
ATOM   7992  C   GLU B1188     195.753 210.540 118.458  1.00 71.76           C  
ATOM   7993  O   GLU B1188     195.205 210.905 117.422  1.00 77.65           O  
ATOM   7994  CB  GLU B1188     196.855 212.182 120.109  1.00 67.34           C  
ATOM   7995  CG  GLU B1188     197.521 212.949 118.952  1.00 73.12           C  
ATOM   7996  CD  GLU B1188     198.705 212.211 118.297  1.00 77.64           C  
ATOM   7997  OE1 GLU B1188     198.799 212.201 117.049  1.00 79.90           O  
ATOM   7998  OE2 GLU B1188     199.601 211.719 119.012  1.00 79.63           O1-
ATOM   7999  N   VAL B1189     196.429 209.389 118.503  1.00 69.33           N  
ATOM   8000  CA  VAL B1189     196.577 208.524 117.319  1.00 62.08           C  
ATOM   8001  C   VAL B1189     195.311 207.747 116.980  1.00 65.34           C  
ATOM   8002  O   VAL B1189     195.155 207.360 115.832  1.00 73.26           O  
ATOM   8003  CB  VAL B1189     197.782 207.578 117.394  1.00 57.04           C  
ATOM   8004  CG1 VAL B1189     199.084 208.348 117.598  1.00 58.92           C  
ATOM   8005  CG2 VAL B1189     197.605 206.519 118.468  1.00 61.71           C  
ATOM   8006  N   ALA B1190     194.353 207.568 117.893  1.00 65.60           N  
ATOM   8007  CA  ALA B1190     193.053 207.014 117.514  1.00 67.74           C  
ATOM   8008  C   ALA B1190     192.330 207.946 116.532  1.00 72.38           C  
ATOM   8009  O   ALA B1190     191.746 207.478 115.552  1.00 77.36           O  
ATOM   8010  CB  ALA B1190     192.195 206.774 118.757  1.00 69.63           C  
ATOM   8011  N   LYS B1191     192.440 209.265 116.733  1.00 76.16           N  
ATOM   8012  CA  LYS B1191     192.024 210.260 115.733  1.00 80.53           C  
ATOM   8013  C   LYS B1191     192.991 210.318 114.545  1.00 79.42           C  
ATOM   8014  O   LYS B1191     192.595 210.028 113.420  1.00 78.59           O  
ATOM   8015  CB  LYS B1191     191.789 211.641 116.373  1.00 81.71           C  
ATOM   8016  CG  LYS B1191     190.621 211.591 117.374  1.00 92.30           C  
ATOM   8017  CD  LYS B1191     190.202 212.986 117.858  1.00 96.88           C  
ATOM   8018  CE  LYS B1191     189.033 212.874 118.843  1.00102.68           C  
ATOM   8019  NZ  LYS B1191     188.482 214.199 119.217  1.00110.20           N  
ATOM   8020  N   ASN B1192     194.264 210.632 114.775  1.00 75.91           N  
ATOM   8021  CA  ASN B1192     195.259 210.862 113.726  1.00 73.92           C  
ATOM   8022  C   ASN B1192     195.635 209.638 112.871  1.00 74.20           C  
ATOM   8023  O   ASN B1192     196.350 209.790 111.886  1.00 72.67           O  
ATOM   8024  CB  ASN B1192     196.489 211.565 114.331  1.00 71.11           C  
ATOM   8025  CG  ASN B1192     196.211 213.002 114.732  1.00 74.64           C  
ATOM   8026  OD1 ASN B1192     195.187 213.590 114.425  1.00 72.26           O  
ATOM   8027  ND2 ASN B1192     197.134 213.640 115.401  1.00 76.40           N  
ATOM   8028  N   LEU B1193     195.159 208.429 113.172  1.00 69.66           N  
ATOM   8029  CA  LEU B1193     195.282 207.284 112.263  1.00 68.51           C  
ATOM   8030  C   LEU B1193     194.278 207.340 111.095  1.00 80.16           C  
ATOM   8031  O   LEU B1193     194.552 206.777 110.038  1.00 82.78           O  
ATOM   8032  CB  LEU B1193     195.237 205.983 113.082  1.00 69.80           C  
ATOM   8033  CG  LEU B1193     195.560 204.687 112.326  1.00 71.26           C  
ATOM   8034  CD1 LEU B1193     196.947 204.702 111.689  1.00 71.40           C  
ATOM   8035  CD2 LEU B1193     195.534 203.512 113.312  1.00 70.47           C  
ATOM   8036  N   ASN B1194     193.181 208.105 111.205  1.00 92.41           N  
ATOM   8037  CA  ASN B1194     192.270 208.369 110.077  1.00 82.52           C  
ATOM   8038  C   ASN B1194     192.920 209.182 108.940  1.00 79.77           C  
ATOM   8039  O   ASN B1194     192.534 209.065 107.774  1.00 75.48           O  
ATOM   8040  CB  ASN B1194     190.990 209.056 110.588  1.00 86.23           C  
ATOM   8041  CG  ASN B1194     189.764 208.259 110.203  1.00 91.93           C  
ATOM   8042  OD1 ASN B1194     189.716 207.078 110.511  1.00 91.30           O  
ATOM   8043  ND2 ASN B1194     188.716 208.890 109.698  1.00 95.88           N  
ATOM   8044  N   GLU B1195     193.973 209.937 109.260  1.00 76.87           N  
ATOM   8045  CA  GLU B1195     194.818 210.614 108.267  1.00 73.04           C  
ATOM   8046  C   GLU B1195     195.635 209.641 107.402  1.00 68.07           C  
ATOM   8047  O   GLU B1195     196.266 210.065 106.436  1.00 71.12           O  
ATOM   8048  CB  GLU B1195     195.759 211.607 108.957  1.00 70.91           C  
ATOM   8049  CG  GLU B1195     195.022 212.704 109.729  1.00 69.09           C  
ATOM   8050  CD  GLU B1195     195.987 213.831 110.099  1.00 74.22           C  
ATOM   8051  OE1 GLU B1195     196.864 213.616 110.965  1.00 76.27           O  
ATOM   8052  OE2 GLU B1195     195.888 214.936 109.524  1.00 79.52           O1-
ATOM   8053  N   SER B1196     195.607 208.341 107.713  1.00 67.34           N  
ATOM   8054  CA  SER B1196     196.221 207.283 106.907  1.00 66.40           C  
ATOM   8055  C   SER B1196     195.220 206.198 106.487  1.00 68.75           C  
ATOM   8056  O   SER B1196     195.622 205.104 106.105  1.00 76.03           O  
ATOM   8057  CB  SER B1196     197.450 206.730 107.639  1.00 67.69           C  
ATOM   8058  OG  SER B1196     198.537 206.613 106.751  1.00 66.16           O  
ATOM   8059  N   LEU B1197     193.915 206.473 106.561  1.00 69.88           N  
ATOM   8060  CA  LEU B1197     192.864 205.569 106.086  1.00 72.02           C  
ATOM   8061  C   LEU B1197     192.882 205.442 104.548  1.00 72.71           C  
ATOM   8062  O   LEU B1197     192.394 206.310 103.822  1.00 75.94           O  
ATOM   8063  CB  LEU B1197     191.516 206.062 106.642  1.00 74.53           C  
ATOM   8064  CG  LEU B1197     190.308 205.174 106.290  1.00 75.02           C  
ATOM   8065  CD1 LEU B1197     190.444 203.773 106.887  1.00 78.28           C  
ATOM   8066  CD2 LEU B1197     189.033 205.808 106.833  1.00 80.70           C  
TER    8067      LEU B1197                                                      
HETATM 8068  C1  NAG D   1     171.927 191.295 263.025  1.00 93.06           C  
HETATM 8069  C2  NAG D   1     171.419 191.934 261.745  1.00 93.06           C  
HETATM 8070  C3  NAG D   1     170.522 190.960 260.999  1.00 96.48           C  
HETATM 8071  C4  NAG D   1     171.248 189.639 260.763  1.00100.95           C  
HETATM 8072  C5  NAG D   1     171.831 189.104 262.074  1.00101.01           C  
HETATM 8073  C6  NAG D   1     172.702 187.881 261.883  1.00104.53           C  
HETATM 8074  C7  NAG D   1     171.019 194.336 261.431  1.00 92.18           C  
HETATM 8075  C8  NAG D   1     170.183 195.514 261.830  1.00 88.47           C  
HETATM 8076  N2  NAG D   1     170.711 193.174 262.018  1.00 92.64           N  
HETATM 8077  O3  NAG D   1     170.145 191.551 259.761  1.00101.97           O  
HETATM 8078  O4  NAG D   1     170.335 188.675 260.247  1.00110.09           O  
HETATM 8079  O5  NAG D   1     172.649 190.103 262.709  1.00 99.94           O  
HETATM 8080  O6  NAG D   1     173.307 187.473 263.102  1.00 92.55           O  
HETATM 8081  O7  NAG D   1     171.932 194.432 260.615  1.00 87.74           O  
HETATM 8082  C1  NAG D   2     170.372 188.609 258.804  1.00109.59           C  
HETATM 8083  C2  NAG D   2     169.683 187.317 258.373  1.00110.28           C  
HETATM 8084  C3  NAG D   2     169.654 187.215 256.852  1.00108.39           C  
HETATM 8085  C4  NAG D   2     169.025 188.463 256.245  1.00106.37           C  
HETATM 8086  C5  NAG D   2     169.722 189.718 256.761  1.00104.14           C  
HETATM 8087  C6  NAG D   2     169.041 190.993 256.314  1.00111.31           C  
HETATM 8088  C7  NAG D   2     169.920 185.560 260.069  1.00114.51           C  
HETATM 8089  C8  NAG D   2     170.722 184.379 260.526  1.00112.63           C  
HETATM 8090  N2  NAG D   2     170.344 186.158 258.951  1.00110.83           N  
HETATM 8091  O3  NAG D   2     168.904 186.066 256.473  1.00107.46           O  
HETATM 8092  O4  NAG D   2     169.129 188.416 254.826  1.00112.72           O  
HETATM 8093  O5  NAG D   2     169.713 189.732 258.197  1.00107.68           O  
HETATM 8094  O6  NAG D   2     167.642 190.947 256.556  1.00103.86           O  
HETATM 8095  O7  NAG D   2     168.934 185.954 260.684  1.00112.84           O  
HETATM 8096  C1  NAG E   1     174.946 196.541 282.070  1.00 77.53           C  
HETATM 8097  C2  NAG E   1     173.664 196.161 282.795  1.00 76.08           C  
HETATM 8098  C3  NAG E   1     173.448 197.088 283.982  1.00 77.31           C  
HETATM 8099  C4  NAG E   1     174.668 197.070 284.894  1.00 81.20           C  
HETATM 8100  C5  NAG E   1     175.951 197.350 284.105  1.00 75.51           C  
HETATM 8101  C6  NAG E   1     177.211 197.123 284.914  1.00 73.54           C  
HETATM 8102  C7  NAG E   1     171.815 195.116 281.563  1.00 78.70           C  
HETATM 8103  C8  NAG E   1     170.666 195.341 280.626  1.00 71.18           C  
HETATM 8104  N2  NAG E   1     172.520 196.203 281.898  1.00 73.58           N  
HETATM 8105  O3  NAG E   1     172.294 196.674 284.703  1.00 79.99           O  
HETATM 8106  O4  NAG E   1     174.495 198.031 285.930  1.00 84.77           O  
HETATM 8107  O5  NAG E   1     176.045 196.469 282.974  1.00 73.37           O  
HETATM 8108  O6  NAG E   1     177.250 195.805 285.446  1.00 76.03           O  
HETATM 8109  O7  NAG E   1     172.096 193.998 281.991  1.00 81.83           O  
HETATM 8110  C1  NAG E   2     174.706 197.335 287.183  1.00 85.10           C  
HETATM 8111  C2  NAG E   2     175.168 198.358 288.206  1.00 85.65           C  
HETATM 8112  C3  NAG E   2     175.501 197.659 289.516  1.00 89.24           C  
HETATM 8113  C4  NAG E   2     174.359 196.745 289.957  1.00 91.67           C  
HETATM 8114  C5  NAG E   2     173.775 195.908 288.811  1.00 88.75           C  
HETATM 8115  C6  NAG E   2     172.464 195.252 289.177  1.00 90.15           C  
HETATM 8116  C7  NAG E   2     176.195 200.290 287.107  1.00 87.14           C  
HETATM 8117  C8  NAG E   2     177.471 200.924 286.643  1.00 79.57           C  
HETATM 8118  N2  NAG E   2     176.314 199.104 287.711  1.00 86.37           N  
HETATM 8119  O3  NAG E   2     175.746 198.651 290.506  1.00 90.00           O  
HETATM 8120  O4  NAG E   2     174.858 195.814 290.910  1.00 91.85           O  
HETATM 8121  O5  NAG E   2     173.519 196.711 287.649  1.00 85.43           O  
HETATM 8122  O6  NAG E   2     171.465 196.218 289.467  1.00 93.96           O  
HETATM 8123  O7  NAG E   2     175.104 200.829 286.946  1.00 86.63           O  
HETATM 8124  C1  MAN E   3     174.815 196.326 292.258  1.00 96.73           C  
HETATM 8125  C2  MAN E   3     174.646 195.103 293.182  1.00 95.89           C  
HETATM 8126  C3  MAN E   3     173.834 195.469 294.421  1.00100.19           C  
HETATM 8127  C4  MAN E   3     174.095 196.926 294.852  1.00 93.20           C  
HETATM 8128  C5  MAN E   3     173.701 197.898 293.725  1.00 94.97           C  
HETATM 8129  C6  MAN E   3     174.595 199.118 293.662  1.00 92.37           C  
HETATM 8130  O2  MAN E   3     175.914 194.638 293.686  1.00 89.66           O  
HETATM 8131  O3  MAN E   3     174.146 194.580 295.494  1.00 98.64           O  
HETATM 8132  O4  MAN E   3     173.317 197.236 295.992  1.00 96.87           O  
HETATM 8133  O5  MAN E   3     173.755 197.244 292.431  1.00 96.35           O  
HETATM 8134  O6  MAN E   3     174.028 200.043 292.749  1.00 94.24           O  
HETATM 8135  C1  MAN E   4     172.945 194.024 296.078  1.00 97.55           C  
HETATM 8136  C2  MAN E   4     173.397 193.135 297.278  1.00 95.08           C  
HETATM 8137  C3  MAN E   4     174.055 191.854 296.768  1.00 93.81           C  
HETATM 8138  C4  MAN E   4     173.093 191.123 295.835  1.00 97.98           C  
HETATM 8139  C5  MAN E   4     172.742 192.035 294.643  1.00 99.58           C  
HETATM 8140  C6  MAN E   4     171.735 191.403 293.701  1.00 95.92           C  
HETATM 8141  O2  MAN E   4     172.279 192.706 298.059  1.00 92.69           O  
HETATM 8142  O3  MAN E   4     174.483 190.992 297.831  1.00 92.69           O  
HETATM 8143  O4  MAN E   4     173.688 189.928 295.357  1.00 98.25           O  
HETATM 8144  O5  MAN E   4     172.171 193.285 295.122  1.00 98.76           O  
HETATM 8145  O6  MAN E   4     171.441 192.327 292.660  1.00 95.78           O  
HETATM 8146  C1  NAG F   1     183.628 211.690 240.946  1.00 80.55           C  
HETATM 8147  C2  NAG F   1     182.301 212.429 240.799  1.00 80.03           C  
HETATM 8148  C3  NAG F   1     181.545 211.909 239.579  1.00 80.02           C  
HETATM 8149  C4  NAG F   1     182.421 211.961 238.332  1.00 83.21           C  
HETATM 8150  C5  NAG F   1     183.774 211.295 238.587  1.00 82.20           C  
HETATM 8151  C6  NAG F   1     184.747 211.502 237.450  1.00 87.64           C  
HETATM 8152  C7  NAG F   1     181.372 213.252 242.920  1.00 86.06           C  
HETATM 8153  C8  NAG F   1     180.485 212.935 244.087  1.00 76.85           C  
HETATM 8154  N2  NAG F   1     181.489 212.292 241.998  1.00 79.96           N  
HETATM 8155  O3  NAG F   1     180.374 212.696 239.386  1.00 84.32           O  
HETATM 8156  O4  NAG F   1     181.779 211.285 237.255  1.00 86.26           O  
HETATM 8157  O5  NAG F   1     184.396 211.849 239.758  1.00 80.82           O  
HETATM 8158  O6  NAG F   1     186.006 210.909 237.731  1.00 91.48           O  
HETATM 8159  O7  NAG F   1     181.956 214.326 242.820  1.00 87.30           O  
HETATM 8160  C1  NAG F   2     181.379 212.250 236.251  1.00 88.61           C  
HETATM 8161  C2  NAG F   2     181.496 211.637 234.853  1.00 93.84           C  
HETATM 8162  C3  NAG F   2     181.071 212.657 233.799  1.00100.72           C  
HETATM 8163  C4  NAG F   2     179.702 213.245 234.126  1.00100.63           C  
HETATM 8164  C5  NAG F   2     179.626 213.720 235.578  1.00 88.02           C  
HETATM 8165  C6  NAG F   2     178.232 214.131 235.991  1.00 94.48           C  
HETATM 8166  C7  NAG F   2     183.232 209.902 234.785  1.00 91.79           C  
HETATM 8167  C8  NAG F   2     184.665 209.592 234.468  1.00 90.70           C  
HETATM 8168  N2  NAG F   2     182.849 211.169 234.595  1.00 96.02           N  
HETATM 8169  O3  NAG F   2     181.039 212.026 232.523  1.00100.54           O  
HETATM 8170  O4  NAG F   2     179.463 214.377 233.298  1.00106.81           O  
HETATM 8171  O5  NAG F   2     180.030 212.673 236.473  1.00 84.92           O  
HETATM 8172  O6  NAG F   2     177.418 213.003 236.277  1.00 99.79           O  
HETATM 8173  O7  NAG F   2     182.458 209.044 235.197  1.00 83.01           O  
HETATM 8174  C1  MAN F   3     178.686 214.043 232.128  1.00105.73           C  
HETATM 8175  C2  MAN F   3     177.847 215.304 231.757  1.00109.07           C  
HETATM 8176  C3  MAN F   3     176.632 214.889 230.931  1.00121.28           C  
HETATM 8177  C4  MAN F   3     176.909 213.588 230.161  1.00118.72           C  
HETATM 8178  C5  MAN F   3     177.118 212.428 231.163  1.00110.34           C  
HETATM 8179  C6  MAN F   3     177.872 211.252 230.566  1.00103.47           C  
HETATM 8180  O2  MAN F   3     178.578 216.248 230.934  1.00105.99           O  
HETATM 8181  O3  MAN F   3     176.227 215.921 230.032  1.00124.50           O  
HETATM 8182  O4  MAN F   3     175.812 213.295 229.309  1.00125.34           O  
HETATM 8183  O5  MAN F   3     177.855 212.900 232.337  1.00107.98           O  
HETATM 8184  O6  MAN F   3     178.689 211.749 229.499  1.00101.10           O  
HETATM 8185  C1  MAN F   4     174.930 216.404 230.445  1.00122.07           C  
HETATM 8186  C2  MAN F   4     174.307 217.147 229.236  1.00119.00           C  
HETATM 8187  C3  MAN F   4     175.065 218.449 228.981  1.00120.23           C  
HETATM 8188  C4  MAN F   4     175.155 219.285 230.265  1.00117.65           C  
HETATM 8189  C5  MAN F   4     175.815 218.453 231.375  1.00118.61           C  
HETATM 8190  C6  MAN F   4     175.887 219.180 232.701  1.00108.70           C  
HETATM 8191  O2  MAN F   4     172.950 217.529 229.493  1.00116.19           O  
HETATM 8192  O3  MAN F   4     174.473 219.214 227.934  1.00119.22           O  
HETATM 8193  O4  MAN F   4     175.927 220.449 230.032  1.00116.48           O  
HETATM 8194  O5  MAN F   4     175.049 217.249 231.581  1.00123.40           O  
HETATM 8195  O6  MAN F   4     174.567 219.586 233.056  1.00116.10           O  
HETATM 8196  C1  NAG G   1     185.002 209.696 192.668  1.00 71.40           C  
HETATM 8197  C2  NAG G   1     183.831 210.361 193.394  1.00 71.40           C  
HETATM 8198  C3  NAG G   1     182.639 209.409 193.467  1.00 77.30           C  
HETATM 8199  C4  NAG G   1     182.290 208.873 192.083  1.00 78.30           C  
HETATM 8200  C5  NAG G   1     183.529 208.278 191.418  1.00 71.60           C  
HETATM 8201  C6  NAG G   1     183.286 207.837 189.993  1.00 79.85           C  
HETATM 8202  C7  NAG G   1     184.717 212.002 194.997  1.00 77.56           C  
HETATM 8203  C8  NAG G   1     185.069 212.262 196.431  1.00 80.43           C  
HETATM 8204  N2  NAG G   1     184.224 210.788 194.727  1.00 75.58           N  
HETATM 8205  O3  NAG G   1     181.526 210.101 194.022  1.00 79.62           O  
HETATM 8206  O4  NAG G   1     181.281 207.873 192.186  1.00 89.02           O  
HETATM 8207  O5  NAG G   1     184.579 209.258 191.374  1.00 74.29           O  
HETATM 8208  O6  NAG G   1     184.388 207.096 189.487  1.00 91.31           O  
HETATM 8209  O7  NAG G   1     184.875 212.850 194.124  1.00 73.23           O  
HETATM 8210  C1  NAG G   2     180.050 208.381 191.619  1.00 88.00           C  
HETATM 8211  C2  NAG G   2     179.184 207.211 191.155  1.00 92.54           C  
HETATM 8212  C3  NAG G   2     177.888 207.733 190.541  1.00 97.79           C  
HETATM 8213  C4  NAG G   2     177.185 208.692 191.496  1.00101.09           C  
HETATM 8214  C5  NAG G   2     178.145 209.769 192.009  1.00 95.60           C  
HETATM 8215  C6  NAG G   2     177.541 210.637 193.088  1.00 95.12           C  
HETATM 8216  C7  NAG G   2     180.561 205.267 190.567  1.00 90.07           C  
HETATM 8217  C8  NAG G   2     181.256 204.528 189.463  1.00 86.29           C  
HETATM 8218  N2  NAG G   2     179.901 206.374 190.207  1.00 90.36           N  
HETATM 8219  O3  NAG G   2     177.039 206.635 190.229  1.00100.11           O  
HETATM 8220  O4  NAG G   2     176.119 209.345 190.819  1.00105.82           O  
HETATM 8221  O5  NAG G   2     179.323 209.167 192.571  1.00 90.84           O  
HETATM 8222  O6  NAG G   2     177.418 209.940 194.318  1.00 94.63           O  
HETATM 8223  O7  NAG G   2     180.596 204.880 191.731  1.00 93.26           O  
HETATM 8224  C1  MAN G   3     174.849 208.701 191.066  1.00107.16           C  
HETATM 8225  C2  MAN G   3     173.742 209.803 191.041  1.00108.00           C  
HETATM 8226  C3  MAN G   3     172.586 209.399 191.951  1.00109.42           C  
HETATM 8227  C4  MAN G   3     172.409 207.863 191.948  1.00108.75           C  
HETATM 8228  C5  MAN G   3     173.661 207.198 192.575  1.00109.09           C  
HETATM 8229  C6  MAN G   3     173.918 205.784 192.075  1.00104.38           C  
HETATM 8230  O2  MAN G   3     173.162 210.004 189.730  1.00106.67           O  
HETATM 8231  O3  MAN G   3     171.377 210.054 191.579  1.00104.78           O  
HETATM 8232  O4  MAN G   3     171.247 207.489 192.683  1.00109.62           O  
HETATM 8233  O5  MAN G   3     174.852 207.993 192.300  1.00106.54           O  
HETATM 8234  O6  MAN G   3     172.787 205.366 191.300  1.00106.74           O  
HETATM 8235  C1  NAG H   1     194.297 183.269 110.012  1.00 94.97           C  
HETATM 8236  C2  NAG H   1     194.465 182.422 111.271  1.00 94.96           C  
HETATM 8237  C3  NAG H   1     195.737 181.589 111.176  1.00 97.09           C  
HETATM 8238  C4  NAG H   1     195.721 180.752 109.902  1.00101.73           C  
HETATM 8239  C5  NAG H   1     195.509 181.654 108.690  1.00 99.85           C  
HETATM 8240  C6  NAG H   1     195.370 180.882 107.396  1.00 94.96           C  
HETATM 8241  C7  NAG H   1     193.400 183.459 113.223  1.00 94.96           C  
HETATM 8242  C8  NAG H   1     193.596 184.336 114.422  1.00 94.96           C  
HETATM 8243  N2  NAG H   1     194.482 183.248 112.467  1.00 94.96           N  
HETATM 8244  O3  NAG H   1     195.835 180.754 112.325  1.00 94.96           O  
HETATM 8245  O4  NAG H   1     196.941 180.036 109.746  1.00100.13           O  
HETATM 8246  O5  NAG H   1     194.302 182.416 108.851  1.00 95.98           O  
HETATM 8247  O6  NAG H   1     195.872 181.619 106.290  1.00 94.96           O  
HETATM 8248  O7  NAG H   1     192.310 182.964 112.950  1.00 94.96           O  
HETATM 8249  C1  NAG H   2     196.711 178.666 110.132  1.00102.00           C  
HETATM 8250  C2  NAG H   2     197.838 177.769 109.612  1.00105.70           C  
HETATM 8251  C3  NAG H   2     197.643 176.335 110.104  1.00103.55           C  
HETATM 8252  C4  NAG H   2     197.476 176.303 111.618  1.00100.14           C  
HETATM 8253  C5  NAG H   2     196.359 177.253 112.040  1.00 97.70           C  
HETATM 8254  C6  NAG H   2     196.206 177.362 113.541  1.00 97.54           C  
HETATM 8255  C7  NAG H   2     198.939 178.311 107.484  1.00 99.73           C  
HETATM 8256  C8  NAG H   2     198.838 178.261 105.989  1.00 97.54           C  
HETATM 8257  N2  NAG H   2     197.903 177.803 108.160  1.00100.77           N  
HETATM 8258  O3  NAG H   2     198.766 175.546 109.724  1.00102.17           O  
HETATM 8259  O4  NAG H   2     197.151 174.985 112.045  1.00 97.54           O  
HETATM 8260  O5  NAG H   2     196.643 178.575 111.559  1.00101.36           O  
HETATM 8261  O6  NAG H   2     195.053 178.117 113.889  1.00 97.54           O  
HETATM 8262  O7  NAG H   2     199.916 178.790 108.054  1.00 98.97           O  
HETATM 8263  C1  NAG I   1     216.875 178.837 263.049  1.00 94.49           C  
HETATM 8264  C2  NAG I   1     216.576 178.076 261.770  1.00 93.28           C  
HETATM 8265  C3  NAG I   1     217.869 177.786 261.024  1.00 94.28           C  
HETATM 8266  C4  NAG I   1     218.649 179.076 260.787  1.00101.92           C  
HETATM 8267  C5  NAG I   1     218.820 179.850 262.097  1.00101.62           C  
HETATM 8268  C6  NAG I   1     219.443 181.216 261.905  1.00104.53           C  
HETATM 8269  C7  NAG I   1     214.697 176.527 261.458  1.00 90.87           C  
HETATM 8270  C8  NAG I   1     214.096 175.214 261.858  1.00 83.76           C  
HETATM 8271  N2  NAG I   1     215.857 176.843 262.044  1.00 92.32           N  
HETATM 8272  O3  NAG I   1     217.546 177.163 259.787  1.00103.03           O  
HETATM 8273  O4  NAG I   1     219.940 178.767 260.271  1.00110.47           O  
HETATM 8274  O5  NAG I   1     217.546 180.059 262.732  1.00 99.02           O  
HETATM 8275  O6  NAG I   1     219.493 181.945 263.123  1.00 93.08           O  
HETATM 8276  O7  NAG I   1     214.157 177.268 260.641  1.00 85.36           O  
HETATM 8277  C1  NAG I   2     219.979 178.831 258.828  1.00109.56           C  
HETATM 8278  C2  NAG I   2     221.443 178.881 258.397  1.00109.44           C  
HETATM 8279  C3  NAG I   2     221.546 178.905 256.876  1.00106.38           C  
HETATM 8280  C4  NAG I   2     220.780 177.735 256.271  1.00105.48           C  
HETATM 8281  C5  NAG I   2     219.345 177.711 256.787  1.00103.51           C  
HETATM 8282  C6  NAG I   2     218.582 176.482 256.341  1.00110.96           C  
HETATM 8283  C7  NAG I   2     222.845 179.967 260.092  1.00113.72           C  
HETATM 8284  C8  NAG I   2     223.466 181.253 260.548  1.00111.48           C  
HETATM 8285  N2  NAG I   2     222.115 180.034 258.974  1.00109.47           N  
HETATM 8286  O3  NAG I   2     222.916 178.830 256.498  1.00106.04           O  
HETATM 8287  O4  NAG I   2     220.769 177.847 254.852  1.00111.54           O  
HETATM 8288  O5  NAG I   2     219.337 177.698 258.223  1.00107.38           O  
HETATM 8289  O6  NAG I   2     219.322 175.295 256.584  1.00102.94           O  
HETATM 8290  O7  NAG I   2     222.997 178.917 260.708  1.00112.88           O  
HETATM 8291  C1  NAG J   1     210.821 178.847 282.094  1.00 80.31           C  
HETATM 8292  C2  NAG J   1     211.792 177.928 282.820  1.00 76.44           C  
HETATM 8293  C3  NAG J   1     211.097 177.278 284.007  1.00 78.33           C  
HETATM 8294  C4  NAG J   1     210.502 178.344 284.918  1.00 80.52           C  
HETATM 8295  C5  NAG J   1     209.617 179.314 284.128  1.00 76.23           C  
HETATM 8296  C6  NAG J   1     209.183 180.519 284.936  1.00 71.18           C  
HETATM 8297  C7  NAG J   1     213.622 176.849 281.589  1.00 76.14           C  
HETATM 8298  C8  NAG J   1     214.003 175.741 280.653  1.00 77.42           C  
HETATM 8299  N2  NAG J   1     212.328 176.915 281.924  1.00 73.93           N  
HETATM 8300  O3  NAG J   1     212.033 176.487 284.729  1.00 80.64           O  
HETATM 8301  O4  NAG J   1     209.757 177.715 285.955  1.00 83.80           O  
HETATM 8302  O5  NAG J   1     210.333 179.835 282.996  1.00 79.28           O  
HETATM 8303  O6  NAG J   1     210.305 181.214 285.467  1.00 73.39           O  
HETATM 8304  O7  NAG J   1     214.449 177.652 282.016  1.00 81.23           O  
HETATM 8305  C1  NAG J   2     210.253 178.247 287.207  1.00 85.22           C  
HETATM 8306  C2  NAG J   2     209.136 178.136 288.230  1.00 84.88           C  
HETATM 8307  C3  NAG J   2     209.575 178.776 289.540  1.00 88.76           C  
HETATM 8308  C4  NAG J   2     210.938 178.245 289.981  1.00 90.69           C  
HETATM 8309  C5  NAG J   2     211.955 178.158 288.836  1.00 88.42           C  
HETATM 8310  C6  NAG J   2     213.179 177.352 289.203  1.00 91.01           C  
HETATM 8311  C7  NAG J   2     206.950 178.057 287.131  1.00 84.06           C  
HETATM 8312  C8  NAG J   2     205.762 178.844 286.666  1.00 79.57           C  
HETATM 8313  N2  NAG J   2     207.917 178.754 287.734  1.00 86.48           N  
HETATM 8314  O3  NAG J   2     208.593 178.493 290.530  1.00 89.46           O  
HETATM 8315  O4  NAG J   2     211.494 179.145 290.933  1.00 91.93           O  
HETATM 8316  O5  NAG J   2     211.388 177.533 287.674  1.00 85.18           O  
HETATM 8317  O6  NAG J   2     212.843 176.003 289.494  1.00 91.95           O  
HETATM 8318  O7  NAG J   2     207.030 176.842 286.972  1.00 83.55           O  
HETATM 8319  C1  MAN J   3     211.072 178.853 292.282  1.00 96.31           C  
HETATM 8320  C2  MAN J   3     212.215 179.320 293.205  1.00 95.90           C  
HETATM 8321  C3  MAN J   3     212.305 178.435 294.445  1.00100.75           C  
HETATM 8322  C4  MAN J   3     210.913 177.932 294.877  1.00 94.48           C  
HETATM 8323  C5  MAN J   3     210.269 177.103 293.751  1.00 95.39           C  
HETATM 8324  C6  MAN J   3     208.765 177.266 293.687  1.00 92.54           C  
HETATM 8325  O2  MAN J   3     211.983 180.651 293.708  1.00 89.66           O  
HETATM 8326  O3  MAN J   3     212.918 179.151 295.517  1.00 99.19           O  
HETATM 8327  O4  MAN J   3     211.034 177.105 296.018  1.00 95.95           O  
HETATM 8328  O5  MAN J   3     210.808 177.476 292.456  1.00 95.92           O  
HETATM 8329  O6  MAN J   3     208.248 176.311 292.775  1.00 95.80           O  
HETATM 8330  C1  MAN J   4     214.001 178.391 296.102  1.00 97.41           C  
HETATM 8331  C2  MAN J   4     214.544 179.228 297.302  1.00 95.96           C  
HETATM 8332  C3  MAN J   4     215.323 180.439 296.790  1.00 96.51           C  
HETATM 8333  C4  MAN J   4     216.438 179.971 295.858  1.00 99.64           C  
HETATM 8334  C5  MAN J   4     215.824 179.209 294.667  1.00100.26           C  
HETATM 8335  C6  MAN J   4     216.875 178.652 293.725  1.00 96.74           C  
HETATM 8336  O2  MAN J   4     215.475 178.476 298.083  1.00 93.60           O  
HETATM 8337  O3  MAN J   4     215.855 181.242 297.852  1.00 92.69           O  
HETATM 8338  O4  MAN J   4     217.174 181.083 295.379  1.00 97.75           O  
HETATM 8339  O5  MAN J   4     215.028 178.089 295.147  1.00 99.26           O  
HETATM 8340  O6  MAN J   4     216.223 177.934 292.685  1.00 97.66           O  
HETATM 8341  C1  NAG K   1     193.364 178.731 240.968  1.00 78.00           C  
HETATM 8342  C2  NAG K   1     193.389 177.212 240.823  1.00 78.56           C  
HETATM 8343  C3  NAG K   1     194.217 176.817 239.604  1.00 79.24           C  
HETATM 8344  C4  NAG K   1     193.734 177.548 238.356  1.00 83.47           C  
HETATM 8345  C5  NAG K   1     193.633 179.053 238.609  1.00 81.48           C  
HETATM 8346  C6  NAG K   1     192.967 179.790 237.471  1.00 84.69           C  
HETATM 8347  C7  NAG K   1     193.141 175.999 242.945  1.00 81.71           C  
HETATM 8348  C8  NAG K   1     193.859 175.391 244.113  1.00 75.43           C  
HETATM 8349  N2  NAG K   1     193.913 176.579 242.023  1.00 76.61           N  
HETATM 8350  O3  NAG K   1     194.122 175.409 239.412  1.00 83.59           O  
HETATM 8351  O4  NAG K   1     194.640 177.329 237.279  1.00 90.73           O  
HETATM 8352  O5  NAG K   1     192.842 179.315 239.780  1.00 79.48           O  
HETATM 8353  O6  NAG K   1     192.850 181.177 237.750  1.00 88.74           O  
HETATM 8354  O7  NAG K   1     191.919 175.966 242.845  1.00 85.83           O  
HETATM 8355  C1  NAG K   2     194.005 176.499 236.276  1.00 89.97           C  
HETATM 8356  C2  NAG K   2     194.478 176.905 234.878  1.00 95.19           C  
HETATM 8357  C3  NAG K   2     193.807 176.025 233.824  1.00101.13           C  
HETATM 8358  C4  NAG K   2     193.984 174.546 234.153  1.00102.03           C  
HETATM 8359  C5  NAG K   2     193.610 174.244 235.606  1.00 88.77           C  
HETATM 8360  C6  NAG K   2     193.952 172.832 236.020  1.00 92.72           C  
HETATM 8361  C7  NAG K   2     195.111 179.276 234.807  1.00 91.22           C  
HETATM 8362  C8  NAG K   2     194.662 180.672 234.488  1.00 88.09           C  
HETATM 8363  N2  NAG K   2     194.205 178.310 234.618  1.00 96.61           N  
HETATM 8364  O3  NAG K   2     194.370 176.312 232.548  1.00100.78           O  
HETATM 8365  O4  NAG K   2     193.123 173.772 233.326  1.00105.42           O  
HETATM 8366  O5  NAG K   2     194.314 175.119 236.500  1.00 86.55           O  
HETATM 8367  O6  NAG K   2     195.336 172.693 236.306  1.00 87.50           O  
HETATM 8368  O7  NAG K   2     196.241 179.036 235.219  1.00 79.43           O  
HETATM 8369  C1  MAN K   3     193.802 173.265 232.157  1.00103.95           C  
HETATM 8370  C2  MAN K   3     193.130 171.907 231.787  1.00107.25           C  
HETATM 8371  C3  MAN K   3     194.098 171.062 230.962  1.00118.86           C  
HETATM 8372  C4  MAN K   3     195.085 171.952 230.191  1.00116.85           C  
HETATM 8373  C5  MAN K   3     195.985 172.715 231.192  1.00106.31           C  
HETATM 8374  C6  MAN K   3     196.625 173.956 230.594  1.00101.40           C  
HETATM 8375  O2  MAN K   3     191.947 172.066 230.964  1.00104.03           O  
HETATM 8376  O3  MAN K   3     193.407 170.194 230.064  1.00123.49           O  
HETATM 8377  O4  MAN K   3     195.888 171.148 229.340  1.00123.51           O  
HETATM 8378  O5  MAN K   3     195.207 173.118 232.366  1.00105.62           O  
HETATM 8379  O6  MAN K   3     195.786 174.413 229.526  1.00 99.22           O  
HETATM 8380  C1  MAN K   4     193.638 168.830 230.479  1.00121.24           C  
HETATM 8381  C2  MAN K   4     193.307 167.917 229.271  1.00118.20           C  
HETATM 8382  C3  MAN K   4     191.800 167.921 229.016  1.00118.78           C  
HETATM 8383  C4  MAN K   4     191.032 167.582 230.300  1.00116.86           C  
HETATM 8384  C5  MAN K   4     191.421 168.571 231.409  1.00118.25           C  
HETATM 8385  C6  MAN K   4     190.756 168.271 232.735  1.00108.32           C  
HETATM 8386  O2  MAN K   4     193.656 166.551 229.529  1.00115.19           O  
HETATM 8387  O3  MAN K   4     191.435 167.024 227.970  1.00118.56           O  
HETATM 8388  O4  MAN K   4     189.637 167.667 230.067  1.00115.33           O  
HETATM 8389  O5  MAN K   4     192.847 168.511 231.615  1.00123.57           O  
HETATM 8390  O6  MAN K   4     191.065 166.926 233.092  1.00116.21           O  
HETATM 8391  C1  NAG L   1     194.406 180.863 192.688  1.00 71.40           C  
HETATM 8392  C2  NAG L   1     194.417 179.517 193.415  1.00 71.68           C  
HETATM 8393  C3  NAG L   1     195.837 178.962 193.489  1.00 77.52           C  
HETATM 8394  C4  NAG L   1     196.476 178.927 192.105  1.00 79.93           C  
HETATM 8395  C5  NAG L   1     196.371 180.296 191.439  1.00 78.08           C  
HETATM 8396  C6  NAG L   1     196.875 180.305 190.014  1.00 81.61           C  
HETATM 8397  C7  NAG L   1     192.552 179.465 195.018  1.00 75.50           C  
HETATM 8398  C8  NAG L   1     192.151 179.641 196.452  1.00 80.45           C  
HETATM 8399  N2  NAG L   1     193.850 179.645 194.748  1.00 77.71           N  
HETATM 8400  O3  NAG L   1     195.796 177.653 194.046  1.00 79.79           O  
HETATM 8401  O4  NAG L   1     197.847 178.554 192.209  1.00 91.06           O  
HETATM 8402  O5  NAG L   1     194.997 180.715 191.394  1.00 75.12           O  
HETATM 8403  O6  NAG L   1     196.965 181.630 189.506  1.00 90.19           O  
HETATM 8404  O7  NAG L   1     191.739 179.176 194.146  1.00 73.38           O  
HETATM 8405  C1  NAG L   2     198.024 177.233 191.643  1.00 89.08           C  
HETATM 8406  C2  NAG L   2     199.470 177.069 191.180  1.00 93.63           C  
HETATM 8407  C3  NAG L   2     199.667 175.685 190.567  1.00 97.52           C  
HETATM 8408  C4  NAG L   2     199.189 174.597 191.524  1.00100.44           C  
HETATM 8409  C5  NAG L   2     197.776 174.890 192.036  1.00 97.05           C  
HETATM 8410  C6  NAG L   2     197.327 173.934 193.116  1.00 95.12           C  
HETATM 8411  C7  NAG L   2     200.464 179.233 190.589  1.00 89.95           C  
HETATM 8412  C8  NAG L   2     200.755 180.204 189.484  1.00 86.29           C  
HETATM 8413  N2  NAG L   2     199.836 178.108 190.231  1.00 88.80           N  
HETATM 8414  O3  NAG L   2     201.042 175.499 190.256  1.00 99.87           O  
HETATM 8415  O4  NAG L   2     199.157 173.347 190.848  1.00104.59           O  
HETATM 8416  O5  NAG L   2     197.707 176.212 192.597  1.00 91.76           O  
HETATM 8417  O6  NAG L   2     197.991 174.178 194.346  1.00 94.24           O  
HETATM 8418  O7  NAG L   2     200.781 179.459 191.753  1.00 92.10           O  
HETATM 8419  C1  MAN L   3     200.350 172.570 191.096  1.00105.92           C  
HETATM 8420  C2  MAN L   3     199.950 171.060 191.073  1.00106.67           C  
HETATM 8421  C3  MAN L   3     200.879 170.263 191.984  1.00105.01           C  
HETATM 8422  C4  MAN L   3     202.297 170.878 191.980  1.00108.80           C  
HETATM 8423  C5  MAN L   3     202.246 172.296 192.605  1.00108.24           C  
HETATM 8424  C6  MAN L   3     203.341 173.226 192.104  1.00105.11           C  
HETATM 8425  O2  MAN L   3     200.067 170.456 189.762  1.00101.95           O  
HETATM 8426  O3  MAN L   3     200.917 168.888 191.613  1.00103.34           O  
HETATM 8427  O4  MAN L   3     203.202 170.061 192.716  1.00107.05           O  
HETATM 8428  O5  MAN L   3     200.962 172.929 192.330  1.00103.49           O  
HETATM 8429  O6  MAN L   3     204.269 172.455 191.330  1.00102.54           O  
HETATM 8430  C1  NAG M   1     212.633 202.038 110.011  1.00 95.48           C  
HETATM 8431  C2  NAG M   1     213.282 202.609 111.269  1.00 95.31           C  
HETATM 8432  C3  NAG M   1     213.367 204.127 111.173  1.00 98.60           C  
HETATM 8433  C4  NAG M   1     214.099 204.531 109.898  1.00102.27           C  
HETATM 8434  C5  NAG M   1     213.425 203.894 108.687  1.00100.56           C  
HETATM 8435  C6  NAG M   1     214.163 204.159 107.393  1.00 94.96           C  
HETATM 8436  C7  NAG M   1     212.918 201.170 113.223  1.00 94.96           C  
HETATM 8437  C8  NAG M   1     212.060 200.902 114.422  1.00 94.96           C  
HETATM 8438  N2  NAG M   1     212.559 202.212 112.466  1.00 94.96           N  
HETATM 8439  O3  NAG M   1     214.040 204.631 112.321  1.00 94.96           O  
HETATM 8440  O4  NAG M   1     214.108 205.945 109.741  1.00104.51           O  
HETATM 8441  O5  NAG M   1     213.369 202.468 108.849  1.00 98.41           O  
HETATM 8442  O6  NAG M   1     213.274 204.223 106.286  1.00 94.96           O  
HETATM 8443  O7  NAG M   1     213.892 200.474 112.951  1.00 94.96           O  
HETATM 8444  C1  NAG M   2     215.410 206.432 110.126  1.00102.48           C  
HETATM 8445  C2  NAG M   2     215.622 207.857 109.604  1.00105.30           C  
HETATM 8446  C3  NAG M   2     216.961 208.406 110.096  1.00103.36           C  
HETATM 8447  C4  NAG M   2     217.072 208.279 111.610  1.00100.24           C  
HETATM 8448  C5  NAG M   2     216.809 206.837 112.034  1.00 97.54           C  
HETATM 8449  C6  NAG M   2     216.791 206.652 113.535  1.00 97.54           C  
HETATM 8450  C7  NAG M   2     214.602 208.536 107.476  1.00 99.86           C  
HETATM 8451  C8  NAG M   2     214.696 208.472 105.981  1.00 99.56           C  
HETATM 8452  N2  NAG M   2     215.560 207.894 108.152  1.00100.55           N  
HETATM 8453  O3  NAG M   2     217.082 209.773 109.714  1.00100.56           O  
HETATM 8454  O4  NAG M   2     218.376 208.658 112.037  1.00 97.54           O  
HETATM 8455  O5  NAG M   2     215.522 206.421 111.553  1.00101.14           O  
HETATM 8456  O6  NAG M   2     216.715 205.276 113.885  1.00 97.54           O  
HETATM 8457  O7  NAG M   2     213.698 209.142 108.045  1.00 97.54           O  
HETATM 8458  C1  NAG N   1     205.189 223.999 263.021  1.00 91.56           C  
HETATM 8459  C2  NAG N   1     205.998 224.119 261.742  1.00 90.43           C  
HETATM 8460  C3  NAG N   1     205.603 225.382 260.994  1.00 87.69           C  
HETATM 8461  C4  NAG N   1     204.096 225.413 260.757  1.00 97.95           C  
HETATM 8462  C5  NAG N   1     203.340 225.176 262.067  1.00 97.85           C  
HETATM 8463  C6  NAG N   1     201.846 225.033 261.874  1.00101.94           C  
HETATM 8464  C7  NAG N   1     208.279 223.265 261.431  1.00 89.97           C  
HETATM 8465  C8  NAG N   1     209.716 223.401 261.831  1.00 86.45           C  
HETATM 8466  N2  NAG N   1     207.425 224.113 262.016  1.00 88.21           N  
HETATM 8467  O3  NAG N   1     206.305 225.412 259.757  1.00 99.62           O  
HETATM 8468  O4  NAG N   1     203.718 226.685 260.239  1.00105.58           O  
HETATM 8469  O5  NAG N   1     203.796 223.969 262.703  1.00 98.49           O  
HETATM 8470  O6  NAG N   1     201.189 224.713 263.093  1.00 90.41           O  
HETATM 8471  O7  NAG N   1     207.907 222.426 260.615  1.00 86.08           O  
HETATM 8472  C1  NAG N   2     203.644 226.685 258.796  1.00107.08           C  
HETATM 8473  C2  NAG N   2     202.870 227.927 258.364  1.00107.50           C  
HETATM 8474  C3  NAG N   2     202.798 228.002 256.842  1.00105.27           C  
HETATM 8475  C4  NAG N   2     204.194 227.923 256.237  1.00103.47           C  
HETATM 8476  C5  NAG N   2     204.932 226.693 256.755  1.00102.24           C  
HETATM 8477  C6  NAG N   2     206.377 226.645 256.309  1.00105.44           C  
HETATM 8478  C7  NAG N   2     201.228 228.601 260.057  1.00112.37           C  
HETATM 8479  C8  NAG N   2     199.803 228.497 260.513  1.00111.08           C  
HETATM 8480  N2  NAG N   2     201.535 227.934 258.940  1.00108.62           N  
HETATM 8481  O3  NAG N   2     202.178 229.226 256.462  1.00103.50           O  
HETATM 8482  O4  NAG N   2     204.103 227.856 254.818  1.00109.67           O  
HETATM 8483  O5  NAG N   2     204.947 226.695 258.191  1.00105.47           O  
HETATM 8484  O6  NAG N   2     207.036 227.880 256.551  1.00101.75           O  
HETATM 8485  O7  NAG N   2     202.061 229.259 260.673  1.00109.80           O  
HETATM 8486  C1  NAG O   1     208.203 218.775 282.073  1.00 74.72           C  
HETATM 8487  C2  NAG O   1     208.513 220.075 282.797  1.00 71.18           C  
HETATM 8488  C3  NAG O   1     209.423 219.800 283.985  1.00 74.92           C  
HETATM 8489  C4  NAG O   1     208.796 218.753 284.897  1.00 79.59           C  
HETATM 8490  C5  NAG O   1     208.399 217.501 284.109  1.00 72.33           C  
HETATM 8491  C6  NAG O   1     207.572 216.524 284.917  1.00 71.18           C  
HETATM 8492  C7  NAG O   1     208.533 222.198 281.564  1.00 72.49           C  
HETATM 8493  C8  NAG O   1     209.303 223.081 280.627  1.00 71.18           C  
HETATM 8494  N2  NAG O   1     209.122 221.045 281.900  1.00 71.18           N  
HETATM 8495  O3  NAG O   1     209.640 221.007 284.706  1.00 79.43           O  
HETATM 8496  O4  NAG O   1     209.714 218.423 285.935  1.00 82.96           O  
HETATM 8497  O5  NAG O   1     207.590 217.859 282.977  1.00 74.72           O  
HETATM 8498  O6  NAG O   1     206.410 217.149 285.448  1.00 72.11           O  
HETATM 8499  O7  NAG O   1     207.424 222.514 281.990  1.00 77.78           O  
HETATM 8500  C1  NAG O   2     209.004 218.589 287.187  1.00 83.80           C  
HETATM 8501  C2  NAG O   2     209.658 217.678 288.211  1.00 84.69           C  
HETATM 8502  C3  NAG O   2     208.885 217.740 289.520  1.00 88.60           C  
HETATM 8503  C4  NAG O   2     208.663 219.186 289.960  1.00 92.59           C  
HETATM 8504  C5  NAG O   2     208.231 220.110 288.813  1.00 89.17           C  
HETATM 8505  C6  NAG O   2     208.318 221.573 289.178  1.00 91.33           C  
HETATM 8506  C7  NAG O   2     210.820 215.823 287.115  1.00 83.65           C  
HETATM 8507  C8  NAG O   2     210.732 214.400 286.651  1.00 79.57           C  
HETATM 8508  N2  NAG O   2     209.733 216.313 287.717  1.00 86.76           N  
HETATM 8509  O3  NAG O   2     209.621 217.033 290.511  1.00 88.92           O  
HETATM 8510  O4  NAG O   2     207.606 219.220 290.912  1.00 91.74           O  
HETATM 8511  O5  NAG O   2     209.056 219.929 287.652  1.00 83.54           O  
HETATM 8512  O6  NAG O   2     209.653 221.956 289.469  1.00 92.98           O  
HETATM 8513  O7  NAG O   2     211.832 216.498 286.954  1.00 85.12           O  
HETATM 8514  C1  MAN O   3     208.070 219.002 292.260  1.00 95.67           C  
HETATM 8515  C2  MAN O   3     207.094 219.760 293.183  1.00 93.99           C  
HETATM 8516  C3  MAN O   3     207.815 220.281 294.422  1.00100.42           C  
HETATM 8517  C4  MAN O   3     208.946 219.328 294.855  1.00 95.50           C  
HETATM 8518  C5  MAN O   3     209.986 219.182 293.730  1.00 95.26           C  
HETATM 8519  C6  MAN O   3     210.597 217.798 293.668  1.00 92.35           C  
HETATM 8520  O2  MAN O   3     206.057 218.894 293.686  1.00 89.66           O  
HETATM 8521  O3  MAN O   3     206.888 220.456 295.494  1.00 99.50           O  
HETATM 8522  O4  MAN O   3     209.602 219.847 295.996  1.00 98.01           O  
HETATM 8523  O5  MAN O   3     209.395 219.462 292.435  1.00 96.22           O  
HETATM 8524  O6  MAN O   3     211.682 217.827 292.756  1.00 94.41           O  
HETATM 8525  C1  MAN O   4     207.006 221.775 296.077  1.00 96.38           C  
HETATM 8526  C2  MAN O   4     206.008 221.828 297.276  1.00 95.81           C  
HETATM 8527  C3  MAN O   4     204.571 221.898 296.764  1.00 95.71           C  
HETATM 8528  C4  MAN O   4     204.419 223.096 295.831  1.00100.03           C  
HETATM 8529  C5  MAN O   4     205.386 222.943 294.640  1.00 99.95           C  
HETATM 8530  C6  MAN O   4     205.343 224.131 293.697  1.00 96.34           C  
HETATM 8531  O2  MAN O   4     206.195 223.011 298.057  1.00 92.69           O  
HETATM 8532  O3  MAN O   4     203.609 221.958 297.826  1.00 94.33           O  
HETATM 8533  O4  MAN O   4     203.087 223.177 295.351  1.00 98.76           O  
HETATM 8534  O5  MAN O   4     206.753 222.814 295.120  1.00 98.48           O  
HETATM 8535  O6  MAN O   4     206.291 223.923 292.657  1.00 97.09           O  
HETATM 8536  C1  NAG P   1     217.035 203.658 240.969  1.00 82.59           C  
HETATM 8537  C2  NAG P   1     218.338 204.439 240.823  1.00 82.62           C  
HETATM 8538  C3  NAG P   1     218.267 205.352 239.602  1.00 83.90           C  
HETATM 8539  C4  NAG P   1     217.876 204.567 238.355  1.00 87.97           C  
HETATM 8540  C5  NAG P   1     216.622 203.728 238.609  1.00 85.96           C  
HETATM 8541  C6  NAG P   1     216.317 202.781 237.472  1.00 87.72           C  
HETATM 8542  C7  NAG P   1     219.513 204.833 242.945  1.00 88.21           C  
HETATM 8543  C8  NAG P   1     219.680 205.761 244.111  1.00 77.89           C  
HETATM 8544  N2  NAG P   1     218.624 205.211 242.021  1.00 84.16           N  
HETATM 8545  O3  NAG P   1     219.534 205.973 239.410  1.00 86.81           O  
HETATM 8546  O4  NAG P   1     217.612 205.460 237.277  1.00 93.86           O  
HETATM 8547  O5  NAG P   1     216.790 202.913 239.781  1.00 84.66           O  
HETATM 8548  O6  NAG P   1     215.174 201.987 237.753  1.00 92.12           O  
HETATM 8549  O7  NAG P   1     220.151 203.791 242.846  1.00 91.01           O  
HETATM 8550  C1  NAG P   2     218.649 205.324 236.274  1.00 94.03           C  
HETATM 8551  C2  NAG P   2     218.061 205.528 234.876  1.00 97.59           C  
HETATM 8552  C3  NAG P   2     219.158 205.386 233.823  1.00103.57           C  
HETATM 8553  C4  NAG P   2     220.351 206.278 234.151  1.00101.81           C  
HETATM 8554  C5  NAG P   2     220.799 206.107 235.603  1.00 90.08           C  
HETATM 8555  C6  NAG P   2     221.851 207.110 236.017  1.00 94.02           C  
HETATM 8556  C7  NAG P   2     215.691 204.891 234.805  1.00 92.64           C  
HETATM 8557  C8  NAG P   2     214.707 203.804 234.488  1.00 89.77           C  
HETATM 8558  N2  NAG P   2     216.980 204.589 234.617  1.00 98.54           N  
HETATM 8559  O3  NAG P   2     218.629 205.728 232.546  1.00101.67           O  
HETATM 8560  O4  NAG P   2     221.452 205.919 233.324  1.00106.91           O  
HETATM 8561  O5  NAG P   2     219.689 206.281 236.497  1.00 88.14           O  
HETATM 8562  O6  NAG P   2     221.280 208.379 236.302  1.00 87.80           O  
HETATM 8563  O7  NAG P   2     215.334 205.990 235.216  1.00 83.92           O  
HETATM 8564  C1  MAN P   3     221.552 206.758 232.154  1.00105.61           C  
HETATM 8565  C2  MAN P   3     223.064 206.854 231.785  1.00108.59           C  
HETATM 8566  C3  MAN P   3     223.313 208.114 230.958  1.00120.74           C  
HETATM 8567  C4  MAN P   3     222.049 208.523 230.186  1.00117.86           C  
HETATM 8568  C5  MAN P   3     220.938 208.922 231.187  1.00107.68           C  
HETATM 8569  C6  MAN P   3     219.543 208.857 230.588  1.00102.52           C  
HETATM 8570  O2  MAN P   3     223.518 205.749 230.963  1.00105.16           O  
HETATM 8571  O3  MAN P   3     224.410 207.948 230.060  1.00126.20           O  
HETATM 8572  O4  MAN P   3     222.344 209.619 229.334  1.00124.11           O  
HETATM 8573  O5  MAN P   3     220.977 208.049 232.361  1.00107.77           O  
HETATM 8574  O6  MAN P   3     219.567 207.900 229.522  1.00101.13           O  
HETATM 8575  C1  MAN P   4     225.476 208.831 230.474  1.00122.86           C  
HETATM 8576  C2  MAN P   4     226.433 208.998 229.266  1.00118.97           C  
HETATM 8577  C3  MAN P   4     227.182 207.691 229.013  1.00119.69           C  
HETATM 8578  C4  MAN P   4     227.860 207.196 230.298  1.00117.92           C  
HETATM 8579  C5  MAN P   4     226.808 207.041 231.407  1.00118.92           C  
HETATM 8580  C6  MAN P   4     227.400 206.616 232.734  1.00108.98           C  
HETATM 8581  O2  MAN P   4     227.441 209.983 229.524  1.00116.43           O  
HETATM 8582  O3  MAN P   4     228.142 207.821 227.967  1.00119.81           O  
HETATM 8583  O4  MAN P   4     228.482 205.946 230.066  1.00116.54           O  
HETATM 8584  O5  MAN P   4     226.148 208.306 231.611  1.00123.61           O  
HETATM 8585  O6  MAN P   4     228.411 207.557 233.089  1.00115.25           O  
HETATM 8586  C1  NAG Q   1     214.677 203.434 192.688  1.00 72.05           C  
HETATM 8587  C2  NAG Q   1     215.837 204.116 193.415  1.00 73.91           C  
HETATM 8588  C3  NAG Q   1     215.608 205.624 193.487  1.00 77.10           C  
HETATM 8589  C4  NAG Q   1     215.320 206.194 192.102  1.00 80.34           C  
HETATM 8590  C5  NAG Q   1     214.186 205.417 191.436  1.00 73.87           C  
HETATM 8591  C6  NAG Q   1     213.927 205.847 190.011  1.00 80.75           C  
HETATM 8592  C7  NAG Q   1     216.814 202.530 195.020  1.00 80.05           C  
HETATM 8593  C8  NAG Q   1     216.862 202.096 196.454  1.00 82.97           C  
HETATM 8594  N2  NAG Q   1     216.009 203.563 194.748  1.00 77.20           N  
HETATM 8595  O3  NAG Q   1     216.763 206.243 194.043  1.00 78.70           O  
HETATM 8596  O4  NAG Q   1     214.958 207.567 192.204  1.00 91.41           O  
HETATM 8597  O5  NAG Q   1     214.511 204.018 191.393  1.00 78.05           O  
HETATM 8598  O6  NAG Q   1     212.735 205.263 189.504  1.00 90.87           O  
HETATM 8599  O7  NAG Q   1     217.471 201.969 194.148  1.00 77.85           O  
HETATM 8600  C1  NAG Q   2     216.014 208.380 191.637  1.00 89.60           C  
HETATM 8601  C2  NAG Q   2     215.433 209.714 191.172  1.00 93.34           C  
HETATM 8602  C3  NAG Q   2     216.534 210.575 190.559  1.00 97.88           C  
HETATM 8603  C4  NAG Q   2     217.715 210.706 191.515  1.00101.51           C  
HETATM 8604  C5  NAG Q   2     218.167 209.336 192.029  1.00 97.70           C  
HETATM 8605  C6  NAG Q   2     219.220 209.427 193.109  1.00 96.15           C  
HETATM 8606  C7  NAG Q   2     213.062 209.492 190.581  1.00 89.98           C  
HETATM 8607  C8  NAG Q   2     212.076 209.259 189.476  1.00 86.29           C  
HETATM 8608  N2  NAG Q   2     214.351 209.511 190.223  1.00 91.42           N  
HETATM 8609  O3  NAG Q   2     216.007 211.859 190.245  1.00 99.36           O  
HETATM 8610  O4  NAG Q   2     218.814 211.303 190.839  1.00106.33           O  
HETATM 8611  O5  NAG Q   2     217.057 208.617 192.590  1.00 92.08           O  
HETATM 8612  O6  NAG Q   2     218.676 209.882 194.338  1.00 95.00           O  
HETATM 8613  O7  NAG Q   2     212.708 209.656 191.745  1.00 91.72           O  
HETATM 8614  C1  MAN Q   3     218.890 212.725 191.085  1.00103.16           C  
HETATM 8615  C2  MAN Q   3     220.398 213.133 191.061  1.00107.95           C  
HETATM 8616  C3  MAN Q   3     220.625 214.337 191.971  1.00109.76           C  
HETATM 8617  C4  MAN Q   3     219.383 215.257 191.966  1.00108.86           C  
HETATM 8618  C5  MAN Q   3     218.180 214.506 192.592  1.00109.32           C  
HETATM 8619  C6  MAN Q   3     216.827 214.989 192.090  1.00103.16           C  
HETATM 8620  O2  MAN Q   3     220.863 213.534 189.751  1.00103.51           O  
HETATM 8621  O3  MAN Q   3     221.796 215.056 191.600  1.00103.89           O  
HETATM 8622  O4  MAN Q   3     219.638 216.451 192.700  1.00106.87           O  
HETATM 8623  O5  MAN Q   3     218.274 213.077 192.318  1.00105.33           O  
HETATM 8624  O6  MAN Q   3     217.031 216.177 191.315  1.00103.24           O  
HETATM 8625  C1  NAG R   1     187.268 208.580 109.969  1.00 96.11           C  
HETATM 8626  C2  NAG R   1     186.449 208.858 111.227  1.00 94.96           C  
HETATM 8627  C3  NAG R   1     185.092 208.172 111.130  1.00 95.49           C  
HETATM 8628  C4  NAG R   1     184.376 208.604 109.855  1.00101.77           C  
HETATM 8629  C5  NAG R   1     185.265 208.336 108.645  1.00 99.66           C  
HETATM 8630  C6  NAG R   1     184.667 208.841 107.349  1.00 94.96           C  
HETATM 8631  C7  NAG R   1     187.877 209.264 113.180  1.00 94.96           C  
HETATM 8632  C8  NAG R   1     188.537 208.656 114.380  1.00 94.96           C  
HETATM 8633  N2  NAG R   1     187.154 208.431 112.424  1.00 94.96           N  
HETATM 8634  O3  NAG R   1     184.318 208.506 112.278  1.00 94.96           O  
HETATM 8635  O4  NAG R   1     183.147 207.905 109.698  1.00 99.99           O  
HETATM 8636  O5  NAG R   1     186.528 209.001 108.807  1.00 96.66           O  
HETATM 8637  O6  NAG R   1     185.056 208.037 106.244  1.00 94.96           O  
HETATM 8638  O7  NAG R   1     187.993 210.455 112.906  1.00 94.96           O  
HETATM 8639  C1  NAG R   2     182.074 208.789 110.083  1.00 99.39           C  
HETATM 8640  C2  NAG R   2     180.735 208.260 109.561  1.00104.31           C  
HETATM 8641  C3  NAG R   2     179.590 209.146 110.051  1.00103.00           C  
HETATM 8642  C4  NAG R   2     179.644 209.308 111.565  1.00100.13           C  
HETATM 8643  C5  NAG R   2     181.024 209.801 111.989  1.00 97.54           C  
HETATM 8644  C6  NAG R   2     181.193 209.880 113.490  1.00 97.54           C  
HETATM 8645  C7  NAG R   2     180.657 207.034 107.434  1.00 98.79           C  
HETATM 8646  C8  NAG R   2     180.666 207.146 105.939  1.00 97.69           C  
HETATM 8647  N2  NAG R   2     180.734 208.186 108.109  1.00 99.53           N  
HETATM 8648  O3  NAG R   2     178.346 208.567 109.670  1.00101.77           O  
HETATM 8649  O4  NAG R   2     178.664 210.248 111.991  1.00 97.54           O  
HETATM 8650  O5  NAG R   2     182.028 208.894 111.509  1.00 99.95           O  
HETATM 8651  O6  NAG R   2     182.423 210.502 113.839  1.00 97.54           O  
HETATM 8652  O7  NAG R   2     180.583 205.949 108.005  1.00 97.54           O  
HETATM 8653  C1  NAG C1401     171.385 205.154 270.844  1.00 65.22           C  
HETATM 8654  C2  NAG C1401     170.287 206.198 270.613  1.00 67.08           C  
HETATM 8655  C3  NAG C1401     169.621 206.538 271.945  1.00 66.11           C  
HETATM 8656  C4  NAG C1401     169.112 205.271 272.622  1.00 66.13           C  
HETATM 8657  C5  NAG C1401     170.244 204.253 272.755  1.00 64.14           C  
HETATM 8658  C6  NAG C1401     169.794 202.928 273.329  1.00 64.42           C  
HETATM 8659  C7  NAG C1401     170.089 208.225 269.233  1.00 66.43           C  
HETATM 8660  C8  NAG C1401     170.809 209.420 268.685  1.00 60.17           C  
HETATM 8661  N2  NAG C1401     170.820 207.399 269.989  1.00 60.79           N  
HETATM 8662  O3  NAG C1401     168.557 207.464 271.751  1.00 70.09           O  
HETATM 8663  O4  NAG C1401     168.604 205.583 273.914  1.00 71.26           O  
HETATM 8664  O5  NAG C1401     170.814 203.981 271.465  1.00 67.59           O  
HETATM 8665  O6  NAG C1401     170.598 201.858 272.853  1.00 66.98           O  
HETATM 8666  O7  NAG C1401     168.903 208.016 269.004  1.00 72.48           O  
HETATM 8667  C1  NAG C1402     181.032 181.732 274.021  1.00 71.48           C  
HETATM 8668  C2  NAG C1402     180.368 180.376 274.250  1.00 73.44           C  
HETATM 8669  C3  NAG C1402     179.948 180.245 275.709  1.00 75.66           C  
HETATM 8670  C4  NAG C1402     181.153 180.462 276.612  1.00 79.50           C  
HETATM 8671  C5  NAG C1402     181.780 181.819 276.311  1.00 73.62           C  
HETATM 8672  C6  NAG C1402     183.037 182.092 277.108  1.00 78.04           C  
HETATM 8673  C7  NAG C1402     179.021 179.055 272.686  1.00 82.44           C  
HETATM 8674  C8  NAG C1402     177.806 179.026 271.804  1.00 80.64           C  
HETATM 8675  N2  NAG C1402     179.229 180.187 273.365  1.00 76.92           N  
HETATM 8676  O3  NAG C1402     179.369 178.969 275.953  1.00 71.42           O  
HETATM 8677  O4  NAG C1402     180.778 180.391 277.983  1.00 73.24           O  
HETATM 8678  O5  NAG C1402     182.147 181.884 274.926  1.00 70.90           O  
HETATM 8679  O6  NAG C1402     183.650 180.890 277.556  1.00 76.57           O  
HETATM 8680  O7  NAG C1402     179.775 178.094 272.789  1.00 86.20           O  
HETATM 8681  C1  MAN C1409     171.183 200.757 294.477  1.00102.27           C  
HETATM 8682  C2  MAN C1409     170.867 201.629 293.245  1.00103.70           C  
HETATM 8683  C3  MAN C1409     171.842 202.810 293.129  1.00103.12           C  
HETATM 8684  C4  MAN C1409     172.012 203.504 294.474  1.00104.88           C  
HETATM 8685  C5  MAN C1409     172.497 202.506 295.505  1.00104.25           C  
HETATM 8686  C6  MAN C1409     172.607 203.131 296.866  1.00 99.32           C  
HETATM 8687  O2  MAN C1409     169.572 202.208 293.349  1.00105.83           O  
HETATM 8688  O3  MAN C1409     171.408 203.762 292.165  1.00 99.32           O  
HETATM 8689  O4  MAN C1409     172.962 204.539 294.365  1.00100.45           O  
HETATM 8690  O5  MAN C1409     171.504 201.480 295.634  1.00105.10           O  
HETATM 8691  O6  MAN C1409     171.273 203.410 297.303  1.00 99.32           O  
HETATM 8692  C1  NAG C1417     181.820 202.152 151.285  1.00103.47           C  
HETATM 8693  C2  NAG C1417     181.623 202.346 149.785  1.00101.60           C  
HETATM 8694  C3  NAG C1417     180.159 202.144 149.425  1.00102.43           C  
HETATM 8695  C4  NAG C1417     179.672 200.787 149.922  1.00107.92           C  
HETATM 8696  C5  NAG C1417     179.954 200.633 151.416  1.00105.26           C  
HETATM 8697  C6  NAG C1417     179.626 199.252 151.943  1.00 98.90           C  
HETATM 8698  C7  NAG C1417     183.035 203.832 148.440  1.00106.34           C  
HETATM 8699  C8  NAG C1417     183.374 205.254 148.102  1.00107.15           C  
HETATM 8700  N2  NAG C1417     182.077 203.659 149.358  1.00105.82           N  
HETATM 8701  O3  NAG C1417     179.998 202.244 148.014  1.00108.43           O  
HETATM 8702  O4  NAG C1417     178.274 200.656 149.686  1.00107.86           O  
HETATM 8703  O5  NAG C1417     181.353 200.848 151.669  1.00104.08           O  
HETATM 8704  O6  NAG C1417     180.390 198.936 153.100  1.00 94.30           O  
HETATM 8705  O7  NAG C1417     183.601 202.884 147.906  1.00105.31           O  
HETATM 8706  C1  NAG A1401     205.148 171.439 270.876  1.00 65.48           C  
HETATM 8707  C2  NAG A1401     204.794 169.966 270.646  1.00 66.35           C  
HETATM 8708  C3  NAG A1401     204.833 169.221 271.979  1.00 67.42           C  
HETATM 8709  C4  NAG A1401     206.185 169.415 272.656  1.00 66.27           C  
HETATM 8710  C5  NAG A1401     206.499 170.905 272.787  1.00 63.64           C  
HETATM 8711  C6  NAG A1401     207.872 171.179 273.361  1.00 64.65           C  
HETATM 8712  C7  NAG A1401     203.139 168.778 269.268  1.00 67.20           C  
HETATM 8713  C8  NAG A1401     201.744 168.803 268.719  1.00 64.08           C  
HETATM 8714  N2  NAG A1401     203.488 169.825 270.022  1.00 61.33           N  
HETATM 8715  O3  NAG A1401     204.564 167.836 271.787  1.00 68.69           O  
HETATM 8716  O4  NAG A1401     206.169 168.821 273.949  1.00 71.14           O  
HETATM 8717  O5  NAG A1401     206.450 171.533 271.497  1.00 69.55           O  
HETATM 8718  O6  NAG A1401     208.396 172.410 272.884  1.00 67.98           O  
HETATM 8719  O7  NAG A1401     203.914 167.856 269.040  1.00 73.32           O  
HETATM 8720  C1  NAG A1402     220.595 191.519 274.031  1.00 71.20           C  
HETATM 8721  C2  NAG A1402     222.101 191.624 274.260  1.00 73.68           C  
HETATM 8722  C3  NAG A1402     222.425 191.327 275.719  1.00 73.93           C  
HETATM 8723  C4  NAG A1402     221.633 192.263 276.621  1.00 80.61           C  
HETATM 8724  C5  NAG A1402     220.145 192.126 276.320  1.00 74.69           C  
HETATM 8725  C6  NAG A1402     219.279 193.078 277.116  1.00 79.09           C  
HETATM 8726  C7  NAG A1402     223.919 191.117 272.697  1.00 82.28           C  
HETATM 8727  C8  NAG A1402     224.552 190.079 271.816  1.00 81.51           C  
HETATM 8728  N2  NAG A1402     222.835 190.731 273.376  1.00 77.01           N  
HETATM 8729  O3  NAG A1402     223.819 191.465 275.963  1.00 73.33           O  
HETATM 8730  O4  NAG A1402     221.883 191.975 277.992  1.00 78.22           O  
HETATM 8731  O5  NAG A1402     219.905 192.409 274.935  1.00 71.09           O  
HETATM 8732  O6  NAG A1402     220.013 194.211 277.563  1.00 83.15           O  
HETATM 8733  O7  NAG A1402     224.374 192.251 272.798  1.00 82.29           O  
HETATM 8734  C1  MAN A1409     209.054 173.493 294.507  1.00103.79           C  
HETATM 8735  C2  MAN A1409     208.457 172.781 293.275  1.00103.53           C  
HETATM 8736  C3  MAN A1409     206.947 173.034 293.159  1.00100.91           C  
HETATM 8737  C4  MAN A1409     206.261 172.835 294.504  1.00104.90           C  
HETATM 8738  C5  MAN A1409     206.882 173.756 295.534  1.00103.25           C  
HETATM 8739  C6  MAN A1409     206.286 173.540 296.895  1.00 99.32           C  
HETATM 8740  O2  MAN A1409     208.605 171.371 293.381  1.00106.64           O  
HETATM 8741  O3  MAN A1409     206.340 172.181 292.196  1.00 99.32           O  
HETATM 8742  O4  MAN A1409     204.890 173.140 294.395  1.00100.89           O  
HETATM 8743  O5  MAN A1409     208.267 173.410 295.664  1.00105.36           O  
HETATM 8744  O6  MAN A1409     206.712 172.246 297.334  1.00 99.32           O  
HETATM 8745  C1  NAG A1417     202.612 181.825 151.228  1.00103.08           C  
HETATM 8746  C2  NAG A1417     202.543 181.556 149.728  1.00103.16           C  
HETATM 8747  C3  NAG A1417     203.451 180.389 149.370  1.00102.74           C  
HETATM 8748  C4  NAG A1417     204.869 180.647 149.867  1.00108.06           C  
HETATM 8749  C5  NAG A1417     204.861 180.970 151.360  1.00105.61           C  
HETATM 8750  C6  NAG A1417     206.221 181.378 151.887  1.00 98.95           C  
HETATM 8751  C7  NAG A1417     200.550 182.032 148.383  1.00105.99           C  
HETATM 8752  C8  NAG A1417     199.149 181.614 148.045  1.00105.92           C  
HETATM 8753  N2  NAG A1417     201.179 181.291 149.302  1.00105.46           N  
HETATM 8754  O3  NAG A1417     203.445 180.198 147.959  1.00107.81           O  
HETATM 8755  O4  NAG A1417     205.682 179.502 149.632  1.00107.84           O  
HETATM 8756  O5  NAG A1417     203.975 182.074 151.612  1.00103.86           O  
HETATM 8757  O6  NAG A1417     206.112 182.199 153.043  1.00 95.26           O  
HETATM 8758  O7  NAG A1417     201.087 182.996 147.848  1.00105.74           O  
HETATM 8759  C1  NAG B1401     217.456 217.548 270.858  1.00 67.21           C  
HETATM 8760  C2  NAG B1401     218.909 217.978 270.629  1.00 67.83           C  
HETATM 8761  C3  NAG B1401     219.535 218.386 271.961  1.00 69.25           C  
HETATM 8762  C4  NAG B1401     218.691 219.460 272.636  1.00 71.33           C  
HETATM 8763  C5  NAG B1401     217.243 218.988 272.768  1.00 69.13           C  
HETATM 8764  C6  NAG B1401     216.320 220.040 273.340  1.00 68.51           C  
HETATM 8765  C7  NAG B1401     220.765 217.136 269.251  1.00 66.34           C  
HETATM 8766  C8  NAG B1401     221.441 215.914 268.705  1.00 65.87           C  
HETATM 8767  N2  NAG B1401     219.684 216.916 270.006  1.00 62.94           N  
HETATM 8768  O3  NAG B1401     220.869 218.844 271.768  1.00 72.46           O  
HETATM 8769  O4  NAG B1401     219.213 219.745 273.929  1.00 79.63           O  
HETATM 8770  O5  NAG B1401     216.724 218.630 271.478  1.00 70.79           O  
HETATM 8771  O6  NAG B1401     214.991 219.878 272.863  1.00 70.94           O  
HETATM 8772  O7  NAG B1401     221.177 218.267 269.022  1.00 72.02           O  
HETATM 8773  C1  NAG B1402     192.343 220.897 274.004  1.00 72.58           C  
HETATM 8774  C2  NAG B1402     191.500 222.150 274.231  1.00 73.92           C  
HETATM 8775  C3  NAG B1402     191.595 222.580 275.690  1.00 76.11           C  
HETATM 8776  C4  NAG B1402     191.180 221.429 276.593  1.00 80.83           C  
HETATM 8777  C5  NAG B1402     192.042 220.207 276.294  1.00 75.03           C  
HETATM 8778  C6  NAG B1402     191.650 218.983 277.091  1.00 77.29           C  
HETATM 8779  C7  NAG B1402     191.031 223.976 272.665  1.00 82.35           C  
HETATM 8780  C8  NAG B1402     191.614 225.042 271.783  1.00 73.89           C  
HETATM 8781  N2  NAG B1402     191.906 223.231 273.346  1.00 76.34           N  
HETATM 8782  O3  NAG B1402     190.778 223.720 275.932  1.00 73.39           O  
HETATM 8783  O4  NAG B1402     191.304 221.790 277.964  1.00 78.79           O  
HETATM 8784  O5  NAG B1402     191.917 219.856 274.909  1.00 71.84           O  
HETATM 8785  O6  NAG B1402     190.302 219.053 277.538  1.00 77.00           O  
HETATM 8786  O7  NAG B1402     189.821 223.803 272.767  1.00 84.84           O  
HETATM 8787  C1  MAN B1409     213.720 219.936 294.485  1.00102.56           C  
HETATM 8788  C2  MAN B1409     214.635 219.773 293.255  1.00100.61           C  
HETATM 8789  C3  MAN B1409     215.171 218.338 293.140  1.00103.00           C  
HETATM 8790  C4  MAN B1409     215.686 217.845 294.486  1.00104.20           C  
HETATM 8791  C5  MAN B1409     214.578 217.924 295.516  1.00104.36           C  
HETATM 8792  C6  MAN B1409     215.062 217.517 296.878  1.00 99.82           C  
HETATM 8793  O2  MAN B1409     215.783 220.605 293.359  1.00104.88           O  
HETATM 8794  O3  MAN B1409     216.214 218.238 292.177  1.00 99.32           O  
HETATM 8795  O4  MAN B1409     216.108 216.505 294.378  1.00100.07           O  
HETATM 8796  O5  MAN B1409     214.185 219.297 295.643  1.00105.32           O  
HETATM 8797  O6  MAN B1409     215.970 218.534 297.315  1.00 99.32           O  
HETATM 8798  C1  NAG B1417     209.762 209.981 151.236  1.00102.88           C  
HETATM 8799  C2  NAG B1417     210.030 210.053 149.736  1.00103.02           C  
HETATM 8800  C3  NAG B1417     210.587 211.422 149.376  1.00101.67           C  
HETATM 8801  C4  NAG B1417     209.654 212.522 149.871  1.00106.59           C  
HETATM 8802  C5  NAG B1417     209.378 212.356 151.365  1.00106.59           C  
HETATM 8803  C6  NAG B1417     208.345 213.330 151.890  1.00101.81           C  
HETATM 8804  C7  NAG B1417     210.613 208.087 148.393  1.00105.83           C  
HETATM 8805  C8  NAG B1417     211.676 207.082 148.057  1.00105.60           C  
HETATM 8806  N2  NAG B1417     210.941 209.004 149.311  1.00105.23           N  
HETATM 8807  O3  NAG B1417     210.756 211.511 147.965  1.00108.21           O  
HETATM 8808  O4  NAG B1417     210.240 213.799 149.635  1.00106.31           O  
HETATM 8809  O5  NAG B1417     208.865 211.037 151.618  1.00104.47           O  
HETATM 8810  O6  NAG B1417     207.689 212.827 153.047  1.00 99.55           O  
HETATM 8811  O7  NAG B1417     209.510 208.070 147.858  1.00105.35           O  
CONECT   52 8653                                                                
CONECT  109 8667                                                                
CONECT  265  432                                                                
CONECT  306  346                                                                
CONECT  346  306                                                                
CONECT  432  265                                                                
CONECT 1427 1513                                                                
CONECT 1513 1427                                                                
CONECT 1756 8068                                                                
CONECT 1812 2170                                                                
CONECT 2170 1812                                                                
CONECT 2227 8146                                                                
CONECT 2434 8196                                                                
CONECT 2665 8235                                                                
CONECT 2741 8706                                                                
CONECT 2798 8720                                                                
CONECT 2954 3121                                                                
CONECT 2995 3035                                                                
CONECT 3035 2995                                                                
CONECT 3121 2954                                                                
CONECT 4116 4202                                                                
CONECT 4202 4116                                                                
CONECT 4445 8263                                                                
CONECT 4501 4859                                                                
CONECT 4859 4501                                                                
CONECT 4916 8341                                                                
CONECT 5123 8391                                                                
CONECT 5354 8430                                                                
CONECT 5430 8759                                                                
CONECT 5487 8773                                                                
CONECT 5643 5810                                                                
CONECT 5684 5724                                                                
CONECT 5724 5684                                                                
CONECT 5810 5643                                                                
CONECT 6805 6891                                                                
CONECT 6891 6805                                                                
CONECT 7134 8458                                                                
CONECT 7190 7548                                                                
CONECT 7548 7190                                                                
CONECT 7605 8536                                                                
CONECT 7812 8586                                                                
CONECT 8043 8625                                                                
CONECT 8068 1756 8069 8079                                                      
CONECT 8069 8068 8070 8076                                                      
CONECT 8070 8069 8071 8077                                                      
CONECT 8071 8070 8072 8078                                                      
CONECT 8072 8071 8073 8079                                                      
CONECT 8073 8072 8080                                                           
CONECT 8074 8075 8076 8081                                                      
CONECT 8075 8074                                                                
CONECT 8076 8069 8074                                                           
CONECT 8077 8070                                                                
CONECT 8078 8071 8082                                                           
CONECT 8079 8068 8072                                                           
CONECT 8080 8073                                                                
CONECT 8081 8074                                                                
CONECT 8082 8078 8083 8093                                                      
CONECT 8083 8082 8084 8090                                                      
CONECT 8084 8083 8085 8091                                                      
CONECT 8085 8084 8086 8092                                                      
CONECT 8086 8085 8087 8093                                                      
CONECT 8087 8086 8094                                                           
CONECT 8088 8089 8090 8095                                                      
CONECT 8089 8088                                                                
CONECT 8090 8083 8088                                                           
CONECT 8091 8084                                                                
CONECT 8092 8085                                                                
CONECT 8093 8082 8086                                                           
CONECT 8094 8087                                                                
CONECT 8095 8088                                                                
CONECT 8096 8097 8107                                                           
CONECT 8097 8096 8098 8104                                                      
CONECT 8098 8097 8099 8105                                                      
CONECT 8099 8098 8100 8106                                                      
CONECT 8100 8099 8101 8107                                                      
CONECT 8101 8100 8108                                                           
CONECT 8102 8103 8104 8109                                                      
CONECT 8103 8102                                                                
CONECT 8104 8097 8102                                                           
CONECT 8105 8098                                                                
CONECT 8106 8099 8110                                                           
CONECT 8107 8096 8100                                                           
CONECT 8108 8101                                                                
CONECT 8109 8102                                                                
CONECT 8110 8106 8111 8121                                                      
CONECT 8111 8110 8112 8118                                                      
CONECT 8112 8111 8113 8119                                                      
CONECT 8113 8112 8114 8120                                                      
CONECT 8114 8113 8115 8121                                                      
CONECT 8115 8114 8122                                                           
CONECT 8116 8117 8118 8123                                                      
CONECT 8117 8116                                                                
CONECT 8118 8111 8116                                                           
CONECT 8119 8112                                                                
CONECT 8120 8113 8124                                                           
CONECT 8121 8110 8114                                                           
CONECT 8122 8115                                                                
CONECT 8123 8116                                                                
CONECT 8124 8120 8125 8133                                                      
CONECT 8125 8124 8126 8130                                                      
CONECT 8126 8125 8127 8131                                                      
CONECT 8127 8126 8128 8132                                                      
CONECT 8128 8127 8129 8133                                                      
CONECT 8129 8128 8134                                                           
CONECT 8130 8125                                                                
CONECT 8131 8126 8135                                                           
CONECT 8132 8127                                                                
CONECT 8133 8124 8128                                                           
CONECT 8134 8129                                                                
CONECT 8135 8131 8136 8144                                                      
CONECT 8136 8135 8137 8141                                                      
CONECT 8137 8136 8138 8142                                                      
CONECT 8138 8137 8139 8143                                                      
CONECT 8139 8138 8140 8144                                                      
CONECT 8140 8139 8145                                                           
CONECT 8141 8136                                                                
CONECT 8142 8137                                                                
CONECT 8143 8138                                                                
CONECT 8144 8135 8139                                                           
CONECT 8145 8140                                                                
CONECT 8146 2227 8147 8157                                                      
CONECT 8147 8146 8148 8154                                                      
CONECT 8148 8147 8149 8155                                                      
CONECT 8149 8148 8150 8156                                                      
CONECT 8150 8149 8151 8157                                                      
CONECT 8151 8150 8158                                                           
CONECT 8152 8153 8154 8159                                                      
CONECT 8153 8152                                                                
CONECT 8154 8147 8152                                                           
CONECT 8155 8148                                                                
CONECT 8156 8149 8160                                                           
CONECT 8157 8146 8150                                                           
CONECT 8158 8151                                                                
CONECT 8159 8152                                                                
CONECT 8160 8156 8161 8171                                                      
CONECT 8161 8160 8162 8168                                                      
CONECT 8162 8161 8163 8169                                                      
CONECT 8163 8162 8164 8170                                                      
CONECT 8164 8163 8165 8171                                                      
CONECT 8165 8164 8172                                                           
CONECT 8166 8167 8168 8173                                                      
CONECT 8167 8166                                                                
CONECT 8168 8161 8166                                                           
CONECT 8169 8162                                                                
CONECT 8170 8163 8174                                                           
CONECT 8171 8160 8164                                                           
CONECT 8172 8165                                                                
CONECT 8173 8166                                                                
CONECT 8174 8170 8175 8183                                                      
CONECT 8175 8174 8176 8180                                                      
CONECT 8176 8175 8177 8181                                                      
CONECT 8177 8176 8178 8182                                                      
CONECT 8178 8177 8179 8183                                                      
CONECT 8179 8178 8184                                                           
CONECT 8180 8175                                                                
CONECT 8181 8176 8185                                                           
CONECT 8182 8177                                                                
CONECT 8183 8174 8178                                                           
CONECT 8184 8179                                                                
CONECT 8185 8181 8186 8194                                                      
CONECT 8186 8185 8187 8191                                                      
CONECT 8187 8186 8188 8192                                                      
CONECT 8188 8187 8189 8193                                                      
CONECT 8189 8188 8190 8194                                                      
CONECT 8190 8189 8195                                                           
CONECT 8191 8186                                                                
CONECT 8192 8187                                                                
CONECT 8193 8188                                                                
CONECT 8194 8185 8189                                                           
CONECT 8195 8190                                                                
CONECT 8196 2434 8197 8207                                                      
CONECT 8197 8196 8198 8204                                                      
CONECT 8198 8197 8199 8205                                                      
CONECT 8199 8198 8200 8206                                                      
CONECT 8200 8199 8201 8207                                                      
CONECT 8201 8200 8208                                                           
CONECT 8202 8203 8204 8209                                                      
CONECT 8203 8202                                                                
CONECT 8204 8197 8202                                                           
CONECT 8205 8198                                                                
CONECT 8206 8199 8210                                                           
CONECT 8207 8196 8200                                                           
CONECT 8208 8201                                                                
CONECT 8209 8202                                                                
CONECT 8210 8206 8211 8221                                                      
CONECT 8211 8210 8212 8218                                                      
CONECT 8212 8211 8213 8219                                                      
CONECT 8213 8212 8214 8220                                                      
CONECT 8214 8213 8215 8221                                                      
CONECT 8215 8214 8222                                                           
CONECT 8216 8217 8218 8223                                                      
CONECT 8217 8216                                                                
CONECT 8218 8211 8216                                                           
CONECT 8219 8212                                                                
CONECT 8220 8213 8224                                                           
CONECT 8221 8210 8214                                                           
CONECT 8222 8215                                                                
CONECT 8223 8216                                                                
CONECT 8224 8220 8225 8233                                                      
CONECT 8225 8224 8226 8230                                                      
CONECT 8226 8225 8227 8231                                                      
CONECT 8227 8226 8228 8232                                                      
CONECT 8228 8227 8229 8233                                                      
CONECT 8229 8228 8234                                                           
CONECT 8230 8225                                                                
CONECT 8231 8226                                                                
CONECT 8232 8227                                                                
CONECT 8233 8224 8228                                                           
CONECT 8234 8229                                                                
CONECT 8235 2665 8236 8246                                                      
CONECT 8236 8235 8237 8243                                                      
CONECT 8237 8236 8238 8244                                                      
CONECT 8238 8237 8239 8245                                                      
CONECT 8239 8238 8240 8246                                                      
CONECT 8240 8239 8247                                                           
CONECT 8241 8242 8243 8248                                                      
CONECT 8242 8241                                                                
CONECT 8243 8236 8241                                                           
CONECT 8244 8237                                                                
CONECT 8245 8238 8249                                                           
CONECT 8246 8235 8239                                                           
CONECT 8247 8240                                                                
CONECT 8248 8241                                                                
CONECT 8249 8245 8250 8260                                                      
CONECT 8250 8249 8251 8257                                                      
CONECT 8251 8250 8252 8258                                                      
CONECT 8252 8251 8253 8259                                                      
CONECT 8253 8252 8254 8260                                                      
CONECT 8254 8253 8261                                                           
CONECT 8255 8256 8257 8262                                                      
CONECT 8256 8255                                                                
CONECT 8257 8250 8255                                                           
CONECT 8258 8251                                                                
CONECT 8259 8252                                                                
CONECT 8260 8249 8253                                                           
CONECT 8261 8254                                                                
CONECT 8262 8255                                                                
CONECT 8263 4445 8264 8274                                                      
CONECT 8264 8263 8265 8271                                                      
CONECT 8265 8264 8266 8272                                                      
CONECT 8266 8265 8267 8273                                                      
CONECT 8267 8266 8268 8274                                                      
CONECT 8268 8267 8275                                                           
CONECT 8269 8270 8271 8276                                                      
CONECT 8270 8269                                                                
CONECT 8271 8264 8269                                                           
CONECT 8272 8265                                                                
CONECT 8273 8266 8277                                                           
CONECT 8274 8263 8267                                                           
CONECT 8275 8268                                                                
CONECT 8276 8269                                                                
CONECT 8277 8273 8278 8288                                                      
CONECT 8278 8277 8279 8285                                                      
CONECT 8279 8278 8280 8286                                                      
CONECT 8280 8279 8281 8287                                                      
CONECT 8281 8280 8282 8288                                                      
CONECT 8282 8281 8289                                                           
CONECT 8283 8284 8285 8290                                                      
CONECT 8284 8283                                                                
CONECT 8285 8278 8283                                                           
CONECT 8286 8279                                                                
CONECT 8287 8280                                                                
CONECT 8288 8277 8281                                                           
CONECT 8289 8282                                                                
CONECT 8290 8283                                                                
CONECT 8291 8292 8302                                                           
CONECT 8292 8291 8293 8299                                                      
CONECT 8293 8292 8294 8300                                                      
CONECT 8294 8293 8295 8301                                                      
CONECT 8295 8294 8296 8302                                                      
CONECT 8296 8295 8303                                                           
CONECT 8297 8298 8299 8304                                                      
CONECT 8298 8297                                                                
CONECT 8299 8292 8297                                                           
CONECT 8300 8293                                                                
CONECT 8301 8294 8305                                                           
CONECT 8302 8291 8295                                                           
CONECT 8303 8296                                                                
CONECT 8304 8297                                                                
CONECT 8305 8301 8306 8316                                                      
CONECT 8306 8305 8307 8313                                                      
CONECT 8307 8306 8308 8314                                                      
CONECT 8308 8307 8309 8315                                                      
CONECT 8309 8308 8310 8316                                                      
CONECT 8310 8309 8317                                                           
CONECT 8311 8312 8313 8318                                                      
CONECT 8312 8311                                                                
CONECT 8313 8306 8311                                                           
CONECT 8314 8307                                                                
CONECT 8315 8308 8319                                                           
CONECT 8316 8305 8309                                                           
CONECT 8317 8310                                                                
CONECT 8318 8311                                                                
CONECT 8319 8315 8320 8328                                                      
CONECT 8320 8319 8321 8325                                                      
CONECT 8321 8320 8322 8326                                                      
CONECT 8322 8321 8323 8327                                                      
CONECT 8323 8322 8324 8328                                                      
CONECT 8324 8323 8329                                                           
CONECT 8325 8320                                                                
CONECT 8326 8321 8330                                                           
CONECT 8327 8322                                                                
CONECT 8328 8319 8323                                                           
CONECT 8329 8324                                                                
CONECT 8330 8326 8331 8339                                                      
CONECT 8331 8330 8332 8336                                                      
CONECT 8332 8331 8333 8337                                                      
CONECT 8333 8332 8334 8338                                                      
CONECT 8334 8333 8335 8339                                                      
CONECT 8335 8334 8340                                                           
CONECT 8336 8331                                                                
CONECT 8337 8332                                                                
CONECT 8338 8333                                                                
CONECT 8339 8330 8334                                                           
CONECT 8340 8335                                                                
CONECT 8341 4916 8342 8352                                                      
CONECT 8342 8341 8343 8349                                                      
CONECT 8343 8342 8344 8350                                                      
CONECT 8344 8343 8345 8351                                                      
CONECT 8345 8344 8346 8352                                                      
CONECT 8346 8345 8353                                                           
CONECT 8347 8348 8349 8354                                                      
CONECT 8348 8347                                                                
CONECT 8349 8342 8347                                                           
CONECT 8350 8343                                                                
CONECT 8351 8344 8355                                                           
CONECT 8352 8341 8345                                                           
CONECT 8353 8346                                                                
CONECT 8354 8347                                                                
CONECT 8355 8351 8356 8366                                                      
CONECT 8356 8355 8357 8363                                                      
CONECT 8357 8356 8358 8364                                                      
CONECT 8358 8357 8359 8365                                                      
CONECT 8359 8358 8360 8366                                                      
CONECT 8360 8359 8367                                                           
CONECT 8361 8362 8363 8368                                                      
CONECT 8362 8361                                                                
CONECT 8363 8356 8361                                                           
CONECT 8364 8357                                                                
CONECT 8365 8358 8369                                                           
CONECT 8366 8355 8359                                                           
CONECT 8367 8360                                                                
CONECT 8368 8361                                                                
CONECT 8369 8365 8370 8378                                                      
CONECT 8370 8369 8371 8375                                                      
CONECT 8371 8370 8372 8376                                                      
CONECT 8372 8371 8373 8377                                                      
CONECT 8373 8372 8374 8378                                                      
CONECT 8374 8373 8379                                                           
CONECT 8375 8370                                                                
CONECT 8376 8371 8380                                                           
CONECT 8377 8372                                                                
CONECT 8378 8369 8373                                                           
CONECT 8379 8374                                                                
CONECT 8380 8376 8381 8389                                                      
CONECT 8381 8380 8382 8386                                                      
CONECT 8382 8381 8383 8387                                                      
CONECT 8383 8382 8384 8388                                                      
CONECT 8384 8383 8385 8389                                                      
CONECT 8385 8384 8390                                                           
CONECT 8386 8381                                                                
CONECT 8387 8382                                                                
CONECT 8388 8383                                                                
CONECT 8389 8380 8384                                                           
CONECT 8390 8385                                                                
CONECT 8391 5123 8392 8402                                                      
CONECT 8392 8391 8393 8399                                                      
CONECT 8393 8392 8394 8400                                                      
CONECT 8394 8393 8395 8401                                                      
CONECT 8395 8394 8396 8402                                                      
CONECT 8396 8395 8403                                                           
CONECT 8397 8398 8399 8404                                                      
CONECT 8398 8397                                                                
CONECT 8399 8392 8397                                                           
CONECT 8400 8393                                                                
CONECT 8401 8394 8405                                                           
CONECT 8402 8391 8395                                                           
CONECT 8403 8396                                                                
CONECT 8404 8397                                                                
CONECT 8405 8401 8406 8416                                                      
CONECT 8406 8405 8407 8413                                                      
CONECT 8407 8406 8408 8414                                                      
CONECT 8408 8407 8409 8415                                                      
CONECT 8409 8408 8410 8416                                                      
CONECT 8410 8409 8417                                                           
CONECT 8411 8412 8413 8418                                                      
CONECT 8412 8411                                                                
CONECT 8413 8406 8411                                                           
CONECT 8414 8407                                                                
CONECT 8415 8408 8419                                                           
CONECT 8416 8405 8409                                                           
CONECT 8417 8410                                                                
CONECT 8418 8411                                                                
CONECT 8419 8415 8420 8428                                                      
CONECT 8420 8419 8421 8425                                                      
CONECT 8421 8420 8422 8426                                                      
CONECT 8422 8421 8423 8427                                                      
CONECT 8423 8422 8424 8428                                                      
CONECT 8424 8423 8429                                                           
CONECT 8425 8420                                                                
CONECT 8426 8421                                                                
CONECT 8427 8422                                                                
CONECT 8428 8419 8423                                                           
CONECT 8429 8424                                                                
CONECT 8430 5354 8431 8441                                                      
CONECT 8431 8430 8432 8438                                                      
CONECT 8432 8431 8433 8439                                                      
CONECT 8433 8432 8434 8440                                                      
CONECT 8434 8433 8435 8441                                                      
CONECT 8435 8434 8442                                                           
CONECT 8436 8437 8438 8443                                                      
CONECT 8437 8436                                                                
CONECT 8438 8431 8436                                                           
CONECT 8439 8432                                                                
CONECT 8440 8433 8444                                                           
CONECT 8441 8430 8434                                                           
CONECT 8442 8435                                                                
CONECT 8443 8436                                                                
CONECT 8444 8440 8445 8455                                                      
CONECT 8445 8444 8446 8452                                                      
CONECT 8446 8445 8447 8453                                                      
CONECT 8447 8446 8448 8454                                                      
CONECT 8448 8447 8449 8455                                                      
CONECT 8449 8448 8456                                                           
CONECT 8450 8451 8452 8457                                                      
CONECT 8451 8450                                                                
CONECT 8452 8445 8450                                                           
CONECT 8453 8446                                                                
CONECT 8454 8447                                                                
CONECT 8455 8444 8448                                                           
CONECT 8456 8449                                                                
CONECT 8457 8450                                                                
CONECT 8458 7134 8459 8469                                                      
CONECT 8459 8458 8460 8466                                                      
CONECT 8460 8459 8461 8467                                                      
CONECT 8461 8460 8462 8468                                                      
CONECT 8462 8461 8463 8469                                                      
CONECT 8463 8462 8470                                                           
CONECT 8464 8465 8466 8471                                                      
CONECT 8465 8464                                                                
CONECT 8466 8459 8464                                                           
CONECT 8467 8460                                                                
CONECT 8468 8461 8472                                                           
CONECT 8469 8458 8462                                                           
CONECT 8470 8463                                                                
CONECT 8471 8464                                                                
CONECT 8472 8468 8473 8483                                                      
CONECT 8473 8472 8474 8480                                                      
CONECT 8474 8473 8475 8481                                                      
CONECT 8475 8474 8476 8482                                                      
CONECT 8476 8475 8477 8483                                                      
CONECT 8477 8476 8484                                                           
CONECT 8478 8479 8480 8485                                                      
CONECT 8479 8478                                                                
CONECT 8480 8473 8478                                                           
CONECT 8481 8474                                                                
CONECT 8482 8475                                                                
CONECT 8483 8472 8476                                                           
CONECT 8484 8477                                                                
CONECT 8485 8478                                                                
CONECT 8486 8487 8497                                                           
CONECT 8487 8486 8488 8494                                                      
CONECT 8488 8487 8489 8495                                                      
CONECT 8489 8488 8490 8496                                                      
CONECT 8490 8489 8491 8497                                                      
CONECT 8491 8490 8498                                                           
CONECT 8492 8493 8494 8499                                                      
CONECT 8493 8492                                                                
CONECT 8494 8487 8492                                                           
CONECT 8495 8488                                                                
CONECT 8496 8489 8500                                                           
CONECT 8497 8486 8490                                                           
CONECT 8498 8491                                                                
CONECT 8499 8492                                                                
CONECT 8500 8496 8501 8511                                                      
CONECT 8501 8500 8502 8508                                                      
CONECT 8502 8501 8503 8509                                                      
CONECT 8503 8502 8504 8510                                                      
CONECT 8504 8503 8505 8511                                                      
CONECT 8505 8504 8512                                                           
CONECT 8506 8507 8508 8513                                                      
CONECT 8507 8506                                                                
CONECT 8508 8501 8506                                                           
CONECT 8509 8502                                                                
CONECT 8510 8503 8514                                                           
CONECT 8511 8500 8504                                                           
CONECT 8512 8505                                                                
CONECT 8513 8506                                                                
CONECT 8514 8510 8515 8523                                                      
CONECT 8515 8514 8516 8520                                                      
CONECT 8516 8515 8517 8521                                                      
CONECT 8517 8516 8518 8522                                                      
CONECT 8518 8517 8519 8523                                                      
CONECT 8519 8518 8524                                                           
CONECT 8520 8515                                                                
CONECT 8521 8516 8525                                                           
CONECT 8522 8517                                                                
CONECT 8523 8514 8518                                                           
CONECT 8524 8519                                                                
CONECT 8525 8521 8526 8534                                                      
CONECT 8526 8525 8527 8531                                                      
CONECT 8527 8526 8528 8532                                                      
CONECT 8528 8527 8529 8533                                                      
CONECT 8529 8528 8530 8534                                                      
CONECT 8530 8529 8535                                                           
CONECT 8531 8526                                                                
CONECT 8532 8527                                                                
CONECT 8533 8528                                                                
CONECT 8534 8525 8529                                                           
CONECT 8535 8530                                                                
CONECT 8536 7605 8537 8547                                                      
CONECT 8537 8536 8538 8544                                                      
CONECT 8538 8537 8539 8545                                                      
CONECT 8539 8538 8540 8546                                                      
CONECT 8540 8539 8541 8547                                                      
CONECT 8541 8540 8548                                                           
CONECT 8542 8543 8544 8549                                                      
CONECT 8543 8542                                                                
CONECT 8544 8537 8542                                                           
CONECT 8545 8538                                                                
CONECT 8546 8539 8550                                                           
CONECT 8547 8536 8540                                                           
CONECT 8548 8541                                                                
CONECT 8549 8542                                                                
CONECT 8550 8546 8551 8561                                                      
CONECT 8551 8550 8552 8558                                                      
CONECT 8552 8551 8553 8559                                                      
CONECT 8553 8552 8554 8560                                                      
CONECT 8554 8553 8555 8561                                                      
CONECT 8555 8554 8562                                                           
CONECT 8556 8557 8558 8563                                                      
CONECT 8557 8556                                                                
CONECT 8558 8551 8556                                                           
CONECT 8559 8552                                                                
CONECT 8560 8553 8564                                                           
CONECT 8561 8550 8554                                                           
CONECT 8562 8555                                                                
CONECT 8563 8556                                                                
CONECT 8564 8560 8565 8573                                                      
CONECT 8565 8564 8566 8570                                                      
CONECT 8566 8565 8567 8571                                                      
CONECT 8567 8566 8568 8572                                                      
CONECT 8568 8567 8569 8573                                                      
CONECT 8569 8568 8574                                                           
CONECT 8570 8565                                                                
CONECT 8571 8566 8575                                                           
CONECT 8572 8567                                                                
CONECT 8573 8564 8568                                                           
CONECT 8574 8569                                                                
CONECT 8575 8571 8576 8584                                                      
CONECT 8576 8575 8577 8581                                                      
CONECT 8577 8576 8578 8582                                                      
CONECT 8578 8577 8579 8583                                                      
CONECT 8579 8578 8580 8584                                                      
CONECT 8580 8579 8585                                                           
CONECT 8581 8576                                                                
CONECT 8582 8577                                                                
CONECT 8583 8578                                                                
CONECT 8584 8575 8579                                                           
CONECT 8585 8580                                                                
CONECT 8586 7812 8587 8597                                                      
CONECT 8587 8586 8588 8594                                                      
CONECT 8588 8587 8589 8595                                                      
CONECT 8589 8588 8590 8596                                                      
CONECT 8590 8589 8591 8597                                                      
CONECT 8591 8590 8598                                                           
CONECT 8592 8593 8594 8599                                                      
CONECT 8593 8592                                                                
CONECT 8594 8587 8592                                                           
CONECT 8595 8588                                                                
CONECT 8596 8589 8600                                                           
CONECT 8597 8586 8590                                                           
CONECT 8598 8591                                                                
CONECT 8599 8592                                                                
CONECT 8600 8596 8601 8611                                                      
CONECT 8601 8600 8602 8608                                                      
CONECT 8602 8601 8603 8609                                                      
CONECT 8603 8602 8604 8610                                                      
CONECT 8604 8603 8605 8611                                                      
CONECT 8605 8604 8612                                                           
CONECT 8606 8607 8608 8613                                                      
CONECT 8607 8606                                                                
CONECT 8608 8601 8606                                                           
CONECT 8609 8602                                                                
CONECT 8610 8603 8614                                                           
CONECT 8611 8600 8604                                                           
CONECT 8612 8605                                                                
CONECT 8613 8606                                                                
CONECT 8614 8610 8615 8623                                                      
CONECT 8615 8614 8616 8620                                                      
CONECT 8616 8615 8617 8621                                                      
CONECT 8617 8616 8618 8622                                                      
CONECT 8618 8617 8619 8623                                                      
CONECT 8619 8618 8624                                                           
CONECT 8620 8615                                                                
CONECT 8621 8616                                                                
CONECT 8622 8617                                                                
CONECT 8623 8614 8618                                                           
CONECT 8624 8619                                                                
CONECT 8625 8043 8626 8636                                                      
CONECT 8626 8625 8627 8633                                                      
CONECT 8627 8626 8628 8634                                                      
CONECT 8628 8627 8629 8635                                                      
CONECT 8629 8628 8630 8636                                                      
CONECT 8630 8629 8637                                                           
CONECT 8631 8632 8633 8638                                                      
CONECT 8632 8631                                                                
CONECT 8633 8626 8631                                                           
CONECT 8634 8627                                                                
CONECT 8635 8628 8639                                                           
CONECT 8636 8625 8629                                                           
CONECT 8637 8630                                                                
CONECT 8638 8631                                                                
CONECT 8639 8635 8640 8650                                                      
CONECT 8640 8639 8641 8647                                                      
CONECT 8641 8640 8642 8648                                                      
CONECT 8642 8641 8643 8649                                                      
CONECT 8643 8642 8644 8650                                                      
CONECT 8644 8643 8651                                                           
CONECT 8645 8646 8647 8652                                                      
CONECT 8646 8645                                                                
CONECT 8647 8640 8645                                                           
CONECT 8648 8641                                                                
CONECT 8649 8642                                                                
CONECT 8650 8639 8643                                                           
CONECT 8651 8644                                                                
CONECT 8652 8645                                                                
CONECT 8653   52 8654 8664                                                      
CONECT 8654 8653 8655 8661                                                      
CONECT 8655 8654 8656 8662                                                      
CONECT 8656 8655 8657 8663                                                      
CONECT 8657 8656 8658 8664                                                      
CONECT 8658 8657 8665                                                           
CONECT 8659 8660 8661 8666                                                      
CONECT 8660 8659                                                                
CONECT 8661 8654 8659                                                           
CONECT 8662 8655                                                                
CONECT 8663 8656                                                                
CONECT 8664 8653 8657                                                           
CONECT 8665 8658                                                                
CONECT 8666 8659                                                                
CONECT 8667  109 8668 8678                                                      
CONECT 8668 8667 8669 8675                                                      
CONECT 8669 8668 8670 8676                                                      
CONECT 8670 8669 8671 8677                                                      
CONECT 8671 8670 8672 8678                                                      
CONECT 8672 8671 8679                                                           
CONECT 8673 8674 8675 8680                                                      
CONECT 8674 8673                                                                
CONECT 8675 8668 8673                                                           
CONECT 8676 8669                                                                
CONECT 8677 8670                                                                
CONECT 8678 8667 8671                                                           
CONECT 8679 8672                                                                
CONECT 8680 8673                                                                
CONECT 8681 8682 8690                                                           
CONECT 8682 8681 8683 8687                                                      
CONECT 8683 8682 8684 8688                                                      
CONECT 8684 8683 8685 8689                                                      
CONECT 8685 8684 8686 8690                                                      
CONECT 8686 8685 8691                                                           
CONECT 8687 8682                                                                
CONECT 8688 8683                                                                
CONECT 8689 8684                                                                
CONECT 8690 8681 8685                                                           
CONECT 8691 8686                                                                
CONECT 8692 8693 8703                                                           
CONECT 8693 8692 8694 8700                                                      
CONECT 8694 8693 8695 8701                                                      
CONECT 8695 8694 8696 8702                                                      
CONECT 8696 8695 8697 8703                                                      
CONECT 8697 8696 8704                                                           
CONECT 8698 8699 8700 8705                                                      
CONECT 8699 8698                                                                
CONECT 8700 8693 8698                                                           
CONECT 8701 8694                                                                
CONECT 8702 8695                                                                
CONECT 8703 8692 8696                                                           
CONECT 8704 8697                                                                
CONECT 8705 8698                                                                
CONECT 8706 2741 8707 8717                                                      
CONECT 8707 8706 8708 8714                                                      
CONECT 8708 8707 8709 8715                                                      
CONECT 8709 8708 8710 8716                                                      
CONECT 8710 8709 8711 8717                                                      
CONECT 8711 8710 8718                                                           
CONECT 8712 8713 8714 8719                                                      
CONECT 8713 8712                                                                
CONECT 8714 8707 8712                                                           
CONECT 8715 8708                                                                
CONECT 8716 8709                                                                
CONECT 8717 8706 8710                                                           
CONECT 8718 8711                                                                
CONECT 8719 8712                                                                
CONECT 8720 2798 8721 8731                                                      
CONECT 8721 8720 8722 8728                                                      
CONECT 8722 8721 8723 8729                                                      
CONECT 8723 8722 8724 8730                                                      
CONECT 8724 8723 8725 8731                                                      
CONECT 8725 8724 8732                                                           
CONECT 8726 8727 8728 8733                                                      
CONECT 8727 8726                                                                
CONECT 8728 8721 8726                                                           
CONECT 8729 8722                                                                
CONECT 8730 8723                                                                
CONECT 8731 8720 8724                                                           
CONECT 8732 8725                                                                
CONECT 8733 8726                                                                
CONECT 8734 8735 8743                                                           
CONECT 8735 8734 8736 8740                                                      
CONECT 8736 8735 8737 8741                                                      
CONECT 8737 8736 8738 8742                                                      
CONECT 8738 8737 8739 8743                                                      
CONECT 8739 8738 8744                                                           
CONECT 8740 8735                                                                
CONECT 8741 8736                                                                
CONECT 8742 8737                                                                
CONECT 8743 8734 8738                                                           
CONECT 8744 8739                                                                
CONECT 8745 8746 8756                                                           
CONECT 8746 8745 8747 8753                                                      
CONECT 8747 8746 8748 8754                                                      
CONECT 8748 8747 8749 8755                                                      
CONECT 8749 8748 8750 8756                                                      
CONECT 8750 8749 8757                                                           
CONECT 8751 8752 8753 8758                                                      
CONECT 8752 8751                                                                
CONECT 8753 8746 8751                                                           
CONECT 8754 8747                                                                
CONECT 8755 8748                                                                
CONECT 8756 8745 8749                                                           
CONECT 8757 8750                                                                
CONECT 8758 8751                                                                
CONECT 8759 5430 8760 8770                                                      
CONECT 8760 8759 8761 8767                                                      
CONECT 8761 8760 8762 8768                                                      
CONECT 8762 8761 8763 8769                                                      
CONECT 8763 8762 8764 8770                                                      
CONECT 8764 8763 8771                                                           
CONECT 8765 8766 8767 8772                                                      
CONECT 8766 8765                                                                
CONECT 8767 8760 8765                                                           
CONECT 8768 8761                                                                
CONECT 8769 8762                                                                
CONECT 8770 8759 8763                                                           
CONECT 8771 8764                                                                
CONECT 8772 8765                                                                
CONECT 8773 5487 8774 8784                                                      
CONECT 8774 8773 8775 8781                                                      
CONECT 8775 8774 8776 8782                                                      
CONECT 8776 8775 8777 8783                                                      
CONECT 8777 8776 8778 8784                                                      
CONECT 8778 8777 8785                                                           
CONECT 8779 8780 8781 8786                                                      
CONECT 8780 8779                                                                
CONECT 8781 8774 8779                                                           
CONECT 8782 8775                                                                
CONECT 8783 8776                                                                
CONECT 8784 8773 8777                                                           
CONECT 8785 8778                                                                
CONECT 8786 8779                                                                
CONECT 8787 8788 8796                                                           
CONECT 8788 8787 8789 8793                                                      
CONECT 8789 8788 8790 8794                                                      
CONECT 8790 8789 8791 8795                                                      
CONECT 8791 8790 8792 8796                                                      
CONECT 8792 8791 8797                                                           
CONECT 8793 8788                                                                
CONECT 8794 8789                                                                
CONECT 8795 8790                                                                
CONECT 8796 8787 8791                                                           
CONECT 8797 8792                                                                
CONECT 8798 8799 8809                                                           
CONECT 8799 8798 8800 8806                                                      
CONECT 8800 8799 8801 8807                                                      
CONECT 8801 8800 8802 8808                                                      
CONECT 8802 8801 8803 8809                                                      
CONECT 8803 8802 8810                                                           
CONECT 8804 8805 8806 8811                                                      
CONECT 8805 8804                                                                
CONECT 8806 8799 8804                                                           
CONECT 8807 8800                                                                
CONECT 8808 8801                                                                
CONECT 8809 8798 8802                                                           
CONECT 8810 8803                                                                
CONECT 8811 8804                                                                
MASTER     3090    0   57   27   34    0    0    6 8808    3  786  303          
END                                                                             
