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***  VIRAL PROTEIN 19-DEC-21 7T9L  ***

elNémo ID: 220221231036115893

Job options:

ID        	=	 220221231036115893
JOBID     	=	 VIRAL PROTEIN 19-DEC-21 7T9L
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    VIRAL PROTEIN                           19-DEC-21   7T9L              
TITLE     CRYO-EM STRUCTURE OF SARS-COV-2 OMICRON SPIKE PROTEIN IN COMPLEX WITH 
TITLE    2 HUMAN ACE2 (FOCUSED REFINEMENT OF RBD AND ACE2)                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: SPIKE GLYCOPROTEIN;                                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: S GLYCOPROTEIN,E2,PEPLOMER PROTEIN;                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: PROCESSED ANGIOTENSIN-CONVERTING ENZYME 2;                 
COMPND   8 CHAIN: D;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS   
SOURCE   3 2;                                                                   
SOURCE   4 ORGANISM_TAXID: 2697049;                                             
SOURCE   5 GENE: S, 2;                                                          
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  10 ORGANISM_COMMON: HUMAN;                                              
SOURCE  11 ORGANISM_TAXID: 9606;                                                
SOURCE  12 GENE: ACE2, UNQ868/PRO1885;                                          
SOURCE  13 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 9606                                        
KEYWDS    SARS-COV-2, GLYCOPROTEIN, FUSION PROTEIN, VIRAL PROTEIN, ACE2         
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    X.ZHU,D.MANNAR,J.W.SAVILLE,S.S.SRIVASTAVA,A.M.BEREZUK,K.S.TUTTLE,     
AUTHOR   2 S.SUBRAMANIAM                                                        
REVDAT   1   29-DEC-21 7T9L    0                                                
JRNL        AUTH   D.MANNAR,J.W.SAVILLE,X.ZHU,S.S.SRIVASTAVA,A.M.BEREZUK,       
JRNL        AUTH 2 K.S.TUTTLE,C.MARQUEZ,I.SEKIROV,S.SUBRAMANIAM                 
JRNL        TITL   SARS-COV-2 OMICRON VARIANT: ACE2 BINDING, CRYO-EM STRUCTURE  
JRNL        TITL 2 OF SPIKE PROTEIN-ACE2 COMPLEX AND ANTIBODY EVASION           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.66 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : NULL                                      
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : NULL                                
REMARK   3   REFINEMENT SPACE             : NULL                                
REMARK   3   REFINEMENT PROTOCOL          : NULL                                
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : NULL                                             
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : NULL                           
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 2.660                          
REMARK   3   NUMBER OF PARTICLES               : 272266                         
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 7T9L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-DEC-21.                  
REMARK 100 THE DEPOSITION ID IS D_1000261879.                                   
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                 : SARS-COV-2 OMICRON SPIKE          
REMARK 245                                    PROTEIN IN COMPLEX WITH HUMAN     
REMARK 245                                    ACE2; SARS-COV-2 OMICRON SPIKE    
REMARK 245                                    PROTEIN; HUMAN ACE2               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 8.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : TFS KRIOS                      
REMARK 245   DETECTOR TYPE                     : FEI FALCON IV (4K X 4K)        
REMARK 245   MINIMUM DEFOCUS (NM)              : 500.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 2000.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : NULL                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : 4000.00                        
REMARK 245   ILLUMINATION MODE                 : FLOOD BEAM                     
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
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 A     4                                                      
REMARK 465     PHE A     5                                                      
REMARK 465     VAL A     6                                                      
REMARK 465     PHE A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     VAL A     9                                                      
REMARK 465     LEU A    10                                                      
REMARK 465     LEU A    11                                                      
REMARK 465     PRO A    12                                                      
REMARK 465     LEU A    13                                                      
REMARK 465     VAL A    14                                                      
REMARK 465     SER A    15                                                      
REMARK 465     SER A    16                                                      
REMARK 465     GLN A    17                                                      
REMARK 465     CYS A    18                                                      
REMARK 465     VAL A    19                                                      
REMARK 465     ASN A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     THR A    22                                                      
REMARK 465     THR A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     THR A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     PRO A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     ALA A    30                                                      
REMARK 465     TYR A    31                                                      
REMARK 465     THR A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     PHE A    35                                                      
REMARK 465     THR A    36                                                      
REMARK 465     ARG A    37                                                      
REMARK 465     GLY A    38                                                      
REMARK 465     VAL A    39                                                      
REMARK 465     TYR A    40                                                      
REMARK 465     TYR A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     ASP A    43                                                      
REMARK 465     LYS A    44                                                      
REMARK 465     VAL A    45                                                      
REMARK 465     PHE A    46                                                      
REMARK 465     ARG A    47                                                      
REMARK 465     SER A    48                                                      
REMARK 465     SER A    49                                                      
REMARK 465     VAL A    50                                                      
REMARK 465     LEU A    51                                                      
REMARK 465     HIS A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     THR A    54                                                      
REMARK 465     GLN A    55                                                      
REMARK 465     ASP A    56                                                      
REMARK 465     LEU A    57                                                      
REMARK 465     PHE A    58                                                      
REMARK 465     LEU A    59                                                      
REMARK 465     PRO A    60                                                      
REMARK 465     PHE A    61                                                      
REMARK 465     PHE A    62                                                      
REMARK 465     SER A    63                                                      
REMARK 465     ASN A    64                                                      
REMARK 465     VAL A    65                                                      
REMARK 465     THR A    66                                                      
REMARK 465     TRP A    67                                                      
REMARK 465     PHE A    68                                                      
REMARK 465     HIS A    69                                                      
REMARK 465     VAL A    70                                                      
REMARK 465     ILE A    71                                                      
REMARK 465     SER A    72                                                      
REMARK 465     GLY A    73                                                      
REMARK 465     THR A    74                                                      
REMARK 465     ASN A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     LYS A    78                                                      
REMARK 465     ARG A    79                                                      
REMARK 465     PHE A    80                                                      
REMARK 465     ASP A    81                                                      
REMARK 465     ASN A    82                                                      
REMARK 465     PRO A    83                                                      
REMARK 465     VAL A    84                                                      
REMARK 465     LEU A    85                                                      
REMARK 465     PRO A    86                                                      
REMARK 465     PHE A    87                                                      
REMARK 465     ASN A    88                                                      
REMARK 465     ASP A    89                                                      
REMARK 465     GLY A    90                                                      
REMARK 465     VAL A    91                                                      
REMARK 465     TYR A    92                                                      
REMARK 465     PHE A    93                                                      
REMARK 465     ALA A    94                                                      
REMARK 465     SER A    95                                                      
REMARK 465     ILE A    96                                                      
REMARK 465     GLU A    97                                                      
REMARK 465     LYS A    98                                                      
REMARK 465     SER A    99                                                      
REMARK 465     ASN A   100                                                      
REMARK 465     ILE A   101                                                      
REMARK 465     ILE A   102                                                      
REMARK 465     ARG A   103                                                      
REMARK 465     GLY A   104                                                      
REMARK 465     TRP A   105                                                      
REMARK 465     ILE A   106                                                      
REMARK 465     PHE A   107                                                      
REMARK 465     GLY A   108                                                      
REMARK 465     THR A   109                                                      
REMARK 465     THR A   110                                                      
REMARK 465     LEU A   111                                                      
REMARK 465     ASP A   112                                                      
REMARK 465     SER A   113                                                      
REMARK 465     LYS A   114                                                      
REMARK 465     THR A   115                                                      
REMARK 465     GLN A   116                                                      
REMARK 465     SER A   117                                                      
REMARK 465     LEU A   118                                                      
REMARK 465     LEU A   119                                                      
REMARK 465     ILE A   120                                                      
REMARK 465     VAL A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     ASN A   123                                                      
REMARK 465     ALA A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     ASN A   126                                                      
REMARK 465     VAL A   127                                                      
REMARK 465     VAL A   128                                                      
REMARK 465     ILE A   129                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     VAL A   131                                                      
REMARK 465     CYS A   132                                                      
REMARK 465     GLU A   133                                                      
REMARK 465     PHE A   134                                                      
REMARK 465     GLN A   135                                                      
REMARK 465     PHE A   136                                                      
REMARK 465     CYS A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     ASP A   139                                                      
REMARK 465     PRO A   140                                                      
REMARK 465     PHE A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     ASP A   143                                                      
REMARK 465     HIS A   144                                                      
REMARK 465     LYS A   145                                                      
REMARK 465     ASN A   146                                                      
REMARK 465     ASN A   147                                                      
REMARK 465     LYS A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     TRP A   150                                                      
REMARK 465     MET A   151                                                      
REMARK 465     GLU A   152                                                      
REMARK 465     SER A   153                                                      
REMARK 465     GLU A   154                                                      
REMARK 465     PHE A   155                                                      
REMARK 465     ARG A   156                                                      
REMARK 465     VAL A   157                                                      
REMARK 465     TYR A   158                                                      
REMARK 465     SER A   159                                                      
REMARK 465     SER A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     ASN A   162                                                      
REMARK 465     ASN A   163                                                      
REMARK 465     CYS A   164                                                      
REMARK 465     THR A   165                                                      
REMARK 465     PHE A   166                                                      
REMARK 465     GLU A   167                                                      
REMARK 465     TYR A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     SER A   170                                                      
REMARK 465     GLN A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     PHE A   173                                                      
REMARK 465     LEU A   174                                                      
REMARK 465     MET A   175                                                      
REMARK 465     ASP A   176                                                      
REMARK 465     LEU A   177                                                      
REMARK 465     GLU A   178                                                      
REMARK 465     GLY A   179                                                      
REMARK 465     LYS A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     GLY A   182                                                      
REMARK 465     ASN A   183                                                      
REMARK 465     PHE A   184                                                      
REMARK 465     LYS A   185                                                      
REMARK 465     ASN A   186                                                      
REMARK 465     LEU A   187                                                      
REMARK 465     ARG A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     PHE A   190                                                      
REMARK 465     VAL A   191                                                      
REMARK 465     PHE A   192                                                      
REMARK 465     LYS A   193                                                      
REMARK 465     ASN A   194                                                      
REMARK 465     ILE A   195                                                      
REMARK 465     ASP A   196                                                      
REMARK 465     GLY A   197                                                      
REMARK 465     TYR A   198                                                      
REMARK 465     PHE A   199                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     ILE A   201                                                      
REMARK 465     TYR A   202                                                      
REMARK 465     SER A   203                                                      
REMARK 465     LYS A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     THR A   206                                                      
REMARK 465     PRO A   207                                                      
REMARK 465     ILE A   208                                                      
REMARK 465     ILE A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     ARG A   211                                                      
REMARK 465     GLU A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     GLU 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     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     LYS 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     GLY 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     TYR 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     LYS A   679                                                      
REMARK 465     SER A   680                                                      
REMARK 465     HIS A   681                                                      
REMARK 465     GLY A   682                                                      
REMARK 465     SER A   683                                                      
REMARK 465     ALA A   684                                                      
REMARK 465     SER 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     ASN A   703                                                      
REMARK 465     SER A   704                                                      
REMARK 465     VAL A   705                                                      
REMARK 465     ALA A   706                                                      
REMARK 465     TYR A   707                                                      
REMARK 465     SER A   708                                                      
REMARK 465     ASN A   709                                                      
REMARK 465     ASN A   710                                                      
REMARK 465     SER A   711                                                      
REMARK 465     ILE A   712                                                      
REMARK 465     ALA A   713                                                      
REMARK 465     ILE A   714                                                      
REMARK 465     PRO A   715                                                      
REMARK 465     THR A   716                                                      
REMARK 465     ASN A   717                                                      
REMARK 465     PHE A   718                                                      
REMARK 465     THR A   719                                                      
REMARK 465     ILE A   720                                                      
REMARK 465     SER A   721                                                      
REMARK 465     VAL A   722                                                      
REMARK 465     THR A   723                                                      
REMARK 465     THR A   724                                                      
REMARK 465     GLU A   725                                                      
REMARK 465     ILE A   726                                                      
REMARK 465     LEU A   727                                                      
REMARK 465     PRO A   728                                                      
REMARK 465     VAL A   729                                                      
REMARK 465     SER A   730                                                      
REMARK 465     MET A   731                                                      
REMARK 465     THR A   732                                                      
REMARK 465     LYS A   733                                                      
REMARK 465     THR A   734                                                      
REMARK 465     SER A   735                                                      
REMARK 465     VAL A   736                                                      
REMARK 465     ASP A   737                                                      
REMARK 465     CYS A   738                                                      
REMARK 465     THR A   739                                                      
REMARK 465     MET A   740                                                      
REMARK 465     TYR A   741                                                      
REMARK 465     ILE A   742                                                      
REMARK 465     CYS A   743                                                      
REMARK 465     GLY A   744                                                      
REMARK 465     ASP A   745                                                      
REMARK 465     SER A   746                                                      
REMARK 465     THR A   747                                                      
REMARK 465     GLU A   748                                                      
REMARK 465     CYS A   749                                                      
REMARK 465     SER A   750                                                      
REMARK 465     ASN A   751                                                      
REMARK 465     LEU A   752                                                      
REMARK 465     LEU A   753                                                      
REMARK 465     LEU A   754                                                      
REMARK 465     GLN A   755                                                      
REMARK 465     TYR A   756                                                      
REMARK 465     GLY A   757                                                      
REMARK 465     SER A   758                                                      
REMARK 465     PHE A   759                                                      
REMARK 465     CYS A   760                                                      
REMARK 465     THR A   761                                                      
REMARK 465     GLN A   762                                                      
REMARK 465     LEU A   763                                                      
REMARK 465     LYS A   764                                                      
REMARK 465     ARG A   765                                                      
REMARK 465     ALA A   766                                                      
REMARK 465     LEU A   767                                                      
REMARK 465     THR A   768                                                      
REMARK 465     GLY A   769                                                      
REMARK 465     ILE A   770                                                      
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     TYR 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     PRO 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     LYS 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     PRO 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     PRO 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     THR A   912                                                      
REMARK 465     GLN A   913                                                      
REMARK 465     ASN A   914                                                      
REMARK 465     VAL A   915                                                      
REMARK 465     LEU A   916                                                      
REMARK 465     TYR A   917                                                      
REMARK 465     GLU A   918                                                      
REMARK 465     ASN A   919                                                      
REMARK 465     GLN A   920                                                      
REMARK 465     LYS A   921                                                      
REMARK 465     LEU A   922                                                      
REMARK 465     ILE A   923                                                      
REMARK 465     ALA A   924                                                      
REMARK 465     ASN A   925                                                      
REMARK 465     GLN A   926                                                      
REMARK 465     PHE A   927                                                      
REMARK 465     ASN A   928                                                      
REMARK 465     SER A   929                                                      
REMARK 465     ALA A   930                                                      
REMARK 465     ILE A   931                                                      
REMARK 465     GLY A   932                                                      
REMARK 465     LYS A   933                                                      
REMARK 465     ILE A   934                                                      
REMARK 465     GLN A   935                                                      
REMARK 465     ASP A   936                                                      
REMARK 465     SER A   937                                                      
REMARK 465     LEU A   938                                                      
REMARK 465     SER A   939                                                      
REMARK 465     SER A   940                                                      
REMARK 465     THR A   941                                                      
REMARK 465     PRO A   942                                                      
REMARK 465     SER A   943                                                      
REMARK 465     ALA A   944                                                      
REMARK 465     LEU A   945                                                      
REMARK 465     GLY A   946                                                      
REMARK 465     LYS A   947                                                      
REMARK 465     LEU A   948                                                      
REMARK 465     GLN A   949                                                      
REMARK 465     ASP A   950                                                      
REMARK 465     VAL A   951                                                      
REMARK 465     VAL A   952                                                      
REMARK 465     ASN A   953                                                      
REMARK 465     HIS A   954                                                      
REMARK 465     ASN A   955                                                      
REMARK 465     ALA A   956                                                      
REMARK 465     GLN A   957                                                      
REMARK 465     ALA A   958                                                      
REMARK 465     LEU A   959                                                      
REMARK 465     ASN A   960                                                      
REMARK 465     THR A   961                                                      
REMARK 465     LEU A   962                                                      
REMARK 465     VAL A   963                                                      
REMARK 465     LYS A   964                                                      
REMARK 465     GLN A   965                                                      
REMARK 465     LEU A   966                                                      
REMARK 465     SER A   967                                                      
REMARK 465     SER A   968                                                      
REMARK 465     LYS A   969                                                      
REMARK 465     PHE A   970                                                      
REMARK 465     GLY A   971                                                      
REMARK 465     ALA A   972                                                      
REMARK 465     ILE A   973                                                      
REMARK 465     SER A   974                                                      
REMARK 465     SER A   975                                                      
REMARK 465     VAL A   976                                                      
REMARK 465     LEU A   977                                                      
REMARK 465     ASN A   978                                                      
REMARK 465     ASP A   979                                                      
REMARK 465     ILE A   980                                                      
REMARK 465     PHE A   981                                                      
REMARK 465     SER A   982                                                      
REMARK 465     ARG A   983                                                      
REMARK 465     LEU A   984                                                      
REMARK 465     ASP A   985                                                      
REMARK 465     PRO A   986                                                      
REMARK 465     PRO A   987                                                      
REMARK 465     GLU A   988                                                      
REMARK 465     ALA A   989                                                      
REMARK 465     GLU A   990                                                      
REMARK 465     VAL A   991                                                      
REMARK 465     GLN A   992                                                      
REMARK 465     ILE A   993                                                      
REMARK 465     ASP A   994                                                      
REMARK 465     ARG A   995                                                      
REMARK 465     LEU A   996                                                      
REMARK 465     ILE A   997                                                      
REMARK 465     THR A   998                                                      
REMARK 465     GLY A   999                                                      
REMARK 465     ARG A  1000                                                      
REMARK 465     LEU A  1001                                                      
REMARK 465     GLN A  1002                                                      
REMARK 465     SER A  1003                                                      
REMARK 465     LEU A  1004                                                      
REMARK 465     GLN A  1005                                                      
REMARK 465     THR A  1006                                                      
REMARK 465     TYR A  1007                                                      
REMARK 465     VAL A  1008                                                      
REMARK 465     THR A  1009                                                      
REMARK 465     GLN A  1010                                                      
REMARK 465     GLN A  1011                                                      
REMARK 465     LEU A  1012                                                      
REMARK 465     ILE A  1013                                                      
REMARK 465     ARG A  1014                                                      
REMARK 465     ALA A  1015                                                      
REMARK 465     ALA A  1016                                                      
REMARK 465     GLU A  1017                                                      
REMARK 465     ILE A  1018                                                      
REMARK 465     ARG A  1019                                                      
REMARK 465     ALA A  1020                                                      
REMARK 465     SER A  1021                                                      
REMARK 465     ALA A  1022                                                      
REMARK 465     ASN A  1023                                                      
REMARK 465     LEU A  1024                                                      
REMARK 465     ALA A  1025                                                      
REMARK 465     ALA A  1026                                                      
REMARK 465     THR A  1027                                                      
REMARK 465     LYS A  1028                                                      
REMARK 465     MET A  1029                                                      
REMARK 465     SER A  1030                                                      
REMARK 465     GLU A  1031                                                      
REMARK 465     CYS A  1032                                                      
REMARK 465     VAL A  1033                                                      
REMARK 465     LEU A  1034                                                      
REMARK 465     GLY A  1035                                                      
REMARK 465     GLN A  1036                                                      
REMARK 465     SER A  1037                                                      
REMARK 465     LYS A  1038                                                      
REMARK 465     ARG A  1039                                                      
REMARK 465     VAL A  1040                                                      
REMARK 465     ASP A  1041                                                      
REMARK 465     PHE A  1042                                                      
REMARK 465     CYS A  1043                                                      
REMARK 465     GLY A  1044                                                      
REMARK 465     LYS A  1045                                                      
REMARK 465     GLY A  1046                                                      
REMARK 465     TYR A  1047                                                      
REMARK 465     HIS A  1048                                                      
REMARK 465     LEU A  1049                                                      
REMARK 465     MET A  1050                                                      
REMARK 465     SER A  1051                                                      
REMARK 465     PHE A  1052                                                      
REMARK 465     PRO A  1053                                                      
REMARK 465     GLN A  1054                                                      
REMARK 465     SER A  1055                                                      
REMARK 465     ALA A  1056                                                      
REMARK 465     PRO A  1057                                                      
REMARK 465     HIS A  1058                                                      
REMARK 465     GLY A  1059                                                      
REMARK 465     VAL A  1060                                                      
REMARK 465     VAL A  1061                                                      
REMARK 465     PHE A  1062                                                      
REMARK 465     LEU A  1063                                                      
REMARK 465     HIS A  1064                                                      
REMARK 465     VAL A  1065                                                      
REMARK 465     THR A  1066                                                      
REMARK 465     TYR A  1067                                                      
REMARK 465     VAL A  1068                                                      
REMARK 465     PRO A  1069                                                      
REMARK 465     ALA A  1070                                                      
REMARK 465     GLN A  1071                                                      
REMARK 465     GLU A  1072                                                      
REMARK 465     LYS A  1073                                                      
REMARK 465     ASN A  1074                                                      
REMARK 465     PHE A  1075                                                      
REMARK 465     THR A  1076                                                      
REMARK 465     THR A  1077                                                      
REMARK 465     ALA A  1078                                                      
REMARK 465     PRO A  1079                                                      
REMARK 465     ALA A  1080                                                      
REMARK 465     ILE A  1081                                                      
REMARK 465     CYS A  1082                                                      
REMARK 465     HIS A  1083                                                      
REMARK 465     ASP A  1084                                                      
REMARK 465     GLY A  1085                                                      
REMARK 465     LYS A  1086                                                      
REMARK 465     ALA A  1087                                                      
REMARK 465     HIS A  1088                                                      
REMARK 465     PHE A  1089                                                      
REMARK 465     PRO A  1090                                                      
REMARK 465     ARG A  1091                                                      
REMARK 465     GLU A  1092                                                      
REMARK 465     GLY A  1093                                                      
REMARK 465     VAL A  1094                                                      
REMARK 465     PHE A  1095                                                      
REMARK 465     VAL A  1096                                                      
REMARK 465     SER A  1097                                                      
REMARK 465     ASN A  1098                                                      
REMARK 465     GLY A  1099                                                      
REMARK 465     THR A  1100                                                      
REMARK 465     HIS A  1101                                                      
REMARK 465     TRP A  1102                                                      
REMARK 465     PHE A  1103                                                      
REMARK 465     VAL A  1104                                                      
REMARK 465     THR A  1105                                                      
REMARK 465     GLN A  1106                                                      
REMARK 465     ARG A  1107                                                      
REMARK 465     ASN A  1108                                                      
REMARK 465     PHE A  1109                                                      
REMARK 465     TYR A  1110                                                      
REMARK 465     GLU A  1111                                                      
REMARK 465     PRO A  1112                                                      
REMARK 465     GLN A  1113                                                      
REMARK 465     ILE A  1114                                                      
REMARK 465     ILE A  1115                                                      
REMARK 465     THR A  1116                                                      
REMARK 465     THR A  1117                                                      
REMARK 465     ASP A  1118                                                      
REMARK 465     ASN A  1119                                                      
REMARK 465     THR A  1120                                                      
REMARK 465     PHE A  1121                                                      
REMARK 465     VAL A  1122                                                      
REMARK 465     SER A  1123                                                      
REMARK 465     GLY A  1124                                                      
REMARK 465     ASN A  1125                                                      
REMARK 465     CYS A  1126                                                      
REMARK 465     ASP A  1127                                                      
REMARK 465     VAL A  1128                                                      
REMARK 465     VAL A  1129                                                      
REMARK 465     ILE A  1130                                                      
REMARK 465     GLY A  1131                                                      
REMARK 465     ILE A  1132                                                      
REMARK 465     VAL A  1133                                                      
REMARK 465     ASN A  1134                                                      
REMARK 465     ASN A  1135                                                      
REMARK 465     THR A  1136                                                      
REMARK 465     VAL A  1137                                                      
REMARK 465     TYR A  1138                                                      
REMARK 465     ASP A  1139                                                      
REMARK 465     PRO A  1140                                                      
REMARK 465     LEU A  1141                                                      
REMARK 465     GLN A  1142                                                      
REMARK 465     PRO A  1143                                                      
REMARK 465     GLU A  1144                                                      
REMARK 465     LEU A  1145                                                      
REMARK 465     ASP A  1146                                                      
REMARK 465     SER A  1147                                                      
REMARK 465     PHE A  1148                                                      
REMARK 465     LYS A  1149                                                      
REMARK 465     GLU A  1150                                                      
REMARK 465     GLU A  1151                                                      
REMARK 465     LEU A  1152                                                      
REMARK 465     ASP A  1153                                                      
REMARK 465     LYS A  1154                                                      
REMARK 465     TYR A  1155                                                      
REMARK 465     PHE A  1156                                                      
REMARK 465     LYS A  1157                                                      
REMARK 465     ASN A  1158                                                      
REMARK 465     HIS A  1159                                                      
REMARK 465     THR A  1160                                                      
REMARK 465     SER A  1161                                                      
REMARK 465     PRO A  1162                                                      
REMARK 465     ASP A  1163                                                      
REMARK 465     VAL A  1164                                                      
REMARK 465     ASP A  1165                                                      
REMARK 465     LEU A  1166                                                      
REMARK 465     GLY A  1167                                                      
REMARK 465     ASP A  1168                                                      
REMARK 465     ILE A  1169                                                      
REMARK 465     SER A  1170                                                      
REMARK 465     GLY A  1171                                                      
REMARK 465     ILE A  1172                                                      
REMARK 465     ASN A  1173                                                      
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     GLN A  1180                                                      
REMARK 465     LYS A  1181                                                      
REMARK 465     GLU A  1182                                                      
REMARK 465     ILE A  1183                                                      
REMARK 465     ASP A  1184                                                      
REMARK 465     ARG A  1185                                                      
REMARK 465     LEU A  1186                                                      
REMARK 465     ASN A  1187                                                      
REMARK 465     GLU A  1188                                                      
REMARK 465     VAL A  1189                                                      
REMARK 465     ALA A  1190                                                      
REMARK 465     LYS A  1191                                                      
REMARK 465     ASN A  1192                                                      
REMARK 465     LEU A  1193                                                      
REMARK 465     ASN A  1194                                                      
REMARK 465     GLU A  1195                                                      
REMARK 465     SER A  1196                                                      
REMARK 465     LEU A  1197                                                      
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     GLY A  1209                                                      
REMARK 465     SER A  1210                                                      
REMARK 465     GLY A  1211                                                      
REMARK 465     TYR A  1212                                                      
REMARK 465     ILE A  1213                                                      
REMARK 465     PRO A  1214                                                      
REMARK 465     GLU A  1215                                                      
REMARK 465     ALA A  1216                                                      
REMARK 465     PRO A  1217                                                      
REMARK 465     ARG A  1218                                                      
REMARK 465     ASP A  1219                                                      
REMARK 465     GLY A  1220                                                      
REMARK 465     GLN A  1221                                                      
REMARK 465     ALA A  1222                                                      
REMARK 465     TYR A  1223                                                      
REMARK 465     VAL A  1224                                                      
REMARK 465     ARG A  1225                                                      
REMARK 465     LYS A  1226                                                      
REMARK 465     ASP A  1227                                                      
REMARK 465     GLY A  1228                                                      
REMARK 465     GLU A  1229                                                      
REMARK 465     TRP A  1230                                                      
REMARK 465     VAL A  1231                                                      
REMARK 465     LEU A  1232                                                      
REMARK 465     LEU A  1233                                                      
REMARK 465     SER A  1234                                                      
REMARK 465     THR A  1235                                                      
REMARK 465     PHE A  1236                                                      
REMARK 465     LEU A  1237                                                      
REMARK 465     GLY A  1238                                                      
REMARK 465     ARG A  1239                                                      
REMARK 465     SER A  1240                                                      
REMARK 465     LEU A  1241                                                      
REMARK 465     GLU A  1242                                                      
REMARK 465     VAL A  1243                                                      
REMARK 465     LEU A  1244                                                      
REMARK 465     PHE A  1245                                                      
REMARK 465     GLN A  1246                                                      
REMARK 465     GLY A  1247                                                      
REMARK 465     PRO A  1248                                                      
REMARK 465     GLY A  1249                                                      
REMARK 465     HIS A  1250                                                      
REMARK 465     HIS A  1251                                                      
REMARK 465     HIS A  1252                                                      
REMARK 465     HIS A  1253                                                      
REMARK 465     HIS A  1254                                                      
REMARK 465     HIS A  1255                                                      
REMARK 465     HIS A  1256                                                      
REMARK 465     HIS A  1257                                                      
REMARK 465     SER A  1258                                                      
REMARK 465     ALA A  1259                                                      
REMARK 465     TRP A  1260                                                      
REMARK 465     SER A  1261                                                      
REMARK 465     HIS A  1262                                                      
REMARK 465     PRO A  1263                                                      
REMARK 465     GLN A  1264                                                      
REMARK 465     PHE A  1265                                                      
REMARK 465     GLU A  1266                                                      
REMARK 465     LYS A  1267                                                      
REMARK 465     GLY A  1268                                                      
REMARK 465     GLY A  1269                                                      
REMARK 465     GLY A  1270                                                      
REMARK 465     SER A  1271                                                      
REMARK 465     GLY A  1272                                                      
REMARK 465     GLY A  1273                                                      
REMARK 465     GLY A  1274                                                      
REMARK 465     GLY A  1275                                                      
REMARK 465     SER A  1276                                                      
REMARK 465     GLY A  1277                                                      
REMARK 465     GLY A  1278                                                      
REMARK 465     SER A  1279                                                      
REMARK 465     ALA A  1280                                                      
REMARK 465     TRP A  1281                                                      
REMARK 465     SER A  1282                                                      
REMARK 465     HIS A  1283                                                      
REMARK 465     PRO A  1284                                                      
REMARK 465     GLN A  1285                                                      
REMARK 465     PHE A  1286                                                      
REMARK 465     GLU A  1287                                                      
REMARK 465     LYS A  1288                                                      
REMARK 465     GLN D    18                                                      
REMARK 465     ALA D   614                                                      
REMARK 465     ASP D   615                                                      
REMARK 465     HIS D   616                                                      
REMARK 465     HIS D   617                                                      
REMARK 465     HIS D   618                                                      
REMARK 465     HIS D   619                                                      
REMARK 465     HIS D   620                                                      
REMARK 465     HIS D   621                                                      
REMARK 465     HIS D   622                                                      
REMARK 465     HIS D   623                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A 343       30.64    -94.65                                   
REMARK 500    ALA A 352       63.07   -102.90                                   
REMARK 500    ASP A 428       59.24    -94.12                                   
REMARK 500    ILE D 484      -60.86    -97.25                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-25761   RELATED DB: EMDB                             
REMARK 900 CRYO-EM STRUCTURE OF SARS-COV-2 OMICRON SPIKE PROTEIN IN COMPLEX     
REMARK 900 WITH HUMAN ACE2 (FOCUSED REFINEMENT OF RBD AND ACE2)                 
DBREF  7T9L A    4  1208  UNP    P0DTC2   SPIKE_SARS2      1   1208             
DBREF  7T9L D   18   615  UNP    Q9BYF1   ACE2_HUMAN      18    615             
SEQADV 7T9L VAL A   70  UNP  P0DTC2    ALA    67 VARIANT                        
SEQADV 7T9L     A       UNP  P0DTC2    HIS    69 DELETION                       
SEQADV 7T9L     A       UNP  P0DTC2    VAL    70 DELETION                       
SEQADV 7T9L ILE A   96  UNP  P0DTC2    THR    95 VARIANT                        
SEQADV 7T9L     A       UNP  P0DTC2    GLY   142 DELETION                       
SEQADV 7T9L     A       UNP  P0DTC2    VAL   143 DELETION                       
SEQADV 7T9L     A       UNP  P0DTC2    TYR   144 DELETION                       
SEQADV 7T9L ASP A  143  UNP  P0DTC2    TYR   145 CONFLICT                       
SEQADV 7T9L ILE A  209  UNP  P0DTC2              INSERTION                      
SEQADV 7T9L VAL A  210  UNP  P0DTC2              INSERTION                      
SEQADV 7T9L ARG A  211  UNP  P0DTC2    ASN   211 CONFLICT                       
SEQADV 7T9L GLU A  212  UNP  P0DTC2    LEU   212 CONFLICT                       
SEQADV 7T9L PRO A  213  UNP  P0DTC2    VAL   213 CONFLICT                       
SEQADV 7T9L GLU A  214  UNP  P0DTC2    ARG   214 CONFLICT                       
SEQADV 7T9L ASP A  339  UNP  P0DTC2    GLY   339 CONFLICT                       
SEQADV 7T9L LEU A  371  UNP  P0DTC2    SER   371 CONFLICT                       
SEQADV 7T9L PRO A  373  UNP  P0DTC2    SER   373 CONFLICT                       
SEQADV 7T9L PHE A  375  UNP  P0DTC2    SER   375 CONFLICT                       
SEQADV 7T9L ASN A  417  UNP  P0DTC2    LYS   417 VARIANT                        
SEQADV 7T9L LYS A  440  UNP  P0DTC2    ASN   440 CONFLICT                       
SEQADV 7T9L SER A  446  UNP  P0DTC2    GLY   446 CONFLICT                       
SEQADV 7T9L ASN A  477  UNP  P0DTC2    SER   477 VARIANT                        
SEQADV 7T9L LYS A  478  UNP  P0DTC2    THR   478 VARIANT                        
SEQADV 7T9L ALA A  484  UNP  P0DTC2    GLU   484 CONFLICT                       
SEQADV 7T9L ARG A  493  UNP  P0DTC2    GLN   493 CONFLICT                       
SEQADV 7T9L SER A  496  UNP  P0DTC2    GLY   496 CONFLICT                       
SEQADV 7T9L ARG A  498  UNP  P0DTC2    GLN   498 CONFLICT                       
SEQADV 7T9L TYR A  501  UNP  P0DTC2    ASN   501 VARIANT                        
SEQADV 7T9L HIS A  505  UNP  P0DTC2    TYR   505 CONFLICT                       
SEQADV 7T9L LYS A  547  UNP  P0DTC2    THR   547 CONFLICT                       
SEQADV 7T9L GLY A  614  UNP  P0DTC2    ASP   614 VARIANT                        
SEQADV 7T9L TYR A  655  UNP  P0DTC2    HIS   655 VARIANT                        
SEQADV 7T9L LYS A  679  UNP  P0DTC2    ASN   679 CONFLICT                       
SEQADV 7T9L HIS A  681  UNP  P0DTC2    PRO   681 VARIANT                        
SEQADV 7T9L GLY A  682  UNP  P0DTC2    ARG   682 CONFLICT                       
SEQADV 7T9L SER A  683  UNP  P0DTC2    ARG   683 CONFLICT                       
SEQADV 7T9L SER A  685  UNP  P0DTC2    ARG   685 CONFLICT                       
SEQADV 7T9L LYS A  764  UNP  P0DTC2    ASN   764 CONFLICT                       
SEQADV 7T9L TYR A  796  UNP  P0DTC2    ASP   796 VARIANT                        
SEQADV 7T9L PRO A  817  UNP  P0DTC2    PHE   817 CONFLICT                       
SEQADV 7T9L LYS A  856  UNP  P0DTC2    ASN   856 CONFLICT                       
SEQADV 7T9L PRO A  892  UNP  P0DTC2    ALA   892 CONFLICT                       
SEQADV 7T9L PRO A  899  UNP  P0DTC2    ALA   899 CONFLICT                       
SEQADV 7T9L PRO A  942  UNP  P0DTC2    ALA   942 CONFLICT                       
SEQADV 7T9L HIS A  954  UNP  P0DTC2    GLN   954 CONFLICT                       
SEQADV 7T9L LYS A  969  UNP  P0DTC2    ASN   969 CONFLICT                       
SEQADV 7T9L PHE A  981  UNP  P0DTC2    LEU   981 CONFLICT                       
SEQADV 7T9L PRO A  986  UNP  P0DTC2    LYS   986 CONFLICT                       
SEQADV 7T9L PRO A  987  UNP  P0DTC2    VAL   987 CONFLICT                       
SEQADV 7T9L GLY A 1209  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1210  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1211  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L TYR A 1212  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ILE A 1213  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PRO A 1214  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLU A 1215  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ALA A 1216  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PRO A 1217  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ARG A 1218  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ASP A 1219  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1220  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLN A 1221  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ALA A 1222  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L TYR A 1223  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L VAL A 1224  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ARG A 1225  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LYS A 1226  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ASP A 1227  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1228  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLU A 1229  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L TRP A 1230  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L VAL A 1231  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LEU A 1232  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LEU A 1233  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1234  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L THR A 1235  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PHE A 1236  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LEU A 1237  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1238  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ARG A 1239  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1240  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LEU A 1241  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLU A 1242  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L VAL A 1243  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LEU A 1244  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PHE A 1245  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLN A 1246  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1247  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PRO A 1248  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1249  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1250  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1251  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1252  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1253  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1254  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1255  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1256  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1257  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1258  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ALA A 1259  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L TRP A 1260  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1261  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1262  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PRO A 1263  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLN A 1264  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PHE A 1265  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLU A 1266  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LYS A 1267  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1268  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1269  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1270  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1271  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1272  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1273  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1274  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1275  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1276  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1277  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLY A 1278  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1279  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L ALA A 1280  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L TRP A 1281  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L SER A 1282  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS A 1283  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PRO A 1284  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLN A 1285  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L PHE A 1286  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L GLU A 1287  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L LYS A 1288  UNP  P0DTC2              EXPRESSION TAG                 
SEQADV 7T9L HIS D  616  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  617  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  618  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  619  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  620  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  621  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  622  UNP  Q9BYF1              EXPRESSION TAG                 
SEQADV 7T9L HIS D  623  UNP  Q9BYF1              EXPRESSION TAG                 
SEQRES   1 A 1285  MET PHE VAL PHE LEU VAL LEU LEU PRO LEU VAL SER SER          
SEQRES   2 A 1285  GLN CYS VAL ASN LEU THR THR ARG THR GLN LEU PRO PRO          
SEQRES   3 A 1285  ALA TYR THR ASN SER PHE THR ARG GLY VAL TYR TYR PRO          
SEQRES   4 A 1285  ASP LYS VAL PHE ARG SER SER VAL LEU HIS SER THR GLN          
SEQRES   5 A 1285  ASP LEU PHE LEU PRO PHE PHE SER ASN VAL THR TRP PHE          
SEQRES   6 A 1285  HIS VAL ILE SER GLY THR ASN GLY THR LYS ARG PHE ASP          
SEQRES   7 A 1285  ASN PRO VAL LEU PRO PHE ASN ASP GLY VAL TYR PHE ALA          
SEQRES   8 A 1285  SER ILE GLU LYS SER ASN ILE ILE ARG GLY TRP ILE PHE          
SEQRES   9 A 1285  GLY THR THR LEU ASP SER LYS THR GLN SER LEU LEU ILE          
SEQRES  10 A 1285  VAL ASN ASN ALA THR ASN VAL VAL ILE LYS VAL CYS GLU          
SEQRES  11 A 1285  PHE GLN PHE CYS ASN ASP PRO PHE LEU ASP HIS LYS ASN          
SEQRES  12 A 1285  ASN LYS SER TRP MET GLU SER GLU PHE ARG VAL TYR SER          
SEQRES  13 A 1285  SER ALA ASN ASN CYS THR PHE GLU TYR VAL SER GLN PRO          
SEQRES  14 A 1285  PHE LEU MET ASP LEU GLU GLY LYS GLN GLY ASN PHE LYS          
SEQRES  15 A 1285  ASN LEU ARG GLU PHE VAL PHE LYS ASN ILE ASP GLY TYR          
SEQRES  16 A 1285  PHE LYS ILE TYR SER LYS HIS THR PRO ILE ILE VAL ARG          
SEQRES  17 A 1285  GLU PRO GLU ASP LEU PRO GLN GLY PHE SER ALA LEU GLU          
SEQRES  18 A 1285  PRO LEU VAL ASP LEU PRO ILE GLY ILE ASN ILE THR ARG          
SEQRES  19 A 1285  PHE GLN THR LEU LEU ALA LEU HIS ARG SER TYR LEU THR          
SEQRES  20 A 1285  PRO GLY ASP SER SER SER GLY TRP THR ALA GLY ALA ALA          
SEQRES  21 A 1285  ALA TYR TYR VAL GLY TYR LEU GLN PRO ARG THR PHE LEU          
SEQRES  22 A 1285  LEU LYS TYR ASN GLU ASN GLY THR ILE THR ASP ALA VAL          
SEQRES  23 A 1285  ASP CYS ALA LEU ASP PRO LEU SER GLU THR LYS CYS THR          
SEQRES  24 A 1285  LEU LYS SER PHE THR VAL GLU LYS GLY ILE TYR GLN THR          
SEQRES  25 A 1285  SER ASN PHE ARG VAL GLN PRO THR GLU SER ILE VAL ARG          
SEQRES  26 A 1285  PHE PRO ASN ILE THR ASN LEU CYS PRO PHE ASP GLU VAL          
SEQRES  27 A 1285  PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP ASN          
SEQRES  28 A 1285  ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER VAL          
SEQRES  29 A 1285  LEU TYR ASN LEU ALA PRO PHE PHE THR PHE LYS CYS TYR          
SEQRES  30 A 1285  GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE THR          
SEQRES  31 A 1285  ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP GLU          
SEQRES  32 A 1285  VAL ARG GLN ILE ALA PRO GLY GLN THR GLY ASN ILE ALA          
SEQRES  33 A 1285  ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY CYS          
SEQRES  34 A 1285  VAL ILE ALA TRP ASN SER ASN LYS LEU ASP SER LYS VAL          
SEQRES  35 A 1285  SER GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG LYS          
SEQRES  36 A 1285  SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR GLU          
SEQRES  37 A 1285  ILE TYR GLN ALA GLY ASN LYS PRO CYS ASN GLY VAL ALA          
SEQRES  38 A 1285  GLY PHE ASN CYS TYR PHE PRO LEU ARG SER TYR SER PHE          
SEQRES  39 A 1285  ARG PRO THR TYR GLY VAL GLY HIS GLN PRO TYR ARG VAL          
SEQRES  40 A 1285  VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA THR          
SEQRES  41 A 1285  VAL CYS GLY PRO LYS LYS SER THR ASN LEU VAL LYS ASN          
SEQRES  42 A 1285  LYS CYS VAL ASN PHE ASN PHE ASN GLY LEU LYS GLY THR          
SEQRES  43 A 1285  GLY VAL LEU THR GLU SER ASN LYS LYS PHE LEU PRO PHE          
SEQRES  44 A 1285  GLN GLN PHE GLY ARG ASP ILE ALA ASP THR THR ASP ALA          
SEQRES  45 A 1285  VAL ARG ASP PRO GLN THR LEU GLU ILE LEU ASP ILE THR          
SEQRES  46 A 1285  PRO CYS SER PHE GLY GLY VAL SER VAL ILE THR PRO GLY          
SEQRES  47 A 1285  THR ASN THR SER ASN GLN VAL ALA VAL LEU TYR GLN GLY          
SEQRES  48 A 1285  VAL ASN CYS THR GLU VAL PRO VAL ALA ILE HIS ALA ASP          
SEQRES  49 A 1285  GLN LEU THR PRO THR TRP ARG VAL TYR SER THR GLY SER          
SEQRES  50 A 1285  ASN VAL PHE GLN THR ARG ALA GLY CYS LEU ILE GLY ALA          
SEQRES  51 A 1285  GLU TYR VAL ASN ASN SER TYR GLU CYS ASP ILE PRO ILE          
SEQRES  52 A 1285  GLY ALA GLY ILE CYS ALA SER TYR GLN THR GLN THR LYS          
SEQRES  53 A 1285  SER HIS GLY SER ALA SER SER VAL ALA SER GLN SER ILE          
SEQRES  54 A 1285  ILE ALA TYR THR MET SER LEU GLY ALA GLU ASN SER VAL          
SEQRES  55 A 1285  ALA TYR SER ASN ASN SER ILE ALA ILE PRO THR ASN PHE          
SEQRES  56 A 1285  THR ILE SER VAL THR THR GLU ILE LEU PRO VAL SER MET          
SEQRES  57 A 1285  THR LYS THR SER VAL ASP CYS THR MET TYR ILE CYS GLY          
SEQRES  58 A 1285  ASP SER THR GLU CYS SER ASN LEU LEU LEU GLN TYR GLY          
SEQRES  59 A 1285  SER PHE CYS THR GLN LEU LYS ARG ALA LEU THR GLY ILE          
SEQRES  60 A 1285  ALA VAL GLU GLN ASP LYS ASN THR GLN GLU VAL PHE ALA          
SEQRES  61 A 1285  GLN VAL LYS GLN ILE TYR LYS THR PRO PRO ILE LYS TYR          
SEQRES  62 A 1285  PHE GLY GLY PHE ASN PHE SER GLN ILE LEU PRO ASP PRO          
SEQRES  63 A 1285  SER LYS PRO SER LYS ARG SER PRO ILE GLU ASP LEU LEU          
SEQRES  64 A 1285  PHE ASN LYS VAL THR LEU ALA ASP ALA GLY PHE ILE LYS          
SEQRES  65 A 1285  GLN TYR GLY ASP CYS LEU GLY ASP ILE ALA ALA ARG ASP          
SEQRES  66 A 1285  LEU ILE CYS ALA GLN LYS PHE LYS GLY LEU THR VAL LEU          
SEQRES  67 A 1285  PRO PRO LEU LEU THR ASP GLU MET ILE ALA GLN TYR THR          
SEQRES  68 A 1285  SER ALA LEU LEU ALA GLY THR ILE THR SER GLY TRP THR          
SEQRES  69 A 1285  PHE GLY ALA GLY PRO ALA LEU GLN ILE PRO PHE PRO MET          
SEQRES  70 A 1285  GLN MET ALA TYR ARG PHE ASN GLY ILE GLY VAL THR GLN          
SEQRES  71 A 1285  ASN VAL LEU TYR GLU ASN GLN LYS LEU ILE ALA ASN GLN          
SEQRES  72 A 1285  PHE ASN SER ALA ILE GLY LYS ILE GLN ASP SER LEU SER          
SEQRES  73 A 1285  SER THR PRO SER ALA LEU GLY LYS LEU GLN ASP VAL VAL          
SEQRES  74 A 1285  ASN HIS ASN ALA GLN ALA LEU ASN THR LEU VAL LYS GLN          
SEQRES  75 A 1285  LEU SER SER LYS PHE GLY ALA ILE SER SER VAL LEU ASN          
SEQRES  76 A 1285  ASP ILE PHE SER ARG LEU ASP PRO PRO GLU ALA GLU VAL          
SEQRES  77 A 1285  GLN ILE ASP ARG LEU ILE THR GLY ARG LEU GLN SER LEU          
SEQRES  78 A 1285  GLN THR TYR VAL THR GLN GLN LEU ILE ARG ALA ALA GLU          
SEQRES  79 A 1285  ILE ARG ALA SER ALA ASN LEU ALA ALA THR LYS MET SER          
SEQRES  80 A 1285  GLU CYS VAL LEU GLY GLN SER LYS ARG VAL ASP PHE CYS          
SEQRES  81 A 1285  GLY LYS GLY TYR HIS LEU MET SER PHE PRO GLN SER ALA          
SEQRES  82 A 1285  PRO HIS GLY VAL VAL PHE LEU HIS VAL THR TYR VAL PRO          
SEQRES  83 A 1285  ALA GLN GLU LYS ASN PHE THR THR ALA PRO ALA ILE CYS          
SEQRES  84 A 1285  HIS ASP GLY LYS ALA HIS PHE PRO ARG GLU GLY VAL PHE          
SEQRES  85 A 1285  VAL SER ASN GLY THR HIS TRP PHE VAL THR GLN ARG ASN          
SEQRES  86 A 1285  PHE TYR GLU PRO GLN ILE ILE THR THR ASP ASN THR PHE          
SEQRES  87 A 1285  VAL SER GLY ASN CYS ASP VAL VAL ILE GLY ILE VAL ASN          
SEQRES  88 A 1285  ASN THR VAL TYR ASP PRO LEU GLN PRO GLU LEU ASP SER          
SEQRES  89 A 1285  PHE LYS GLU GLU LEU ASP LYS TYR PHE LYS ASN HIS THR          
SEQRES  90 A 1285  SER PRO ASP VAL ASP LEU GLY ASP ILE SER GLY ILE ASN          
SEQRES  91 A 1285  ALA SER VAL VAL ASN ILE GLN LYS GLU ILE ASP ARG LEU          
SEQRES  92 A 1285  ASN GLU VAL ALA LYS ASN LEU ASN GLU SER LEU ILE ASP          
SEQRES  93 A 1285  LEU GLN GLU LEU GLY LYS TYR GLU GLN GLY SER GLY TYR          
SEQRES  94 A 1285  ILE PRO GLU ALA PRO ARG ASP GLY GLN ALA TYR VAL ARG          
SEQRES  95 A 1285  LYS ASP GLY GLU TRP VAL LEU LEU SER THR PHE LEU GLY          
SEQRES  96 A 1285  ARG SER LEU GLU VAL LEU PHE GLN GLY PRO GLY HIS HIS          
SEQRES  97 A 1285  HIS HIS HIS HIS HIS HIS SER ALA TRP SER HIS PRO GLN          
SEQRES  98 A 1285  PHE GLU LYS GLY GLY GLY SER GLY GLY GLY GLY SER GLY          
SEQRES  99 A 1285  GLY SER ALA TRP SER HIS PRO GLN PHE GLU LYS                  
SEQRES   1 D  606  GLN SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP          
SEQRES   2 D  606  LYS PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER          
SEQRES   3 D  606  SER LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU          
SEQRES   4 D  606  GLU ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP          
SEQRES   5 D  606  SER ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET          
SEQRES   6 D  606  TYR PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU          
SEQRES   7 D  606  GLN LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU          
SEQRES   8 D  606  SER GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN          
SEQRES   9 D  606  THR MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN          
SEQRES  10 D  606  PRO ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY          
SEQRES  11 D  606  LEU ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU          
SEQRES  12 D  606  ARG LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY          
SEQRES  13 D  606  LYS GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU          
SEQRES  14 D  606  LYS ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR          
SEQRES  15 D  606  GLY ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL          
SEQRES  16 D  606  ASP GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP          
SEQRES  17 D  606  VAL GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU          
SEQRES  18 D  606  HIS LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA          
SEQRES  19 D  606  TYR PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA          
SEQRES  20 D  606  HIS LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN          
SEQRES  21 D  606  LEU TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN          
SEQRES  22 D  606  ILE ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP          
SEQRES  23 D  606  ALA GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL          
SEQRES  24 D  606  SER VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU          
SEQRES  25 D  606  ASN SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA          
SEQRES  26 D  606  VAL CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP          
SEQRES  27 D  606  PHE ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP          
SEQRES  28 D  606  PHE LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR          
SEQRES  29 D  606  ASP MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN          
SEQRES  30 D  606  GLY ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE          
SEQRES  31 D  606  MET SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER          
SEQRES  32 D  606  ILE GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU          
SEQRES  33 D  606  THR GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE          
SEQRES  34 D  606  VAL GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP          
SEQRES  35 D  606  ARG TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN          
SEQRES  36 D  606  TRP MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL          
SEQRES  37 D  606  GLY VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS          
SEQRES  38 D  606  ASP PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER          
SEQRES  39 D  606  PHE ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN          
SEQRES  40 D  606  PHE GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY          
SEQRES  41 D  606  PRO LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA          
SEQRES  42 D  606  GLY GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER          
SEQRES  43 D  606  GLU PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA          
SEQRES  44 D  606  LYS ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU          
SEQRES  45 D  606  PRO LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER          
SEQRES  46 D  606  PHE VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP          
SEQRES  47 D  606  HIS HIS HIS HIS HIS HIS HIS HIS                              
HET    NAG  A1301      14                                                       
HET    NAG  D 701      14                                                       
HET    NAG  D 702      14                                                       
HET    NAG  D 703      14                                                       
HET    NAG  D 704      14                                                       
HET    NAG  D 705      14                                                       
HET    NAG  D 706      14                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETSYN     NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA-           
HETSYN   2 NAG  D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO-          
HETSYN   3 NAG  2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE                         
FORMUL   3  NAG    7(C8 H15 N O6)                                               
HELIX    1 AA1 PHE A  338  ASN A  343  1                                   6    
HELIX    2 AA2 TYR A  365  ASN A  370  1                                   6    
HELIX    3 AA3 PRO A  384  ASP A  389  5                                   6    
HELIX    4 AA4 GLY A  416  ASN A  422  1                                   7    
HELIX    5 AA5 SER A  438  SER A  443  1                                   6    
HELIX    6 AA6 THR D   20  THR D   52  1                                  33    
HELIX    7 AA7 THR D   55  GLN D   81  1                                  27    
HELIX    8 AA8 ASN D   90  GLN D  101  1                                  12    
HELIX    9 AA9 ASN D  103  LEU D  108  5                                   6    
HELIX   10 AB1 SER D  109  THR D  129  1                                  21    
HELIX   11 AB2 GLY D  147  SER D  155  1                                   9    
HELIX   12 AB3 ASP D  157  ASN D  194  1                                  38    
HELIX   13 AB4 ASP D  198  GLY D  205  1                                   8    
HELIX   14 AB5 ASP D  206  GLU D  208  5                                   3    
HELIX   15 AB6 GLY D  220  TYR D  252  1                                  33    
HELIX   16 AB7 HIS D  265  LEU D  267  5                                   3    
HELIX   17 AB8 TRP D  275  TYR D  279  5                                   5    
HELIX   18 AB9 VAL D  293  GLN D  300  1                                   8    
HELIX   19 AC1 ASP D  303  GLY D  319  1                                  17    
HELIX   20 AC2 THR D  324  SER D  331  1                                   8    
HELIX   21 AC3 THR D  365  TYR D  385  1                                  21    
HELIX   22 AC4 ALA D  386  GLN D  388  5                                   3    
HELIX   23 AC5 PRO D  389  ARG D  393  5                                   5    
HELIX   24 AC6 ASN D  397  ALA D  413  1                                  17    
HELIX   25 AC7 THR D  414  ILE D  421  1                                   8    
HELIX   26 AC8 ASP D  431  VAL D  447  1                                  17    
HELIX   27 AC9 GLY D  448  GLY D  466  1                                  19    
HELIX   28 AD1 PRO D  469  ASP D  471  5                                   3    
HELIX   29 AD2 GLN D  472  ILE D  484  1                                  13    
HELIX   30 AD3 ASP D  499  SER D  502  5                                   4    
HELIX   31 AD4 LEU D  503  ASN D  508  1                                   6    
HELIX   32 AD5 PHE D  512  ALA D  533  1                                  22    
HELIX   33 AD6 PRO D  538  CYS D  542  5                                   5    
HELIX   34 AD7 SER D  547  ARG D  559  1                                  13    
HELIX   35 AD8 PRO D  565  GLY D  575  1                                  11    
HELIX   36 AD9 VAL D  581  PHE D  588  1                                   8    
HELIX   37 AE1 PHE D  588  ASN D  599  1                                  12    
SHEET    1 AA1 5 ASN A 354  ILE A 358  0                                        
SHEET    2 AA1 5 ASN A 394  ILE A 402 -1  O  ALA A 397   N  LYS A 356           
SHEET    3 AA1 5 TYR A 508  GLU A 516 -1  O  TYR A 508   N  ILE A 402           
SHEET    4 AA1 5 GLY A 431  ASN A 437 -1  N  ILE A 434   O  VAL A 511           
SHEET    5 AA1 5 CYS A 379  TYR A 380 -1  N  TYR A 380   O  GLY A 431           
SHEET    1 AA2 2 LEU A 452  ARG A 454  0                                        
SHEET    2 AA2 2 LEU A 492  SER A 494 -1  O  ARG A 493   N  TYR A 453           
SHEET    1 AA3 2 TYR A 473  GLN A 474  0                                        
SHEET    2 AA3 2 CYS A 488  TYR A 489 -1  O  TYR A 489   N  TYR A 473           
SHEET    1 AA4 2 LEU D 262  PRO D 263  0                                        
SHEET    2 AA4 2 VAL D 487  VAL D 488  1  O  VAL D 488   N  LEU D 262           
SHEET    1 AA5 2 THR D 347  GLY D 352  0                                        
SHEET    2 AA5 2 ASP D 355  LEU D 359 -1  O  ARG D 357   N  TRP D 349           
SSBOND   1 CYS A  336    CYS A  361                          1555   1555  2.03  
SSBOND   2 CYS A  379    CYS A  432                          1555   1555  2.04  
SSBOND   3 CYS A  391    CYS A  525                          1555   1555  2.03  
SSBOND   4 CYS A  480    CYS A  488                          1555   1555  2.03  
SSBOND   5 CYS D  133    CYS D  141                          1555   1555  2.03  
SSBOND   6 CYS D  530    CYS D  542                          1555   1555  2.02  
LINK         ND2 ASN A 343                 C1  NAG A1301     1555   1555  1.44  
LINK         ND2 ASN D  53                 C1  NAG D 701     1555   1555  1.44  
LINK         ND2 ASN D  90                 C1  NAG D 702     1555   1555  1.44  
LINK         ND2 ASN D 103                 C1  NAG D 703     1555   1555  1.44  
LINK         ND2 ASN D 322                 C1  NAG D 704     1555   1555  1.44  
LINK         ND2 ASN D 432                 C1  NAG D 705     1555   1555  1.44  
LINK         ND2 ASN D 546                 C1  NAG D 706     1555   1555  1.45  
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   PRO A 330     223.615 171.429 203.046  1.00 77.84           N  
ATOM      2  CA  PRO A 330     224.844 170.802 202.552  1.00 77.84           C  
ATOM      3  C   PRO A 330     225.455 169.871 203.582  1.00 77.84           C  
ATOM      4  O   PRO A 330     224.898 169.693 204.662  1.00 77.84           O  
ATOM      5  CB  PRO A 330     225.783 171.979 202.279  1.00 77.84           C  
ATOM      6  CG  PRO A 330     224.981 173.198 202.396  1.00 77.84           C  
ATOM      7  CD  PRO A 330     223.660 172.897 203.000  1.00 77.84           C  
ATOM      8  N   ASN A 331     226.584 169.271 203.226  1.00 83.10           N  
ATOM      9  CA  ASN A 331     227.228 168.294 204.090  1.00 83.10           C  
ATOM     10  C   ASN A 331     227.834 168.986 205.302  1.00 83.10           C  
ATOM     11  O   ASN A 331     228.592 169.949 205.163  1.00 83.10           O  
ATOM     12  CB  ASN A 331     228.303 167.552 203.306  1.00 83.10           C  
ATOM     13  CG  ASN A 331     227.760 166.925 202.040  1.00 83.10           C  
ATOM     14  OD1 ASN A 331     226.703 166.295 202.049  1.00 83.10           O  
ATOM     15  ND2 ASN A 331     228.475 167.104 200.938  1.00 83.10           N  
ATOM     16  N   ILE A 332     227.491 168.507 206.490  1.00 89.70           N  
ATOM     17  CA  ILE A 332     227.744 169.241 207.724  1.00 89.70           C  
ATOM     18  C   ILE A 332     228.912 168.619 208.484  1.00 89.70           C  
ATOM     19  O   ILE A 332     229.052 167.390 208.563  1.00 89.70           O  
ATOM     20  CB  ILE A 332     226.466 169.345 208.587  1.00 89.70           C  
ATOM     21  CG1 ILE A 332     226.639 170.431 209.651  1.00 89.70           C  
ATOM     22  CG2 ILE A 332     225.995 168.000 209.156  1.00 89.70           C  
ATOM     23  CD1 ILE A 332     226.561 171.835 209.095  1.00 89.70           C  
ATOM     24  N   THR A 333     229.807 169.481 208.967  1.00 93.60           N  
ATOM     25  CA  THR A 333     230.906 169.116 209.859  1.00 93.60           C  
ATOM     26  C   THR A 333     231.013 170.205 210.917  1.00 93.60           C  
ATOM     27  O   THR A 333     230.119 171.044 211.050  1.00 93.60           O  
ATOM     28  CB  THR A 333     232.252 168.986 209.124  1.00 93.60           C  
ATOM     29  OG1 THR A 333     232.590 170.241 208.520  1.00 93.60           O  
ATOM     30  CG2 THR A 333     232.261 167.876 208.071  1.00 93.60           C  
ATOM     31  N   ASN A 334     232.125 170.175 211.659  1.00 96.07           N  
ATOM     32  CA  ASN A 334     232.520 171.187 212.649  1.00 96.07           C  
ATOM     33  C   ASN A 334     231.479 171.359 213.760  1.00 96.07           C  
ATOM     34  O   ASN A 334     230.898 172.429 213.945  1.00 96.07           O  
ATOM     35  CB  ASN A 334     232.822 172.526 211.962  1.00 96.07           C  
ATOM     36  CG  ASN A 334     233.597 173.479 212.849  1.00 96.07           C  
ATOM     37  OD1 ASN A 334     234.628 173.119 213.415  1.00 96.07           O  
ATOM     38  ND2 ASN A 334     233.100 174.704 212.977  1.00 96.07           N  
ATOM     39  N   LEU A 335     231.267 170.281 214.511  1.00 96.74           N  
ATOM     40  CA  LEU A 335     230.320 170.298 215.617  1.00 96.74           C  
ATOM     41  C   LEU A 335     230.834 171.171 216.759  1.00 96.74           C  
ATOM     42  O   LEU A 335     232.041 171.344 216.942  1.00 96.74           O  
ATOM     43  CB  LEU A 335     230.018 168.869 216.081  1.00 96.74           C  
ATOM     44  CG  LEU A 335     231.071 167.887 216.616  1.00 96.74           C  
ATOM     45  CD1 LEU A 335     231.389 168.040 218.104  1.00 96.74           C  
ATOM     46  CD2 LEU A 335     230.636 166.458 216.316  1.00 96.74           C  
ATOM     47  N   CYS A 336     229.898 171.740 217.515  1.00 96.93           N  
ATOM     48  CA  CYS A 336     230.256 172.579 218.651  1.00 96.93           C  
ATOM     49  C   CYS A 336     230.852 171.735 219.775  1.00 96.93           C  
ATOM     50  O   CYS A 336     230.417 170.601 219.998  1.00 96.93           O  
ATOM     51  CB  CYS A 336     229.028 173.334 219.163  1.00 96.93           C  
ATOM     52  SG  CYS A 336     228.541 174.769 218.190  1.00 96.93           S  
ATOM     53  N   PRO A 337     231.837 172.266 220.521  1.00 92.56           N  
ATOM     54  CA  PRO A 337     232.509 171.454 221.557  1.00 92.56           C  
ATOM     55  C   PRO A 337     231.686 171.335 222.834  1.00 92.56           C  
ATOM     56  O   PRO A 337     232.040 171.823 223.908  1.00 92.56           O  
ATOM     57  CB  PRO A 337     233.820 172.214 221.766  1.00 92.56           C  
ATOM     58  CG  PRO A 337     233.470 173.628 221.507  1.00 92.56           C  
ATOM     59  CD  PRO A 337     232.401 173.627 220.448  1.00 92.56           C  
ATOM     60  N   PHE A 338     230.548 170.657 222.720  1.00 88.77           N  
ATOM     61  CA  PHE A 338     229.744 170.335 223.887  1.00 88.77           C  
ATOM     62  C   PHE A 338     230.338 169.181 224.676  1.00 88.77           C  
ATOM     63  O   PHE A 338     230.013 169.019 225.856  1.00 88.77           O  
ATOM     64  CB  PHE A 338     228.310 170.006 223.466  1.00 88.77           C  
ATOM     65  CG  PHE A 338     227.436 171.217 223.270  1.00 88.77           C  
ATOM     66  CD1 PHE A 338     227.758 172.188 222.339  1.00 88.77           C  
ATOM     67  CD2 PHE A 338     226.285 171.376 224.013  1.00 88.77           C  
ATOM     68  CE1 PHE A 338     226.951 173.298 222.161  1.00 88.77           C  
ATOM     69  CE2 PHE A 338     225.476 172.484 223.840  1.00 88.77           C  
ATOM     70  CZ  PHE A 338     225.811 173.444 222.912  1.00 88.77           C  
ATOM     71  N   ASP A 339     231.191 168.373 224.044  1.00 92.86           N  
ATOM     72  CA  ASP A 339     231.867 167.295 224.753  1.00 92.86           C  
ATOM     73  C   ASP A 339     232.875 167.840 225.753  1.00 92.86           C  
ATOM     74  O   ASP A 339     233.089 167.235 226.808  1.00 92.86           O  
ATOM     75  CB  ASP A 339     232.558 166.368 223.753  1.00 92.86           C  
ATOM     76  CG  ASP A 339     232.918 165.021 224.350  1.00 92.86           C  
ATOM     77  OD1 ASP A 339     233.874 164.952 225.150  1.00 92.86           O  
ATOM     78  OD2 ASP A 339     232.240 164.026 224.019  1.00 92.86           O  
ATOM     79  N   GLU A 340     233.503 168.973 225.440  1.00 88.57           N  
ATOM     80  CA  GLU A 340     234.414 169.598 226.386  1.00 88.57           C  
ATOM     81  C   GLU A 340     233.681 170.249 227.548  1.00 88.57           C  
ATOM     82  O   GLU A 340     234.290 170.475 228.598  1.00 88.57           O  
ATOM     83  CB  GLU A 340     235.272 170.635 225.667  1.00 88.57           C  
ATOM     84  CG  GLU A 340     236.093 170.063 224.527  1.00 88.57           C  
ATOM     85  CD  GLU A 340     237.443 170.733 224.385  1.00 88.57           C  
ATOM     86  OE1 GLU A 340     237.485 171.982 224.348  1.00 88.57           O  
ATOM     87  OE2 GLU A 340     238.461 170.013 224.308  1.00 88.57           O  
ATOM     88  N   VAL A 341     232.399 170.559 227.387  1.00 80.69           N  
ATOM     89  CA  VAL A 341     231.622 171.166 228.462  1.00 80.69           C  
ATOM     90  C   VAL A 341     230.959 170.113 229.332  1.00 80.69           C  
ATOM     91  O   VAL A 341     231.041 170.166 230.557  1.00 80.69           O  
ATOM     92  CB  VAL A 341     230.581 172.143 227.880  1.00 80.69           C  
ATOM     93  CG1 VAL A 341     229.837 172.838 228.999  1.00 80.69           C  
ATOM     94  CG2 VAL A 341     231.257 173.161 226.983  1.00 80.69           C  
ATOM     95  N   PHE A 342     230.293 169.139 228.718  1.00 79.52           N  
ATOM     96  CA  PHE A 342     229.511 168.170 229.478  1.00 79.52           C  
ATOM     97  C   PHE A 342     230.375 167.028 229.989  1.00 79.52           C  
ATOM     98  O   PHE A 342     230.266 166.630 231.152  1.00 79.52           O  
ATOM     99  CB  PHE A 342     228.354 167.647 228.633  1.00 79.52           C  
ATOM    100  CG  PHE A 342     227.242 168.634 228.470  1.00 79.52           C  
ATOM    101  CD1 PHE A 342     227.329 169.653 227.541  1.00 79.52           C  
ATOM    102  CD2 PHE A 342     226.106 168.543 229.250  1.00 79.52           C  
ATOM    103  CE1 PHE A 342     226.313 170.562 227.399  1.00 79.52           C  
ATOM    104  CE2 PHE A 342     225.083 169.450 229.105  1.00 79.52           C  
ATOM    105  CZ  PHE A 342     225.193 170.459 228.176  1.00 79.52           C  
ATOM    106  N   ASN A 343     231.233 166.479 229.133  1.00 91.12           N  
ATOM    107  CA  ASN A 343     232.030 165.314 229.485  1.00 91.12           C  
ATOM    108  C   ASN A 343     233.408 165.694 230.000  1.00 91.12           C  
ATOM    109  O   ASN A 343     234.369 164.938 229.816  1.00 91.12           O  
ATOM    110  CB  ASN A 343     232.145 164.380 228.281  1.00 91.12           C  
ATOM    111  CG  ASN A 343     230.816 163.766 227.896  1.00 91.12           C  
ATOM    112  OD1 ASN A 343     229.763 164.201 228.357  1.00 91.12           O  
ATOM    113  ND2 ASN A 343     230.855 162.757 227.040  1.00 91.12           N  
ATOM    114  N   ALA A 344     233.525 166.851 230.644  1.00 80.68           N  
ATOM    115  CA  ALA A 344     234.755 167.224 231.321  1.00 80.68           C  
ATOM    116  C   ALA A 344     234.950 166.381 232.573  1.00 80.68           C  
ATOM    117  O   ALA A 344     233.991 165.918 233.193  1.00 80.68           O  
ATOM    118  CB  ALA A 344     234.736 168.706 231.686  1.00 80.68           C  
ATOM    119  N   THR A 345     236.216 166.175 232.934  1.00 77.97           N  
ATOM    120  CA  THR A 345     236.530 165.348 234.093  1.00 77.97           C  
ATOM    121  C   THR A 345     236.202 166.065 235.395  1.00 77.97           C  
ATOM    122  O   THR A 345     235.756 165.436 236.362  1.00 77.97           O  
ATOM    123  CB  THR A 345     238.003 164.953 234.069  1.00 77.97           C  
ATOM    124  OG1 THR A 345     238.811 166.133 234.129  1.00 77.97           O  
ATOM    125  CG2 THR A 345     238.323 164.196 232.793  1.00 77.97           C  
ATOM    126  N   ARG A 346     236.411 167.376 235.438  1.00 74.06           N  
ATOM    127  CA  ARG A 346     236.255 168.167 236.650  1.00 74.06           C  
ATOM    128  C   ARG A 346     235.473 169.430 236.334  1.00 74.06           C  
ATOM    129  O   ARG A 346     235.811 170.144 235.387  1.00 74.06           O  
ATOM    130  CB  ARG A 346     237.633 168.530 237.212  1.00 74.06           C  
ATOM    131  CG  ARG A 346     237.639 169.602 238.278  1.00 74.06           C  
ATOM    132  CD  ARG A 346     236.939 169.180 239.562  1.00 74.06           C  
ATOM    133  NE  ARG A 346     237.649 169.672 240.739  1.00 74.06           N  
ATOM    134  CZ  ARG A 346     237.647 170.932 241.160  1.00 74.06           C  
ATOM    135  NH1 ARG A 346     236.911 171.862 240.573  1.00 74.06           N  
ATOM    136  NH2 ARG A 346     238.401 171.268 242.202  1.00 74.06           N  
ATOM    137  N   PHE A 347     234.446 169.717 237.127  1.00 65.16           N  
ATOM    138  CA  PHE A 347     233.740 170.980 236.983  1.00 65.16           C  
ATOM    139  C   PHE A 347     234.193 171.955 238.053  1.00 65.16           C  
ATOM    140  O   PHE A 347     234.772 171.579 239.072  1.00 65.16           O  
ATOM    141  CB  PHE A 347     232.219 170.836 237.070  1.00 65.16           C  
ATOM    142  CG  PHE A 347     231.582 170.269 235.846  1.00 65.16           C  
ATOM    143  CD1 PHE A 347     232.308 170.079 234.689  1.00 65.16           C  
ATOM    144  CD2 PHE A 347     230.220 170.063 235.809  1.00 65.16           C  
ATOM    145  CE1 PHE A 347     231.706 169.579 233.564  1.00 65.16           C  
ATOM    146  CE2 PHE A 347     229.611 169.588 234.672  1.00 65.16           C  
ATOM    147  CZ  PHE A 347     230.352 169.341 233.555  1.00 65.16           C  
ATOM    148  N   ALA A 348     233.903 173.223 237.816  1.00 59.18           N  
ATOM    149  CA  ALA A 348     234.279 174.240 238.772  1.00 59.18           C  
ATOM    150  C   ALA A 348     233.252 174.330 239.893  1.00 59.18           C  
ATOM    151  O   ALA A 348     232.160 173.763 239.825  1.00 59.18           O  
ATOM    152  CB  ALA A 348     234.425 175.583 238.072  1.00 59.18           C  
ATOM    153  N   SER A 349     233.622 175.053 240.943  1.00 57.21           N  
ATOM    154  CA  SER A 349     232.713 175.317 242.041  1.00 57.21           C  
ATOM    155  C   SER A 349     231.644 176.313 241.607  1.00 57.21           C  
ATOM    156  O   SER A 349     231.775 176.994 240.590  1.00 57.21           O  
ATOM    157  CB  SER A 349     233.480 175.852 243.243  1.00 57.21           C  
ATOM    158  OG  SER A 349     234.443 174.914 243.682  1.00 57.21           O  
ATOM    159  N   VAL A 350     230.565 176.385 242.386  1.00 52.33           N  
ATOM    160  CA  VAL A 350     229.457 177.251 242.000  1.00 52.33           C  
ATOM    161  C   VAL A 350     229.801 178.720 242.231  1.00 52.33           C  
ATOM    162  O   VAL A 350     229.303 179.595 241.515  1.00 52.33           O  
ATOM    163  CB  VAL A 350     228.164 176.810 242.719  1.00 52.33           C  
ATOM    164  CG1 VAL A 350     228.300 176.921 244.205  1.00 52.33           C  
ATOM    165  CG2 VAL A 350     226.941 177.574 242.214  1.00 52.33           C  
ATOM    166  N   TYR A 351     230.681 179.025 243.188  1.00 55.42           N  
ATOM    167  CA  TYR A 351     231.065 180.420 243.377  1.00 55.42           C  
ATOM    168  C   TYR A 351     231.961 180.889 242.234  1.00 55.42           C  
ATOM    169  O   TYR A 351     231.818 182.017 241.752  1.00 55.42           O  
ATOM    170  CB  TYR A 351     231.719 180.617 244.754  1.00 55.42           C  
ATOM    171  CG  TYR A 351     233.191 180.300 244.846  1.00 55.42           C  
ATOM    172  CD1 TYR A 351     233.628 178.999 245.000  1.00 55.42           C  
ATOM    173  CD2 TYR A 351     234.142 181.311 244.802  1.00 55.42           C  
ATOM    174  CE1 TYR A 351     234.969 178.706 245.082  1.00 55.42           C  
ATOM    175  CE2 TYR A 351     235.485 181.028 244.889  1.00 55.42           C  
ATOM    176  CZ  TYR A 351     235.891 179.723 245.027  1.00 55.42           C  
ATOM    177  OH  TYR A 351     237.229 179.433 245.113  1.00 55.42           O  
ATOM    178  N   ALA A 352     232.890 180.047 241.796  1.00 54.76           N  
ATOM    179  CA  ALA A 352     233.717 180.326 240.626  1.00 54.76           C  
ATOM    180  C   ALA A 352     233.224 179.530 239.420  1.00 54.76           C  
ATOM    181  O   ALA A 352     233.944 178.700 238.885  1.00 54.76           O  
ATOM    182  CB  ALA A 352     235.176 180.007 240.931  1.00 54.76           C  
ATOM    183  N   TRP A 353     231.996 179.802 238.984  1.00 57.11           N  
ATOM    184  CA  TRP A 353     231.383 178.993 237.936  1.00 57.11           C  
ATOM    185  C   TRP A 353     232.035 179.252 236.584  1.00 57.11           C  
ATOM    186  O   TRP A 353     232.292 180.398 236.212  1.00 57.11           O  
ATOM    187  CB  TRP A 353     229.878 179.256 237.867  1.00 57.11           C  
ATOM    188  CG  TRP A 353     229.470 180.693 237.911  1.00 57.11           C  
ATOM    189  CD1 TRP A 353     229.198 181.428 239.020  1.00 57.11           C  
ATOM    190  CD2 TRP A 353     229.234 181.557 236.795  1.00 57.11           C  
ATOM    191  NE1 TRP A 353     228.835 182.701 238.673  1.00 57.11           N  
ATOM    192  CE2 TRP A 353     228.848 182.806 237.310  1.00 57.11           C  
ATOM    193  CE3 TRP A 353     229.324 181.399 235.413  1.00 57.11           C  
ATOM    194  CZ2 TRP A 353     228.550 183.887 236.493  1.00 57.11           C  
ATOM    195  CZ3 TRP A 353     229.031 182.474 234.606  1.00 57.11           C  
ATOM    196  CH2 TRP A 353     228.649 183.701 235.146  1.00 57.11           C  
ATOM    197  N   ASN A 354     232.322 178.175 235.853  1.00 60.52           N  
ATOM    198  CA  ASN A 354     232.968 178.318 234.555  1.00 60.52           C  
ATOM    199  C   ASN A 354     231.992 178.803 233.500  1.00 60.52           C  
ATOM    200  O   ASN A 354     230.862 178.329 233.419  1.00 60.52           O  
ATOM    201  CB  ASN A 354     233.589 177.001 234.099  1.00 60.52           C  
ATOM    202  CG  ASN A 354     235.034 176.870 234.509  1.00 60.52           C  
ATOM    203  OD1 ASN A 354     235.773 177.852 234.535  1.00 60.52           O  
ATOM    204  ND2 ASN A 354     235.455 175.650 234.809  1.00 60.52           N  
ATOM    205  N   ARG A 355     232.432 179.758 232.691  1.00 63.49           N  
ATOM    206  CA  ARG A 355     231.656 180.239 231.557  1.00 63.49           C  
ATOM    207  C   ARG A 355     232.446 179.954 230.291  1.00 63.49           C  
ATOM    208  O   ARG A 355     233.579 180.421 230.146  1.00 63.49           O  
ATOM    209  CB  ARG A 355     231.349 181.729 231.680  1.00 63.49           C  
ATOM    210  CG  ARG A 355     230.866 182.357 230.396  1.00 63.49           C  
ATOM    211  CD  ARG A 355     230.017 183.573 230.674  1.00 63.49           C  
ATOM    212  NE  ARG A 355     228.622 183.210 230.878  1.00 63.49           N  
ATOM    213  CZ  ARG A 355     227.628 184.081 230.970  1.00 63.49           C  
ATOM    214  NH1 ARG A 355     227.840 185.382 230.888  1.00 63.49           N  
ATOM    215  NH2 ARG A 355     226.389 183.634 231.146  1.00 63.49           N  
ATOM    216  N   LYS A 356     231.852 179.188 229.383  1.00 71.47           N  
ATOM    217  CA  LYS A 356     232.463 178.870 228.101  1.00 71.47           C  
ATOM    218  C   LYS A 356     231.601 179.456 227.000  1.00 71.47           C  
ATOM    219  O   LYS A 356     230.401 179.176 226.937  1.00 71.47           O  
ATOM    220  CB  LYS A 356     232.598 177.359 227.918  1.00 71.47           C  
ATOM    221  CG  LYS A 356     233.144 176.939 226.567  1.00 71.47           C  
ATOM    222  CD  LYS A 356     234.611 176.569 226.650  1.00 71.47           C  
ATOM    223  CE  LYS A 356     235.286 176.673 225.293  1.00 71.47           C  
ATOM    224  NZ  LYS A 356     235.706 178.066 224.981  1.00 71.47           N  
ATOM    225  N   ARG A 357     232.200 180.272 226.143  1.00 78.66           N  
ATOM    226  CA  ARG A 357     231.461 180.840 225.031  1.00 78.66           C  
ATOM    227  C   ARG A 357     231.543 179.905 223.834  1.00 78.66           C  
ATOM    228  O   ARG A 357     232.578 179.285 223.574  1.00 78.66           O  
ATOM    229  CB  ARG A 357     231.973 182.232 224.665  1.00 78.66           C  
ATOM    230  CG  ARG A 357     233.440 182.321 224.285  1.00 78.66           C  
ATOM    231  CD  ARG A 357     233.814 183.699 223.735  1.00 78.66           C  
ATOM    232  NE  ARG A 357     233.126 184.028 222.490  1.00 78.66           N  
ATOM    233  CZ  ARG A 357     232.067 184.821 222.395  1.00 78.66           C  
ATOM    234  NH1 ARG A 357     231.530 185.387 223.463  1.00 78.66           N  
ATOM    235  NH2 ARG A 357     231.529 185.045 221.200  1.00 78.66           N  
ATOM    236  N   ILE A 358     230.428 179.782 223.129  1.00 80.79           N  
ATOM    237  CA  ILE A 358     230.283 178.887 221.998  1.00 80.79           C  
ATOM    238  C   ILE A 358     229.914 179.738 220.799  1.00 80.79           C  
ATOM    239  O   ILE A 358     228.884 180.435 220.815  1.00 80.79           O  
ATOM    240  CB  ILE A 358     229.228 177.805 222.262  1.00 80.79           C  
ATOM    241  CG1 ILE A 358     229.744 176.805 223.292  1.00 80.79           C  
ATOM    242  CG2 ILE A 358     228.863 177.094 220.990  1.00 80.79           C  
ATOM    243  CD1 ILE A 358     228.648 176.118 224.053  1.00 80.79           C  
ATOM    244  N   SER A 359     230.768 179.688 219.778  1.00 87.97           N  
ATOM    245  CA  SER A 359     230.672 180.490 218.572  1.00 87.97           C  
ATOM    246  C   SER A 359     231.147 179.657 217.391  1.00 87.97           C  
ATOM    247  O   SER A 359     231.842 178.653 217.561  1.00 87.97           O  
ATOM    248  CB  SER A 359     231.490 181.778 218.679  1.00 87.97           C  
ATOM    249  OG  SER A 359     232.845 181.486 218.964  1.00 87.97           O  
ATOM    250  N   ASN A 360     230.717 180.094 216.203  1.00 91.32           N  
ATOM    251  CA  ASN A 360     231.100 179.624 214.855  1.00 91.32           C  
ATOM    252  C   ASN A 360     231.214 178.103 214.709  1.00 91.32           C  
ATOM    253  O   ASN A 360     232.170 177.568 214.145  1.00 91.32           O  
ATOM    254  CB  ASN A 360     232.365 180.351 214.347  1.00 91.32           C  
ATOM    255  CG  ASN A 360     233.605 180.179 215.235  1.00 91.32           C  
ATOM    256  OD1 ASN A 360     233.917 179.101 215.733  1.00 91.32           O  
ATOM    257  ND2 ASN A 360     234.322 181.279 215.427  1.00 91.32           N  
ATOM    258  N   CYS A 361     230.195 177.403 215.196  1.00 95.39           N  
ATOM    259  CA  CYS A 361     230.104 175.964 215.006  1.00 95.39           C  
ATOM    260  C   CYS A 361     228.637 175.591 214.838  1.00 95.39           C  
ATOM    261  O   CYS A 361     227.747 176.439 214.937  1.00 95.39           O  
ATOM    262  CB  CYS A 361     230.760 175.217 216.168  1.00 95.39           C  
ATOM    263  SG  CYS A 361     230.268 175.770 217.818  1.00 95.39           S  
ATOM    264  N   VAL A 362     228.378 174.308 214.588  1.00 96.02           N  
ATOM    265  CA  VAL A 362     227.018 173.786 214.490  1.00 96.02           C  
ATOM    266  C   VAL A 362     226.658 173.097 215.803  1.00 96.02           C  
ATOM    267  O   VAL A 362     227.432 172.288 216.333  1.00 96.02           O  
ATOM    268  CB  VAL A 362     226.837 172.867 213.262  1.00 96.02           C  
ATOM    269  CG1 VAL A 362     227.795 171.696 213.239  1.00 96.02           C  
ATOM    270  CG2 VAL A 362     225.409 172.372 213.168  1.00 96.02           C  
ATOM    271  N   ALA A 363     225.526 173.483 216.381  1.00 99.58           N  
ATOM    272  CA  ALA A 363     225.180 173.098 217.743  1.00 99.58           C  
ATOM    273  C   ALA A 363     224.035 172.097 217.695  1.00 99.58           C  
ATOM    274  O   ALA A 363     222.888 172.466 217.430  1.00 99.58           O  
ATOM    275  CB  ALA A 363     224.802 174.321 218.574  1.00 99.58           C  
ATOM    276  N   ASP A 364     224.356 170.833 217.946  1.00105.25           N  
ATOM    277  CA  ASP A 364     223.382 169.746 217.939  1.00105.25           C  
ATOM    278  C   ASP A 364     222.897 169.533 219.369  1.00105.25           C  
ATOM    279  O   ASP A 364     223.565 168.893 220.182  1.00105.25           O  
ATOM    280  CB  ASP A 364     223.989 168.495 217.315  1.00105.25           C  
ATOM    281  CG  ASP A 364     225.384 168.206 217.825  1.00105.25           C  
ATOM    282  OD1 ASP A 364     226.210 169.141 217.845  1.00105.25           O  
ATOM    283  OD2 ASP A 364     225.658 167.047 218.196  1.00105.25           O  
ATOM    284  N   TYR A 365     221.722 170.072 219.677  1.00104.33           N  
ATOM    285  CA  TYR A 365     221.107 169.867 220.980  1.00104.33           C  
ATOM    286  C   TYR A 365     220.432 168.511 221.120  1.00104.33           C  
ATOM    287  O   TYR A 365     220.023 168.157 222.231  1.00104.33           O  
ATOM    288  CB  TYR A 365     220.099 170.979 221.261  1.00104.33           C  
ATOM    289  CG  TYR A 365     220.697 172.361 221.180  1.00104.33           C  
ATOM    290  CD1 TYR A 365     221.421 172.885 222.241  1.00104.33           C  
ATOM    291  CD2 TYR A 365     220.541 173.142 220.042  1.00104.33           C  
ATOM    292  CE1 TYR A 365     221.971 174.150 222.174  1.00104.33           C  
ATOM    293  CE2 TYR A 365     221.088 174.407 219.965  1.00104.33           C  
ATOM    294  CZ  TYR A 365     221.801 174.904 221.033  1.00104.33           C  
ATOM    295  OH  TYR A 365     222.346 176.162 220.962  1.00104.33           O  
ATOM    296  N   SER A 366     220.301 167.750 220.031  1.00112.45           N  
ATOM    297  CA  SER A 366     219.624 166.461 220.086  1.00112.45           C  
ATOM    298  C   SER A 366     220.441 165.422 220.839  1.00112.45           C  
ATOM    299  O   SER A 366     219.877 164.426 221.303  1.00112.45           O  
ATOM    300  CB  SER A 366     219.325 165.957 218.674  1.00112.45           C  
ATOM    301  OG  SER A 366     218.555 166.898 217.950  1.00112.45           O  
ATOM    302  N   VAL A 367     221.755 165.629 220.956  1.00112.96           N  
ATOM    303  CA  VAL A 367     222.588 164.748 221.765  1.00112.96           C  
ATOM    304  C   VAL A 367     222.244 164.906 223.241  1.00112.96           C  
ATOM    305  O   VAL A 367     222.128 163.915 223.972  1.00112.96           O  
ATOM    306  CB  VAL A 367     224.074 165.030 221.480  1.00112.96           C  
ATOM    307  CG1 VAL A 367     224.978 164.321 222.476  1.00112.96           C  
ATOM    308  CG2 VAL A 367     224.414 164.604 220.067  1.00112.96           C  
ATOM    309  N   LEU A 368     222.043 166.148 223.691  1.00107.91           N  
ATOM    310  CA  LEU A 368     221.778 166.404 225.105  1.00107.91           C  
ATOM    311  C   LEU A 368     220.414 165.863 225.514  1.00107.91           C  
ATOM    312  O   LEU A 368     220.240 165.386 226.641  1.00107.91           O  
ATOM    313  CB  LEU A 368     221.861 167.900 225.386  1.00107.91           C  
ATOM    314  CG  LEU A 368     223.179 168.545 224.975  1.00107.91           C  
ATOM    315  CD1 LEU A 368     223.121 170.038 225.203  1.00107.91           C  
ATOM    316  CD2 LEU A 368     224.334 167.916 225.727  1.00107.91           C  
ATOM    317  N   TYR A 369     219.439 165.935 224.607  1.00116.89           N  
ATOM    318  CA  TYR A 369     218.094 165.459 224.905  1.00116.89           C  
ATOM    319  C   TYR A 369     218.047 163.939 224.979  1.00116.89           C  
ATOM    320  O   TYR A 369     217.284 163.380 225.776  1.00116.89           O  
ATOM    321  CB  TYR A 369     217.114 165.973 223.850  1.00116.89           C  
ATOM    322  CG  TYR A 369     215.723 165.390 223.959  1.00116.89           C  
ATOM    323  CD1 TYR A 369     214.981 165.521 225.128  1.00116.89           C  
ATOM    324  CD2 TYR A 369     215.157 164.697 222.895  1.00116.89           C  
ATOM    325  CE1 TYR A 369     213.710 164.982 225.233  1.00116.89           C  
ATOM    326  CE2 TYR A 369     213.886 164.155 222.989  1.00116.89           C  
ATOM    327  CZ  TYR A 369     213.169 164.301 224.160  1.00116.89           C  
ATOM    328  OH  TYR A 369     211.905 163.766 224.258  1.00116.89           O  
ATOM    329  N   ASN A 370     218.871 163.258 224.188  1.00118.79           N  
ATOM    330  CA  ASN A 370     218.767 161.817 224.011  1.00118.79           C  
ATOM    331  C   ASN A 370     219.607 161.024 225.004  1.00118.79           C  
ATOM    332  O   ASN A 370     219.639 159.792 224.916  1.00118.79           O  
ATOM    333  CB  ASN A 370     219.168 161.436 222.583  1.00118.79           C  
ATOM    334  CG  ASN A 370     218.013 161.544 221.606  1.00118.79           C  
ATOM    335  OD1 ASN A 370     216.873 161.790 222.000  1.00118.79           O  
ATOM    336  ND2 ASN A 370     218.304 161.363 220.324  1.00118.79           N  
ATOM    337  N   LEU A 371     220.283 161.686 225.938  1.00112.05           N  
ATOM    338  CA  LEU A 371     221.027 161.007 226.992  1.00112.05           C  
ATOM    339  C   LEU A 371     220.164 160.942 228.245  1.00112.05           C  
ATOM    340  O   LEU A 371     219.751 161.977 228.780  1.00112.05           O  
ATOM    341  CB  LEU A 371     222.359 161.700 227.280  1.00112.05           C  
ATOM    342  CG  LEU A 371     223.624 161.189 226.578  1.00112.05           C  
ATOM    343  CD1 LEU A 371     223.963 159.801 227.096  1.00112.05           C  
ATOM    344  CD2 LEU A 371     223.499 161.153 225.066  1.00112.05           C  
ATOM    345  N   ALA A 372     219.897 159.724 228.700  1.00107.91           N  
ATOM    346  CA  ALA A 372     219.057 159.421 229.856  1.00107.91           C  
ATOM    347  C   ALA A 372     219.633 159.754 231.240  1.00107.91           C  
ATOM    348  O   ALA A 372     218.831 160.047 232.136  1.00107.91           O  
ATOM    349  CB  ALA A 372     218.650 157.943 229.815  1.00107.91           C  
ATOM    350  N   PRO A 373     220.953 159.681 231.511  1.00103.91           N  
ATOM    351  CA  PRO A 373     221.436 160.200 232.807  1.00103.91           C  
ATOM    352  C   PRO A 373     221.211 161.690 233.035  1.00103.91           C  
ATOM    353  O   PRO A 373     221.125 162.102 234.198  1.00103.91           O  
ATOM    354  CB  PRO A 373     222.937 159.868 232.796  1.00103.91           C  
ATOM    355  CG  PRO A 373     223.249 159.412 231.428  1.00103.91           C  
ATOM    356  CD  PRO A 373     221.994 158.817 230.917  1.00103.91           C  
ATOM    357  N   PHE A 374     221.094 162.510 231.990  1.00 96.10           N  
ATOM    358  CA  PHE A 374     220.830 163.937 232.197  1.00 96.10           C  
ATOM    359  C   PHE A 374     219.346 164.086 232.491  1.00 96.10           C  
ATOM    360  O   PHE A 374     218.525 164.274 231.592  1.00 96.10           O  
ATOM    361  CB  PHE A 374     221.250 164.788 231.000  1.00 96.10           C  
ATOM    362  CG  PHE A 374     222.658 164.536 230.498  1.00 96.10           C  
ATOM    363  CD1 PHE A 374     223.686 164.148 231.353  1.00 96.10           C  
ATOM    364  CD2 PHE A 374     222.952 164.713 229.156  1.00 96.10           C  
ATOM    365  CE1 PHE A 374     224.963 163.924 230.877  1.00 96.10           C  
ATOM    366  CE2 PHE A 374     224.230 164.492 228.673  1.00 96.10           C  
ATOM    367  CZ  PHE A 374     225.236 164.098 229.537  1.00 96.10           C  
ATOM    368  N   PHE A 375     219.007 163.987 233.778  1.00 93.46           N  
ATOM    369  CA  PHE A 375     217.618 163.807 234.180  1.00 93.46           C  
ATOM    370  C   PHE A 375     216.813 165.087 234.000  1.00 93.46           C  
ATOM    371  O   PHE A 375     215.712 165.068 233.439  1.00 93.46           O  
ATOM    372  CB  PHE A 375     217.552 163.346 235.635  1.00 93.46           C  
ATOM    373  CG  PHE A 375     218.344 162.103 235.917  1.00 93.46           C  
ATOM    374  CD1 PHE A 375     218.152 160.957 235.161  1.00 93.46           C  
ATOM    375  CD2 PHE A 375     219.281 162.082 236.939  1.00 93.46           C  
ATOM    376  CE1 PHE A 375     218.881 159.808 235.420  1.00 93.46           C  
ATOM    377  CE2 PHE A 375     220.014 160.938 237.202  1.00 93.46           C  
ATOM    378  CZ  PHE A 375     219.814 159.801 236.442  1.00 93.46           C  
ATOM    379  N   THR A 376     217.348 166.207 234.468  1.00 83.37           N  
ATOM    380  CA  THR A 376     216.628 167.472 234.486  1.00 83.37           C  
ATOM    381  C   THR A 376     216.995 168.320 233.277  1.00 83.37           C  
ATOM    382  O   THR A 376     218.152 168.722 233.126  1.00 83.37           O  
ATOM    383  CB  THR A 376     216.928 168.235 235.774  1.00 83.37           C  
ATOM    384  OG1 THR A 376     216.523 167.449 236.900  1.00 83.37           O  
ATOM    385  CG2 THR A 376     216.180 169.549 235.788  1.00 83.37           C  
ATOM    386  N   PHE A 377     216.021 168.567 232.410  1.00 85.98           N  
ATOM    387  CA  PHE A 377     216.185 169.459 231.267  1.00 85.98           C  
ATOM    388  C   PHE A 377     215.094 170.527 231.330  1.00 85.98           C  
ATOM    389  O   PHE A 377     214.190 170.546 230.494  1.00 85.98           O  
ATOM    390  CB  PHE A 377     216.110 168.658 229.969  1.00 85.98           C  
ATOM    391  CG  PHE A 377     216.933 169.219 228.851  1.00 85.98           C  
ATOM    392  CD1 PHE A 377     216.557 170.389 228.213  1.00 85.98           C  
ATOM    393  CD2 PHE A 377     218.061 168.552 228.409  1.00 85.98           C  
ATOM    394  CE1 PHE A 377     217.307 170.898 227.171  1.00 85.98           C  
ATOM    395  CE2 PHE A 377     218.814 169.054 227.365  1.00 85.98           C  
ATOM    396  CZ  PHE A 377     218.438 170.230 226.748  1.00 85.98           C  
ATOM    397  N   LYS A 378     215.182 171.420 232.311  1.00 85.09           N  
ATOM    398  CA  LYS A 378     214.202 172.494 232.454  1.00 85.09           C  
ATOM    399  C   LYS A 378     214.609 173.651 231.556  1.00 85.09           C  
ATOM    400  O   LYS A 378     215.570 174.364 231.855  1.00 85.09           O  
ATOM    401  CB  LYS A 378     214.073 172.941 233.906  1.00 85.09           C  
ATOM    402  CG  LYS A 378     213.327 171.960 234.791  1.00 85.09           C  
ATOM    403  CD  LYS A 378     213.186 172.484 236.212  1.00 85.09           C  
ATOM    404  CE  LYS A 378     214.537 172.701 236.873  1.00 85.09           C  
ATOM    405  NZ  LYS A 378     214.423 173.509 238.118  1.00 85.09           N  
ATOM    406  N   CYS A 379     213.891 173.847 230.459  1.00 89.77           N  
ATOM    407  CA  CYS A 379     214.218 174.897 229.508  1.00 89.77           C  
ATOM    408  C   CYS A 379     213.178 176.009 229.583  1.00 89.77           C  
ATOM    409  O   CYS A 379     211.974 175.739 229.551  1.00 89.77           O  
ATOM    410  CB  CYS A 379     214.323 174.347 228.088  1.00 89.77           C  
ATOM    411  SG  CYS A 379     215.051 175.567 227.011  1.00 89.77           S  
ATOM    412  N   TYR A 380     213.645 177.252 229.693  1.00 86.62           N  
ATOM    413  CA  TYR A 380     212.785 178.416 229.877  1.00 86.62           C  
ATOM    414  C   TYR A 380     212.998 179.418 228.753  1.00 86.62           C  
ATOM    415  O   TYR A 380     214.138 179.713 228.384  1.00 86.62           O  
ATOM    416  CB  TYR A 380     213.043 179.122 231.211  1.00 86.62           C  
ATOM    417  CG  TYR A 380     213.415 178.231 232.365  1.00 86.62           C  
ATOM    418  CD1 TYR A 380     212.435 177.588 233.106  1.00 86.62           C  
ATOM    419  CD2 TYR A 380     214.740 178.041 232.721  1.00 86.62           C  
ATOM    420  CE1 TYR A 380     212.764 176.778 234.169  1.00 86.62           C  
ATOM    421  CE2 TYR A 380     215.080 177.231 233.781  1.00 86.62           C  
ATOM    422  CZ  TYR A 380     214.088 176.602 234.501  1.00 86.62           C  
ATOM    423  OH  TYR A 380     214.421 175.796 235.562  1.00 86.62           O  
ATOM    424  N   GLY A 381     211.896 179.935 228.217  1.00 90.98           N  
ATOM    425  CA  GLY A 381     211.922 180.982 227.220  1.00 90.98           C  
ATOM    426  C   GLY A 381     212.147 180.524 225.799  1.00 90.98           C  
ATOM    427  O   GLY A 381     212.177 181.371 224.896  1.00 90.98           O  
ATOM    428  N   VAL A 382     212.261 179.219 225.569  1.00 94.48           N  
ATOM    429  CA  VAL A 382     212.491 178.651 224.245  1.00 94.48           C  
ATOM    430  C   VAL A 382     212.142 177.170 224.338  1.00 94.48           C  
ATOM    431  O   VAL A 382     212.356 176.535 225.374  1.00 94.48           O  
ATOM    432  CB  VAL A 382     213.947 178.908 223.767  1.00 94.48           C  
ATOM    433  CG1 VAL A 382     214.965 178.419 224.775  1.00 94.48           C  
ATOM    434  CG2 VAL A 382     214.218 178.351 222.374  1.00 94.48           C  
ATOM    435  N   SER A 383     211.571 176.630 223.265  1.00100.99           N  
ATOM    436  CA  SER A 383     211.184 175.232 223.379  1.00100.99           C  
ATOM    437  C   SER A 383     212.363 174.327 223.033  1.00100.99           C  
ATOM    438  O   SER A 383     213.149 174.651 222.138  1.00100.99           O  
ATOM    439  CB  SER A 383     210.012 174.923 222.453  1.00100.99           C  
ATOM    440  OG  SER A 383     209.469 173.641 222.716  1.00100.99           O  
ATOM    441  N   PRO A 384     212.509 173.207 223.752  1.00101.35           N  
ATOM    442  CA  PRO A 384     213.601 172.268 223.443  1.00101.35           C  
ATOM    443  C   PRO A 384     213.482 171.608 222.083  1.00101.35           C  
ATOM    444  O   PRO A 384     214.505 171.178 221.536  1.00101.35           O  
ATOM    445  CB  PRO A 384     213.502 171.230 224.568  1.00101.35           C  
ATOM    446  CG  PRO A 384     212.101 171.354 225.075  1.00101.35           C  
ATOM    447  CD  PRO A 384     211.769 172.804 224.958  1.00101.35           C  
ATOM    448  N   THR A 385     212.277 171.510 221.523  1.00103.92           N  
ATOM    449  CA  THR A 385     212.119 170.877 220.219  1.00103.92           C  
ATOM    450  C   THR A 385     212.634 171.777 219.103  1.00103.92           C  
ATOM    451  O   THR A 385     213.202 171.291 218.119  1.00103.92           O  
ATOM    452  CB  THR A 385     210.654 170.520 219.985  1.00103.92           C  
ATOM    453  OG1 THR A 385     209.864 171.715 220.004  1.00103.92           O  
ATOM    454  CG2 THR A 385     210.160 169.576 221.067  1.00103.92           C  
ATOM    455  N   LYS A 386     212.452 173.088 219.240  1.00104.25           N  
ATOM    456  CA  LYS A 386     212.818 174.037 218.200  1.00104.25           C  
ATOM    457  C   LYS A 386     214.195 174.650 218.421  1.00104.25           C  
ATOM    458  O   LYS A 386     214.521 175.662 217.793  1.00104.25           O  
ATOM    459  CB  LYS A 386     211.746 175.125 218.080  1.00104.25           C  
ATOM    460  CG  LYS A 386     211.617 176.059 219.269  1.00104.25           C  
ATOM    461  CD  LYS A 386     210.502 177.065 219.027  1.00104.25           C  
ATOM    462  CE  LYS A 386     210.314 177.998 220.212  1.00104.25           C  
ATOM    463  NZ  LYS A 386     211.483 178.895 220.404  1.00104.25           N  
ATOM    464  N   LEU A 387     215.007 174.057 219.300  1.00103.06           N  
ATOM    465  CA  LEU A 387     216.386 174.506 219.473  1.00103.06           C  
ATOM    466  C   LEU A 387     217.229 174.232 218.238  1.00103.06           C  
ATOM    467  O   LEU A 387     218.161 174.988 217.945  1.00103.06           O  
ATOM    468  CB  LEU A 387     217.028 173.824 220.677  1.00103.06           C  
ATOM    469  CG  LEU A 387     216.515 174.163 222.067  1.00103.06           C  
ATOM    470  CD1 LEU A 387     217.231 173.319 223.099  1.00103.06           C  
ATOM    471  CD2 LEU A 387     216.761 175.627 222.325  1.00103.06           C  
ATOM    472  N   ASN A 388     216.920 173.161 217.510  1.00106.35           N  
ATOM    473  CA  ASN A 388     217.715 172.789 216.351  1.00106.35           C  
ATOM    474  C   ASN A 388     217.481 173.709 215.158  1.00106.35           C  
ATOM    475  O   ASN A 388     218.288 173.705 214.223  1.00106.35           O  
ATOM    476  CB  ASN A 388     217.414 171.344 215.968  1.00106.35           C  
ATOM    477  CG  ASN A 388     218.534 170.716 215.180  1.00106.35           C  
ATOM    478  OD1 ASN A 388     219.702 170.996 215.434  1.00106.35           O  
ATOM    479  ND2 ASN A 388     218.190 169.864 214.220  1.00106.35           N  
ATOM    480  N   ASP A 389     216.406 174.492 215.165  1.00105.15           N  
ATOM    481  CA  ASP A 389     216.079 175.392 214.066  1.00105.15           C  
ATOM    482  C   ASP A 389     216.457 176.836 214.353  1.00105.15           C  
ATOM    483  O   ASP A 389     216.970 177.525 213.466  1.00105.15           O  
ATOM    484  CB  ASP A 389     214.585 175.313 213.744  1.00105.15           C  
ATOM    485  CG  ASP A 389     214.077 173.889 213.703  1.00105.15           C  
ATOM    486  OD1 ASP A 389     214.821 173.008 213.225  1.00105.15           O  
ATOM    487  OD2 ASP A 389     212.936 173.648 214.150  1.00105.15           O  
ATOM    488  N   LEU A 390     216.189 177.309 215.567  1.00102.58           N  
ATOM    489  CA  LEU A 390     216.533 178.669 215.963  1.00102.58           C  
ATOM    490  C   LEU A 390     218.046 178.839 216.045  1.00102.58           C  
ATOM    491  O   LEU A 390     218.731 178.068 216.723  1.00102.58           O  
ATOM    492  CB  LEU A 390     215.883 179.009 217.302  1.00102.58           C  
ATOM    493  CG  LEU A 390     215.590 180.490 217.558  1.00102.58           C  
ATOM    494  CD1 LEU A 390     214.912 181.137 216.359  1.00102.58           C  
ATOM    495  CD2 LEU A 390     214.746 180.664 218.812  1.00102.58           C  
ATOM    496  N   CYS A 391     218.566 179.839 215.338  1.00 99.34           N  
ATOM    497  CA  CYS A 391     219.988 180.148 215.326  1.00 99.34           C  
ATOM    498  C   CYS A 391     220.274 181.389 216.163  1.00 99.34           C  
ATOM    499  O   CYS A 391     219.527 182.369 216.110  1.00 99.34           O  
ATOM    500  CB  CYS A 391     220.473 180.383 213.894  1.00 99.34           C  
ATOM    501  SG  CYS A 391     222.225 180.748 213.799  1.00 99.34           S  
ATOM    502  N   PHE A 392     221.366 181.344 216.928  1.00 91.83           N  
ATOM    503  CA  PHE A 392     221.731 182.410 217.852  1.00 91.83           C  
ATOM    504  C   PHE A 392     223.151 182.890 217.595  1.00 91.83           C  
ATOM    505  O   PHE A 392     223.957 182.212 216.954  1.00 91.83           O  
ATOM    506  CB  PHE A 392     221.621 181.982 219.321  1.00 91.83           C  
ATOM    507  CG  PHE A 392     220.545 180.983 219.587  1.00 91.83           C  
ATOM    508  CD1 PHE A 392     219.242 181.400 219.788  1.00 91.83           C  
ATOM    509  CD2 PHE A 392     220.832 179.631 219.646  1.00 91.83           C  
ATOM    510  CE1 PHE A 392     218.244 180.490 220.040  1.00 91.83           C  
ATOM    511  CE2 PHE A 392     219.835 178.711 219.893  1.00 91.83           C  
ATOM    512  CZ  PHE A 392     218.539 179.142 220.089  1.00 91.83           C  
ATOM    513  N   THR A 393     223.441 184.085 218.110  1.00 90.94           N  
ATOM    514  CA  THR A 393     224.753 184.685 217.911  1.00 90.94           C  
ATOM    515  C   THR A 393     225.798 184.023 218.797  1.00 90.94           C  
ATOM    516  O   THR A 393     226.885 183.668 218.328  1.00 90.94           O  
ATOM    517  CB  THR A 393     224.687 186.184 218.203  1.00 90.94           C  
ATOM    518  OG1 THR A 393     223.738 186.803 217.328  1.00 90.94           O  
ATOM    519  CG2 THR A 393     226.044 186.829 217.989  1.00 90.94           C  
ATOM    520  N   ASN A 394     225.481 183.827 220.077  1.00 84.84           N  
ATOM    521  CA  ASN A 394     226.444 183.261 221.012  1.00 84.84           C  
ATOM    522  C   ASN A 394     225.730 182.346 221.989  1.00 84.84           C  
ATOM    523  O   ASN A 394     224.570 182.581 222.347  1.00 84.84           O  
ATOM    524  CB  ASN A 394     227.200 184.336 221.794  1.00 84.84           C  
ATOM    525  CG  ASN A 394     228.309 184.971 220.991  1.00 84.84           C  
ATOM    526  OD1 ASN A 394     229.019 184.294 220.250  1.00 84.84           O  
ATOM    527  ND2 ASN A 394     228.475 186.279 221.142  1.00 84.84           N  
ATOM    528  N   VAL A 395     226.422 181.291 222.414  1.00 77.57           N  
ATOM    529  CA  VAL A 395     225.862 180.361 223.388  1.00 77.57           C  
ATOM    530  C   VAL A 395     226.803 180.303 224.580  1.00 77.57           C  
ATOM    531  O   VAL A 395     227.978 179.966 224.430  1.00 77.57           O  
ATOM    532  CB  VAL A 395     225.648 178.964 222.789  1.00 77.57           C  
ATOM    533  CG1 VAL A 395     225.290 177.971 223.875  1.00 77.57           C  
ATOM    534  CG2 VAL A 395     224.567 179.005 221.733  1.00 77.57           C  
ATOM    535  N   TYR A 396     226.292 180.604 225.763  1.00 71.14           N  
ATOM    536  CA  TYR A 396     227.098 180.601 226.974  1.00 71.14           C  
ATOM    537  C   TYR A 396     226.783 179.345 227.771  1.00 71.14           C  
ATOM    538  O   TYR A 396     225.631 179.120 228.147  1.00 71.14           O  
ATOM    539  CB  TYR A 396     226.825 181.852 227.800  1.00 71.14           C  
ATOM    540  CG  TYR A 396     227.489 183.084 227.247  1.00 71.14           C  
ATOM    541  CD1 TYR A 396     228.844 183.085 226.950  1.00 71.14           C  
ATOM    542  CD2 TYR A 396     226.762 184.238 227.000  1.00 71.14           C  
ATOM    543  CE1 TYR A 396     229.459 184.205 226.440  1.00 71.14           C  
ATOM    544  CE2 TYR A 396     227.367 185.363 226.488  1.00 71.14           C  
ATOM    545  CZ  TYR A 396     228.716 185.339 226.209  1.00 71.14           C  
ATOM    546  OH  TYR A 396     229.329 186.458 225.699  1.00 71.14           O  
ATOM    547  N   ALA A 397     227.801 178.536 228.026  1.00 64.35           N  
ATOM    548  CA  ALA A 397     227.671 177.308 228.799  1.00 64.35           C  
ATOM    549  C   ALA A 397     228.333 177.549 230.149  1.00 64.35           C  
ATOM    550  O   ALA A 397     229.562 177.579 230.248  1.00 64.35           O  
ATOM    551  CB  ALA A 397     228.300 176.133 228.064  1.00 64.35           C  
ATOM    552  N   ASP A 398     227.518 177.782 231.173  1.00 61.47           N  
ATOM    553  CA  ASP A 398     228.003 177.973 232.533  1.00 61.47           C  
ATOM    554  C   ASP A 398     227.922 176.646 233.270  1.00 61.47           C  
ATOM    555  O   ASP A 398     226.846 176.068 233.392  1.00 61.47           O  
ATOM    556  CB  ASP A 398     227.194 179.042 233.260  1.00 61.47           C  
ATOM    557  CG  ASP A 398     227.005 180.287 232.430  1.00 61.47           C  
ATOM    558  OD1 ASP A 398     228.018 180.870 232.000  1.00 61.47           O  
ATOM    559  OD2 ASP A 398     225.846 180.690 232.209  1.00 61.47           O  
ATOM    560  N   SER A 399     229.047 176.182 233.786  1.00 58.36           N  
ATOM    561  CA  SER A 399     229.141 174.857 234.373  1.00 58.36           C  
ATOM    562  C   SER A 399     229.639 174.956 235.804  1.00 58.36           C  
ATOM    563  O   SER A 399     230.588 175.703 236.088  1.00 58.36           O  
ATOM    564  CB  SER A 399     230.066 173.966 233.546  1.00 58.36           C  
ATOM    565  OG  SER A 399     231.423 174.199 233.868  1.00 58.36           O  
ATOM    566  N   PHE A 400     228.963 174.232 236.699  1.00 53.63           N  
ATOM    567  CA  PHE A 400     229.299 174.210 238.117  1.00 53.63           C  
ATOM    568  C   PHE A 400     228.705 172.954 238.745  1.00 53.63           C  
ATOM    569  O   PHE A 400     228.059 172.145 238.075  1.00 53.63           O  
ATOM    570  CB  PHE A 400     228.816 175.471 238.838  1.00 53.63           C  
ATOM    571  CG  PHE A 400     227.402 175.858 238.531  1.00 53.63           C  
ATOM    572  CD1 PHE A 400     226.354 175.338 239.268  1.00 53.63           C  
ATOM    573  CD2 PHE A 400     227.123 176.776 237.538  1.00 53.63           C  
ATOM    574  CE1 PHE A 400     225.061 175.700 239.000  1.00 53.63           C  
ATOM    575  CE2 PHE A 400     225.829 177.136 237.264  1.00 53.63           C  
ATOM    576  CZ  PHE A 400     224.798 176.600 237.998  1.00 53.63           C  
ATOM    577  N   VAL A 401     228.945 172.790 240.045  1.00 53.79           N  
ATOM    578  CA  VAL A 401     228.492 171.634 240.812  1.00 53.79           C  
ATOM    579  C   VAL A 401     227.772 172.144 242.053  1.00 53.79           C  
ATOM    580  O   VAL A 401     228.323 172.960 242.799  1.00 53.79           O  
ATOM    581  CB  VAL A 401     229.664 170.712 241.202  1.00 53.79           C  
ATOM    582  CG1 VAL A 401     229.252 169.729 242.276  1.00 53.79           C  
ATOM    583  CG2 VAL A 401     230.157 169.963 240.002  1.00 53.79           C  
ATOM    584  N   ILE A 402     226.546 171.671 242.275  1.00 53.32           N  
ATOM    585  CA  ILE A 402     225.789 172.031 243.472  1.00 53.32           C  
ATOM    586  C   ILE A 402     225.224 170.768 244.097  1.00 53.32           C  
ATOM    587  O   ILE A 402     225.564 169.661 243.682  1.00 53.32           O  
ATOM    588  CB  ILE A 402     224.663 173.030 243.169  1.00 53.32           C  
ATOM    589  CG1 ILE A 402     223.893 172.603 241.930  1.00 53.32           C  
ATOM    590  CG2 ILE A 402     225.218 174.410 243.002  1.00 53.32           C  
ATOM    591  CD1 ILE A 402     222.747 173.498 241.617  1.00 53.32           C  
ATOM    592  N   ARG A 403     224.390 170.916 245.120  1.00 58.00           N  
ATOM    593  CA  ARG A 403     223.802 169.758 245.767  1.00 58.00           C  
ATOM    594  C   ARG A 403     222.508 169.397 245.050  1.00 58.00           C  
ATOM    595  O   ARG A 403     222.127 170.019 244.061  1.00 58.00           O  
ATOM    596  CB  ARG A 403     223.540 170.045 247.242  1.00 58.00           C  
ATOM    597  CG  ARG A 403     224.603 169.550 248.178  1.00 58.00           C  
ATOM    598  CD  ARG A 403     224.168 169.473 249.640  1.00 58.00           C  
ATOM    599  NE  ARG A 403     223.516 170.670 250.158  1.00 58.00           N  
ATOM    600  CZ  ARG A 403     222.218 170.775 250.410  1.00 58.00           C  
ATOM    601  NH1 ARG A 403     221.387 169.774 250.182  1.00 58.00           N  
ATOM    602  NH2 ARG A 403     221.746 171.909 250.915  1.00 58.00           N  
ATOM    603  N   GLY A 404     221.818 168.376 245.555  1.00 61.06           N  
ATOM    604  CA  GLY A 404     220.558 167.981 244.947  1.00 61.06           C  
ATOM    605  C   GLY A 404     219.436 168.962 245.225  1.00 61.06           C  
ATOM    606  O   GLY A 404     218.629 169.260 244.343  1.00 61.06           O  
ATOM    607  N   ASP A 405     219.372 169.477 246.455  1.00 68.12           N  
ATOM    608  CA  ASP A 405     218.278 170.350 246.858  1.00 68.12           C  
ATOM    609  C   ASP A 405     218.364 171.735 246.241  1.00 68.12           C  
ATOM    610  O   ASP A 405     217.359 172.450 246.225  1.00 68.12           O  
ATOM    611  CB  ASP A 405     218.234 170.480 248.379  1.00 68.12           C  
ATOM    612  CG  ASP A 405     217.800 169.205 249.058  1.00 68.12           C  
ATOM    613  OD1 ASP A 405     217.026 168.445 248.442  1.00 68.12           O  
ATOM    614  OD2 ASP A 405     218.224 168.965 250.208  1.00 68.12           O  
ATOM    615  N   GLU A 406     219.532 172.145 245.759  1.00 64.78           N  
ATOM    616  CA  GLU A 406     219.695 173.478 245.205  1.00 64.78           C  
ATOM    617  C   GLU A 406     219.680 173.496 243.685  1.00 64.78           C  
ATOM    618  O   GLU A 406     220.001 174.526 243.091  1.00 64.78           O  
ATOM    619  CB  GLU A 406     220.976 174.116 245.744  1.00 64.78           C  
ATOM    620  CG  GLU A 406     220.966 174.242 247.256  1.00 64.78           C  
ATOM    621  CD  GLU A 406     222.322 174.088 247.896  1.00 64.78           C  
ATOM    622  OE1 GLU A 406     222.690 172.957 248.229  1.00 64.78           O  
ATOM    623  OE2 GLU A 406     223.011 175.098 248.115  1.00 64.78           O  
ATOM    624  N   VAL A 407     219.298 172.387 243.047  1.00 65.42           N  
ATOM    625  CA  VAL A 407     219.089 172.379 241.601  1.00 65.42           C  
ATOM    626  C   VAL A 407     217.902 173.259 241.232  1.00 65.42           C  
ATOM    627  O   VAL A 407     217.921 173.959 240.212  1.00 65.42           O  
ATOM    628  CB  VAL A 407     218.920 170.932 241.101  1.00 65.42           C  
ATOM    629  CG1 VAL A 407     218.652 170.891 239.615  1.00 65.42           C  
ATOM    630  CG2 VAL A 407     220.161 170.133 241.401  1.00 65.42           C  
ATOM    631  N   ARG A 408     216.870 173.277 242.078  1.00 71.04           N  
ATOM    632  CA  ARG A 408     215.689 174.089 241.811  1.00 71.04           C  
ATOM    633  C   ARG A 408     215.964 175.580 241.928  1.00 71.04           C  
ATOM    634  O   ARG A 408     215.170 176.382 241.429  1.00 71.04           O  
ATOM    635  CB  ARG A 408     214.558 173.717 242.765  1.00 71.04           C  
ATOM    636  CG  ARG A 408     215.005 173.527 244.192  1.00 71.04           C  
ATOM    637  CD  ARG A 408     213.898 173.861 245.165  1.00 71.04           C  
ATOM    638  NE  ARG A 408     213.631 175.293 245.191  1.00 71.04           N  
ATOM    639  CZ  ARG A 408     214.238 176.150 246.000  1.00 71.04           C  
ATOM    640  NH1 ARG A 408     215.158 175.753 246.863  1.00 71.04           N  
ATOM    641  NH2 ARG A 408     213.918 177.439 245.937  1.00 71.04           N  
ATOM    642  N   GLN A 409     217.058 175.973 242.574  1.00 67.80           N  
ATOM    643  CA  GLN A 409     217.390 177.383 242.672  1.00 67.80           C  
ATOM    644  C   GLN A 409     218.044 177.915 241.408  1.00 67.80           C  
ATOM    645  O   GLN A 409     218.195 179.132 241.275  1.00 67.80           O  
ATOM    646  CB  GLN A 409     218.313 177.623 243.860  1.00 67.80           C  
ATOM    647  CG  GLN A 409     217.914 176.831 245.074  1.00 67.80           C  
ATOM    648  CD  GLN A 409     218.519 177.357 246.343  1.00 67.80           C  
ATOM    649  OE1 GLN A 409     217.807 177.812 247.227  1.00 67.80           O  
ATOM    650  NE2 GLN A 409     219.836 177.328 246.431  1.00 67.80           N  
ATOM    651  N   ILE A 410     218.433 177.042 240.484  1.00 64.68           N  
ATOM    652  CA  ILE A 410     218.937 177.482 239.175  1.00 64.68           C  
ATOM    653  C   ILE A 410     217.710 177.623 238.285  1.00 64.68           C  
ATOM    654  O   ILE A 410     217.371 176.759 237.474  1.00 64.68           O  
ATOM    655  CB  ILE A 410     219.977 176.519 238.606  1.00 64.68           C  
ATOM    656  CG1 ILE A 410     221.000 176.163 239.677  1.00 64.68           C  
ATOM    657  CG2 ILE A 410     220.668 177.136 237.414  1.00 64.68           C  
ATOM    658  CD1 ILE A 410     221.852 177.319 240.108  1.00 64.68           C  
ATOM    659  N   ALA A 411     217.044 178.760 238.426  1.00 74.45           N  
ATOM    660  CA  ALA A 411     215.784 179.055 237.760  1.00 74.45           C  
ATOM    661  C   ALA A 411     215.531 180.551 237.893  1.00 74.45           C  
ATOM    662  O   ALA A 411     216.072 181.187 238.799  1.00 74.45           O  
ATOM    663  CB  ALA A 411     214.623 178.254 238.375  1.00 74.45           C  
ATOM    664  N   PRO A 412     214.739 181.135 236.995  1.00 79.58           N  
ATOM    665  CA  PRO A 412     214.370 182.543 237.166  1.00 79.58           C  
ATOM    666  C   PRO A 412     213.450 182.744 238.358  1.00 79.58           C  
ATOM    667  O   PRO A 412     212.508 181.981 238.575  1.00 79.58           O  
ATOM    668  CB  PRO A 412     213.657 182.880 235.853  1.00 79.58           C  
ATOM    669  CG  PRO A 412     214.212 181.918 234.881  1.00 79.58           C  
ATOM    670  CD  PRO A 412     214.388 180.652 235.649  1.00 79.58           C  
ATOM    671  N   GLY A 413     213.740 183.781 239.138  1.00 80.12           N  
ATOM    672  CA  GLY A 413     212.870 184.158 240.231  1.00 80.12           C  
ATOM    673  C   GLY A 413     213.022 183.362 241.505  1.00 80.12           C  
ATOM    674  O   GLY A 413     212.223 183.551 242.428  1.00 80.12           O  
ATOM    675  N   GLN A 414     214.012 182.483 241.595  1.00 78.00           N  
ATOM    676  CA  GLN A 414     214.199 181.684 242.795  1.00 78.00           C  
ATOM    677  C   GLN A 414     215.196 182.348 243.735  1.00 78.00           C  
ATOM    678  O   GLN A 414     215.951 183.243 243.350  1.00 78.00           O  
ATOM    679  CB  GLN A 414     214.678 180.279 242.441  1.00 78.00           C  
ATOM    680  CG  GLN A 414     213.635 179.440 241.744  1.00 78.00           C  
ATOM    681  CD  GLN A 414     212.634 178.844 242.704  1.00 78.00           C  
ATOM    682  OE1 GLN A 414     212.884 178.758 243.905  1.00 78.00           O  
ATOM    683  NE2 GLN A 414     211.489 178.428 242.181  1.00 78.00           N  
ATOM    684  N   THR A 415     215.184 181.899 244.987  1.00 74.35           N  
ATOM    685  CA  THR A 415     216.038 182.473 246.012  1.00 74.35           C  
ATOM    686  C   THR A 415     216.635 181.359 246.859  1.00 74.35           C  
ATOM    687  O   THR A 415     216.165 180.220 246.850  1.00 74.35           O  
ATOM    688  CB  THR A 415     215.272 183.466 246.897  1.00 74.35           C  
ATOM    689  OG1 THR A 415     216.187 184.124 247.780  1.00 74.35           O  
ATOM    690  CG2 THR A 415     214.207 182.753 247.713  1.00 74.35           C  
ATOM    691  N   GLY A 416     217.677 181.708 247.590  1.00 68.08           N  
ATOM    692  CA  GLY A 416     218.401 180.765 248.412  1.00 68.08           C  
ATOM    693  C   GLY A 416     219.853 181.182 248.469  1.00 68.08           C  
ATOM    694  O   GLY A 416     220.203 182.279 248.067  1.00 68.08           O  
ATOM    695  N   ASN A 417     220.699 180.286 248.981  1.00 65.99           N  
ATOM    696  CA  ASN A 417     222.126 180.595 249.027  1.00 65.99           C  
ATOM    697  C   ASN A 417     222.746 180.639 247.635  1.00 65.99           C  
ATOM    698  O   ASN A 417     223.543 181.535 247.340  1.00 65.99           O  
ATOM    699  CB  ASN A 417     222.862 179.591 249.908  1.00 65.99           C  
ATOM    700  CG  ASN A 417     222.342 179.576 251.325  1.00 65.99           C  
ATOM    701  OD1 ASN A 417     222.133 180.626 251.930  1.00 65.99           O  
ATOM    702  ND2 ASN A 417     222.130 178.384 251.865  1.00 65.99           N  
ATOM    703  N   ILE A 418     222.352 179.720 246.750  1.00 60.76           N  
ATOM    704  CA  ILE A 418     222.954 179.669 245.421  1.00 60.76           C  
ATOM    705  C   ILE A 418     222.449 180.813 244.558  1.00 60.76           C  
ATOM    706  O   ILE A 418     223.223 181.447 243.832  1.00 60.76           O  
ATOM    707  CB  ILE A 418     222.682 178.306 244.762  1.00 60.76           C  
ATOM    708  CG1 ILE A 418     223.168 177.181 245.661  1.00 60.76           C  
ATOM    709  CG2 ILE A 418     223.371 178.201 243.422  1.00 60.76           C  
ATOM    710  CD1 ILE A 418     224.630 177.258 246.000  1.00 60.76           C  
ATOM    711  N   ALA A 419     221.152 181.103 244.631  1.00 62.65           N  
ATOM    712  CA  ALA A 419     220.582 182.136 243.779  1.00 62.65           C  
ATOM    713  C   ALA A 419     221.012 183.524 244.229  1.00 62.65           C  
ATOM    714  O   ALA A 419     221.317 184.384 243.398  1.00 62.65           O  
ATOM    715  CB  ALA A 419     219.061 182.019 243.763  1.00 62.65           C  
ATOM    716  N   ASP A 420     221.038 183.767 245.538  1.00 66.16           N  
ATOM    717  CA  ASP A 420     221.439 185.082 246.018  1.00 66.16           C  
ATOM    718  C   ASP A 420     222.945 185.283 245.934  1.00 66.16           C  
ATOM    719  O   ASP A 420     223.402 186.358 245.536  1.00 66.16           O  
ATOM    720  CB  ASP A 420     220.970 185.300 247.453  1.00 66.16           C  
ATOM    721  CG  ASP A 420     219.466 185.403 247.565  1.00 66.16           C  
ATOM    722  OD1 ASP A 420     218.824 185.854 246.594  1.00 66.16           O  
ATOM    723  OD2 ASP A 420     218.922 185.029 248.624  1.00 66.16           O  
ATOM    724  N   TYR A 421     223.736 184.280 246.320  1.00 61.09           N  
ATOM    725  CA  TYR A 421     225.139 184.525 246.607  1.00 61.09           C  
ATOM    726  C   TYR A 421     226.107 183.847 245.651  1.00 61.09           C  
ATOM    727  O   TYR A 421     227.271 184.248 245.602  1.00 61.09           O  
ATOM    728  CB  TYR A 421     225.477 184.074 248.034  1.00 61.09           C  
ATOM    729  CG  TYR A 421     224.601 184.677 249.106  1.00 61.09           C  
ATOM    730  CD1 TYR A 421     224.208 186.005 249.048  1.00 61.09           C  
ATOM    731  CD2 TYR A 421     224.197 183.924 250.196  1.00 61.09           C  
ATOM    732  CE1 TYR A 421     223.419 186.560 250.029  1.00 61.09           C  
ATOM    733  CE2 TYR A 421     223.410 184.470 251.186  1.00 61.09           C  
ATOM    734  CZ  TYR A 421     223.024 185.787 251.097  1.00 61.09           C  
ATOM    735  OH  TYR A 421     222.238 186.333 252.082  1.00 61.09           O  
ATOM    736  N   ASN A 422     225.675 182.835 244.903  1.00 57.79           N  
ATOM    737  CA  ASN A 422     226.591 182.052 244.081  1.00 57.79           C  
ATOM    738  C   ASN A 422     226.320 182.191 242.591  1.00 57.79           C  
ATOM    739  O   ASN A 422     227.230 182.554 241.842  1.00 57.79           O  
ATOM    740  CB  ASN A 422     226.543 180.578 244.491  1.00 57.79           C  
ATOM    741  CG  ASN A 422     226.952 180.365 245.920  1.00 57.79           C  
ATOM    742  OD1 ASN A 422     228.119 180.124 246.205  1.00 57.79           O  
ATOM    743  ND2 ASN A 422     225.998 180.458 246.832  1.00 57.79           N  
ATOM    744  N   TYR A 423     225.107 181.906 242.132  1.00 57.84           N  
ATOM    745  CA  TYR A 423     224.787 181.979 240.713  1.00 57.84           C  
ATOM    746  C   TYR A 423     223.358 182.463 240.554  1.00 57.84           C  
ATOM    747  O   TYR A 423     222.422 181.782 240.977  1.00 57.84           O  
ATOM    748  CB  TYR A 423     224.964 180.611 240.052  1.00 57.84           C  
ATOM    749  CG  TYR A 423     224.862 180.638 238.555  1.00 57.84           C  
ATOM    750  CD1 TYR A 423     225.910 181.097 237.780  1.00 57.84           C  
ATOM    751  CD2 TYR A 423     223.713 180.206 237.915  1.00 57.84           C  
ATOM    752  CE1 TYR A 423     225.818 181.127 236.410  1.00 57.84           C  
ATOM    753  CE2 TYR A 423     223.612 180.233 236.545  1.00 57.84           C  
ATOM    754  CZ  TYR A 423     224.668 180.695 235.800  1.00 57.84           C  
ATOM    755  OH  TYR A 423     224.574 180.725 234.434  1.00 57.84           O  
ATOM    756  N   LYS A 424     223.190 183.616 239.920  1.00 64.07           N  
ATOM    757  CA  LYS A 424     221.885 184.237 239.760  1.00 64.07           C  
ATOM    758  C   LYS A 424     221.493 184.231 238.291  1.00 64.07           C  
ATOM    759  O   LYS A 424     222.281 184.637 237.433  1.00 64.07           O  
ATOM    760  CB  LYS A 424     221.886 185.664 240.306  1.00 64.07           C  
ATOM    761  CG  LYS A 424     220.589 186.407 240.075  1.00 64.07           C  
ATOM    762  CD  LYS A 424     219.488 185.849 240.953  1.00 64.07           C  
ATOM    763  CE  LYS A 424     218.484 186.917 241.315  1.00 64.07           C  
ATOM    764  NZ  LYS A 424     219.145 188.073 241.976  1.00 64.07           N  
ATOM    765  N   LEU A 425     220.279 183.774 238.010  1.00 70.59           N  
ATOM    766  CA  LEU A 425     219.646 183.761 236.703  1.00 70.59           C  
ATOM    767  C   LEU A 425     218.680 184.931 236.572  1.00 70.59           C  
ATOM    768  O   LEU A 425     217.964 185.250 237.526  1.00 70.59           O  
ATOM    769  CB  LEU A 425     218.886 182.454 236.486  1.00 70.59           C  
ATOM    770  CG  LEU A 425     219.675 181.294 235.888  1.00 70.59           C  
ATOM    771  CD1 LEU A 425     218.754 180.134 235.597  1.00 70.59           C  
ATOM    772  CD2 LEU A 425     220.388 181.727 234.635  1.00 70.59           C  
ATOM    773  N   PRO A 426     218.639 185.594 235.420  1.00 76.78           N  
ATOM    774  CA  PRO A 426     217.666 186.670 235.218  1.00 76.78           C  
ATOM    775  C   PRO A 426     216.255 186.127 235.072  1.00 76.78           C  
ATOM    776  O   PRO A 426     216.037 184.945 234.805  1.00 76.78           O  
ATOM    777  CB  PRO A 426     218.134 187.333 233.922  1.00 76.78           C  
ATOM    778  CG  PRO A 426     218.857 186.262 233.204  1.00 76.78           C  
ATOM    779  CD  PRO A 426     219.508 185.412 234.247  1.00 76.78           C  
ATOM    780  N   ASP A 427     215.282 187.015 235.280  1.00 85.47           N  
ATOM    781  CA  ASP A 427     213.886 186.620 235.119  1.00 85.47           C  
ATOM    782  C   ASP A 427     213.525 186.430 233.650  1.00 85.47           C  
ATOM    783  O   ASP A 427     212.736 185.542 233.309  1.00 85.47           O  
ATOM    784  CB  ASP A 427     212.972 187.653 235.772  1.00 85.47           C  
ATOM    785  CG  ASP A 427     213.251 187.818 237.249  1.00 85.47           C  
ATOM    786  OD1 ASP A 427     213.616 186.817 237.899  1.00 85.47           O  
ATOM    787  OD2 ASP A 427     213.108 188.947 237.762  1.00 85.47           O  
ATOM    788  N   ASP A 428     214.102 187.241 232.767  1.00 84.63           N  
ATOM    789  CA  ASP A 428     213.884 187.106 231.328  1.00 84.63           C  
ATOM    790  C   ASP A 428     214.984 186.249 230.702  1.00 84.63           C  
ATOM    791  O   ASP A 428     215.721 186.664 229.810  1.00 84.63           O  
ATOM    792  CB  ASP A 428     213.806 188.481 230.676  1.00 84.63           C  
ATOM    793  CG  ASP A 428     214.933 189.397 231.110  1.00 84.63           C  
ATOM    794  OD1 ASP A 428     215.722 189.000 231.991  1.00 84.63           O  
ATOM    795  OD2 ASP A 428     215.030 190.516 230.567  1.00 84.63           O  
ATOM    796  N   PHE A 429     215.079 185.021 231.193  1.00 77.93           N  
ATOM    797  CA  PHE A 429     216.182 184.138 230.846  1.00 77.93           C  
ATOM    798  C   PHE A 429     215.801 183.278 229.650  1.00 77.93           C  
ATOM    799  O   PHE A 429     214.844 182.500 229.710  1.00 77.93           O  
ATOM    800  CB  PHE A 429     216.563 183.277 232.047  1.00 77.93           C  
ATOM    801  CG  PHE A 429     217.524 182.184 231.726  1.00 77.93           C  
ATOM    802  CD1 PHE A 429     218.803 182.475 231.289  1.00 77.93           C  
ATOM    803  CD2 PHE A 429     217.164 180.864 231.906  1.00 77.93           C  
ATOM    804  CE1 PHE A 429     219.688 181.466 231.001  1.00 77.93           C  
ATOM    805  CE2 PHE A 429     218.049 179.855 231.629  1.00 77.93           C  
ATOM    806  CZ  PHE A 429     219.308 180.156 231.170  1.00 77.93           C  
ATOM    807  N   THR A 430     216.556 183.425 228.569  1.00 81.86           N  
ATOM    808  CA  THR A 430     216.335 182.703 227.321  1.00 81.86           C  
ATOM    809  C   THR A 430     217.408 181.628 227.248  1.00 81.86           C  
ATOM    810  O   THR A 430     218.551 181.904 226.880  1.00 81.86           O  
ATOM    811  CB  THR A 430     216.399 183.636 226.118  1.00 81.86           C  
ATOM    812  OG1 THR A 430     217.701 184.228 226.043  1.00 81.86           O  
ATOM    813  CG2 THR A 430     215.359 184.737 226.245  1.00 81.86           C  
ATOM    814  N   GLY A 431     217.048 180.412 227.616  1.00 79.39           N  
ATOM    815  CA  GLY A 431     218.021 179.342 227.661  1.00 79.39           C  
ATOM    816  C   GLY A 431     217.552 178.231 228.564  1.00 79.39           C  
ATOM    817  O   GLY A 431     216.560 178.349 229.279  1.00 79.39           O  
ATOM    818  N   CYS A 432     218.258 177.114 228.478  1.00 80.10           N  
ATOM    819  CA  CYS A 432     217.873 175.939 229.239  1.00 80.10           C  
ATOM    820  C   CYS A 432     218.902 175.648 230.320  1.00 80.10           C  
ATOM    821  O   CYS A 432     220.047 176.095 230.254  1.00 80.10           O  
ATOM    822  CB  CYS A 432     217.736 174.708 228.334  1.00 80.10           C  
ATOM    823  SG  CYS A 432     216.957 174.920 226.698  1.00 80.10           S  
ATOM    824  N   VAL A 433     218.475 174.922 231.347  1.00 70.99           N  
ATOM    825  CA  VAL A 433     219.381 174.431 232.376  1.00 70.99           C  
ATOM    826  C   VAL A 433     219.384 172.914 232.269  1.00 70.99           C  
ATOM    827  O   VAL A 433     218.377 172.303 231.891  1.00 70.99           O  
ATOM    828  CB  VAL A 433     219.022 174.927 233.796  1.00 70.99           C  
ATOM    829  CG1 VAL A 433     218.758 176.414 233.780  1.00 70.99           C  
ATOM    830  CG2 VAL A 433     217.828 174.207 234.386  1.00 70.99           C  
ATOM    831  N   ILE A 434     220.542 172.312 232.507  1.00 67.09           N  
ATOM    832  CA  ILE A 434     220.718 170.870 232.439  1.00 67.09           C  
ATOM    833  C   ILE A 434     221.412 170.446 233.718  1.00 67.09           C  
ATOM    834  O   ILE A 434     222.431 171.029 234.091  1.00 67.09           O  
ATOM    835  CB  ILE A 434     221.546 170.462 231.204  1.00 67.09           C  
ATOM    836  CG1 ILE A 434     220.844 170.897 229.919  1.00 67.09           C  
ATOM    837  CG2 ILE A 434     221.781 168.971 231.181  1.00 67.09           C  
ATOM    838  CD1 ILE A 434     221.680 170.789 228.699  1.00 67.09           C  
ATOM    839  N   ALA A 435     220.862 169.457 234.401  1.00 64.40           N  
ATOM    840  CA  ALA A 435     221.458 169.011 235.646  1.00 64.40           C  
ATOM    841  C   ALA A 435     221.414 167.499 235.699  1.00 64.40           C  
ATOM    842  O   ALA A 435     220.428 166.889 235.284  1.00 64.40           O  
ATOM    843  CB  ALA A 435     220.737 169.600 236.853  1.00 64.40           C  
ATOM    844  N   TRP A 436     222.477 166.896 236.215  1.00 62.36           N  
ATOM    845  CA  TRP A 436     222.451 165.452 236.372  1.00 62.36           C  
ATOM    846  C   TRP A 436     223.246 165.052 237.600  1.00 62.36           C  
ATOM    847  O   TRP A 436     224.159 165.760 238.030  1.00 62.36           O  
ATOM    848  CB  TRP A 436     222.978 164.730 235.127  1.00 62.36           C  
ATOM    849  CG  TRP A 436     224.422 164.922 234.840  1.00 62.36           C  
ATOM    850  CD1 TRP A 436     225.436 164.070 235.143  1.00 62.36           C  
ATOM    851  CD2 TRP A 436     225.012 166.016 234.138  1.00 62.36           C  
ATOM    852  NE1 TRP A 436     226.628 164.579 234.700  1.00 62.36           N  
ATOM    853  CE2 TRP A 436     226.392 165.773 234.075  1.00 62.36           C  
ATOM    854  CE3 TRP A 436     224.507 167.185 233.569  1.00 62.36           C  
ATOM    855  CZ2 TRP A 436     227.272 166.654 233.467  1.00 62.36           C  
ATOM    856  CZ3 TRP A 436     225.380 168.055 232.970  1.00 62.36           C  
ATOM    857  CH2 TRP A 436     226.748 167.788 232.922  1.00 62.36           C  
ATOM    858  N   ASN A 437     222.887 163.901 238.152  1.00 60.30           N  
ATOM    859  CA  ASN A 437     223.573 163.376 239.319  1.00 60.30           C  
ATOM    860  C   ASN A 437     224.974 162.927 238.941  1.00 60.30           C  
ATOM    861  O   ASN A 437     225.187 162.314 237.893  1.00 60.30           O  
ATOM    862  CB  ASN A 437     222.777 162.212 239.903  1.00 60.30           C  
ATOM    863  CG  ASN A 437     223.307 161.746 241.234  1.00 60.30           C  
ATOM    864  OD1 ASN A 437     224.326 161.070 241.306  1.00 60.30           O  
ATOM    865  ND2 ASN A 437     222.601 162.082 242.299  1.00 60.30           N  
ATOM    866  N   SER A 438     225.934 163.229 239.806  1.00 60.02           N  
ATOM    867  CA  SER A 438     227.314 162.823 239.593  1.00 60.02           C  
ATOM    868  C   SER A 438     227.902 162.291 240.890  1.00 60.02           C  
ATOM    869  O   SER A 438     228.988 162.684 241.313  1.00 60.02           O  
ATOM    870  CB  SER A 438     228.144 163.978 239.049  1.00 60.02           C  
ATOM    871  OG  SER A 438     228.276 165.000 240.013  1.00 60.02           O  
ATOM    872  N   ASN A 439     227.167 161.392 241.547  1.00 64.69           N  
ATOM    873  CA  ASN A 439     227.649 160.811 242.793  1.00 64.69           C  
ATOM    874  C   ASN A 439     228.829 159.879 242.556  1.00 64.69           C  
ATOM    875  O   ASN A 439     229.675 159.718 243.438  1.00 64.69           O  
ATOM    876  CB  ASN A 439     226.523 160.069 243.505  1.00 64.69           C  
ATOM    877  CG  ASN A 439     226.820 159.834 244.961  1.00 64.69           C  
ATOM    878  OD1 ASN A 439     227.397 160.686 245.631  1.00 64.69           O  
ATOM    879  ND2 ASN A 439     226.426 158.675 245.465  1.00 64.69           N  
ATOM    880  N   LYS A 440     228.903 159.260 241.379  1.00 70.53           N  
ATOM    881  CA  LYS A 440     229.985 158.323 241.108  1.00 70.53           C  
ATOM    882  C   LYS A 440     231.294 159.049 240.844  1.00 70.53           C  
ATOM    883  O   LYS A 440     232.370 158.480 241.055  1.00 70.53           O  
ATOM    884  CB  LYS A 440     229.646 157.418 239.912  1.00 70.53           C  
ATOM    885  CG  LYS A 440     228.187 156.898 239.715  1.00 70.53           C  
ATOM    886  CD  LYS A 440     227.378 156.394 240.942  1.00 70.53           C  
ATOM    887  CE  LYS A 440     228.105 155.338 241.791  1.00 70.53           C  
ATOM    888  NZ  LYS A 440     227.261 154.843 242.914  1.00 70.53           N  
ATOM    889  N   LEU A 441     231.223 160.295 240.385  1.00 66.29           N  
ATOM    890  CA  LEU A 441     232.396 161.061 239.993  1.00 66.29           C  
ATOM    891  C   LEU A 441     232.874 162.008 241.081  1.00 66.29           C  
ATOM    892  O   LEU A 441     234.079 162.104 241.327  1.00 66.29           O  
ATOM    893  CB  LEU A 441     232.091 161.865 238.730  1.00 66.29           C  
ATOM    894  CG  LEU A 441     231.914 161.052 237.453  1.00 66.29           C  
ATOM    895  CD1 LEU A 441     231.470 161.955 236.320  1.00 66.29           C  
ATOM    896  CD2 LEU A 441     233.208 160.344 237.105  1.00 66.29           C  
ATOM    897  N   ASP A 442     231.953 162.711 241.737  1.00 63.47           N  
ATOM    898  CA  ASP A 442     232.276 163.845 242.589  1.00 63.47           C  
ATOM    899  C   ASP A 442     232.232 163.520 244.074  1.00 63.47           C  
ATOM    900  O   ASP A 442     232.275 164.440 244.893  1.00 63.47           O  
ATOM    901  CB  ASP A 442     231.332 165.006 242.291  1.00 63.47           C  
ATOM    902  CG  ASP A 442     231.558 165.602 240.927  1.00 63.47           C  
ATOM    903  OD1 ASP A 442     232.703 165.551 240.438  1.00 63.47           O  
ATOM    904  OD2 ASP A 442     230.585 166.107 240.334  1.00 63.47           O  
ATOM    905  N   SER A 443     232.147 162.249 244.448  1.00 63.16           N  
ATOM    906  CA  SER A 443     232.047 161.880 245.851  1.00 63.16           C  
ATOM    907  C   SER A 443     233.147 160.901 246.216  1.00 63.16           C  
ATOM    908  O   SER A 443     233.440 159.972 245.459  1.00 63.16           O  
ATOM    909  CB  SER A 443     230.697 161.242 246.159  1.00 63.16           C  
ATOM    910  OG  SER A 443     229.647 162.175 246.032  1.00 63.16           O  
ATOM    911  N   LYS A 444     233.751 161.112 247.380  1.00 70.38           N  
ATOM    912  CA  LYS A 444     234.791 160.241 247.901  1.00 70.38           C  
ATOM    913  C   LYS A 444     234.383 159.777 249.289  1.00 70.38           C  
ATOM    914  O   LYS A 444     233.636 160.473 249.983  1.00 70.38           O  
ATOM    915  CB  LYS A 444     236.141 160.960 247.983  1.00 70.38           C  
ATOM    916  CG  LYS A 444     236.513 161.768 246.756  1.00 70.38           C  
ATOM    917  CD  LYS A 444     237.613 162.773 247.066  1.00 70.38           C  
ATOM    918  CE  LYS A 444     238.815 162.117 247.731  1.00 70.38           C  
ATOM    919  NZ  LYS A 444     239.497 161.153 246.826  1.00 70.38           N  
ATOM    920  N   VAL A 445     234.890 158.602 249.687  1.00 72.51           N  
ATOM    921  CA  VAL A 445     234.536 158.014 250.980  1.00 72.51           C  
ATOM    922  C   VAL A 445     235.000 158.917 252.121  1.00 72.51           C  
ATOM    923  O   VAL A 445     234.272 159.136 253.098  1.00 72.51           O  
ATOM    924  CB  VAL A 445     235.102 156.581 251.078  1.00 72.51           C  
ATOM    925  CG1 VAL A 445     236.501 156.496 250.474  1.00 72.51           C  
ATOM    926  CG2 VAL A 445     235.090 156.061 252.510  1.00 72.51           C  
ATOM    927  N   SER A 446     236.217 159.459 252.003  1.00 73.52           N  
ATOM    928  CA  SER A 446     236.731 160.415 252.979  1.00 73.52           C  
ATOM    929  C   SER A 446     235.895 161.686 252.974  1.00 73.52           C  
ATOM    930  O   SER A 446     235.661 162.300 254.021  1.00 73.52           O  
ATOM    931  CB  SER A 446     238.195 160.732 252.684  1.00 73.52           C  
ATOM    932  OG  SER A 446     238.346 161.242 251.373  1.00 73.52           O  
ATOM    933  N   GLY A 447     235.448 162.093 251.792  1.00 70.92           N  
ATOM    934  CA  GLY A 447     234.681 163.298 251.576  1.00 70.92           C  
ATOM    935  C   GLY A 447     235.393 164.187 250.584  1.00 70.92           C  
ATOM    936  O   GLY A 447     236.621 164.296 250.610  1.00 70.92           O  
ATOM    937  N   ASN A 448     234.637 164.829 249.705  1.00 65.28           N  
ATOM    938  CA  ASN A 448     235.198 165.692 248.679  1.00 65.28           C  
ATOM    939  C   ASN A 448     235.124 167.125 249.167  1.00 65.28           C  
ATOM    940  O   ASN A 448     234.061 167.582 249.570  1.00 65.28           O  
ATOM    941  CB  ASN A 448     234.431 165.547 247.366  1.00 65.28           C  
ATOM    942  CG  ASN A 448     235.257 165.926 246.165  1.00 65.28           C  
ATOM    943  OD1 ASN A 448     236.361 166.444 246.297  1.00 65.28           O  
ATOM    944  ND2 ASN A 448     234.725 165.671 244.980  1.00 65.28           N  
ATOM    945  N   TYR A 449     236.252 167.823 249.166  1.00 67.57           N  
ATOM    946  CA  TYR A 449     236.279 169.187 249.672  1.00 67.57           C  
ATOM    947  C   TYR A 449     236.695 170.185 248.605  1.00 67.57           C  
ATOM    948  O   TYR A 449     236.872 171.369 248.908  1.00 67.57           O  
ATOM    949  CB  TYR A 449     237.187 169.285 250.899  1.00 67.57           C  
ATOM    950  CG  TYR A 449     236.561 168.664 252.123  1.00 67.57           C  
ATOM    951  CD1 TYR A 449     236.735 167.317 252.410  1.00 67.57           C  
ATOM    952  CD2 TYR A 449     235.768 169.418 252.975  1.00 67.57           C  
ATOM    953  CE1 TYR A 449     236.148 166.744 253.522  1.00 67.57           C  
ATOM    954  CE2 TYR A 449     235.178 168.855 254.087  1.00 67.57           C  
ATOM    955  CZ  TYR A 449     235.372 167.519 254.354  1.00 67.57           C  
ATOM    956  OH  TYR A 449     234.790 166.957 255.463  1.00 67.57           O  
ATOM    957  N   ASN A 450     236.865 169.732 247.367  1.00 66.47           N  
ATOM    958  CA  ASN A 450     237.222 170.586 246.246  1.00 66.47           C  
ATOM    959  C   ASN A 450     236.074 171.445 245.736  1.00 66.47           C  
ATOM    960  O   ASN A 450     236.308 172.268 244.848  1.00 66.47           O  
ATOM    961  CB  ASN A 450     237.758 169.721 245.110  1.00 66.47           C  
ATOM    962  CG  ASN A 450     239.123 169.151 245.414  1.00 66.47           C  
ATOM    963  OD1 ASN A 450     239.978 169.826 245.982  1.00 66.47           O  
ATOM    964  ND2 ASN A 450     239.336 167.899 245.034  1.00 66.47           N  
ATOM    965  N   TYR A 451     234.858 171.295 246.250  1.00 61.24           N  
ATOM    966  CA  TYR A 451     233.716 172.075 245.794  1.00 61.24           C  
ATOM    967  C   TYR A 451     233.269 173.021 246.895  1.00 61.24           C  
ATOM    968  O   TYR A 451     233.047 172.594 248.029  1.00 61.24           O  
ATOM    969  CB  TYR A 451     232.567 171.161 245.375  1.00 61.24           C  
ATOM    970  CG  TYR A 451     232.877 170.365 244.136  1.00 61.24           C  
ATOM    971  CD1 TYR A 451     233.040 170.993 242.912  1.00 61.24           C  
ATOM    972  CD2 TYR A 451     233.021 168.988 244.192  1.00 61.24           C  
ATOM    973  CE1 TYR A 451     233.333 170.272 241.776  1.00 61.24           C  
ATOM    974  CE2 TYR A 451     233.313 168.258 243.061  1.00 61.24           C  
ATOM    975  CZ  TYR A 451     233.468 168.906 241.857  1.00 61.24           C  
ATOM    976  OH  TYR A 451     233.758 168.182 240.727  1.00 61.24           O  
ATOM    977  N   LEU A 452     233.133 174.299 246.556  1.00 56.22           N  
ATOM    978  CA  LEU A 452     232.828 175.338 247.524  1.00 56.22           C  
ATOM    979  C   LEU A 452     231.645 176.163 247.046  1.00 56.22           C  
ATOM    980  O   LEU A 452     231.423 176.320 245.845  1.00 56.22           O  
ATOM    981  CB  LEU A 452     234.027 176.263 247.758  1.00 56.22           C  
ATOM    982  CG  LEU A 452     235.196 175.803 248.630  1.00 56.22           C  
ATOM    983  CD1 LEU A 452     236.144 174.886 247.892  1.00 56.22           C  
ATOM    984  CD2 LEU A 452     235.948 177.007 249.153  1.00 56.22           C  
ATOM    985  N   TYR A 453     230.880 176.678 248.000  1.00 56.92           N  
ATOM    986  CA  TYR A 453     229.817 177.630 247.729  1.00 56.92           C  
ATOM    987  C   TYR A 453     229.934 178.805 248.685  1.00 56.92           C  
ATOM    988  O   TYR A 453     230.417 178.666 249.809  1.00 56.92           O  
ATOM    989  CB  TYR A 453     228.422 177.000 247.856  1.00 56.92           C  
ATOM    990  CG  TYR A 453     227.989 176.642 249.252  1.00 56.92           C  
ATOM    991  CD1 TYR A 453     228.481 175.514 249.888  1.00 56.92           C  
ATOM    992  CD2 TYR A 453     227.056 177.419 249.924  1.00 56.92           C  
ATOM    993  CE1 TYR A 453     228.075 175.184 251.158  1.00 56.92           C  
ATOM    994  CE2 TYR A 453     226.647 177.098 251.194  1.00 56.92           C  
ATOM    995  CZ  TYR A 453     227.158 175.979 251.806  1.00 56.92           C  
ATOM    996  OH  TYR A 453     226.750 175.652 253.075  1.00 56.92           O  
ATOM    997  N   ARG A 454     229.503 179.971 248.226  1.00 55.81           N  
ATOM    998  CA  ARG A 454     229.546 181.163 249.056  1.00 55.81           C  
ATOM    999  C   ARG A 454     228.315 181.217 249.946  1.00 55.81           C  
ATOM   1000  O   ARG A 454     227.185 181.143 249.457  1.00 55.81           O  
ATOM   1001  CB  ARG A 454     229.610 182.410 248.183  1.00 55.81           C  
ATOM   1002  CG  ARG A 454     229.472 183.701 248.944  1.00 55.81           C  
ATOM   1003  CD  ARG A 454     229.718 184.881 248.039  1.00 55.81           C  
ATOM   1004  NE  ARG A 454     230.876 184.704 247.176  1.00 55.81           N  
ATOM   1005  CZ  ARG A 454     232.117 185.000 247.530  1.00 55.81           C  
ATOM   1006  NH1 ARG A 454     232.394 185.501 248.720  1.00 55.81           N  
ATOM   1007  NH2 ARG A 454     233.103 184.794 246.665  1.00 55.81           N  
ATOM   1008  N   LEU A 455     228.528 181.330 251.254  1.00 59.17           N  
ATOM   1009  CA  LEU A 455     227.419 181.307 252.198  1.00 59.17           C  
ATOM   1010  C   LEU A 455     226.984 182.697 252.632  1.00 59.17           C  
ATOM   1011  O   LEU A 455     225.801 182.904 252.912  1.00 59.17           O  
ATOM   1012  CB  LEU A 455     227.782 180.467 253.429  1.00 59.17           C  
ATOM   1013  CG  LEU A 455     226.698 180.187 254.476  1.00 59.17           C  
ATOM   1014  CD1 LEU A 455     225.484 179.569 253.830  1.00 59.17           C  
ATOM   1015  CD2 LEU A 455     227.219 179.274 255.558  1.00 59.17           C  
ATOM   1016  N   PHE A 456     227.898 183.663 252.664  1.00 61.98           N  
ATOM   1017  CA  PHE A 456     227.590 185.000 253.153  1.00 61.98           C  
ATOM   1018  C   PHE A 456     228.059 186.054 252.163  1.00 61.98           C  
ATOM   1019  O   PHE A 456     229.241 186.089 251.811  1.00 61.98           O  
ATOM   1020  CB  PHE A 456     228.263 185.265 254.496  1.00 61.98           C  
ATOM   1021  CG  PHE A 456     228.053 184.201 255.522  1.00 61.98           C  
ATOM   1022  CD1 PHE A 456     226.826 184.041 256.134  1.00 61.98           C  
ATOM   1023  CD2 PHE A 456     229.110 183.406 255.925  1.00 61.98           C  
ATOM   1024  CE1 PHE A 456     226.646 183.076 257.095  1.00 61.98           C  
ATOM   1025  CE2 PHE A 456     228.936 182.442 256.886  1.00 61.98           C  
ATOM   1026  CZ  PHE A 456     227.704 182.280 257.473  1.00 61.98           C  
ATOM   1027  N   ARG A 457     227.142 186.900 251.710  1.00 63.51           N  
ATOM   1028  CA  ARG A 457     227.474 188.061 250.895  1.00 63.51           C  
ATOM   1029  C   ARG A 457     226.739 189.263 251.461  1.00 63.51           C  
ATOM   1030  O   ARG A 457     225.637 189.121 251.997  1.00 63.51           O  
ATOM   1031  CB  ARG A 457     227.135 187.899 249.419  1.00 63.51           C  
ATOM   1032  CG  ARG A 457     228.297 188.256 248.518  1.00 63.51           C  
ATOM   1033  CD  ARG A 457     228.000 188.016 247.058  1.00 63.51           C  
ATOM   1034  NE  ARG A 457     227.175 189.076 246.496  1.00 63.51           N  
ATOM   1035  CZ  ARG A 457     227.658 190.128 245.850  1.00 63.51           C  
ATOM   1036  NH1 ARG A 457     228.956 190.287 245.664  1.00 63.51           N  
ATOM   1037  NH2 ARG A 457     226.816 191.036 245.370  1.00 63.51           N  
ATOM   1038  N   LYS A 458     227.375 190.436 251.386  1.00 65.30           N  
ATOM   1039  CA  LYS A 458     226.725 191.661 251.843  1.00 65.30           C  
ATOM   1040  C   LYS A 458     225.494 191.986 251.006  1.00 65.30           C  
ATOM   1041  O   LYS A 458     224.477 192.443 251.538  1.00 65.30           O  
ATOM   1042  CB  LYS A 458     227.713 192.823 251.792  1.00 65.30           C  
ATOM   1043  CG  LYS A 458     228.905 192.667 252.707  1.00 65.30           C  
ATOM   1044  CD  LYS A 458     229.773 193.909 252.684  1.00 65.30           C  
ATOM   1045  CE  LYS A 458     230.929 193.789 253.659  1.00 65.30           C  
ATOM   1046  NZ  LYS A 458     231.624 195.091 253.856  1.00 65.30           N  
ATOM   1047  N   SER A 459     225.564 191.755 249.700  1.00 67.56           N  
ATOM   1048  CA  SER A 459     224.453 192.007 248.798  1.00 67.56           C  
ATOM   1049  C   SER A 459     224.205 190.786 247.924  1.00 67.56           C  
ATOM   1050  O   SER A 459     225.117 190.000 247.663  1.00 67.56           O  
ATOM   1051  CB  SER A 459     224.719 193.239 247.929  1.00 67.56           C  
ATOM   1052  OG  SER A 459     225.832 193.034 247.080  1.00 67.56           O  
ATOM   1053  N   ASN A 460     222.957 190.622 247.491  1.00 66.10           N  
ATOM   1054  CA  ASN A 460     222.625 189.559 246.553  1.00 66.10           C  
ATOM   1055  C   ASN A 460     223.233 189.854 245.190  1.00 66.10           C  
ATOM   1056  O   ASN A 460     223.441 191.010 244.815  1.00 66.10           O  
ATOM   1057  CB  ASN A 460     221.115 189.385 246.422  1.00 66.10           C  
ATOM   1058  CG  ASN A 460     220.453 189.067 247.734  1.00 66.10           C  
ATOM   1059  OD1 ASN A 460     221.117 188.930 248.757  1.00 66.10           O  
ATOM   1060  ND2 ASN A 460     219.136 188.934 247.714  1.00 66.10           N  
ATOM   1061  N   LEU A 461     223.532 188.793 244.452  1.00 64.99           N  
ATOM   1062  CA  LEU A 461     224.274 188.941 243.214  1.00 64.99           C  
ATOM   1063  C   LEU A 461     223.382 189.442 242.089  1.00 64.99           C  
ATOM   1064  O   LEU A 461     222.174 189.196 242.062  1.00 64.99           O  
ATOM   1065  CB  LEU A 461     224.863 187.598 242.793  1.00 64.99           C  
ATOM   1066  CG  LEU A 461     226.240 187.179 243.282  1.00 64.99           C  
ATOM   1067  CD1 LEU A 461     226.583 185.826 242.709  1.00 64.99           C  
ATOM   1068  CD2 LEU A 461     227.272 188.199 242.906  1.00 64.99           C  
ATOM   1069  N   LYS A 462     224.000 190.151 241.150  1.00 71.43           N  
ATOM   1070  CA  LYS A 462     223.355 190.497 239.901  1.00 71.43           C  
ATOM   1071  C   LYS A 462     223.291 189.250 239.022  1.00 71.43           C  
ATOM   1072  O   LYS A 462     224.020 188.287 239.267  1.00 71.43           O  
ATOM   1073  CB  LYS A 462     224.121 191.624 239.216  1.00 71.43           C  
ATOM   1074  CG  LYS A 462     224.061 192.934 239.973  1.00 71.43           C  
ATOM   1075  CD  LYS A 462     224.789 194.037 239.231  1.00 71.43           C  
ATOM   1076  CE  LYS A 462     224.792 195.326 240.035  1.00 71.43           C  
ATOM   1077  NZ  LYS A 462     223.424 195.901 240.163  1.00 71.43           N  
ATOM   1078  N   PRO A 463     222.392 189.214 238.032  1.00 69.40           N  
ATOM   1079  CA  PRO A 463     222.365 188.065 237.118  1.00 69.40           C  
ATOM   1080  C   PRO A 463     223.659 187.929 236.328  1.00 69.40           C  
ATOM   1081  O   PRO A 463     224.216 188.915 235.842  1.00 69.40           O  
ATOM   1082  CB  PRO A 463     221.179 188.376 236.204  1.00 69.40           C  
ATOM   1083  CG  PRO A 463     220.275 189.153 237.069  1.00 69.40           C  
ATOM   1084  CD  PRO A 463     221.179 190.037 237.876  1.00 69.40           C  
ATOM   1085  N   PHE A 464     224.119 186.677 236.218  1.00 68.08           N  
ATOM   1086  CA  PHE A 464     225.367 186.287 235.549  1.00 68.08           C  
ATOM   1087  C   PHE A 464     226.583 187.027 236.100  1.00 68.08           C  
ATOM   1088  O   PHE A 464     227.473 187.433 235.353  1.00 68.08           O  
ATOM   1089  CB  PHE A 464     225.267 186.463 234.035  1.00 68.08           C  
ATOM   1090  CG  PHE A 464     224.206 185.623 233.401  1.00 68.08           C  
ATOM   1091  CD1 PHE A 464     224.130 184.270 233.671  1.00 68.08           C  
ATOM   1092  CD2 PHE A 464     223.283 186.184 232.539  1.00 68.08           C  
ATOM   1093  CE1 PHE A 464     223.159 183.491 233.087  1.00 68.08           C  
ATOM   1094  CE2 PHE A 464     222.307 185.409 231.953  1.00 68.08           C  
ATOM   1095  CZ  PHE A 464     222.246 184.061 232.229  1.00 68.08           C  
ATOM   1096  N   GLU A 465     226.630 187.202 237.416  1.00 69.05           N  
ATOM   1097  CA  GLU A 465     227.767 187.821 238.079  1.00 69.05           C  
ATOM   1098  C   GLU A 465     228.560 186.742 238.803  1.00 69.05           C  
ATOM   1099  O   GLU A 465     227.980 185.858 239.440  1.00 69.05           O  
ATOM   1100  CB  GLU A 465     227.323 188.915 239.051  1.00 69.05           C  
ATOM   1101  CG  GLU A 465     228.478 189.632 239.731  1.00 69.05           C  
ATOM   1102  CD  GLU A 465     228.042 190.837 240.528  1.00 69.05           C  
ATOM   1103  OE1 GLU A 465     226.864 190.892 240.934  1.00 69.05           O  
ATOM   1104  OE2 GLU A 465     228.885 191.725 240.762  1.00 69.05           O  
ATOM   1105  N   ARG A 466     229.881 186.808 238.697  1.00 63.22           N  
ATOM   1106  CA  ARG A 466     230.777 185.867 239.352  1.00 63.22           C  
ATOM   1107  C   ARG A 466     231.573 186.589 240.428  1.00 63.22           C  
ATOM   1108  O   ARG A 466     232.247 187.584 240.145  1.00 63.22           O  
ATOM   1109  CB  ARG A 466     231.703 185.199 238.339  1.00 63.22           C  
ATOM   1110  CG  ARG A 466     232.596 184.132 238.932  1.00 63.22           C  
ATOM   1111  CD  ARG A 466     233.829 183.796 238.090  1.00 63.22           C  
ATOM   1112  NE  ARG A 466     233.531 183.030 236.883  1.00 63.22           N  
ATOM   1113  CZ  ARG A 466     233.246 183.542 235.692  1.00 63.22           C  
ATOM   1114  NH1 ARG A 466     233.290 184.844 235.466  1.00 63.22           N  
ATOM   1115  NH2 ARG A 466     232.938 182.721 234.693  1.00 63.22           N  
ATOM   1116  N   ASP A 467     231.494 186.083 241.655  1.00 65.76           N  
ATOM   1117  CA  ASP A 467     232.185 186.648 242.808  1.00 65.76           C  
ATOM   1118  C   ASP A 467     233.182 185.620 243.324  1.00 65.76           C  
ATOM   1119  O   ASP A 467     232.787 184.595 243.888  1.00 65.76           O  
ATOM   1120  CB  ASP A 467     231.183 187.021 243.899  1.00 65.76           C  
ATOM   1121  CG  ASP A 467     231.677 188.134 244.794  1.00 65.76           C  
ATOM   1122  OD1 ASP A 467     232.898 188.226 245.028  1.00 65.76           O  
ATOM   1123  OD2 ASP A 467     230.836 188.912 245.284  1.00 65.76           O  
ATOM   1124  N   ILE A 468     234.469 185.891 243.133  1.00 63.46           N  
ATOM   1125  CA  ILE A 468     235.522 184.967 243.524  1.00 63.46           C  
ATOM   1126  C   ILE A 468     236.334 185.512 244.694  1.00 63.46           C  
ATOM   1127  O   ILE A 468     237.432 185.033 244.957  1.00 63.46           O  
ATOM   1128  CB  ILE A 468     236.439 184.632 242.341  1.00 63.46           C  
ATOM   1129  CG1 ILE A 468     236.798 185.903 241.576  1.00 63.46           C  
ATOM   1130  CG2 ILE A 468     235.762 183.655 241.420  1.00 63.46           C  
ATOM   1131  CD1 ILE A 468     237.798 185.682 240.471  1.00 63.46           C  
ATOM   1132  N   SER A 469     235.818 186.514 245.394  1.00 69.48           N  
ATOM   1133  CA  SER A 469     236.558 187.119 246.488  1.00 69.48           C  
ATOM   1134  C   SER A 469     236.555 186.221 247.715  1.00 69.48           C  
ATOM   1135  O   SER A 469     235.572 185.532 248.000  1.00 69.48           O  
ATOM   1136  CB  SER A 469     235.957 188.478 246.842  1.00 69.48           C  
ATOM   1137  OG  SER A 469     236.705 189.112 247.861  1.00 69.48           O  
ATOM   1138  N   THR A 470     237.670 186.226 248.440  1.00 73.10           N  
ATOM   1139  CA  THR A 470     237.790 185.514 249.702  1.00 73.10           C  
ATOM   1140  C   THR A 470     237.957 186.489 250.859  1.00 73.10           C  
ATOM   1141  O   THR A 470     238.628 186.187 251.846  1.00 73.10           O  
ATOM   1142  CB  THR A 470     238.963 184.538 249.667  1.00 73.10           C  
ATOM   1143  OG1 THR A 470     240.181 185.264 249.468  1.00 73.10           O  
ATOM   1144  CG2 THR A 470     238.793 183.547 248.534  1.00 73.10           C  
ATOM   1145  N   GLU A 471     237.352 187.663 250.743  1.00 77.21           N  
ATOM   1146  CA  GLU A 471     237.443 188.668 251.784  1.00 77.21           C  
ATOM   1147  C   GLU A 471     236.531 188.252 252.930  1.00 77.21           C  
ATOM   1148  O   GLU A 471     235.480 187.646 252.716  1.00 77.21           O  
ATOM   1149  CB  GLU A 471     237.092 190.039 251.194  1.00 77.21           C  
ATOM   1150  CG  GLU A 471     237.372 191.263 252.053  1.00 77.21           C  
ATOM   1151  CD  GLU A 471     236.261 191.581 253.014  1.00 77.21           C  
ATOM   1152  OE1 GLU A 471     235.103 191.245 252.691  1.00 77.21           O  
ATOM   1153  OE2 GLU A 471     236.537 192.169 254.083  1.00 77.21           O  
ATOM   1154  N   ILE A 472     236.960 188.556 254.155  1.00 72.29           N  
ATOM   1155  CA  ILE A 472     236.233 188.115 255.340  1.00 72.29           C  
ATOM   1156  C   ILE A 472     234.906 188.852 255.457  1.00 72.29           C  
ATOM   1157  O   ILE A 472     234.837 190.078 255.317  1.00 72.29           O  
ATOM   1158  CB  ILE A 472     237.120 188.323 256.579  1.00 72.29           C  
ATOM   1159  CG1 ILE A 472     238.379 187.461 256.473  1.00 72.29           C  
ATOM   1160  CG2 ILE A 472     236.389 188.000 257.854  1.00 72.29           C  
ATOM   1161  CD1 ILE A 472     238.151 185.981 256.695  1.00 72.29           C  
ATOM   1162  N   TYR A 473     233.850 188.110 255.774  1.00 67.99           N  
ATOM   1163  CA  TYR A 473     232.507 188.657 255.859  1.00 67.99           C  
ATOM   1164  C   TYR A 473     232.274 189.201 257.255  1.00 67.99           C  
ATOM   1165  O   TYR A 473     232.469 188.489 258.242  1.00 67.99           O  
ATOM   1166  CB  TYR A 473     231.466 187.587 255.538  1.00 67.99           C  
ATOM   1167  CG  TYR A 473     230.035 188.041 255.708  1.00 67.99           C  
ATOM   1168  CD1 TYR A 473     229.412 188.798 254.731  1.00 67.99           C  
ATOM   1169  CD2 TYR A 473     229.301 187.695 256.837  1.00 67.99           C  
ATOM   1170  CE1 TYR A 473     228.108 189.208 254.873  1.00 67.99           C  
ATOM   1171  CE2 TYR A 473     227.993 188.098 256.985  1.00 67.99           C  
ATOM   1172  CZ  TYR A 473     227.403 188.856 256.001  1.00 67.99           C  
ATOM   1173  OH  TYR A 473     226.099 189.262 256.144  1.00 67.99           O  
ATOM   1174  N   GLN A 474     231.847 190.453 257.339  1.00 76.38           N  
ATOM   1175  CA  GLN A 474     231.640 191.101 258.623  1.00 76.38           C  
ATOM   1176  C   GLN A 474     230.148 191.099 258.916  1.00 76.38           C  
ATOM   1177  O   GLN A 474     229.372 191.781 258.240  1.00 76.38           O  
ATOM   1178  CB  GLN A 474     232.198 192.521 258.614  1.00 76.38           C  
ATOM   1179  CG  GLN A 474     231.755 193.372 259.787  1.00 76.38           C  
ATOM   1180  CD  GLN A 474     231.750 194.845 259.464  1.00 76.38           C  
ATOM   1181  OE1 GLN A 474     232.707 195.370 258.899  1.00 76.38           O  
ATOM   1182  NE2 GLN A 474     230.671 195.523 259.823  1.00 76.38           N  
ATOM   1183  N   ALA A 475     229.750 190.304 259.904  1.00 76.04           N  
ATOM   1184  CA  ALA A 475     228.363 190.225 260.320  1.00 76.04           C  
ATOM   1185  C   ALA A 475     228.069 191.137 261.494  1.00 76.04           C  
ATOM   1186  O   ALA A 475     226.898 191.355 261.816  1.00 76.04           O  
ATOM   1187  CB  ALA A 475     227.998 188.785 260.687  1.00 76.04           C  
ATOM   1188  N   GLY A 476     229.102 191.682 262.122  1.00 81.04           N  
ATOM   1189  CA  GLY A 476     228.948 192.486 263.312  1.00 81.04           C  
ATOM   1190  C   GLY A 476     229.279 193.934 263.050  1.00 81.04           C  
ATOM   1191  O   GLY A 476     229.062 194.439 261.947  1.00 81.04           O  
ATOM   1192  N   ASN A 477     229.813 194.613 264.060  1.00 88.15           N  
ATOM   1193  CA  ASN A 477     230.099 196.034 263.971  1.00 88.15           C  
ATOM   1194  C   ASN A 477     231.584 196.338 263.962  1.00 88.15           C  
ATOM   1195  O   ASN A 477     232.004 197.284 263.295  1.00 88.15           O  
ATOM   1196  CB  ASN A 477     229.441 196.780 265.135  1.00 88.15           C  
ATOM   1197  CG  ASN A 477     227.932 196.789 265.035  1.00 88.15           C  
ATOM   1198  OD1 ASN A 477     227.371 196.669 263.948  1.00 88.15           O  
ATOM   1199  ND2 ASN A 477     227.265 196.922 266.174  1.00 88.15           N  
ATOM   1200  N   LYS A 478     232.379 195.560 264.687  1.00 94.76           N  
ATOM   1201  CA  LYS A 478     233.810 195.782 264.736  1.00 94.76           C  
ATOM   1202  C   LYS A 478     234.440 195.356 263.411  1.00 94.76           C  
ATOM   1203  O   LYS A 478     233.916 194.471 262.730  1.00 94.76           O  
ATOM   1204  CB  LYS A 478     234.426 194.994 265.888  1.00 94.76           C  
ATOM   1205  CG  LYS A 478     233.820 195.296 267.246  1.00 94.76           C  
ATOM   1206  CD  LYS A 478     234.151 196.711 267.689  1.00 94.76           C  
ATOM   1207  CE  LYS A 478     232.977 197.370 268.392  1.00 94.76           C  
ATOM   1208  NZ  LYS A 478     231.837 197.610 267.467  1.00 94.76           N  
ATOM   1209  N   PRO A 479     235.537 195.995 263.003  1.00 93.99           N  
ATOM   1210  CA  PRO A 479     236.214 195.568 261.774  1.00 93.99           C  
ATOM   1211  C   PRO A 479     236.850 194.198 261.930  1.00 93.99           C  
ATOM   1212  O   PRO A 479     237.350 193.832 262.995  1.00 93.99           O  
ATOM   1213  CB  PRO A 479     237.276 196.653 261.558  1.00 93.99           C  
ATOM   1214  CG  PRO A 479     236.801 197.818 262.362  1.00 93.99           C  
ATOM   1215  CD  PRO A 479     236.138 197.220 263.553  1.00 93.99           C  
ATOM   1216  N   CYS A 480     236.827 193.439 260.836  1.00 92.14           N  
ATOM   1217  CA  CYS A 480     237.323 192.069 260.869  1.00 92.14           C  
ATOM   1218  C   CYS A 480     238.843 192.012 260.838  1.00 92.14           C  
ATOM   1219  O   CYS A 480     239.437 191.140 261.484  1.00 92.14           O  
ATOM   1220  CB  CYS A 480     236.737 191.275 259.708  1.00 92.14           C  
ATOM   1221  SG  CYS A 480     235.036 190.785 260.001  1.00 92.14           S  
ATOM   1222  N   ASN A 481     239.468 192.911 260.065  1.00 91.52           N  
ATOM   1223  CA  ASN A 481     240.924 193.006 259.888  1.00 91.52           C  
ATOM   1224  C   ASN A 481     241.530 191.719 259.326  1.00 91.52           C  
ATOM   1225  O   ASN A 481     242.692 191.403 259.586  1.00 91.52           O  
ATOM   1226  CB  ASN A 481     241.632 193.417 261.185  1.00 91.52           C  
ATOM   1227  CG  ASN A 481     241.461 194.889 261.497  1.00 91.52           C  
ATOM   1228  OD1 ASN A 481     240.358 195.351 261.785  1.00 91.52           O  
ATOM   1229  ND2 ASN A 481     242.556 195.636 261.439  1.00 91.52           N  
ATOM   1230  N   GLY A 482     240.748 190.966 258.553  1.00 85.92           N  
ATOM   1231  CA  GLY A 482     241.241 189.776 257.896  1.00 85.92           C  
ATOM   1232  C   GLY A 482     241.317 188.537 258.757  1.00 85.92           C  
ATOM   1233  O   GLY A 482     241.765 187.494 258.268  1.00 85.92           O  
ATOM   1234  N   VAL A 483     240.900 188.610 260.017  1.00 85.25           N  
ATOM   1235  CA  VAL A 483     240.974 187.486 260.942  1.00 85.25           C  
ATOM   1236  C   VAL A 483     239.556 187.008 261.216  1.00 85.25           C  
ATOM   1237  O   VAL A 483     238.695 187.794 261.630  1.00 85.25           O  
ATOM   1238  CB  VAL A 483     241.691 187.871 262.243  1.00 85.25           C  
ATOM   1239  CG1 VAL A 483     241.670 186.711 263.225  1.00 85.25           C  
ATOM   1240  CG2 VAL A 483     243.117 188.302 261.946  1.00 85.25           C  
ATOM   1241  N   ALA A 484     239.311 185.720 260.974  1.00 80.35           N  
ATOM   1242  CA  ALA A 484     237.979 185.132 261.105  1.00 80.35           C  
ATOM   1243  C   ALA A 484     237.705 184.768 262.566  1.00 80.35           C  
ATOM   1244  O   ALA A 484     237.696 183.604 262.968  1.00 80.35           O  
ATOM   1245  CB  ALA A 484     237.848 183.919 260.197  1.00 80.35           C  
ATOM   1246  N   GLY A 485     237.470 185.800 263.370  1.00 80.60           N  
ATOM   1247  CA  GLY A 485     237.150 185.600 264.770  1.00 80.60           C  
ATOM   1248  C   GLY A 485     235.664 185.677 265.053  1.00 80.60           C  
ATOM   1249  O   GLY A 485     234.861 185.058 264.350  1.00 80.60           O  
ATOM   1250  N   PHE A 486     235.286 186.420 266.092  1.00 84.01           N  
ATOM   1251  CA  PHE A 486     233.877 186.595 266.414  1.00 84.01           C  
ATOM   1252  C   PHE A 486     233.224 187.522 265.401  1.00 84.01           C  
ATOM   1253  O   PHE A 486     233.773 188.579 265.076  1.00 84.01           O  
ATOM   1254  CB  PHE A 486     233.712 187.182 267.812  1.00 84.01           C  
ATOM   1255  CG  PHE A 486     232.290 187.222 268.285  1.00 84.01           C  
ATOM   1256  CD1 PHE A 486     231.407 186.203 267.966  1.00 84.01           C  
ATOM   1257  CD2 PHE A 486     231.820 188.313 268.996  1.00 84.01           C  
ATOM   1258  CE1 PHE A 486     230.095 186.251 268.387  1.00 84.01           C  
ATOM   1259  CE2 PHE A 486     230.507 188.369 269.415  1.00 84.01           C  
ATOM   1260  CZ  PHE A 486     229.644 187.338 269.109  1.00 84.01           C  
ATOM   1261  N   ASN A 487     232.063 187.100 264.885  1.00 81.34           N  
ATOM   1262  CA  ASN A 487     231.252 187.819 263.897  1.00 81.34           C  
ATOM   1263  C   ASN A 487     232.003 188.095 262.600  1.00 81.34           C  
ATOM   1264  O   ASN A 487     231.622 188.987 261.839  1.00 81.34           O  
ATOM   1265  CB  ASN A 487     230.679 189.121 264.465  1.00 81.34           C  
ATOM   1266  CG  ASN A 487     229.429 188.894 265.274  1.00 81.34           C  
ATOM   1267  OD1 ASN A 487     228.671 187.965 265.009  1.00 81.34           O  
ATOM   1268  ND2 ASN A 487     229.200 189.745 266.265  1.00 81.34           N  
ATOM   1269  N   CYS A 488     233.057 187.335 262.326  1.00 79.30           N  
ATOM   1270  CA  CYS A 488     233.804 187.427 261.084  1.00 79.30           C  
ATOM   1271  C   CYS A 488     234.000 186.019 260.560  1.00 79.30           C  
ATOM   1272  O   CYS A 488     234.657 185.201 261.209  1.00 79.30           O  
ATOM   1273  CB  CYS A 488     235.154 188.108 261.310  1.00 79.30           C  
ATOM   1274  SG  CYS A 488     235.051 189.827 261.788  1.00 79.30           S  
ATOM   1275  N   TYR A 489     233.430 185.736 259.399  1.00 69.94           N  
ATOM   1276  CA  TYR A 489     233.426 184.391 258.860  1.00 69.94           C  
ATOM   1277  C   TYR A 489     234.087 184.379 257.494  1.00 69.94           C  
ATOM   1278  O   TYR A 489     234.001 185.349 256.738  1.00 69.94           O  
ATOM   1279  CB  TYR A 489     232.004 183.852 258.742  1.00 69.94           C  
ATOM   1280  CG  TYR A 489     231.162 184.089 259.968  1.00 69.94           C  
ATOM   1281  CD1 TYR A 489     231.530 183.565 261.196  1.00 69.94           C  
ATOM   1282  CD2 TYR A 489     230.001 184.844 259.896  1.00 69.94           C  
ATOM   1283  CE1 TYR A 489     230.762 183.780 262.318  1.00 69.94           C  
ATOM   1284  CE2 TYR A 489     229.228 185.064 261.012  1.00 69.94           C  
ATOM   1285  CZ  TYR A 489     229.613 184.531 262.219  1.00 69.94           C  
ATOM   1286  OH  TYR A 489     228.844 184.753 263.333  1.00 69.94           O  
ATOM   1287  N   PHE A 490     234.758 183.283 257.195  1.00 65.82           N  
ATOM   1288  CA  PHE A 490     235.247 183.065 255.848  1.00 65.82           C  
ATOM   1289  C   PHE A 490     234.031 182.780 254.980  1.00 65.82           C  
ATOM   1290  O   PHE A 490     233.261 181.866 255.299  1.00 65.82           O  
ATOM   1291  CB  PHE A 490     236.239 181.914 255.818  1.00 65.82           C  
ATOM   1292  CG  PHE A 490     236.973 181.783 254.523  1.00 65.82           C  
ATOM   1293  CD1 PHE A 490     237.891 182.743 254.137  1.00 65.82           C  
ATOM   1294  CD2 PHE A 490     236.763 180.692 253.700  1.00 65.82           C  
ATOM   1295  CE1 PHE A 490     238.573 182.625 252.949  1.00 65.82           C  
ATOM   1296  CE2 PHE A 490     237.444 180.568 252.510  1.00 65.82           C  
ATOM   1297  CZ  PHE A 490     238.350 181.536 252.134  1.00 65.82           C  
ATOM   1298  N   PRO A 491     233.798 183.541 253.908  1.00 60.88           N  
ATOM   1299  CA  PRO A 491     232.509 183.466 253.207  1.00 60.88           C  
ATOM   1300  C   PRO A 491     232.279 182.197 252.406  1.00 60.88           C  
ATOM   1301  O   PRO A 491     231.158 182.000 251.927  1.00 60.88           O  
ATOM   1302  CB  PRO A 491     232.564 184.688 252.294  1.00 60.88           C  
ATOM   1303  CG  PRO A 491     234.002 184.725 251.923  1.00 60.88           C  
ATOM   1304  CD  PRO A 491     234.712 184.471 253.228  1.00 60.88           C  
ATOM   1305  N   LEU A 492     233.266 181.322 252.262  1.00 58.87           N  
ATOM   1306  CA  LEU A 492     233.155 180.176 251.374  1.00 58.87           C  
ATOM   1307  C   LEU A 492     233.216 178.890 252.177  1.00 58.87           C  
ATOM   1308  O   LEU A 492     234.166 178.666 252.932  1.00 58.87           O  
ATOM   1309  CB  LEU A 492     234.261 180.174 250.324  1.00 58.87           C  
ATOM   1310  CG  LEU A 492     234.250 181.351 249.361  1.00 58.87           C  
ATOM   1311  CD1 LEU A 492     235.622 181.523 248.761  1.00 58.87           C  
ATOM   1312  CD2 LEU A 492     233.215 181.142 248.298  1.00 58.87           C  
ATOM   1313  N   ARG A 493     232.212 178.047 251.996  1.00 62.94           N  
ATOM   1314  CA  ARG A 493     232.060 176.816 252.742  1.00 62.94           C  
ATOM   1315  C   ARG A 493     232.134 175.678 251.741  1.00 62.94           C  
ATOM   1316  O   ARG A 493     231.838 175.860 250.563  1.00 62.94           O  
ATOM   1317  CB  ARG A 493     230.733 176.788 253.488  1.00 62.94           C  
ATOM   1318  CG  ARG A 493     230.475 178.014 254.346  1.00 62.94           C  
ATOM   1319  CD  ARG A 493     230.921 177.862 255.785  1.00 62.94           C  
ATOM   1320  NE  ARG A 493     232.368 177.943 255.923  1.00 62.94           N  
ATOM   1321  CZ  ARG A 493     233.011 177.891 257.079  1.00 62.94           C  
ATOM   1322  NH1 ARG A 493     232.363 177.752 258.223  1.00 62.94           N  
ATOM   1323  NH2 ARG A 493     234.337 177.984 257.088  1.00 62.94           N  
ATOM   1324  N   SER A 494     232.539 174.504 252.191  1.00 59.80           N  
ATOM   1325  CA  SER A 494     232.777 173.409 251.267  1.00 59.80           C  
ATOM   1326  C   SER A 494     231.655 172.385 251.321  1.00 59.80           C  
ATOM   1327  O   SER A 494     231.196 172.010 252.399  1.00 59.80           O  
ATOM   1328  CB  SER A 494     234.104 172.729 251.587  1.00 59.80           C  
ATOM   1329  OG  SER A 494     234.286 171.591 250.776  1.00 59.80           O  
ATOM   1330  N   TYR A 495     231.270 171.877 250.157  1.00 57.11           N  
ATOM   1331  CA  TYR A 495     230.271 170.823 250.078  1.00 57.11           C  
ATOM   1332  C   TYR A 495     231.034 169.530 250.282  1.00 57.11           C  
ATOM   1333  O   TYR A 495     231.776 169.115 249.394  1.00 57.11           O  
ATOM   1334  CB  TYR A 495     229.635 170.783 248.695  1.00 57.11           C  
ATOM   1335  CG  TYR A 495     228.534 171.738 248.343  1.00 57.11           C  
ATOM   1336  CD1 TYR A 495     227.361 171.782 249.072  1.00 57.11           C  
ATOM   1337  CD2 TYR A 495     228.637 172.537 247.216  1.00 57.11           C  
ATOM   1338  CE1 TYR A 495     226.344 172.635 248.719  1.00 57.11           C  
ATOM   1339  CE2 TYR A 495     227.627 173.387 246.856  1.00 57.11           C  
ATOM   1340  CZ  TYR A 495     226.483 173.430 247.609  1.00 57.11           C  
ATOM   1341  OH  TYR A 495     225.470 174.281 247.254  1.00 57.11           O  
ATOM   1342  N   SER A 496     230.830 168.866 251.414  1.00 61.70           N  
ATOM   1343  CA  SER A 496     231.599 167.659 251.714  1.00 61.70           C  
ATOM   1344  C   SER A 496     230.923 166.419 251.131  1.00 61.70           C  
ATOM   1345  O   SER A 496     230.386 165.591 251.861  1.00 61.70           O  
ATOM   1346  CB  SER A 496     231.795 167.525 253.216  1.00 61.70           C  
ATOM   1347  OG  SER A 496     230.566 167.704 253.894  1.00 61.70           O  
ATOM   1348  N   PHE A 497     230.971 166.291 249.800  1.00 56.33           N  
ATOM   1349  CA  PHE A 497     230.253 165.206 249.131  1.00 56.33           C  
ATOM   1350  C   PHE A 497     230.818 163.834 249.482  1.00 56.33           C  
ATOM   1351  O   PHE A 497     232.025 163.600 249.378  1.00 56.33           O  
ATOM   1352  CB  PHE A 497     230.295 165.384 247.616  1.00 56.33           C  
ATOM   1353  CG  PHE A 497     229.579 166.597 247.114  1.00 56.33           C  
ATOM   1354  CD1 PHE A 497     228.270 166.838 247.476  1.00 56.33           C  
ATOM   1355  CD2 PHE A 497     230.202 167.476 246.250  1.00 56.33           C  
ATOM   1356  CE1 PHE A 497     227.601 167.940 247.000  1.00 56.33           C  
ATOM   1357  CE2 PHE A 497     229.535 168.583 245.774  1.00 56.33           C  
ATOM   1358  CZ  PHE A 497     228.229 168.807 246.143  1.00 56.33           C  
ATOM   1359  N   ARG A 498     229.936 162.931 249.897  1.00 62.70           N  
ATOM   1360  CA  ARG A 498     230.224 161.541 250.204  1.00 62.70           C  
ATOM   1361  C   ARG A 498     229.259 160.643 249.446  1.00 62.70           C  
ATOM   1362  O   ARG A 498     228.113 161.037 249.213  1.00 62.70           O  
ATOM   1363  CB  ARG A 498     230.121 161.293 251.712  1.00 62.70           C  
ATOM   1364  CG  ARG A 498     231.303 161.867 252.456  1.00 62.70           C  
ATOM   1365  CD  ARG A 498     231.226 161.636 253.936  1.00 62.70           C  
ATOM   1366  NE  ARG A 498     232.374 162.222 254.612  1.00 62.70           N  
ATOM   1367  CZ  ARG A 498     232.392 163.444 255.124  1.00 62.70           C  
ATOM   1368  NH1 ARG A 498     231.332 164.231 255.068  1.00 62.70           N  
ATOM   1369  NH2 ARG A 498     233.499 163.884 255.712  1.00 62.70           N  
ATOM   1370  N   PRO A 499     229.685 159.427 249.034  1.00 65.34           N  
ATOM   1371  CA  PRO A 499     228.807 158.577 248.212  1.00 65.34           C  
ATOM   1372  C   PRO A 499     227.599 157.988 248.937  1.00 65.34           C  
ATOM   1373  O   PRO A 499     226.851 157.204 248.347  1.00 65.34           O  
ATOM   1374  CB  PRO A 499     229.754 157.463 247.754  1.00 65.34           C  
ATOM   1375  CG  PRO A 499     230.740 157.384 248.839  1.00 65.34           C  
ATOM   1376  CD  PRO A 499     231.004 158.803 249.196  1.00 65.34           C  
ATOM   1377  N   THR A 500     227.378 158.369 250.195  1.00 65.88           N  
ATOM   1378  CA  THR A 500     226.386 157.749 251.061  1.00 65.88           C  
ATOM   1379  C   THR A 500     225.355 158.771 251.504  1.00 65.88           C  
ATOM   1380  O   THR A 500     224.624 158.543 252.468  1.00 65.88           O  
ATOM   1381  CB  THR A 500     227.041 157.094 252.276  1.00 65.88           C  
ATOM   1382  OG1 THR A 500     227.769 158.078 253.017  1.00 65.88           O  
ATOM   1383  CG2 THR A 500     227.989 155.991 251.847  1.00 65.88           C  
ATOM   1384  N   TYR A 501     225.287 159.890 250.800  1.00 60.23           N  
ATOM   1385  CA  TYR A 501     224.361 160.966 251.090  1.00 60.23           C  
ATOM   1386  C   TYR A 501     223.069 160.721 250.340  1.00 60.23           C  
ATOM   1387  O   TYR A 501     223.046 160.016 249.329  1.00 60.23           O  
ATOM   1388  CB  TYR A 501     224.919 162.311 250.636  1.00 60.23           C  
ATOM   1389  CG  TYR A 501     225.953 162.955 251.510  1.00 60.23           C  
ATOM   1390  CD1 TYR A 501     226.441 162.327 252.640  1.00 60.23           C  
ATOM   1391  CD2 TYR A 501     226.440 164.209 251.194  1.00 60.23           C  
ATOM   1392  CE1 TYR A 501     227.389 162.935 253.428  1.00 60.23           C  
ATOM   1393  CE2 TYR A 501     227.375 164.822 251.974  1.00 60.23           C  
ATOM   1394  CZ  TYR A 501     227.856 164.180 253.088  1.00 60.23           C  
ATOM   1395  OH  TYR A 501     228.801 164.796 253.873  1.00 60.23           O  
ATOM   1396  N   GLY A 502     221.981 161.276 250.864  1.00 60.31           N  
ATOM   1397  CA  GLY A 502     220.705 161.237 250.178  1.00 60.31           C  
ATOM   1398  C   GLY A 502     220.701 161.916 248.821  1.00 60.31           C  
ATOM   1399  O   GLY A 502     221.685 162.547 248.426  1.00 60.31           O  
ATOM   1400  N   VAL A 503     219.574 161.831 248.112  1.00 60.26           N  
ATOM   1401  CA  VAL A 503     219.486 162.406 246.773  1.00 60.26           C  
ATOM   1402  C   VAL A 503     219.533 163.932 246.837  1.00 60.26           C  
ATOM   1403  O   VAL A 503     219.997 164.587 245.897  1.00 60.26           O  
ATOM   1404  CB  VAL A 503     218.232 161.863 246.052  1.00 60.26           C  
ATOM   1405  CG1 VAL A 503     216.942 162.345 246.708  1.00 60.26           C  
ATOM   1406  CG2 VAL A 503     218.256 162.184 244.565  1.00 60.26           C  
ATOM   1407  N   GLY A 504     219.118 164.520 247.959  1.00 59.64           N  
ATOM   1408  CA  GLY A 504     219.163 165.957 248.119  1.00 59.64           C  
ATOM   1409  C   GLY A 504     220.514 166.511 248.495  1.00 59.64           C  
ATOM   1410  O   GLY A 504     220.685 167.732 248.506  1.00 59.64           O  
ATOM   1411  N   HIS A 505     221.480 165.649 248.796  1.00 59.43           N  
ATOM   1412  CA  HIS A 505     222.811 166.090 249.169  1.00 59.43           C  
ATOM   1413  C   HIS A 505     223.886 165.457 248.305  1.00 59.43           C  
ATOM   1414  O   HIS A 505     225.072 165.692 248.548  1.00 59.43           O  
ATOM   1415  CB  HIS A 505     223.109 165.768 250.642  1.00 59.43           C  
ATOM   1416  CG  HIS A 505     222.180 166.425 251.614  1.00 59.43           C  
ATOM   1417  ND1 HIS A 505     222.575 167.457 252.435  1.00 59.43           N  
ATOM   1418  CD2 HIS A 505     220.885 166.177 251.919  1.00 59.43           C  
ATOM   1419  CE1 HIS A 505     221.559 167.830 253.190  1.00 59.43           C  
ATOM   1420  NE2 HIS A 505     220.521 167.069 252.897  1.00 59.43           N  
ATOM   1421  N   GLN A 506     223.503 164.667 247.313  1.00 58.60           N  
ATOM   1422  CA  GLN A 506     224.441 164.136 246.348  1.00 58.60           C  
ATOM   1423  C   GLN A 506     224.870 165.239 245.382  1.00 58.60           C  
ATOM   1424  O   GLN A 506     224.114 166.180 245.135  1.00 58.60           O  
ATOM   1425  CB  GLN A 506     223.797 162.974 245.604  1.00 58.60           C  
ATOM   1426  CG  GLN A 506     224.052 161.644 246.272  1.00 58.60           C  
ATOM   1427  CD  GLN A 506     223.234 160.531 245.675  1.00 58.60           C  
ATOM   1428  OE1 GLN A 506     222.687 160.666 244.584  1.00 58.60           O  
ATOM   1429  NE2 GLN A 506     223.131 159.425 246.394  1.00 58.60           N  
ATOM   1430  N   PRO A 507     226.088 165.165 244.843  1.00 56.88           N  
ATOM   1431  CA  PRO A 507     226.547 166.209 243.917  1.00 56.88           C  
ATOM   1432  C   PRO A 507     225.839 166.145 242.572  1.00 56.88           C  
ATOM   1433  O   PRO A 507     225.730 165.084 241.957  1.00 56.88           O  
ATOM   1434  CB  PRO A 507     228.042 165.917 243.773  1.00 56.88           C  
ATOM   1435  CG  PRO A 507     228.171 164.497 244.106  1.00 56.88           C  
ATOM   1436  CD  PRO A 507     227.172 164.229 245.172  1.00 56.88           C  
ATOM   1437  N   TYR A 508     225.353 167.297 242.127  1.00 56.87           N  
ATOM   1438  CA  TYR A 508     224.686 167.455 240.844  1.00 56.87           C  
ATOM   1439  C   TYR A 508     225.514 168.396 239.985  1.00 56.87           C  
ATOM   1440  O   TYR A 508     225.781 169.535 240.385  1.00 56.87           O  
ATOM   1441  CB  TYR A 508     223.270 167.995 241.018  1.00 56.87           C  
ATOM   1442  CG  TYR A 508     222.243 166.913 241.210  1.00 56.87           C  
ATOM   1443  CD1 TYR A 508     222.288 166.085 242.320  1.00 56.87           C  
ATOM   1444  CD2 TYR A 508     221.235 166.712 240.282  1.00 56.87           C  
ATOM   1445  CE1 TYR A 508     221.359 165.094 242.506  1.00 56.87           C  
ATOM   1446  CE2 TYR A 508     220.299 165.718 240.459  1.00 56.87           C  
ATOM   1447  CZ  TYR A 508     220.369 164.912 241.574  1.00 56.87           C  
ATOM   1448  OH  TYR A 508     219.440 163.918 241.763  1.00 56.87           O  
ATOM   1449  N   ARG A 509     225.928 167.915 238.820  1.00 58.79           N  
ATOM   1450  CA  ARG A 509     226.624 168.740 237.843  1.00 58.79           C  
ATOM   1451  C   ARG A 509     225.616 169.484 236.982  1.00 58.79           C  
ATOM   1452  O   ARG A 509     224.716 168.866 236.399  1.00 58.79           O  
ATOM   1453  CB  ARG A 509     227.543 167.893 236.976  1.00 58.79           C  
ATOM   1454  CG  ARG A 509     228.748 167.362 237.698  1.00 58.79           C  
ATOM   1455  CD  ARG A 509     229.637 166.574 236.769  1.00 58.79           C  
ATOM   1456  NE  ARG A 509     230.977 166.434 237.322  1.00 58.79           N  
ATOM   1457  CZ  ARG A 509     232.016 165.956 236.656  1.00 58.79           C  
ATOM   1458  NH1 ARG A 509     231.907 165.557 235.402  1.00 58.79           N  
ATOM   1459  NH2 ARG A 509     233.194 165.876 237.263  1.00 58.79           N  
ATOM   1460  N   VAL A 510     225.726 170.812 236.951  1.00 55.68           N  
ATOM   1461  CA  VAL A 510     224.766 171.676 236.280  1.00 55.68           C  
ATOM   1462  C   VAL A 510     225.486 172.453 235.187  1.00 55.68           C  
ATOM   1463  O   VAL A 510     226.538 173.058 235.433  1.00 55.68           O  
ATOM   1464  CB  VAL A 510     224.087 172.637 237.273  1.00 55.68           C  
ATOM   1465  CG1 VAL A 510     223.135 173.576 236.563  1.00 55.68           C  
ATOM   1466  CG2 VAL A 510     223.354 171.856 238.325  1.00 55.68           C  
ATOM   1467  N   VAL A 511     224.924 172.414 233.981  1.00 60.17           N  
ATOM   1468  CA  VAL A 511     225.366 173.206 232.840  1.00 60.17           C  
ATOM   1469  C   VAL A 511     224.177 174.041 232.386  1.00 60.17           C  
ATOM   1470  O   VAL A 511     223.114 173.496 232.076  1.00 60.17           O  
ATOM   1471  CB  VAL A 511     225.888 172.325 231.696  1.00 60.17           C  
ATOM   1472  CG1 VAL A 511     226.076 173.144 230.444  1.00 60.17           C  
ATOM   1473  CG2 VAL A 511     227.186 171.661 232.088  1.00 60.17           C  
ATOM   1474  N   VAL A 512     224.352 175.352 232.337  1.00 61.79           N  
ATOM   1475  CA  VAL A 512     223.292 176.279 231.975  1.00 61.79           C  
ATOM   1476  C   VAL A 512     223.645 176.870 230.623  1.00 61.79           C  
ATOM   1477  O   VAL A 512     224.686 177.521 230.479  1.00 61.79           O  
ATOM   1478  CB  VAL A 512     223.136 177.383 233.028  1.00 61.79           C  
ATOM   1479  CG1 VAL A 512     222.084 178.370 232.606  1.00 61.79           C  
ATOM   1480  CG2 VAL A 512     222.801 176.781 234.367  1.00 61.79           C  
ATOM   1481  N   LEU A 513     222.798 176.621 229.627  1.00 68.58           N  
ATOM   1482  CA  LEU A 513     222.982 177.162 228.291  1.00 68.58           C  
ATOM   1483  C   LEU A 513     222.139 178.421 228.166  1.00 68.58           C  
ATOM   1484  O   LEU A 513     220.915 178.372 228.330  1.00 68.58           O  
ATOM   1485  CB  LEU A 513     222.581 176.142 227.229  1.00 68.58           C  
ATOM   1486  CG  LEU A 513     223.331 174.813 227.239  1.00 68.58           C  
ATOM   1487  CD1 LEU A 513     222.697 173.860 226.256  1.00 68.58           C  
ATOM   1488  CD2 LEU A 513     224.792 175.016 226.915  1.00 68.58           C  
ATOM   1489  N   SER A 514     222.797 179.533 227.866  1.00 74.48           N  
ATOM   1490  CA  SER A 514     222.173 180.831 227.650  1.00 74.48           C  
ATOM   1491  C   SER A 514     222.373 181.197 226.189  1.00 74.48           C  
ATOM   1492  O   SER A 514     223.506 181.211 225.705  1.00 74.48           O  
ATOM   1493  CB  SER A 514     222.777 181.891 228.566  1.00 74.48           C  
ATOM   1494  OG  SER A 514     222.298 183.178 228.230  1.00 74.48           O  
ATOM   1495  N   PHE A 515     221.290 181.496 225.487  1.00 80.41           N  
ATOM   1496  CA  PHE A 515     221.354 181.784 224.061  1.00 80.41           C  
ATOM   1497  C   PHE A 515     221.126 183.269 223.849  1.00 80.41           C  
ATOM   1498  O   PHE A 515     220.095 183.802 224.270  1.00 80.41           O  
ATOM   1499  CB  PHE A 515     220.280 180.995 223.318  1.00 80.41           C  
ATOM   1500  CG  PHE A 515     220.275 179.537 223.631  1.00 80.41           C  
ATOM   1501  CD1 PHE A 515     221.439 178.795 223.577  1.00 80.41           C  
ATOM   1502  CD2 PHE A 515     219.105 178.914 224.020  1.00 80.41           C  
ATOM   1503  CE1 PHE A 515     221.431 177.449 223.875  1.00 80.41           C  
ATOM   1504  CE2 PHE A 515     219.091 177.575 224.324  1.00 80.41           C  
ATOM   1505  CZ  PHE A 515     220.256 176.841 224.250  1.00 80.41           C  
ATOM   1506  N   GLU A 516     222.074 183.943 223.200  1.00 90.63           N  
ATOM   1507  CA  GLU A 516     221.928 185.374 222.997  1.00 90.63           C  
ATOM   1508  C   GLU A 516     222.065 185.704 221.519  1.00 90.63           C  
ATOM   1509  O   GLU A 516     222.823 185.062 220.779  1.00 90.63           O  
ATOM   1510  CB  GLU A 516     222.932 186.189 223.831  1.00 90.63           C  
ATOM   1511  CG  GLU A 516     224.384 186.031 223.451  1.00 90.63           C  
ATOM   1512  CD  GLU A 516     225.271 187.045 224.139  1.00 90.63           C  
ATOM   1513  OE1 GLU A 516     224.798 187.701 225.090  1.00 90.63           O  
ATOM   1514  OE2 GLU A 516     226.441 187.189 223.728  1.00 90.63           O  
ATOM   1515  N   LEU A 517     221.315 186.726 221.110  1.00 92.44           N  
ATOM   1516  CA  LEU A 517     221.325 187.246 219.752  1.00 92.44           C  
ATOM   1517  C   LEU A 517     221.836 188.678 219.743  1.00 92.44           C  
ATOM   1518  O   LEU A 517     221.390 189.509 220.540  1.00 92.44           O  
ATOM   1519  CB  LEU A 517     219.925 187.190 219.143  1.00 92.44           C  
ATOM   1520  CG  LEU A 517     219.622 185.976 218.274  1.00 92.44           C  
ATOM   1521  CD1 LEU A 517     218.131 185.872 218.009  1.00 92.44           C  
ATOM   1522  CD2 LEU A 517     220.394 186.069 216.971  1.00 92.44           C  
ATOM   1523  N   LEU A 518     222.766 188.955 218.840  1.00 96.82           N  
ATOM   1524  CA  LEU A 518     223.427 190.242 218.722  1.00 96.82           C  
ATOM   1525  C   LEU A 518     223.322 190.702 217.277  1.00 96.82           C  
ATOM   1526  O   LEU A 518     222.978 189.919 216.388  1.00 96.82           O  
ATOM   1527  CB  LEU A 518     224.895 190.182 219.154  1.00 96.82           C  
ATOM   1528  CG  LEU A 518     225.154 189.868 220.628  1.00 96.82           C  
ATOM   1529  CD1 LEU A 518     226.642 189.698 220.882  1.00 96.82           C  
ATOM   1530  CD2 LEU A 518     224.572 190.955 221.516  1.00 96.82           C  
ATOM   1531  N   HIS A 519     223.575 192.001 217.057  1.00101.68           N  
ATOM   1532  CA  HIS A 519     223.604 192.582 215.710  1.00101.68           C  
ATOM   1533  C   HIS A 519     224.582 191.888 214.760  1.00101.68           C  
ATOM   1534  O   HIS A 519     224.454 192.044 213.541  1.00101.68           O  
ATOM   1535  CB  HIS A 519     223.978 194.057 215.792  1.00101.68           C  
ATOM   1536  CG  HIS A 519     225.300 194.302 216.446  1.00101.68           C  
ATOM   1537  ND1 HIS A 519     226.473 194.414 215.731  1.00101.68           N  
ATOM   1538  CD2 HIS A 519     225.639 194.446 217.749  1.00101.68           C  
ATOM   1539  CE1 HIS A 519     227.476 194.622 216.564  1.00101.68           C  
ATOM   1540  NE2 HIS A 519     226.997 194.647 217.795  1.00101.68           N  
ATOM   1541  N   ALA A 520     225.557 191.147 215.287  1.00 99.29           N  
ATOM   1542  CA  ALA A 520     226.503 190.399 214.488  1.00 99.29           C  
ATOM   1543  C   ALA A 520     225.774 189.247 213.800  1.00 99.29           C  
ATOM   1544  O   ALA A 520     224.710 188.825 214.257  1.00 99.29           O  
ATOM   1545  CB  ALA A 520     227.632 189.875 215.373  1.00 99.29           C  
ATOM   1546  N   PRO A 521     226.300 188.750 212.677  1.00 98.26           N  
ATOM   1547  CA  PRO A 521     225.673 187.589 212.023  1.00 98.26           C  
ATOM   1548  C   PRO A 521     225.726 186.342 212.895  1.00 98.26           C  
ATOM   1549  O   PRO A 521     226.799 185.895 213.308  1.00 98.26           O  
ATOM   1550  CB  PRO A 521     226.494 187.416 210.738  1.00 98.26           C  
ATOM   1551  CG  PRO A 521     227.696 188.281 210.899  1.00 98.26           C  
ATOM   1552  CD  PRO A 521     227.290 189.391 211.796  1.00 98.26           C  
ATOM   1553  N   ALA A 522     224.538 185.821 213.210  1.00 94.05           N  
ATOM   1554  CA  ALA A 522     224.384 184.654 214.070  1.00 94.05           C  
ATOM   1555  C   ALA A 522     225.014 183.437 213.424  1.00 94.05           C  
ATOM   1556  O   ALA A 522     224.619 183.033 212.328  1.00 94.05           O  
ATOM   1557  CB  ALA A 522     222.905 184.398 214.344  1.00 94.05           C  
ATOM   1558  N   THR A 523     225.989 182.845 214.104  1.00 96.74           N  
ATOM   1559  CA  THR A 523     226.747 181.755 213.521  1.00 96.74           C  
ATOM   1560  C   THR A 523     226.642 180.439 214.279  1.00 96.74           C  
ATOM   1561  O   THR A 523     227.266 179.457 213.861  1.00 96.74           O  
ATOM   1562  CB  THR A 523     228.217 182.163 213.393  1.00 96.74           C  
ATOM   1563  OG1 THR A 523     228.966 181.087 212.818  1.00 96.74           O  
ATOM   1564  CG2 THR A 523     228.780 182.530 214.752  1.00 96.74           C  
ATOM   1565  N   VAL A 524     225.890 180.377 215.373  1.00 95.43           N  
ATOM   1566  CA  VAL A 524     225.662 179.123 216.079  1.00 95.43           C  
ATOM   1567  C   VAL A 524     224.249 178.683 215.722  1.00 95.43           C  
ATOM   1568  O   VAL A 524     223.276 179.134 216.330  1.00 95.43           O  
ATOM   1569  CB  VAL A 524     225.837 179.272 217.591  1.00 95.43           C  
ATOM   1570  CG1 VAL A 524     226.035 177.914 218.227  1.00 95.43           C  
ATOM   1571  CG2 VAL A 524     227.000 180.184 217.901  1.00 95.43           C  
ATOM   1572  N   CYS A 525     224.138 177.753 214.778  1.00100.73           N  
ATOM   1573  CA  CYS A 525     222.855 177.248 214.315  1.00100.73           C  
ATOM   1574  C   CYS A 525     222.928 175.732 214.233  1.00100.73           C  
ATOM   1575  O   CYS A 525     224.010 175.147 214.269  1.00100.73           O  
ATOM   1576  CB  CYS A 525     222.466 177.783 212.928  1.00100.73           C  
ATOM   1577  SG  CYS A 525     222.978 179.454 212.428  1.00100.73           S  
ATOM   1578  N   GLY A 526     221.766 175.092 214.144  1.00100.76           N  
ATOM   1579  CA  GLY A 526     221.726 173.655 214.018  1.00100.76           C  
ATOM   1580  C   GLY A 526     221.863 173.268 212.559  1.00100.76           C  
ATOM   1581  O   GLY A 526     221.879 174.132 211.678  1.00100.76           O  
ATOM   1582  N   PRO A 527     221.983 171.973 212.270  1.00 95.04           N  
ATOM   1583  CA  PRO A 527     222.159 171.545 210.878  1.00 95.04           C  
ATOM   1584  C   PRO A 527     220.884 171.708 210.069  1.00 95.04           C  
ATOM   1585  O   PRO A 527     219.787 171.872 210.605  1.00 95.04           O  
ATOM   1586  CB  PRO A 527     222.541 170.069 211.005  1.00 95.04           C  
ATOM   1587  CG  PRO A 527     221.990 169.647 212.309  1.00 95.04           C  
ATOM   1588  CD  PRO A 527     222.028 170.839 213.206  1.00 95.04           C  
ATOM   1589  N   LYS A 528     221.042 171.656 208.752  1.00 87.74           N  
ATOM   1590  CA  LYS A 528     219.924 171.777 207.832  1.00 87.74           C  
ATOM   1591  C   LYS A 528     219.770 170.460 207.082  1.00 87.74           C  
ATOM   1592  O   LYS A 528     220.763 169.839 206.692  1.00 87.74           O  
ATOM   1593  CB  LYS A 528     220.134 172.958 206.874  1.00 87.74           C  
ATOM   1594  CG  LYS A 528     218.922 173.321 206.016  1.00 87.74           C  
ATOM   1595  CD  LYS A 528     219.052 172.864 204.576  1.00 87.74           C  
ATOM   1596  CE  LYS A 528     220.149 173.614 203.852  1.00 87.74           C  
ATOM   1597  NZ  LYS A 528     220.276 173.162 202.441  1.00 87.74           N  
ATOM   1598  N   LYS A 529     218.529 170.037 206.880  1.00 78.30           N  
ATOM   1599  CA  LYS A 529     218.245 168.756 206.255  1.00 78.30           C  
ATOM   1600  C   LYS A 529     218.141 168.890 204.740  1.00 78.30           C  
ATOM   1601  O   LYS A 529     217.684 169.908 204.220  1.00 78.30           O  
ATOM   1602  CB  LYS A 529     216.950 168.179 206.821  1.00 78.30           C  
ATOM   1603  CG  LYS A 529     216.915 167.933 208.346  1.00 78.30           C  
ATOM   1604  CD  LYS A 529     217.775 166.773 208.865  1.00 78.30           C  
ATOM   1605  CE  LYS A 529     219.157 167.191 209.369  1.00 78.30           C  
ATOM   1606  NZ  LYS A 529     219.894 166.035 209.953  1.00 78.30           N  
ATOM   1607  N   SER A 530     218.565 167.843 204.038  1.00 59.08           N  
ATOM   1608  CA  SER A 530     218.651 167.870 202.578  1.00 59.08           C  
ATOM   1609  C   SER A 530     217.311 167.940 201.882  1.00 59.08           C  
ATOM   1610  O   SER A 530     217.172 167.424 200.777  1.00 59.08           O  
ATOM   1611  CB  SER A 530     219.390 166.643 202.062  1.00 59.08           C  
ATOM   1612  OG  SER A 530     219.556 166.731 200.660  1.00 59.08           O  
TER    1613      SER A 530                                                      
ATOM   1614  N   SER D  19     223.186 193.920 261.104  1.00 86.75           N  
ATOM   1615  CA  SER D  19     223.618 195.018 261.957  1.00 86.75           C  
ATOM   1616  C   SER D  19     223.124 194.821 263.380  1.00 86.75           C  
ATOM   1617  O   SER D  19     223.813 195.168 264.336  1.00 86.75           O  
ATOM   1618  CB  SER D  19     223.120 196.355 261.408  1.00 86.75           C  
ATOM   1619  OG  SER D  19     223.649 197.437 262.154  1.00 86.75           O  
ATOM   1620  N   THR D  20     221.924 194.266 263.518  1.00 86.41           N  
ATOM   1621  CA  THR D  20     221.370 194.013 264.836  1.00 86.41           C  
ATOM   1622  C   THR D  20     221.882 192.681 265.371  1.00 86.41           C  
ATOM   1623  O   THR D  20     222.599 191.944 264.693  1.00 86.41           O  
ATOM   1624  CB  THR D  20     219.847 194.028 264.791  1.00 86.41           C  
ATOM   1625  OG1 THR D  20     219.334 193.945 266.126  1.00 86.41           O  
ATOM   1626  CG2 THR D  20     219.334 192.853 263.992  1.00 86.41           C  
ATOM   1627  N   ILE D  21     221.499 192.371 266.611  1.00 89.30           N  
ATOM   1628  CA  ILE D  21     221.921 191.129 267.251  1.00 89.30           C  
ATOM   1629  C   ILE D  21     221.260 189.927 266.587  1.00 89.30           C  
ATOM   1630  O   ILE D  21     221.871 188.855 266.477  1.00 89.30           O  
ATOM   1631  CB  ILE D  21     221.628 191.193 268.764  1.00 89.30           C  
ATOM   1632  CG1 ILE D  21     222.240 192.454 269.381  1.00 89.30           C  
ATOM   1633  CG2 ILE D  21     222.197 189.988 269.491  1.00 89.30           C  
ATOM   1634  CD1 ILE D  21     221.236 193.550 269.721  1.00 89.30           C  
ATOM   1635  N   GLU D  22     220.022 190.086 266.113  1.00 88.76           N  
ATOM   1636  CA  GLU D  22     219.278 188.957 265.564  1.00 88.76           C  
ATOM   1637  C   GLU D  22     219.870 188.501 264.232  1.00 88.76           C  
ATOM   1638  O   GLU D  22     219.932 187.298 263.953  1.00 88.76           O  
ATOM   1639  CB  GLU D  22     217.805 189.342 265.421  1.00 88.76           C  
ATOM   1640  CG  GLU D  22     216.828 188.189 265.214  1.00 88.76           C  
ATOM   1641  CD  GLU D  22     216.673 187.783 263.766  1.00 88.76           C  
ATOM   1642  OE1 GLU D  22     216.877 188.640 262.881  1.00 88.76           O  
ATOM   1643  OE2 GLU D  22     216.338 186.609 263.513  1.00 88.76           O  
ATOM   1644  N   GLU D  23     220.324 189.445 263.402  1.00 87.74           N  
ATOM   1645  CA  GLU D  23     220.980 189.074 262.150  1.00 87.74           C  
ATOM   1646  C   GLU D  23     222.342 188.437 262.391  1.00 87.74           C  
ATOM   1647  O   GLU D  23     222.747 187.539 261.637  1.00 87.74           O  
ATOM   1648  CB  GLU D  23     221.125 190.298 261.246  1.00 87.74           C  
ATOM   1649  CG  GLU D  23     219.812 190.956 260.828  1.00 87.74           C  
ATOM   1650  CD  GLU D  23     218.905 190.062 259.992  1.00 87.74           C  
ATOM   1651  OE1 GLU D  23     219.400 189.132 259.317  1.00 87.74           O  
ATOM   1652  OE2 GLU D  23     217.678 190.296 260.010  1.00 87.74           O  
ATOM   1653  N   GLN D  24     223.053 188.885 263.432  1.00 82.58           N  
ATOM   1654  CA  GLN D  24     224.286 188.224 263.847  1.00 82.58           C  
ATOM   1655  C   GLN D  24     224.016 186.791 264.270  1.00 82.58           C  
ATOM   1656  O   GLN D  24     224.783 185.879 263.935  1.00 82.58           O  
ATOM   1657  CB  GLN D  24     224.929 188.990 265.000  1.00 82.58           C  
ATOM   1658  CG  GLN D  24     225.442 190.364 264.657  1.00 82.58           C  
ATOM   1659  CD  GLN D  24     226.033 191.059 265.861  1.00 82.58           C  
ATOM   1660  OE1 GLN D  24     226.000 190.531 266.969  1.00 82.58           O  
ATOM   1661  NE2 GLN D  24     226.545 192.262 265.661  1.00 82.58           N  
ATOM   1662  N   ALA D  25     222.910 186.577 264.986  1.00 79.94           N  
ATOM   1663  CA  ALA D  25     222.519 185.236 265.398  1.00 79.94           C  
ATOM   1664  C   ALA D  25     222.161 184.371 264.200  1.00 79.94           C  
ATOM   1665  O   ALA D  25     222.500 183.186 264.169  1.00 79.94           O  
ATOM   1666  CB  ALA D  25     221.350 185.310 266.375  1.00 79.94           C  
ATOM   1667  N   LYS D  26     221.491 184.947 263.200  1.00 80.66           N  
ATOM   1668  CA  LYS D  26     221.138 184.182 262.006  1.00 80.66           C  
ATOM   1669  C   LYS D  26     222.367 183.777 261.197  1.00 80.66           C  
ATOM   1670  O   LYS D  26     222.457 182.630 260.738  1.00 80.66           O  
ATOM   1671  CB  LYS D  26     220.177 184.983 261.134  1.00 80.66           C  
ATOM   1672  CG  LYS D  26     218.770 185.065 261.674  1.00 80.66           C  
ATOM   1673  CD  LYS D  26     217.872 185.811 260.709  1.00 80.66           C  
ATOM   1674  CE  LYS D  26     217.578 184.978 259.476  1.00 80.66           C  
ATOM   1675  NZ  LYS D  26     216.595 185.647 258.579  1.00 80.66           N  
ATOM   1676  N   THR D  27     223.329 184.691 261.019  1.00 75.27           N  
ATOM   1677  CA  THR D  27     224.551 184.343 260.290  1.00 75.27           C  
ATOM   1678  C   THR D  27     225.390 183.324 261.054  1.00 75.27           C  
ATOM   1679  O   THR D  27     225.940 182.382 260.455  1.00 75.27           O  
ATOM   1680  CB  THR D  27     225.379 185.592 260.002  1.00 75.27           C  
ATOM   1681  OG1 THR D  27     225.602 186.308 261.221  1.00 75.27           O  
ATOM   1682  CG2 THR D  27     224.654 186.491 259.022  1.00 75.27           C  
ATOM   1683  N   PHE D  28     225.476 183.487 262.380  1.00 73.39           N  
ATOM   1684  CA  PHE D  28     226.197 182.534 263.213  1.00 73.39           C  
ATOM   1685  C   PHE D  28     225.545 181.163 263.164  1.00 73.39           C  
ATOM   1686  O   PHE D  28     226.237 180.141 263.110  1.00 73.39           O  
ATOM   1687  CB  PHE D  28     226.253 183.043 264.651  1.00 73.39           C  
ATOM   1688  CG  PHE D  28     226.613 181.990 265.651  1.00 73.39           C  
ATOM   1689  CD1 PHE D  28     227.895 181.477 265.700  1.00 73.39           C  
ATOM   1690  CD2 PHE D  28     225.665 181.502 266.534  1.00 73.39           C  
ATOM   1691  CE1 PHE D  28     228.226 180.506 266.615  1.00 73.39           C  
ATOM   1692  CE2 PHE D  28     225.992 180.526 267.444  1.00 73.39           C  
ATOM   1693  CZ  PHE D  28     227.274 180.029 267.485  1.00 73.39           C  
ATOM   1694  N   LEU D  29     224.214 181.124 263.146  1.00 73.63           N  
ATOM   1695  CA  LEU D  29     223.515 179.854 263.084  1.00 73.63           C  
ATOM   1696  C   LEU D  29     223.656 179.200 261.720  1.00 73.63           C  
ATOM   1697  O   LEU D  29     223.689 177.974 261.642  1.00 73.63           O  
ATOM   1698  CB  LEU D  29     222.046 180.049 263.441  1.00 73.63           C  
ATOM   1699  CG  LEU D  29     221.768 180.035 264.942  1.00 73.63           C  
ATOM   1700  CD1 LEU D  29     220.332 180.418 265.209  1.00 73.63           C  
ATOM   1701  CD2 LEU D  29     222.091 178.685 265.541  1.00 73.63           C  
ATOM   1702  N   ASP D  30     223.749 179.986 260.641  1.00 74.75           N  
ATOM   1703  CA  ASP D  30     224.000 179.396 259.326  1.00 74.75           C  
ATOM   1704  C   ASP D  30     225.376 178.741 259.252  1.00 74.75           C  
ATOM   1705  O   ASP D  30     225.507 177.595 258.778  1.00 74.75           O  
ATOM   1706  CB  ASP D  30     223.878 180.462 258.240  1.00 74.75           C  
ATOM   1707  CG  ASP D  30     222.456 180.927 258.034  1.00 74.75           C  
ATOM   1708  OD1 ASP D  30     221.531 180.251 258.528  1.00 74.75           O  
ATOM   1709  OD2 ASP D  30     222.263 181.967 257.374  1.00 74.75           O  
ATOM   1710  N   LYS D  31     226.401 179.423 259.777  1.00 69.59           N  
ATOM   1711  CA  LYS D  31     227.739 178.836 259.760  1.00 69.59           C  
ATOM   1712  C   LYS D  31     227.834 177.642 260.707  1.00 69.59           C  
ATOM   1713  O   LYS D  31     228.459 176.616 260.365  1.00 69.59           O  
ATOM   1714  CB  LYS D  31     228.770 179.909 260.108  1.00 69.59           C  
ATOM   1715  CG  LYS D  31     230.183 179.408 260.296  1.00 69.59           C  
ATOM   1716  CD  LYS D  31     230.778 179.873 261.601  1.00 69.59           C  
ATOM   1717  CE  LYS D  31     232.085 179.157 261.876  1.00 69.59           C  
ATOM   1718  NZ  LYS D  31     232.642 179.517 263.204  1.00 69.59           N  
ATOM   1719  N   PHE D  32     227.105 177.705 261.829  1.00 71.49           N  
ATOM   1720  CA  PHE D  32     227.062 176.584 262.753  1.00 71.49           C  
ATOM   1721  C   PHE D  32     226.330 175.409 262.140  1.00 71.49           C  
ATOM   1722  O   PHE D  32     226.723 174.268 262.368  1.00 71.49           O  
ATOM   1723  CB  PHE D  32     226.386 176.981 264.067  1.00 71.49           C  
ATOM   1724  CG  PHE D  32     225.965 175.804 264.901  1.00 71.49           C  
ATOM   1725  CD1 PHE D  32     226.915 175.017 265.527  1.00 71.49           C  
ATOM   1726  CD2 PHE D  32     224.628 175.459 265.027  1.00 71.49           C  
ATOM   1727  CE1 PHE D  32     226.544 173.926 266.276  1.00 71.49           C  
ATOM   1728  CE2 PHE D  32     224.254 174.364 265.773  1.00 71.49           C  
ATOM   1729  CZ  PHE D  32     225.213 173.600 266.399  1.00 71.49           C  
ATOM   1730  N   ASN D  33     225.298 175.666 261.336  1.00 70.28           N  
ATOM   1731  CA  ASN D  33     224.488 174.575 260.821  1.00 70.28           C  
ATOM   1732  C   ASN D  33     225.262 173.813 259.769  1.00 70.28           C  
ATOM   1733  O   ASN D  33     225.249 172.578 259.760  1.00 70.28           O  
ATOM   1734  CB  ASN D  33     223.179 175.099 260.237  1.00 70.28           C  
ATOM   1735  CG  ASN D  33     222.124 175.329 261.288  1.00 70.28           C  
ATOM   1736  OD1 ASN D  33     222.179 174.761 262.374  1.00 70.28           O  
ATOM   1737  ND2 ASN D  33     221.154 176.173 260.972  1.00 70.28           N  
ATOM   1738  N   HIS D  34     226.038 174.531 258.954  1.00 69.90           N  
ATOM   1739  CA  HIS D  34     226.840 173.860 257.935  1.00 69.90           C  
ATOM   1740  C   HIS D  34     227.952 173.019 258.569  1.00 69.90           C  
ATOM   1741  O   HIS D  34     228.096 171.813 258.265  1.00 69.90           O  
ATOM   1742  CB  HIS D  34     227.405 174.913 256.983  1.00 69.90           C  
ATOM   1743  CG  HIS D  34     228.555 174.436 256.161  1.00 69.90           C  
ATOM   1744  ND1 HIS D  34     228.382 173.832 254.937  1.00 69.90           N  
ATOM   1745  CD2 HIS D  34     229.891 174.496 256.368  1.00 69.90           C  
ATOM   1746  CE1 HIS D  34     229.561 173.523 254.434  1.00 69.90           C  
ATOM   1747  NE2 HIS D  34     230.494 173.912 255.283  1.00 69.90           N  
ATOM   1748  N   GLU D  35     228.685 173.610 259.524  1.00 71.88           N  
ATOM   1749  CA  GLU D  35     229.785 172.880 260.150  1.00 71.88           C  
ATOM   1750  C   GLU D  35     229.267 171.742 261.024  1.00 71.88           C  
ATOM   1751  O   GLU D  35     229.884 170.667 261.088  1.00 71.88           O  
ATOM   1752  CB  GLU D  35     230.650 173.836 260.961  1.00 71.88           C  
ATOM   1753  CG  GLU D  35     231.390 174.847 260.117  1.00 71.88           C  
ATOM   1754  CD  GLU D  35     232.362 175.671 260.927  1.00 71.88           C  
ATOM   1755  OE1 GLU D  35     232.246 175.675 262.168  1.00 71.88           O  
ATOM   1756  OE2 GLU D  35     233.243 176.315 260.323  1.00 71.88           O  
ATOM   1757  N   ALA D  36     228.124 171.960 261.683  1.00 71.95           N  
ATOM   1758  CA  ALA D  36     227.498 170.939 262.507  1.00 71.95           C  
ATOM   1759  C   ALA D  36     227.057 169.748 261.677  1.00 71.95           C  
ATOM   1760  O   ALA D  36     227.203 168.609 262.122  1.00 71.95           O  
ATOM   1761  CB  ALA D  36     226.322 171.540 263.265  1.00 71.95           C  
ATOM   1762  N   GLU D  37     226.521 169.976 260.469  1.00 73.67           N  
ATOM   1763  CA  GLU D  37     226.008 168.830 259.721  1.00 73.67           C  
ATOM   1764  C   GLU D  37     227.158 168.004 259.173  1.00 73.67           C  
ATOM   1765  O   GLU D  37     227.079 166.768 259.182  1.00 73.67           O  
ATOM   1766  CB  GLU D  37     225.049 169.224 258.596  1.00 73.67           C  
ATOM   1767  CG  GLU D  37     223.764 169.879 259.046  1.00 73.67           C  
ATOM   1768  CD  GLU D  37     223.047 170.592 257.919  1.00 73.67           C  
ATOM   1769  OE1 GLU D  37     223.259 170.218 256.747  1.00 73.67           O  
ATOM   1770  OE2 GLU D  37     222.271 171.528 258.205  1.00 73.67           O  
ATOM   1771  N   ASP D  38     228.290 168.650 258.862  1.00 71.29           N  
ATOM   1772  CA  ASP D  38     229.432 167.865 258.388  1.00 71.29           C  
ATOM   1773  C   ASP D  38     230.063 167.064 259.528  1.00 71.29           C  
ATOM   1774  O   ASP D  38     230.317 165.852 259.388  1.00 71.29           O  
ATOM   1775  CB  ASP D  38     230.467 168.780 257.744  1.00 71.29           C  
ATOM   1776  CG  ASP D  38     231.694 168.030 257.283  1.00 71.29           C  
ATOM   1777  OD1 ASP D  38     231.542 166.917 256.741  1.00 71.29           O  
ATOM   1778  OD2 ASP D  38     232.812 168.549 257.466  1.00 71.29           O  
ATOM   1779  N   LEU D  39     230.303 167.716 260.673  1.00 69.97           N  
ATOM   1780  CA  LEU D  39     230.952 167.032 261.790  1.00 69.97           C  
ATOM   1781  C   LEU D  39     230.045 165.951 262.368  1.00 69.97           C  
ATOM   1782  O   LEU D  39     230.525 164.869 262.745  1.00 69.97           O  
ATOM   1783  CB  LEU D  39     231.384 168.038 262.852  1.00 69.97           C  
ATOM   1784  CG  LEU D  39     232.630 168.858 262.490  1.00 69.97           C  
ATOM   1785  CD1 LEU D  39     233.296 169.365 263.735  1.00 69.97           C  
ATOM   1786  CD2 LEU D  39     233.642 168.071 261.664  1.00 69.97           C  
ATOM   1787  N   PHE D  40     228.740 166.245 262.480  1.00 70.86           N  
ATOM   1788  CA  PHE D  40     227.775 165.261 262.950  1.00 70.86           C  
ATOM   1789  C   PHE D  40     227.763 164.059 262.022  1.00 70.86           C  
ATOM   1790  O   PHE D  40     227.586 162.929 262.491  1.00 70.86           O  
ATOM   1791  CB  PHE D  40     226.386 165.878 263.056  1.00 70.86           C  
ATOM   1792  CG  PHE D  40     225.336 164.910 263.495  1.00 70.86           C  
ATOM   1793  CD1 PHE D  40     225.334 164.424 264.790  1.00 70.86           C  
ATOM   1794  CD2 PHE D  40     224.358 164.477 262.618  1.00 70.86           C  
ATOM   1795  CE1 PHE D  40     224.374 163.528 265.205  1.00 70.86           C  
ATOM   1796  CE2 PHE D  40     223.395 163.581 263.027  1.00 70.86           C  
ATOM   1797  CZ  PHE D  40     223.403 163.106 264.322  1.00 70.86           C  
ATOM   1798  N   TYR D  41     227.852 164.290 260.696  1.00 67.59           N  
ATOM   1799  CA  TYR D  41     227.805 163.171 259.761  1.00 67.59           C  
ATOM   1800  C   TYR D  41     228.988 162.251 259.990  1.00 67.59           C  
ATOM   1801  O   TYR D  41     228.838 161.025 259.959  1.00 67.59           O  
ATOM   1802  CB  TYR D  41     227.802 163.629 258.306  1.00 67.59           C  
ATOM   1803  CG  TYR D  41     227.529 162.466 257.372  1.00 67.59           C  
ATOM   1804  CD1 TYR D  41     226.245 161.993 257.177  1.00 67.59           C  
ATOM   1805  CD2 TYR D  41     228.574 161.807 256.729  1.00 67.59           C  
ATOM   1806  CE1 TYR D  41     226.003 160.919 256.349  1.00 67.59           C  
ATOM   1807  CE2 TYR D  41     228.341 160.730 255.916  1.00 67.59           C  
ATOM   1808  CZ  TYR D  41     227.056 160.296 255.721  1.00 67.59           C  
ATOM   1809  OH  TYR D  41     226.824 159.228 254.894  1.00 67.59           O  
ATOM   1810  N   GLN D  42     230.180 162.833 260.170  1.00 70.17           N  
ATOM   1811  CA  GLN D  42     231.368 162.009 260.393  1.00 70.17           C  
ATOM   1812  C   GLN D  42     231.245 161.220 261.694  1.00 70.17           C  
ATOM   1813  O   GLN D  42     231.577 160.024 261.739  1.00 70.17           O  
ATOM   1814  CB  GLN D  42     232.631 162.862 260.387  1.00 70.17           C  
ATOM   1815  CG  GLN D  42     232.822 163.649 259.112  1.00 70.17           C  
ATOM   1816  CD  GLN D  42     234.014 164.570 259.178  1.00 70.17           C  
ATOM   1817  OE1 GLN D  42     234.106 165.539 258.430  1.00 70.17           O  
ATOM   1818  NE2 GLN D  42     234.950 164.259 260.065  1.00 70.17           N  
ATOM   1819  N   SER D  43     230.734 161.869 262.749  1.00 73.77           N  
ATOM   1820  CA  SER D  43     230.552 161.201 264.038  1.00 73.77           C  
ATOM   1821  C   SER D  43     229.546 160.059 263.941  1.00 73.77           C  
ATOM   1822  O   SER D  43     229.772 158.970 264.487  1.00 73.77           O  
ATOM   1823  CB  SER D  43     230.104 162.213 265.088  1.00 73.77           C  
ATOM   1824  OG  SER D  43     229.899 161.587 266.339  1.00 73.77           O  
ATOM   1825  N   SER D  44     228.447 160.280 263.219  1.00 72.16           N  
ATOM   1826  CA  SER D  44     227.409 159.265 263.112  1.00 72.16           C  
ATOM   1827  C   SER D  44     227.865 158.116 262.226  1.00 72.16           C  
ATOM   1828  O   SER D  44     227.533 156.957 262.494  1.00 72.16           O  
ATOM   1829  CB  SER D  44     226.126 159.893 262.582  1.00 72.16           C  
ATOM   1830  OG  SER D  44     225.759 161.015 263.358  1.00 72.16           O  
ATOM   1831  N   LEU D  45     228.648 158.413 261.182  1.00 74.96           N  
ATOM   1832  CA  LEU D  45     229.194 157.361 260.331  1.00 74.96           C  
ATOM   1833  C   LEU D  45     230.187 156.506 261.099  1.00 74.96           C  
ATOM   1834  O   LEU D  45     230.247 155.290 260.894  1.00 74.96           O  
ATOM   1835  CB  LEU D  45     229.849 157.955 259.090  1.00 74.96           C  
ATOM   1836  CG  LEU D  45     230.075 156.948 257.964  1.00 74.96           C  
ATOM   1837  CD1 LEU D  45     228.768 156.315 257.543  1.00 74.96           C  
ATOM   1838  CD2 LEU D  45     230.759 157.608 256.782  1.00 74.96           C  
ATOM   1839  N   ALA D  46     230.914 157.105 262.041  1.00 79.03           N  
ATOM   1840  CA  ALA D  46     231.924 156.341 262.758  1.00 79.03           C  
ATOM   1841  C   ALA D  46     231.260 155.489 263.832  1.00 79.03           C  
ATOM   1842  O   ALA D  46     231.671 154.345 264.065  1.00 79.03           O  
ATOM   1843  CB  ALA D  46     232.968 157.272 263.368  1.00 79.03           C  
ATOM   1844  N   SER D  47     230.223 156.032 264.480  1.00 81.06           N  
ATOM   1845  CA  SER D  47     229.425 155.243 265.416  1.00 81.06           C  
ATOM   1846  C   SER D  47     228.719 154.090 264.708  1.00 81.06           C  
ATOM   1847  O   SER D  47     228.601 152.994 265.267  1.00 81.06           O  
ATOM   1848  CB  SER D  47     228.409 156.134 266.126  1.00 81.06           C  
ATOM   1849  OG  SER D  47     229.054 157.049 266.991  1.00 81.06           O  
ATOM   1850  N   TRP D  48     228.225 154.325 263.487  1.00 79.33           N  
ATOM   1851  CA  TRP D  48     227.620 153.252 262.703  1.00 79.33           C  
ATOM   1852  C   TRP D  48     228.637 152.180 262.345  1.00 79.33           C  
ATOM   1853  O   TRP D  48     228.329 150.986 262.406  1.00 79.33           O  
ATOM   1854  CB  TRP D  48     226.988 153.816 261.430  1.00 79.33           C  
ATOM   1855  CG  TRP D  48     226.475 152.764 260.478  1.00 79.33           C  
ATOM   1856  CD1 TRP D  48     227.160 152.182 259.448  1.00 79.33           C  
ATOM   1857  CD2 TRP D  48     225.174 152.174 260.470  1.00 79.33           C  
ATOM   1858  NE1 TRP D  48     226.368 151.268 258.807  1.00 79.33           N  
ATOM   1859  CE2 TRP D  48     225.142 151.245 259.413  1.00 79.33           C  
ATOM   1860  CE3 TRP D  48     224.031 152.341 261.253  1.00 79.33           C  
ATOM   1861  CZ2 TRP D  48     224.015 150.489 259.122  1.00 79.33           C  
ATOM   1862  CZ3 TRP D  48     222.917 151.591 260.960  1.00 79.33           C  
ATOM   1863  CH2 TRP D  48     222.916 150.675 259.907  1.00 79.33           C  
ATOM   1864  N   ASN D  49     229.846 152.586 261.947  1.00 85.56           N  
ATOM   1865  CA  ASN D  49     230.873 151.609 261.602  1.00 85.56           C  
ATOM   1866  C   ASN D  49     231.339 150.822 262.818  1.00 85.56           C  
ATOM   1867  O   ASN D  49     231.747 149.666 262.680  1.00 85.56           O  
ATOM   1868  CB  ASN D  49     232.053 152.300 260.928  1.00 85.56           C  
ATOM   1869  CG  ASN D  49     231.719 152.789 259.539  1.00 85.56           C  
ATOM   1870  OD1 ASN D  49     230.805 152.280 258.896  1.00 85.56           O  
ATOM   1871  ND2 ASN D  49     232.461 153.778 259.065  1.00 85.56           N  
ATOM   1872  N   TYR D  50     231.297 151.422 264.009  1.00 93.24           N  
ATOM   1873  CA  TYR D  50     231.568 150.641 265.212  1.00 93.24           C  
ATOM   1874  C   TYR D  50     230.428 149.678 265.518  1.00 93.24           C  
ATOM   1875  O   TYR D  50     230.669 148.522 265.885  1.00 93.24           O  
ATOM   1876  CB  TYR D  50     231.812 151.554 266.411  1.00 93.24           C  
ATOM   1877  CG  TYR D  50     231.675 150.834 267.737  1.00 93.24           C  
ATOM   1878  CD1 TYR D  50     232.603 149.878 268.129  1.00 93.24           C  
ATOM   1879  CD2 TYR D  50     230.610 151.098 268.590  1.00 93.24           C  
ATOM   1880  CE1 TYR D  50     232.474 149.211 269.331  1.00 93.24           C  
ATOM   1881  CE2 TYR D  50     230.479 150.440 269.795  1.00 93.24           C  
ATOM   1882  CZ  TYR D  50     231.414 149.499 270.159  1.00 93.24           C  
ATOM   1883  OH  TYR D  50     231.289 148.838 271.357  1.00 93.24           O  
ATOM   1884  N   ASN D  51     229.182 150.134 265.380  1.00 90.64           N  
ATOM   1885  CA  ASN D  51     228.046 149.340 265.838  1.00 90.64           C  
ATOM   1886  C   ASN D  51     227.752 148.162 264.920  1.00 90.64           C  
ATOM   1887  O   ASN D  51     227.270 147.126 265.387  1.00 90.64           O  
ATOM   1888  CB  ASN D  51     226.815 150.226 265.975  1.00 90.64           C  
ATOM   1889  CG  ASN D  51     226.811 151.014 267.262  1.00 90.64           C  
ATOM   1890  OD1 ASN D  51     226.203 150.607 268.249  1.00 90.64           O  
ATOM   1891  ND2 ASN D  51     227.493 152.150 267.262  1.00 90.64           N  
ATOM   1892  N   THR D  52     228.022 148.291 263.626  1.00 94.19           N  
ATOM   1893  CA  THR D  52     227.856 147.168 262.716  1.00 94.19           C  
ATOM   1894  C   THR D  52     229.118 146.330 262.576  1.00 94.19           C  
ATOM   1895  O   THR D  52     229.073 145.268 261.948  1.00 94.19           O  
ATOM   1896  CB  THR D  52     227.414 147.658 261.330  1.00 94.19           C  
ATOM   1897  OG1 THR D  52     226.903 146.553 260.578  1.00 94.19           O  
ATOM   1898  CG2 THR D  52     228.578 148.261 260.569  1.00 94.19           C  
ATOM   1899  N   ASN D  53     230.237 146.780 263.142  1.00102.20           N  
ATOM   1900  CA  ASN D  53     231.517 146.085 263.010  1.00102.20           C  
ATOM   1901  C   ASN D  53     232.341 146.418 264.255  1.00102.20           C  
ATOM   1902  O   ASN D  53     233.036 147.434 264.296  1.00102.20           O  
ATOM   1903  CB  ASN D  53     232.222 146.518 261.735  1.00102.20           C  
ATOM   1904  CG  ASN D  53     233.258 145.533 261.271  1.00102.20           C  
ATOM   1905  OD1 ASN D  53     233.815 144.773 262.059  1.00102.20           O  
ATOM   1906  ND2 ASN D  53     233.537 145.553 259.976  1.00102.20           N  
ATOM   1907  N   ILE D  54     232.263 145.551 265.262  1.00101.24           N  
ATOM   1908  CA  ILE D  54     232.928 145.826 266.531  1.00101.24           C  
ATOM   1909  C   ILE D  54     234.390 145.419 266.433  1.00101.24           C  
ATOM   1910  O   ILE D  54     234.747 144.262 266.682  1.00101.24           O  
ATOM   1911  CB  ILE D  54     232.233 145.112 267.703  1.00101.24           C  
ATOM   1912  CG1 ILE D  54     230.729 145.369 267.664  1.00101.24           C  
ATOM   1913  CG2 ILE D  54     232.806 145.583 269.027  1.00101.24           C  
ATOM   1914  CD1 ILE D  54     229.925 144.377 268.467  1.00101.24           C  
ATOM   1915  N   THR D  55     235.238 146.367 266.047  1.00106.20           N  
ATOM   1916  CA  THR D  55     236.667 146.145 265.900  1.00106.20           C  
ATOM   1917  C   THR D  55     237.355 147.395 266.440  1.00106.20           C  
ATOM   1918  O   THR D  55     236.777 148.483 266.402  1.00106.20           O  
ATOM   1919  CB  THR D  55     237.000 145.858 264.419  1.00106.20           C  
ATOM   1920  OG1 THR D  55     236.234 144.731 263.983  1.00106.20           O  
ATOM   1921  CG2 THR D  55     238.453 145.472 264.229  1.00106.20           C  
ATOM   1922  N   GLU D  56     238.579 147.236 266.968  1.00108.66           N  
ATOM   1923  CA  GLU D  56     239.202 148.281 267.783  1.00108.66           C  
ATOM   1924  C   GLU D  56     239.548 149.536 266.980  1.00108.66           C  
ATOM   1925  O   GLU D  56     239.556 150.640 267.543  1.00108.66           O  
ATOM   1926  CB  GLU D  56     240.446 147.733 268.489  1.00108.66           C  
ATOM   1927  CG  GLU D  56     241.571 147.262 267.578  1.00108.66           C  
ATOM   1928  CD  GLU D  56     241.455 145.798 267.197  1.00108.66           C  
ATOM   1929  OE1 GLU D  56     240.366 145.212 267.371  1.00108.66           O  
ATOM   1930  OE2 GLU D  56     242.461 145.228 266.724  1.00108.66           O  
ATOM   1931  N   GLU D  57     239.824 149.404 265.678  1.00108.12           N  
ATOM   1932  CA  GLU D  57     240.039 150.607 264.880  1.00108.12           C  
ATOM   1933  C   GLU D  57     238.736 151.367 264.666  1.00108.12           C  
ATOM   1934  O   GLU D  57     238.743 152.602 264.621  1.00108.12           O  
ATOM   1935  CB  GLU D  57     240.713 150.278 263.545  1.00108.12           C  
ATOM   1936  CG  GLU D  57     239.985 149.306 262.647  1.00108.12           C  
ATOM   1937  CD  GLU D  57     240.521 147.900 262.779  1.00108.12           C  
ATOM   1938  OE1 GLU D  57     241.227 147.623 263.772  1.00108.12           O  
ATOM   1939  OE2 GLU D  57     240.244 147.071 261.887  1.00108.12           O  
ATOM   1940  N   ASN D  58     237.607 150.658 264.584  1.00102.43           N  
ATOM   1941  CA  ASN D  58     236.317 151.336 264.570  1.00102.43           C  
ATOM   1942  C   ASN D  58     236.024 151.988 265.915  1.00102.43           C  
ATOM   1943  O   ASN D  58     235.389 153.049 265.958  1.00102.43           O  
ATOM   1944  CB  ASN D  58     235.207 150.358 264.195  1.00102.43           C  
ATOM   1945  CG  ASN D  58     235.290 149.912 262.755  1.00102.43           C  
ATOM   1946  OD1 ASN D  58     235.916 150.568 261.926  1.00102.43           O  
ATOM   1947  ND2 ASN D  58     234.658 148.791 262.449  1.00102.43           N  
ATOM   1948  N   VAL D  59     236.506 151.385 267.007  1.00102.58           N  
ATOM   1949  CA  VAL D  59     236.346 151.971 268.338  1.00102.58           C  
ATOM   1950  C   VAL D  59     237.098 153.291 268.431  1.00102.58           C  
ATOM   1951  O   VAL D  59     236.555 154.304 268.891  1.00102.58           O  
ATOM   1952  CB  VAL D  59     236.824 150.985 269.420  1.00102.58           C  
ATOM   1953  CG1 VAL D  59     236.769 151.628 270.798  1.00102.58           C  
ATOM   1954  CG2 VAL D  59     236.014 149.714 269.389  1.00102.58           C  
ATOM   1955  N   GLN D  60     238.353 153.310 267.972  1.00103.92           N  
ATOM   1956  CA  GLN D  60     239.116 154.552 268.055  1.00103.92           C  
ATOM   1957  C   GLN D  60     238.635 155.586 267.039  1.00103.92           C  
ATOM   1958  O   GLN D  60     238.732 156.788 267.305  1.00103.92           O  
ATOM   1959  CB  GLN D  60     240.621 154.273 267.923  1.00103.92           C  
ATOM   1960  CG  GLN D  60     241.114 153.666 266.615  1.00103.92           C  
ATOM   1961  CD  GLN D  60     241.383 154.685 265.524  1.00103.92           C  
ATOM   1962  OE1 GLN D  60     241.738 155.829 265.801  1.00103.92           O  
ATOM   1963  NE2 GLN D  60     241.209 154.272 264.274  1.00103.92           N  
ATOM   1964  N   ASN D  61     238.097 155.150 265.892  1.00102.04           N  
ATOM   1965  CA  ASN D  61     237.486 156.091 264.955  1.00102.04           C  
ATOM   1966  C   ASN D  61     236.249 156.751 265.552  1.00102.04           C  
ATOM   1967  O   ASN D  61     236.068 157.973 265.430  1.00102.04           O  
ATOM   1968  CB  ASN D  61     237.125 155.378 263.654  1.00102.04           C  
ATOM   1969  CG  ASN D  61     238.319 155.173 262.755  1.00102.04           C  
ATOM   1970  OD1 ASN D  61     239.240 155.988 262.733  1.00102.04           O  
ATOM   1971  ND2 ASN D  61     238.312 154.080 262.003  1.00102.04           N  
ATOM   1972  N   MET D  62     235.405 155.959 266.226  1.00 96.98           N  
ATOM   1973  CA  MET D  62     234.233 156.508 266.898  1.00 96.98           C  
ATOM   1974  C   MET D  62     234.639 157.443 268.027  1.00 96.98           C  
ATOM   1975  O   MET D  62     234.015 158.492 268.224  1.00 96.98           O  
ATOM   1976  CB  MET D  62     233.348 155.380 267.425  1.00 96.98           C  
ATOM   1977  CG  MET D  62     232.080 155.868 268.103  1.00 96.98           C  
ATOM   1978  SD  MET D  62     231.123 154.565 268.884  1.00 96.98           S  
ATOM   1979  CE  MET D  62     232.072 154.292 270.375  1.00 96.98           C  
ATOM   1980  N   ASN D  63     235.702 157.091 268.760  1.00 98.80           N  
ATOM   1981  CA  ASN D  63     236.188 157.949 269.837  1.00 98.80           C  
ATOM   1982  C   ASN D  63     236.725 159.270 269.300  1.00 98.80           C  
ATOM   1983  O   ASN D  63     236.439 160.330 269.869  1.00 98.80           O  
ATOM   1984  CB  ASN D  63     237.251 157.219 270.651  1.00 98.80           C  
ATOM   1985  CG  ASN D  63     236.671 156.097 271.480  1.00 98.80           C  
ATOM   1986  OD1 ASN D  63     235.467 155.850 271.449  1.00 98.80           O  
ATOM   1987  ND2 ASN D  63     237.525 155.408 272.226  1.00 98.80           N  
ATOM   1988  N   ASN D  64     237.478 159.234 268.192  1.00 96.30           N  
ATOM   1989  CA  ASN D  64     238.049 160.460 267.642  1.00 96.30           C  
ATOM   1990  C   ASN D  64     236.963 161.358 267.072  1.00 96.30           C  
ATOM   1991  O   ASN D  64     237.021 162.585 267.233  1.00 96.30           O  
ATOM   1992  CB  ASN D  64     239.082 160.139 266.564  1.00 96.30           C  
ATOM   1993  CG  ASN D  64     240.326 159.493 267.126  1.00 96.30           C  
ATOM   1994  OD1 ASN D  64     240.530 159.463 268.339  1.00 96.30           O  
ATOM   1995  ND2 ASN D  64     241.171 158.973 266.245  1.00 96.30           N  
ATOM   1996  N   ALA D  65     235.904 160.764 266.522  1.00 89.67           N  
ATOM   1997  CA  ALA D  65     234.881 161.592 265.904  1.00 89.67           C  
ATOM   1998  C   ALA D  65     233.964 162.168 266.975  1.00 89.67           C  
ATOM   1999  O   ALA D  65     233.560 163.337 266.888  1.00 89.67           O  
ATOM   2000  CB  ALA D  65     234.104 160.776 264.878  1.00 89.67           C  
ATOM   2001  N   GLY D  66     233.631 161.354 267.985  1.00 89.56           N  
ATOM   2002  CA  GLY D  66     232.886 161.849 269.131  1.00 89.56           C  
ATOM   2003  C   GLY D  66     233.624 162.962 269.849  1.00 89.56           C  
ATOM   2004  O   GLY D  66     233.011 163.932 270.301  1.00 89.56           O  
ATOM   2005  N   ASP D  67     234.950 162.816 269.991  1.00 93.53           N  
ATOM   2006  CA  ASP D  67     235.760 163.856 270.616  1.00 93.53           C  
ATOM   2007  C   ASP D  67     235.731 165.136 269.793  1.00 93.53           C  
ATOM   2008  O   ASP D  67     235.599 166.234 270.352  1.00 93.53           O  
ATOM   2009  CB  ASP D  67     237.194 163.365 270.802  1.00 93.53           C  
ATOM   2010  CG  ASP D  67     238.027 164.314 271.638  1.00 93.53           C  
ATOM   2011  OD1 ASP D  67     237.460 164.953 272.549  1.00 93.53           O  
ATOM   2012  OD2 ASP D  67     239.245 164.422 271.384  1.00 93.53           O  
ATOM   2013  N   LYS D  68     235.796 165.019 268.456  1.00 88.31           N  
ATOM   2014  CA  LYS D  68     235.833 166.228 267.642  1.00 88.31           C  
ATOM   2015  C   LYS D  68     234.463 166.885 267.574  1.00 88.31           C  
ATOM   2016  O   LYS D  68     234.380 168.115 267.481  1.00 88.31           O  
ATOM   2017  CB  LYS D  68     236.323 165.913 266.231  1.00 88.31           C  
ATOM   2018  CG  LYS D  68     237.841 165.831 266.101  1.00 88.31           C  
ATOM   2019  CD  LYS D  68     238.337 165.124 264.825  1.00 88.31           C  
ATOM   2020  CE  LYS D  68     237.263 164.910 263.758  1.00 88.31           C  
ATOM   2021  NZ  LYS D  68     237.744 164.039 262.651  1.00 88.31           N  
ATOM   2022  N   TRP D  69     233.422 166.137 267.918  1.00 82.21           N  
ATOM   2023  CA  TRP D  69     232.059 166.638 267.884  1.00 82.21           C  
ATOM   2024  C   TRP D  69     231.761 167.322 269.203  1.00 82.21           C  
ATOM   2025  O   TRP D  69     231.156 168.401 269.222  1.00 82.21           O  
ATOM   2026  CB  TRP D  69     231.090 165.483 267.621  1.00 82.21           C  
ATOM   2027  CG  TRP D  69     229.618 165.802 267.604  1.00 82.21           C  
ATOM   2028  CD1 TRP D  69     228.659 165.194 268.356  1.00 82.21           C  
ATOM   2029  CD2 TRP D  69     228.931 166.763 266.788  1.00 82.21           C  
ATOM   2030  NE1 TRP D  69     227.426 165.717 268.074  1.00 82.21           N  
ATOM   2031  CE2 TRP D  69     227.563 166.680 267.112  1.00 82.21           C  
ATOM   2032  CE3 TRP D  69     229.337 167.685 265.820  1.00 82.21           C  
ATOM   2033  CZ2 TRP D  69     226.602 167.484 266.507  1.00 82.21           C  
ATOM   2034  CZ3 TRP D  69     228.382 168.484 265.225  1.00 82.21           C  
ATOM   2035  CH2 TRP D  69     227.032 168.381 265.572  1.00 82.21           C  
ATOM   2036  N   SER D  70     232.216 166.726 270.304  1.00 86.60           N  
ATOM   2037  CA  SER D  70     231.977 167.315 271.611  1.00 86.60           C  
ATOM   2038  C   SER D  70     232.802 168.587 271.764  1.00 86.60           C  
ATOM   2039  O   SER D  70     232.320 169.581 272.319  1.00 86.60           O  
ATOM   2040  CB  SER D  70     232.309 166.312 272.711  1.00 86.60           C  
ATOM   2041  OG  SER D  70     233.691 166.005 272.709  1.00 86.60           O  
ATOM   2042  N   ALA D  71     234.041 168.584 271.248  1.00 84.42           N  
ATOM   2043  CA  ALA D  71     234.853 169.797 271.261  1.00 84.42           C  
ATOM   2044  C   ALA D  71     234.271 170.871 270.350  1.00 84.42           C  
ATOM   2045  O   ALA D  71     234.346 172.068 270.679  1.00 84.42           O  
ATOM   2046  CB  ALA D  71     236.287 169.475 270.849  1.00 84.42           C  
ATOM   2047  N   PHE D  72     233.664 170.464 269.226  1.00 79.74           N  
ATOM   2048  CA  PHE D  72     233.022 171.423 268.335  1.00 79.74           C  
ATOM   2049  C   PHE D  72     231.840 172.101 269.012  1.00 79.74           C  
ATOM   2050  O   PHE D  72     231.713 173.326 268.962  1.00 79.74           O  
ATOM   2051  CB  PHE D  72     232.575 170.724 267.056  1.00 79.74           C  
ATOM   2052  CG  PHE D  72     231.726 171.578 266.157  1.00 79.74           C  
ATOM   2053  CD1 PHE D  72     232.302 172.562 265.377  1.00 79.74           C  
ATOM   2054  CD2 PHE D  72     230.357 171.381 266.076  1.00 79.74           C  
ATOM   2055  CE1 PHE D  72     231.529 173.342 264.547  1.00 79.74           C  
ATOM   2056  CE2 PHE D  72     229.581 172.161 265.254  1.00 79.74           C  
ATOM   2057  CZ  PHE D  72     230.167 173.141 264.489  1.00 79.74           C  
ATOM   2058  N   LEU D  73     230.970 171.323 269.666  1.00 81.73           N  
ATOM   2059  CA  LEU D  73     229.864 171.949 270.395  1.00 81.73           C  
ATOM   2060  C   LEU D  73     230.319 172.727 271.618  1.00 81.73           C  
ATOM   2061  O   LEU D  73     229.648 173.690 271.993  1.00 81.73           O  
ATOM   2062  CB  LEU D  73     228.795 170.940 270.812  1.00 81.73           C  
ATOM   2063  CG  LEU D  73     227.721 170.548 269.800  1.00 81.73           C  
ATOM   2064  CD1 LEU D  73     228.245 169.723 268.693  1.00 81.73           C  
ATOM   2065  CD2 LEU D  73     226.598 169.816 270.510  1.00 81.73           C  
ATOM   2066  N   LYS D  74     231.445 172.357 272.232  1.00 86.25           N  
ATOM   2067  CA  LYS D  74     231.972 173.158 273.333  1.00 86.25           C  
ATOM   2068  C   LYS D  74     232.379 174.548 272.855  1.00 86.25           C  
ATOM   2069  O   LYS D  74     231.957 175.565 273.428  1.00 86.25           O  
ATOM   2070  CB  LYS D  74     233.153 172.441 273.981  1.00 86.25           C  
ATOM   2071  CG  LYS D  74     233.850 173.250 275.064  1.00 86.25           C  
ATOM   2072  CD  LYS D  74     234.920 172.438 275.787  1.00 86.25           C  
ATOM   2073  CE  LYS D  74     235.897 171.772 274.823  1.00 86.25           C  
ATOM   2074  NZ  LYS D  74     236.491 172.729 273.844  1.00 86.25           N  
ATOM   2075  N   GLU D  75     233.136 174.616 271.755  1.00 85.59           N  
ATOM   2076  CA  GLU D  75     233.567 175.927 271.278  1.00 85.59           C  
ATOM   2077  C   GLU D  75     232.419 176.701 270.635  1.00 85.59           C  
ATOM   2078  O   GLU D  75     232.360 177.931 270.760  1.00 85.59           O  
ATOM   2079  CB  GLU D  75     234.760 175.797 270.328  1.00 85.59           C  
ATOM   2080  CG  GLU D  75     234.514 175.033 269.047  1.00 85.59           C  
ATOM   2081  CD  GLU D  75     235.762 174.918 268.196  1.00 85.59           C  
ATOM   2082  OE1 GLU D  75     236.815 175.446 268.611  1.00 85.59           O  
ATOM   2083  OE2 GLU D  75     235.691 174.300 267.113  1.00 85.59           O  
ATOM   2084  N   GLN D  76     231.469 176.013 269.997  1.00 81.81           N  
ATOM   2085  CA  GLN D  76     230.343 176.726 269.411  1.00 81.81           C  
ATOM   2086  C   GLN D  76     229.344 177.191 270.461  1.00 81.81           C  
ATOM   2087  O   GLN D  76     228.714 178.230 270.272  1.00 81.81           O  
ATOM   2088  CB  GLN D  76     229.646 175.868 268.358  1.00 81.81           C  
ATOM   2089  CG  GLN D  76     230.482 175.652 267.113  1.00 81.81           C  
ATOM   2090  CD  GLN D  76     230.675 176.905 266.304  1.00 81.81           C  
ATOM   2091  OE1 GLN D  76     229.778 177.735 266.199  1.00 81.81           O  
ATOM   2092  NE2 GLN D  76     231.859 177.057 265.729  1.00 81.81           N  
ATOM   2093  N   SER D  77     229.220 176.492 271.592  1.00 82.91           N  
ATOM   2094  CA  SER D  77     228.398 177.020 272.673  1.00 82.91           C  
ATOM   2095  C   SER D  77     229.087 178.187 273.362  1.00 82.91           C  
ATOM   2096  O   SER D  77     228.413 179.139 273.781  1.00 82.91           O  
ATOM   2097  CB  SER D  77     228.080 175.921 273.681  1.00 82.91           C  
ATOM   2098  OG  SER D  77     227.329 176.437 274.763  1.00 82.91           O  
ATOM   2099  N   THR D  78     230.425 178.156 273.425  1.00 84.43           N  
ATOM   2100  CA  THR D  78     231.174 179.296 273.947  1.00 84.43           C  
ATOM   2101  C   THR D  78     230.953 180.526 273.075  1.00 84.43           C  
ATOM   2102  O   THR D  78     230.711 181.626 273.588  1.00 84.43           O  
ATOM   2103  CB  THR D  78     232.660 178.948 274.039  1.00 84.43           C  
ATOM   2104  OG1 THR D  78     232.841 177.895 274.992  1.00 84.43           O  
ATOM   2105  CG2 THR D  78     233.476 180.150 274.485  1.00 84.43           C  
ATOM   2106  N   LEU D  79     230.975 180.351 271.753  1.00 83.51           N  
ATOM   2107  CA  LEU D  79     230.690 181.480 270.877  1.00 83.51           C  
ATOM   2108  C   LEU D  79     229.203 181.805 270.811  1.00 83.51           C  
ATOM   2109  O   LEU D  79     228.845 182.913 270.403  1.00 83.51           O  
ATOM   2110  CB  LEU D  79     231.205 181.206 269.465  1.00 83.51           C  
ATOM   2111  CG  LEU D  79     232.698 180.934 269.327  1.00 83.51           C  
ATOM   2112  CD1 LEU D  79     233.032 180.520 267.907  1.00 83.51           C  
ATOM   2113  CD2 LEU D  79     233.496 182.155 269.734  1.00 83.51           C  
ATOM   2114  N   ALA D  80     228.332 180.876 271.208  1.00 82.75           N  
ATOM   2115  CA  ALA D  80     226.898 181.108 271.127  1.00 82.75           C  
ATOM   2116  C   ALA D  80     226.370 181.865 272.328  1.00 82.75           C  
ATOM   2117  O   ALA D  80     225.295 182.463 272.242  1.00 82.75           O  
ATOM   2118  CB  ALA D  80     226.147 179.786 271.000  1.00 82.75           C  
ATOM   2119  N   GLN D  81     227.094 181.851 273.443  1.00 88.85           N  
ATOM   2120  CA  GLN D  81     226.582 182.531 274.628  1.00 88.85           C  
ATOM   2121  C   GLN D  81     226.898 184.019 274.625  1.00 88.85           C  
ATOM   2122  O   GLN D  81     226.549 184.712 275.586  1.00 88.85           O  
ATOM   2123  CB  GLN D  81     227.117 181.873 275.898  1.00 88.85           C  
ATOM   2124  CG  GLN D  81     226.605 180.467 276.056  1.00 88.85           C  
ATOM   2125  CD  GLN D  81     227.305 179.688 277.132  1.00 88.85           C  
ATOM   2126  OE1 GLN D  81     228.376 180.070 277.599  1.00 88.85           O  
ATOM   2127  NE2 GLN D  81     226.729 178.551 277.497  1.00 88.85           N  
ATOM   2128  N   MET D  82     227.546 184.523 273.575  1.00 88.05           N  
ATOM   2129  CA  MET D  82     227.762 185.952 273.412  1.00 88.05           C  
ATOM   2130  C   MET D  82     226.543 186.666 272.848  1.00 88.05           C  
ATOM   2131  O   MET D  82     226.560 187.896 272.749  1.00 88.05           O  
ATOM   2132  CB  MET D  82     228.963 186.206 272.503  1.00 88.05           C  
ATOM   2133  CG  MET D  82     230.199 185.413 272.871  1.00 88.05           C  
ATOM   2134  SD  MET D  82     231.664 186.000 272.002  1.00 88.05           S  
ATOM   2135  CE  MET D  82     232.933 184.990 272.757  1.00 88.05           C  
ATOM   2136  N   TYR D  83     225.503 185.928 272.457  1.00 84.22           N  
ATOM   2137  CA  TYR D  83     224.267 186.523 271.974  1.00 84.22           C  
ATOM   2138  C   TYR D  83     223.216 186.400 273.063  1.00 84.22           C  
ATOM   2139  O   TYR D  83     222.734 185.285 273.315  1.00 84.22           O  
ATOM   2140  CB  TYR D  83     223.792 185.826 270.702  1.00 84.22           C  
ATOM   2141  CG  TYR D  83     224.778 185.874 269.565  1.00 84.22           C  
ATOM   2142  CD1 TYR D  83     225.126 187.079 268.975  1.00 84.22           C  
ATOM   2143  CD2 TYR D  83     225.359 184.713 269.079  1.00 84.22           C  
ATOM   2144  CE1 TYR D  83     226.029 187.125 267.934  1.00 84.22           C  
ATOM   2145  CE2 TYR D  83     226.263 184.751 268.040  1.00 84.22           C  
ATOM   2146  CZ  TYR D  83     226.593 185.959 267.473  1.00 84.22           C  
ATOM   2147  OH  TYR D  83     227.493 186.000 266.438  1.00 84.22           O  
ATOM   2148  N   PRO D  84     222.851 187.481 273.749  1.00 93.66           N  
ATOM   2149  CA  PRO D  84     221.754 187.405 274.719  1.00 93.66           C  
ATOM   2150  C   PRO D  84     220.416 187.160 274.040  1.00 93.66           C  
ATOM   2151  O   PRO D  84     220.184 187.577 272.903  1.00 93.66           O  
ATOM   2152  CB  PRO D  84     221.786 188.778 275.397  1.00 93.66           C  
ATOM   2153  CG  PRO D  84     223.170 189.275 275.177  1.00 93.66           C  
ATOM   2154  CD  PRO D  84     223.558 188.767 273.825  1.00 93.66           C  
ATOM   2155  N   LEU D  85     219.528 186.473 274.756  1.00 93.31           N  
ATOM   2156  CA  LEU D  85     218.273 186.024 274.169  1.00 93.31           C  
ATOM   2157  C   LEU D  85     217.145 187.027 274.333  1.00 93.31           C  
ATOM   2158  O   LEU D  85     216.144 186.931 273.616  1.00 93.31           O  
ATOM   2159  CB  LEU D  85     217.816 184.697 274.786  1.00 93.31           C  
ATOM   2160  CG  LEU D  85     218.334 183.348 274.278  1.00 93.31           C  
ATOM   2161  CD1 LEU D  85     218.000 183.161 272.816  1.00 93.31           C  
ATOM   2162  CD2 LEU D  85     219.807 183.173 274.507  1.00 93.31           C  
ATOM   2163  N   GLN D  86     217.270 187.972 275.267  1.00100.79           N  
ATOM   2164  CA  GLN D  86     216.153 188.850 275.591  1.00100.79           C  
ATOM   2165  C   GLN D  86     215.871 189.882 274.507  1.00100.79           C  
ATOM   2166  O   GLN D  86     214.796 190.490 274.520  1.00100.79           O  
ATOM   2167  CB  GLN D  86     216.409 189.550 276.926  1.00100.79           C  
ATOM   2168  CG  GLN D  86     217.589 190.503 276.917  1.00100.79           C  
ATOM   2169  CD  GLN D  86     218.879 189.840 277.361  1.00100.79           C  
ATOM   2170  OE1 GLN D  86     218.983 188.613 277.387  1.00100.79           O  
ATOM   2171  NE2 GLN D  86     219.871 190.650 277.711  1.00100.79           N  
ATOM   2172  N   GLU D  87     216.799 190.101 273.574  1.00100.72           N  
ATOM   2173  CA  GLU D  87     216.566 191.016 272.464  1.00100.72           C  
ATOM   2174  C   GLU D  87     216.316 190.288 271.147  1.00100.72           C  
ATOM   2175  O   GLU D  87     216.364 190.910 270.081  1.00100.72           O  
ATOM   2176  CB  GLU D  87     217.724 192.007 272.323  1.00100.72           C  
ATOM   2177  CG  GLU D  87     219.053 191.425 271.872  1.00100.72           C  
ATOM   2178  CD  GLU D  87     219.895 190.881 273.008  1.00100.72           C  
ATOM   2179  OE1 GLU D  87     219.367 190.668 274.118  1.00100.72           O  
ATOM   2180  OE2 GLU D  87     221.105 190.683 272.787  1.00100.72           O  
ATOM   2181  N   ILE D  88     216.029 188.992 271.195  1.00 93.85           N  
ATOM   2182  CA  ILE D  88     215.746 188.206 270.000  1.00 93.85           C  
ATOM   2183  C   ILE D  88     214.256 187.906 269.991  1.00 93.85           C  
ATOM   2184  O   ILE D  88     213.728 187.311 270.939  1.00 93.85           O  
ATOM   2185  CB  ILE D  88     216.578 186.917 269.960  1.00 93.85           C  
ATOM   2186  CG1 ILE D  88     218.058 187.265 269.842  1.00 93.85           C  
ATOM   2187  CG2 ILE D  88     216.149 186.036 268.808  1.00 93.85           C  
ATOM   2188  CD1 ILE D  88     218.960 186.092 270.000  1.00 93.85           C  
ATOM   2189  N   GLN D  89     213.582 188.307 268.916  1.00 95.27           N  
ATOM   2190  CA  GLN D  89     212.135 188.180 268.820  1.00 95.27           C  
ATOM   2191  C   GLN D  89     211.680 187.000 267.977  1.00 95.27           C  
ATOM   2192  O   GLN D  89     210.552 186.532 268.162  1.00 95.27           O  
ATOM   2193  CB  GLN D  89     211.512 189.465 268.253  1.00 95.27           C  
ATOM   2194  CG  GLN D  89     211.477 190.669 269.205  1.00 95.27           C  
ATOM   2195  CD  GLN D  89     212.844 191.268 269.492  1.00 95.27           C  
ATOM   2196  OE1 GLN D  89     213.289 191.309 270.638  1.00 95.27           O  
ATOM   2197  NE2 GLN D  89     213.522 191.724 268.445  1.00 95.27           N  
ATOM   2198  N   ASN D  90     212.512 186.515 267.062  1.00 91.61           N  
ATOM   2199  CA  ASN D  90     212.138 185.355 266.268  1.00 91.61           C  
ATOM   2200  C   ASN D  90     212.225 184.101 267.120  1.00 91.61           C  
ATOM   2201  O   ASN D  90     213.219 183.876 267.811  1.00 91.61           O  
ATOM   2202  CB  ASN D  90     213.042 185.236 265.043  1.00 91.61           C  
ATOM   2203  CG  ASN D  90     212.462 184.331 263.974  1.00 91.61           C  
ATOM   2204  OD1 ASN D  90     211.446 183.670 264.181  1.00 91.61           O  
ATOM   2205  ND2 ASN D  90     213.098 184.312 262.812  1.00 91.61           N  
ATOM   2206  N   LEU D  91     211.176 183.280 267.064  1.00 88.50           N  
ATOM   2207  CA  LEU D  91     211.085 182.131 267.954  1.00 88.50           C  
ATOM   2208  C   LEU D  91     211.987 180.989 267.516  1.00 88.50           C  
ATOM   2209  O   LEU D  91     212.483 180.246 268.368  1.00 88.50           O  
ATOM   2210  CB  LEU D  91     209.639 181.637 268.054  1.00 88.50           C  
ATOM   2211  CG  LEU D  91     208.648 182.288 269.032  1.00 88.50           C  
ATOM   2212  CD1 LEU D  91     209.116 182.087 270.467  1.00 88.50           C  
ATOM   2213  CD2 LEU D  91     208.356 183.762 268.757  1.00 88.50           C  
ATOM   2214  N   THR D  92     212.208 180.826 266.210  1.00 84.89           N  
ATOM   2215  CA  THR D  92     213.056 179.734 265.740  1.00 84.89           C  
ATOM   2216  C   THR D  92     214.518 179.991 266.074  1.00 84.89           C  
ATOM   2217  O   THR D  92     215.227 179.081 266.519  1.00 84.89           O  
ATOM   2218  CB  THR D  92     212.883 179.530 264.239  1.00 84.89           C  
ATOM   2219  OG1 THR D  92     213.274 180.721 263.550  1.00 84.89           O  
ATOM   2220  CG2 THR D  92     211.436 179.218 263.913  1.00 84.89           C  
ATOM   2221  N   VAL D  93     214.979 181.227 265.870  1.00 82.77           N  
ATOM   2222  CA  VAL D  93     216.347 181.601 266.211  1.00 82.77           C  
ATOM   2223  C   VAL D  93     216.558 181.531 267.717  1.00 82.77           C  
ATOM   2224  O   VAL D  93     217.603 181.065 268.191  1.00 82.77           O  
ATOM   2225  CB  VAL D  93     216.655 183.000 265.649  1.00 82.77           C  
ATOM   2226  CG1 VAL D  93     218.061 183.438 266.000  1.00 82.77           C  
ATOM   2227  CG2 VAL D  93     216.455 183.009 264.151  1.00 82.77           C  
ATOM   2228  N   LYS D  94     215.552 181.952 268.487  1.00 82.06           N  
ATOM   2229  CA  LYS D  94     215.609 181.859 269.943  1.00 82.06           C  
ATOM   2230  C   LYS D  94     215.664 180.409 270.404  1.00 82.06           C  
ATOM   2231  O   LYS D  94     216.395 180.081 271.342  1.00 82.06           O  
ATOM   2232  CB  LYS D  94     214.404 182.573 270.551  1.00 82.06           C  
ATOM   2233  CG  LYS D  94     214.433 182.718 272.053  1.00 82.06           C  
ATOM   2234  CD  LYS D  94     213.313 183.615 272.535  1.00 82.06           C  
ATOM   2235  CE  LYS D  94     213.383 183.822 274.035  1.00 82.06           C  
ATOM   2236  NZ  LYS D  94     212.325 184.752 274.511  1.00 82.06           N  
ATOM   2237  N   LEU D  95     214.910 179.527 269.745  1.00 79.74           N  
ATOM   2238  CA  LEU D  95     214.921 178.110 270.094  1.00 79.74           C  
ATOM   2239  C   LEU D  95     216.263 177.462 269.775  1.00 79.74           C  
ATOM   2240  O   LEU D  95     216.786 176.679 270.580  1.00 79.74           O  
ATOM   2241  CB  LEU D  95     213.795 177.391 269.356  1.00 79.74           C  
ATOM   2242  CG  LEU D  95     212.459 177.317 270.087  1.00 79.74           C  
ATOM   2243  CD1 LEU D  95     211.453 176.551 269.259  1.00 79.74           C  
ATOM   2244  CD2 LEU D  95     212.633 176.678 271.449  1.00 79.74           C  
ATOM   2245  N   GLN D  96     216.834 177.780 268.608  1.00 78.69           N  
ATOM   2246  CA  GLN D  96     218.142 177.241 268.242  1.00 78.69           C  
ATOM   2247  C   GLN D  96     219.234 177.752 269.171  1.00 78.69           C  
ATOM   2248  O   GLN D  96     220.138 176.999 269.548  1.00 78.69           O  
ATOM   2249  CB  GLN D  96     218.476 177.588 266.795  1.00 78.69           C  
ATOM   2250  CG  GLN D  96     217.567 176.948 265.775  1.00 78.69           C  
ATOM   2251  CD  GLN D  96     217.868 177.410 264.371  1.00 78.69           C  
ATOM   2252  OE1 GLN D  96     217.001 177.945 263.684  1.00 78.69           O  
ATOM   2253  NE2 GLN D  96     219.098 177.191 263.929  1.00 78.69           N  
ATOM   2254  N   LEU D  97     219.158 179.022 269.571  1.00 79.23           N  
ATOM   2255  CA  LEU D  97     220.165 179.544 270.483  1.00 79.23           C  
ATOM   2256  C   LEU D  97     219.979 179.010 271.896  1.00 79.23           C  
ATOM   2257  O   LEU D  97     220.963 178.843 272.618  1.00 79.23           O  
ATOM   2258  CB  LEU D  97     220.147 181.069 270.477  1.00 79.23           C  
ATOM   2259  CG  LEU D  97     221.067 181.726 269.449  1.00 79.23           C  
ATOM   2260  CD1 LEU D  97     221.226 183.182 269.766  1.00 79.23           C  
ATOM   2261  CD2 LEU D  97     222.428 181.054 269.397  1.00 79.23           C  
ATOM   2262  N   GLN D  98     218.738 178.736 272.307  1.00 80.92           N  
ATOM   2263  CA  GLN D  98     218.511 178.111 273.606  1.00 80.92           C  
ATOM   2264  C   GLN D  98     219.035 176.685 273.628  1.00 80.92           C  
ATOM   2265  O   GLN D  98     219.555 176.227 274.651  1.00 80.92           O  
ATOM   2266  CB  GLN D  98     217.025 178.119 273.952  1.00 80.92           C  
ATOM   2267  CG  GLN D  98     216.549 179.328 274.727  1.00 80.92           C  
ATOM   2268  CD  GLN D  98     215.043 179.326 274.912  1.00 80.92           C  
ATOM   2269  OE1 GLN D  98     214.370 178.344 274.600  1.00 80.92           O  
ATOM   2270  NE2 GLN D  98     214.507 180.428 275.421  1.00 80.92           N  
ATOM   2271  N   ALA D  99     218.897 175.966 272.513  1.00 78.01           N  
ATOM   2272  CA  ALA D  99     219.467 174.626 272.438  1.00 78.01           C  
ATOM   2273  C   ALA D  99     220.988 174.668 272.404  1.00 78.01           C  
ATOM   2274  O   ALA D  99     221.650 173.789 272.965  1.00 78.01           O  
ATOM   2275  CB  ALA D  99     218.924 173.896 271.212  1.00 78.01           C  
ATOM   2276  N   LEU D 100     221.563 175.675 271.748  1.00 77.74           N  
ATOM   2277  CA  LEU D 100     223.015 175.734 271.629  1.00 77.74           C  
ATOM   2278  C   LEU D 100     223.694 176.225 272.902  1.00 77.74           C  
ATOM   2279  O   LEU D 100     224.791 175.761 273.226  1.00 77.74           O  
ATOM   2280  CB  LEU D 100     223.414 176.620 270.451  1.00 77.74           C  
ATOM   2281  CG  LEU D 100     224.842 176.446 269.933  1.00 77.74           C  
ATOM   2282  CD1 LEU D 100     225.207 174.979 269.823  1.00 77.74           C  
ATOM   2283  CD2 LEU D 100     224.991 177.123 268.591  1.00 77.74           C  
ATOM   2284  N   GLN D 101     223.069 177.140 273.642  1.00 84.40           N  
ATOM   2285  CA  GLN D 101     223.736 177.795 274.762  1.00 84.40           C  
ATOM   2286  C   GLN D 101     223.700 176.997 276.054  1.00 84.40           C  
ATOM   2287  O   GLN D 101     224.142 177.518 277.082  1.00 84.40           O  
ATOM   2288  CB  GLN D 101     223.108 179.158 275.042  1.00 84.40           C  
ATOM   2289  CG  GLN D 101     223.496 180.254 274.091  1.00 84.40           C  
ATOM   2290  CD  GLN D 101     223.000 181.588 274.572  1.00 84.40           C  
ATOM   2291  OE1 GLN D 101     222.458 181.690 275.669  1.00 84.40           O  
ATOM   2292  NE2 GLN D 101     223.163 182.617 273.754  1.00 84.40           N  
ATOM   2293  N   GLN D 102     223.158 175.784 276.045  1.00 91.15           N  
ATOM   2294  CA  GLN D 102     223.095 174.979 277.257  1.00 91.15           C  
ATOM   2295  C   GLN D 102     224.497 174.542 277.668  1.00 91.15           C  
ATOM   2296  O   GLN D 102     225.222 173.935 276.873  1.00 91.15           O  
ATOM   2297  CB  GLN D 102     222.195 173.770 277.031  1.00 91.15           C  
ATOM   2298  CG  GLN D 102     220.731 174.046 277.298  1.00 91.15           C  
ATOM   2299  CD  GLN D 102     219.845 172.869 276.952  1.00 91.15           C  
ATOM   2300  OE1 GLN D 102     220.242 171.977 276.204  1.00 91.15           O  
ATOM   2301  NE2 GLN D 102     218.635 172.859 277.498  1.00 91.15           N  
ATOM   2302  N   ASN D 103     224.882 174.875 278.905  1.00101.85           N  
ATOM   2303  CA  ASN D 103     226.221 174.551 279.389  1.00101.85           C  
ATOM   2304  C   ASN D 103     226.416 173.051 279.555  1.00101.85           C  
ATOM   2305  O   ASN D 103     227.480 172.517 279.223  1.00101.85           O  
ATOM   2306  CB  ASN D 103     226.495 175.246 280.721  1.00101.85           C  
ATOM   2307  CG  ASN D 103     227.237 176.551 280.565  1.00101.85           C  
ATOM   2308  OD1 ASN D 103     228.410 176.564 280.197  1.00101.85           O  
ATOM   2309  ND2 ASN D 103     226.573 177.656 280.884  1.00101.85           N  
ATOM   2310  N   GLY D 104     225.403 172.358 280.059  1.00104.39           N  
ATOM   2311  CA  GLY D 104     225.586 170.961 280.411  1.00104.39           C  
ATOM   2312  C   GLY D 104     226.430 170.852 281.664  1.00104.39           C  
ATOM   2313  O   GLY D 104     226.184 171.536 282.662  1.00104.39           O  
ATOM   2314  N   SER D 105     227.453 170.004 281.614  1.00109.83           N  
ATOM   2315  CA  SER D 105     228.370 169.832 282.733  1.00109.83           C  
ATOM   2316  C   SER D 105     229.543 170.801 282.697  1.00109.83           C  
ATOM   2317  O   SER D 105     230.385 170.765 283.598  1.00109.83           O  
ATOM   2318  CB  SER D 105     228.896 168.395 282.765  1.00109.83           C  
ATOM   2319  OG  SER D 105     229.505 168.052 281.534  1.00109.83           O  
ATOM   2320  N   SER D 106     229.610 171.672 281.692  1.00108.30           N  
ATOM   2321  CA  SER D 106     230.739 172.576 281.526  1.00108.30           C  
ATOM   2322  C   SER D 106     230.701 173.754 282.487  1.00108.30           C  
ATOM   2323  O   SER D 106     231.705 174.462 282.614  1.00108.30           O  
ATOM   2324  CB  SER D 106     230.787 173.094 280.089  1.00108.30           C  
ATOM   2325  OG  SER D 106     229.938 174.217 279.930  1.00108.30           O  
ATOM   2326  N   VAL D 107     229.571 173.980 283.160  1.00107.04           N  
ATOM   2327  CA  VAL D 107     229.424 175.130 284.040  1.00107.04           C  
ATOM   2328  C   VAL D 107     230.205 174.949 285.340  1.00107.04           C  
ATOM   2329  O   VAL D 107     230.538 175.936 286.005  1.00107.04           O  
ATOM   2330  CB  VAL D 107     227.917 175.378 284.272  1.00107.04           C  
ATOM   2331  CG1 VAL D 107     227.291 174.260 285.097  1.00107.04           C  
ATOM   2332  CG2 VAL D 107     227.642 176.761 284.861  1.00107.04           C  
ATOM   2333  N   LEU D 108     230.550 173.715 285.703  1.00115.09           N  
ATOM   2334  CA  LEU D 108     231.272 173.464 286.941  1.00115.09           C  
ATOM   2335  C   LEU D 108     232.745 173.828 286.787  1.00115.09           C  
ATOM   2336  O   LEU D 108     233.212 174.237 285.720  1.00115.09           O  
ATOM   2337  CB  LEU D 108     231.184 171.994 287.352  1.00115.09           C  
ATOM   2338  CG  LEU D 108     229.978 171.326 288.015  1.00115.09           C  
ATOM   2339  CD1 LEU D 108     229.657 171.947 289.372  1.00115.09           C  
ATOM   2340  CD2 LEU D 108     228.779 171.286 287.105  1.00115.09           C  
ATOM   2341  N   SER D 109     233.492 173.662 287.873  1.00122.59           N  
ATOM   2342  CA  SER D 109     234.941 173.646 287.780  1.00122.59           C  
ATOM   2343  C   SER D 109     235.393 172.363 287.089  1.00122.59           C  
ATOM   2344  O   SER D 109     234.643 171.389 286.980  1.00122.59           O  
ATOM   2345  CB  SER D 109     235.577 173.756 289.164  1.00122.59           C  
ATOM   2346  OG  SER D 109     235.373 172.573 289.908  1.00122.59           O  
ATOM   2347  N   GLU D 110     236.636 172.380 286.598  1.00127.45           N  
ATOM   2348  CA  GLU D 110     237.150 171.252 285.827  1.00127.45           C  
ATOM   2349  C   GLU D 110     237.323 170.009 286.693  1.00127.45           C  
ATOM   2350  O   GLU D 110     237.091 168.889 286.219  1.00127.45           O  
ATOM   2351  CB  GLU D 110     238.474 171.641 285.165  1.00127.45           C  
ATOM   2352  CG  GLU D 110     239.109 170.574 284.273  1.00127.45           C  
ATOM   2353  CD  GLU D 110     238.143 169.957 283.274  1.00127.45           C  
ATOM   2354  OE1 GLU D 110     237.391 170.706 282.611  1.00127.45           O  
ATOM   2355  OE2 GLU D 110     238.137 168.714 283.151  1.00127.45           O  
ATOM   2356  N   ASP D 111     237.696 170.190 287.963  1.00127.69           N  
ATOM   2357  CA  ASP D 111     237.855 169.059 288.873  1.00127.69           C  
ATOM   2358  C   ASP D 111     236.517 168.390 289.174  1.00127.69           C  
ATOM   2359  O   ASP D 111     236.417 167.157 289.158  1.00127.69           O  
ATOM   2360  CB  ASP D 111     238.522 169.523 290.167  1.00127.69           C  
ATOM   2361  CG  ASP D 111     238.723 168.395 291.156  1.00127.69           C  
ATOM   2362  OD1 ASP D 111     239.014 167.261 290.720  1.00127.69           O  
ATOM   2363  OD2 ASP D 111     238.590 168.640 292.373  1.00127.69           O  
ATOM   2364  N   LYS D 112     235.474 169.188 289.419  1.00124.14           N  
ATOM   2365  CA  LYS D 112     234.163 168.624 289.726  1.00124.14           C  
ATOM   2366  C   LYS D 112     233.533 167.993 288.491  1.00124.14           C  
ATOM   2367  O   LYS D 112     232.849 166.970 288.596  1.00124.14           O  
ATOM   2368  CB  LYS D 112     233.245 169.699 290.312  1.00124.14           C  
ATOM   2369  CG  LYS D 112     233.717 170.308 291.637  1.00124.14           C  
ATOM   2370  CD  LYS D 112     234.273 169.295 292.637  1.00124.14           C  
ATOM   2371  CE  LYS D 112     233.188 168.419 293.251  1.00124.14           C  
ATOM   2372  NZ  LYS D 112     233.764 167.346 294.109  1.00124.14           N  
ATOM   2373  N   SER D 113     233.760 168.585 287.315  1.00123.05           N  
ATOM   2374  CA  SER D 113     233.277 167.991 286.071  1.00123.05           C  
ATOM   2375  C   SER D 113     233.972 166.666 285.788  1.00123.05           C  
ATOM   2376  O   SER D 113     233.327 165.700 285.359  1.00123.05           O  
ATOM   2377  CB  SER D 113     233.488 168.958 284.908  1.00123.05           C  
ATOM   2378  OG  SER D 113     232.740 170.146 285.083  1.00123.05           O  
ATOM   2379  N   LYS D 114     235.286 166.607 286.023  1.00125.42           N  
ATOM   2380  CA  LYS D 114     236.027 165.363 285.847  1.00125.42           C  
ATOM   2381  C   LYS D 114     235.566 164.302 286.838  1.00125.42           C  
ATOM   2382  O   LYS D 114     235.464 163.120 286.488  1.00125.42           O  
ATOM   2383  CB  LYS D 114     237.525 165.620 285.994  1.00125.42           C  
ATOM   2384  CG  LYS D 114     238.401 164.528 285.406  1.00125.42           C  
ATOM   2385  CD  LYS D 114     239.872 164.911 285.452  1.00125.42           C  
ATOM   2386  CE  LYS D 114     240.328 165.186 286.875  1.00125.42           C  
ATOM   2387  NZ  LYS D 114     240.260 163.965 287.723  1.00125.42           N  
ATOM   2388  N   ARG D 115     235.265 164.709 288.076  1.00121.35           N  
ATOM   2389  CA  ARG D 115     234.748 163.764 289.061  1.00121.35           C  
ATOM   2390  C   ARG D 115     233.356 163.270 288.679  1.00121.35           C  
ATOM   2391  O   ARG D 115     233.031 162.097 288.888  1.00121.35           O  
ATOM   2392  CB  ARG D 115     234.736 164.399 290.452  1.00121.35           C  
ATOM   2393  CG  ARG D 115     234.340 163.425 291.543  1.00121.35           C  
ATOM   2394  CD  ARG D 115     235.359 162.297 291.590  1.00121.35           C  
ATOM   2395  NE  ARG D 115     234.772 161.014 291.956  1.00121.35           N  
ATOM   2396  CZ  ARG D 115     234.567 160.609 293.201  1.00121.35           C  
ATOM   2397  NH1 ARG D 115     234.898 161.362 294.237  1.00121.35           N  
ATOM   2398  NH2 ARG D 115     234.014 159.418 293.412  1.00121.35           N  
ATOM   2399  N   LEU D 116     232.530 164.146 288.096  1.00118.05           N  
ATOM   2400  CA  LEU D 116     231.204 163.743 287.632  1.00118.05           C  
ATOM   2401  C   LEU D 116     231.285 162.750 286.479  1.00118.05           C  
ATOM   2402  O   LEU D 116     230.536 161.764 286.454  1.00118.05           O  
ATOM   2403  CB  LEU D 116     230.395 164.970 287.220  1.00118.05           C  
ATOM   2404  CG  LEU D 116     228.944 164.695 286.821  1.00118.05           C  
ATOM   2405  CD1 LEU D 116     228.197 164.000 287.943  1.00118.05           C  
ATOM   2406  CD2 LEU D 116     228.245 165.984 286.429  1.00118.05           C  
ATOM   2407  N   ASN D 117     232.181 162.990 285.516  1.00120.40           N  
ATOM   2408  CA  ASN D 117     232.354 162.027 284.429  1.00120.40           C  
ATOM   2409  C   ASN D 117     232.948 160.716 284.929  1.00120.40           C  
ATOM   2410  O   ASN D 117     232.585 159.643 284.432  1.00120.40           O  
ATOM   2411  CB  ASN D 117     233.222 162.607 283.312  1.00120.40           C  
ATOM   2412  CG  ASN D 117     232.558 163.762 282.593  1.00120.40           C  
ATOM   2413  OD1 ASN D 117     233.030 164.895 282.640  1.00120.40           O  
ATOM   2414  ND2 ASN D 117     231.451 163.475 281.918  1.00120.40           N  
ATOM   2415  N   THR D 118     233.843 160.779 285.922  1.00120.26           N  
ATOM   2416  CA  THR D 118     234.375 159.563 286.530  1.00120.26           C  
ATOM   2417  C   THR D 118     233.283 158.770 287.238  1.00120.26           C  
ATOM   2418  O   THR D 118     233.228 157.539 287.122  1.00120.26           O  
ATOM   2419  CB  THR D 118     235.492 159.919 287.511  1.00120.26           C  
ATOM   2420  OG1 THR D 118     236.442 160.777 286.866  1.00120.26           O  
ATOM   2421  CG2 THR D 118     236.204 158.667 288.001  1.00120.26           C  
ATOM   2422  N   ILE D 119     232.391 159.469 287.948  1.00117.84           N  
ATOM   2423  CA  ILE D 119     231.274 158.820 288.630  1.00117.84           C  
ATOM   2424  C   ILE D 119     230.325 158.179 287.627  1.00117.84           C  
ATOM   2425  O   ILE D 119     229.918 157.028 287.801  1.00117.84           O  
ATOM   2426  CB  ILE D 119     230.554 159.827 289.551  1.00117.84           C  
ATOM   2427  CG1 ILE D 119     231.325 159.993 290.858  1.00117.84           C  
ATOM   2428  CG2 ILE D 119     229.130 159.396 289.864  1.00117.84           C  
ATOM   2429  CD1 ILE D 119     230.949 161.234 291.628  1.00117.84           C  
ATOM   2430  N   LEU D 120     229.998 158.890 286.542  1.00117.18           N  
ATOM   2431  CA  LEU D 120     229.103 158.333 285.527  1.00117.18           C  
ATOM   2432  C   LEU D 120     229.717 157.123 284.828  1.00117.18           C  
ATOM   2433  O   LEU D 120     229.029 156.119 284.590  1.00117.18           O  
ATOM   2434  CB  LEU D 120     228.740 159.409 284.504  1.00117.18           C  
ATOM   2435  CG  LEU D 120     227.779 160.508 284.955  1.00117.18           C  
ATOM   2436  CD1 LEU D 120     227.337 161.341 283.764  1.00117.18           C  
ATOM   2437  CD2 LEU D 120     226.578 159.919 285.672  1.00117.18           C  
ATOM   2438  N   ASN D 121     231.019 157.186 284.531  1.00119.10           N  
ATOM   2439  CA  ASN D 121     231.702 156.053 283.917  1.00119.10           C  
ATOM   2440  C   ASN D 121     231.752 154.850 284.851  1.00119.10           C  
ATOM   2441  O   ASN D 121     231.559 153.714 284.408  1.00119.10           O  
ATOM   2442  CB  ASN D 121     233.110 156.460 283.490  1.00119.10           C  
ATOM   2443  CG  ASN D 121     233.106 157.393 282.299  1.00119.10           C  
ATOM   2444  OD1 ASN D 121     232.328 157.217 281.362  1.00119.10           O  
ATOM   2445  ND2 ASN D 121     233.973 158.397 282.331  1.00119.10           N  
ATOM   2446  N   THR D 122     231.991 155.070 286.146  1.00118.51           N  
ATOM   2447  CA  THR D 122     232.060 153.914 287.030  1.00118.51           C  
ATOM   2448  C   THR D 122     230.679 153.357 287.381  1.00118.51           C  
ATOM   2449  O   THR D 122     230.566 152.150 287.614  1.00118.51           O  
ATOM   2450  CB  THR D 122     232.898 154.232 288.279  1.00118.51           C  
ATOM   2451  OG1 THR D 122     233.190 153.018 288.983  1.00118.51           O  
ATOM   2452  CG2 THR D 122     232.222 155.201 289.202  1.00118.51           C  
ATOM   2453  N   MET D 123     229.616 154.178 287.359  1.00117.80           N  
ATOM   2454  CA  MET D 123     228.257 153.628 287.397  1.00117.80           C  
ATOM   2455  C   MET D 123     227.970 152.773 286.169  1.00117.80           C  
ATOM   2456  O   MET D 123     227.354 151.705 286.281  1.00117.80           O  
ATOM   2457  CB  MET D 123     227.207 154.739 287.498  1.00117.80           C  
ATOM   2458  CG  MET D 123     227.254 155.633 288.725  1.00117.80           C  
ATOM   2459  SD  MET D 123     226.166 155.202 290.081  1.00117.80           S  
ATOM   2460  CE  MET D 123     224.871 156.408 289.832  1.00117.80           C  
ATOM   2461  N   SER D 124     228.415 153.229 284.991  1.00118.92           N  
ATOM   2462  CA  SER D 124     228.233 152.452 283.767  1.00118.92           C  
ATOM   2463  C   SER D 124     228.983 151.125 283.821  1.00118.92           C  
ATOM   2464  O   SER D 124     228.457 150.090 283.394  1.00118.92           O  
ATOM   2465  CB  SER D 124     228.678 153.272 282.557  1.00118.92           C  
ATOM   2466  OG  SER D 124     230.090 153.273 282.433  1.00118.92           O  
ATOM   2467  N   THR D 125     230.211 151.132 284.348  1.00122.54           N  
ATOM   2468  CA  THR D 125     230.980 149.892 284.417  1.00122.54           C  
ATOM   2469  C   THR D 125     230.461 148.955 285.501  1.00122.54           C  
ATOM   2470  O   THR D 125     230.560 147.734 285.349  1.00122.54           O  
ATOM   2471  CB  THR D 125     232.467 150.171 284.643  1.00122.54           C  
ATOM   2472  OG1 THR D 125     232.647 150.879 285.874  1.00122.54           O  
ATOM   2473  CG2 THR D 125     233.058 150.959 283.483  1.00122.54           C  
ATOM   2474  N   ILE D 126     229.925 149.494 286.600  1.00121.14           N  
ATOM   2475  CA  ILE D 126     229.317 148.636 287.614  1.00121.14           C  
ATOM   2476  C   ILE D 126     228.043 147.994 287.077  1.00121.14           C  
ATOM   2477  O   ILE D 126     227.814 146.793 287.269  1.00121.14           O  
ATOM   2478  CB  ILE D 126     229.078 149.422 288.918  1.00121.14           C  
ATOM   2479  CG1 ILE D 126     230.403 149.635 289.650  1.00121.14           C  
ATOM   2480  CG2 ILE D 126     228.109 148.705 289.832  1.00121.14           C  
ATOM   2481  CD1 ILE D 126     230.316 150.593 290.811  1.00121.14           C  
ATOM   2482  N   TYR D 127     227.213 148.763 286.366  1.00118.08           N  
ATOM   2483  CA  TYR D 127     225.982 148.192 285.826  1.00118.08           C  
ATOM   2484  C   TYR D 127     226.256 147.203 284.699  1.00118.08           C  
ATOM   2485  O   TYR D 127     225.579 146.174 284.597  1.00118.08           O  
ATOM   2486  CB  TYR D 127     225.053 149.294 285.329  1.00118.08           C  
ATOM   2487  CG  TYR D 127     223.673 148.773 285.035  1.00118.08           C  
ATOM   2488  CD1 TYR D 127     222.823 148.385 286.058  1.00118.08           C  
ATOM   2489  CD2 TYR D 127     223.238 148.625 283.725  1.00118.08           C  
ATOM   2490  CE1 TYR D 127     221.568 147.892 285.786  1.00118.08           C  
ATOM   2491  CE2 TYR D 127     221.987 148.128 283.443  1.00118.08           C  
ATOM   2492  CZ  TYR D 127     221.154 147.765 284.478  1.00118.08           C  
ATOM   2493  OH  TYR D 127     219.901 147.271 284.203  1.00118.08           O  
ATOM   2494  N   SER D 128     227.236 147.495 283.841  1.00125.88           N  
ATOM   2495  CA  SER D 128     227.498 146.618 282.705  1.00125.88           C  
ATOM   2496  C   SER D 128     228.190 145.332 283.140  1.00125.88           C  
ATOM   2497  O   SER D 128     227.885 144.251 282.622  1.00125.88           O  
ATOM   2498  CB  SER D 128     228.336 147.351 281.659  1.00125.88           C  
ATOM   2499  OG  SER D 128     228.593 146.518 280.543  1.00125.88           O  
ATOM   2500  N   THR D 129     229.118 145.424 284.092  1.00130.38           N  
ATOM   2501  CA  THR D 129     229.911 144.282 284.529  1.00130.38           C  
ATOM   2502  C   THR D 129     229.490 143.775 285.902  1.00130.38           C  
ATOM   2503  O   THR D 129     230.292 143.143 286.598  1.00130.38           O  
ATOM   2504  CB  THR D 129     231.400 144.627 284.534  1.00130.38           C  
ATOM   2505  OG1 THR D 129     231.695 145.461 285.661  1.00130.38           O  
ATOM   2506  CG2 THR D 129     231.784 145.354 283.254  1.00130.38           C  
ATOM   2507  N   GLY D 130     228.257 144.047 286.314  1.00134.98           N  
ATOM   2508  CA  GLY D 130     227.777 143.545 287.583  1.00134.98           C  
ATOM   2509  C   GLY D 130     227.462 142.068 287.511  1.00134.98           C  
ATOM   2510  O   GLY D 130     226.509 141.657 286.845  1.00134.98           O  
ATOM   2511  N   LYS D 131     228.267 141.260 288.193  1.00144.07           N  
ATOM   2512  CA  LYS D 131     228.093 139.815 288.217  1.00144.07           C  
ATOM   2513  C   LYS D 131     227.746 139.372 289.630  1.00144.07           C  
ATOM   2514  O   LYS D 131     228.472 139.677 290.583  1.00144.07           O  
ATOM   2515  CB  LYS D 131     229.349 139.104 287.698  1.00144.07           C  
ATOM   2516  CG  LYS D 131     230.670 139.657 288.224  1.00144.07           C  
ATOM   2517  CD  LYS D 131     231.860 138.993 287.556  1.00144.07           C  
ATOM   2518  CE  LYS D 131     231.988 137.542 287.986  1.00144.07           C  
ATOM   2519  NZ  LYS D 131     232.381 137.429 289.418  1.00144.07           N  
ATOM   2520  N   VAL D 132     226.611 138.695 289.766  1.00148.60           N  
ATOM   2521  CA  VAL D 132     226.104 138.229 291.049  1.00148.60           C  
ATOM   2522  C   VAL D 132     225.747 136.760 290.882  1.00148.60           C  
ATOM   2523  O   VAL D 132     225.007 136.402 289.959  1.00148.60           O  
ATOM   2524  CB  VAL D 132     224.882 139.046 291.513  1.00148.60           C  
ATOM   2525  CG1 VAL D 132     224.217 138.382 292.686  1.00148.60           C  
ATOM   2526  CG2 VAL D 132     225.292 140.464 291.888  1.00148.60           C  
ATOM   2527  N   CYS D 133     226.272 135.912 291.765  1.00161.29           N  
ATOM   2528  CA  CYS D 133     226.109 134.474 291.620  1.00161.29           C  
ATOM   2529  C   CYS D 133     225.897 133.804 292.970  1.00161.29           C  
ATOM   2530  O   CYS D 133     225.842 134.451 294.020  1.00161.29           O  
ATOM   2531  CB  CYS D 133     227.318 133.887 290.890  1.00161.29           C  
ATOM   2532  SG  CYS D 133     228.871 134.059 291.796  1.00161.29           S  
ATOM   2533  N   ASN D 134     225.779 132.481 292.911  1.00166.45           N  
ATOM   2534  CA  ASN D 134     225.472 131.676 294.080  1.00166.45           C  
ATOM   2535  C   ASN D 134     226.689 131.590 294.997  1.00166.45           C  
ATOM   2536  O   ASN D 134     227.816 131.422 294.518  1.00166.45           O  
ATOM   2537  CB  ASN D 134     225.038 130.274 293.648  1.00166.45           C  
ATOM   2538  CG  ASN D 134     224.100 129.611 294.641  1.00166.45           C  
ATOM   2539  OD1 ASN D 134     224.324 129.643 295.849  1.00166.45           O  
ATOM   2540  ND2 ASN D 134     223.037 129.003 294.128  1.00166.45           N  
ATOM   2541  N   PRO D 135     226.502 131.736 296.309  1.00173.60           N  
ATOM   2542  CA  PRO D 135     227.573 131.388 297.248  1.00173.60           C  
ATOM   2543  C   PRO D 135     227.908 129.904 297.182  1.00173.60           C  
ATOM   2544  O   PRO D 135     227.064 129.073 296.837  1.00173.60           O  
ATOM   2545  CB  PRO D 135     226.984 131.769 298.609  1.00173.60           C  
ATOM   2546  CG  PRO D 135     226.039 132.876 298.291  1.00173.60           C  
ATOM   2547  CD  PRO D 135     225.429 132.504 296.965  1.00173.60           C  
ATOM   2548  N   ASP D 136     229.179 129.599 297.467  1.00181.23           N  
ATOM   2549  CA  ASP D 136     229.836 128.287 297.458  1.00181.23           C  
ATOM   2550  C   ASP D 136     229.993 127.683 296.065  1.00181.23           C  
ATOM   2551  O   ASP D 136     230.467 126.547 295.958  1.00181.23           O  
ATOM   2552  CB  ASP D 136     229.147 127.256 298.369  1.00181.23           C  
ATOM   2553  CG  ASP D 136     229.292 127.590 299.839  1.00181.23           C  
ATOM   2554  OD1 ASP D 136     230.306 128.219 300.209  1.00181.23           O  
ATOM   2555  OD2 ASP D 136     228.392 127.226 300.625  1.00181.23           O  
ATOM   2556  N   ASN D 137     229.618 128.388 295.000  1.00184.62           N  
ATOM   2557  CA  ASN D 137     229.886 127.951 293.629  1.00184.62           C  
ATOM   2558  C   ASN D 137     230.510 129.098 292.842  1.00184.62           C  
ATOM   2559  O   ASN D 137     229.856 129.711 291.989  1.00184.62           O  
ATOM   2560  CB  ASN D 137     228.603 127.463 292.955  1.00184.62           C  
ATOM   2561  CG  ASN D 137     228.048 126.210 293.600  1.00184.62           C  
ATOM   2562  OD1 ASN D 137     226.954 126.222 294.164  1.00184.62           O  
ATOM   2563  ND2 ASN D 137     228.801 125.119 293.520  1.00184.62           N  
ATOM   2564  N   PRO D 138     231.780 129.416 293.100  1.00188.61           N  
ATOM   2565  CA  PRO D 138     232.406 130.586 292.459  1.00188.61           C  
ATOM   2566  C   PRO D 138     233.233 130.296 291.210  1.00188.61           C  
ATOM   2567  O   PRO D 138     233.920 131.213 290.747  1.00188.61           O  
ATOM   2568  CB  PRO D 138     233.311 131.103 293.582  1.00188.61           C  
ATOM   2569  CG  PRO D 138     233.738 129.843 294.322  1.00188.61           C  
ATOM   2570  CD  PRO D 138     232.737 128.743 293.998  1.00188.61           C  
ATOM   2571  N   GLN D 139     233.208 129.070 290.672  1.00188.03           N  
ATOM   2572  CA  GLN D 139     234.103 128.739 289.564  1.00188.03           C  
ATOM   2573  C   GLN D 139     233.682 129.430 288.271  1.00188.03           C  
ATOM   2574  O   GLN D 139     234.533 129.730 287.426  1.00188.03           O  
ATOM   2575  CB  GLN D 139     234.188 127.221 289.383  1.00188.03           C  
ATOM   2576  CG  GLN D 139     232.858 126.508 289.214  1.00188.03           C  
ATOM   2577  CD  GLN D 139     232.303 125.986 290.525  1.00188.03           C  
ATOM   2578  OE1 GLN D 139     232.689 126.442 291.601  1.00188.03           O  
ATOM   2579  NE2 GLN D 139     231.393 125.022 290.440  1.00188.03           N  
ATOM   2580  N   GLU D 140     232.389 129.688 288.099  1.00181.71           N  
ATOM   2581  CA  GLU D 140     231.912 130.706 287.177  1.00181.71           C  
ATOM   2582  C   GLU D 140     230.708 131.378 287.818  1.00181.71           C  
ATOM   2583  O   GLU D 140     230.079 130.828 288.724  1.00181.71           O  
ATOM   2584  CB  GLU D 140     231.545 130.151 285.789  1.00181.71           C  
ATOM   2585  CG  GLU D 140     230.249 129.353 285.724  1.00181.71           C  
ATOM   2586  CD  GLU D 140     230.456 127.867 285.945  1.00181.71           C  
ATOM   2587  OE1 GLU D 140     231.554 127.476 286.386  1.00181.71           O  
ATOM   2588  OE2 GLU D 140     229.517 127.089 285.675  1.00181.71           O  
ATOM   2589  N   CYS D 141     230.387 132.577 287.339  1.00167.58           N  
ATOM   2590  CA  CYS D 141     229.241 133.312 287.850  1.00167.58           C  
ATOM   2591  C   CYS D 141     228.462 133.925 286.698  1.00167.58           C  
ATOM   2592  O   CYS D 141     228.926 133.980 285.556  1.00167.58           O  
ATOM   2593  CB  CYS D 141     229.659 134.369 288.884  1.00167.58           C  
ATOM   2594  SG  CYS D 141     230.293 133.626 290.412  1.00167.58           S  
ATOM   2595  N   LEU D 142     227.259 134.391 287.020  1.00149.72           N  
ATOM   2596  CA  LEU D 142     226.252 134.718 286.023  1.00149.72           C  
ATOM   2597  C   LEU D 142     225.999 136.219 285.974  1.00149.72           C  
ATOM   2598  O   LEU D 142     225.848 136.865 287.017  1.00149.72           O  
ATOM   2599  CB  LEU D 142     224.960 133.966 286.337  1.00149.72           C  
ATOM   2600  CG  LEU D 142     223.813 134.104 285.351  1.00149.72           C  
ATOM   2601  CD1 LEU D 142     224.271 133.527 284.024  1.00149.72           C  
ATOM   2602  CD2 LEU D 142     222.599 133.365 285.879  1.00149.72           C  
ATOM   2603  N   LEU D 143     225.950 136.762 284.762  1.00142.97           N  
ATOM   2604  CA  LEU D 143     225.743 138.180 284.516  1.00142.97           C  
ATOM   2605  C   LEU D 143     224.254 138.495 284.383  1.00142.97           C  
ATOM   2606  O   LEU D 143     223.414 137.606 284.230  1.00142.97           O  
ATOM   2607  CB  LEU D 143     226.494 138.629 283.262  1.00142.97           C  
ATOM   2608  CG  LEU D 143     227.971 139.017 283.378  1.00142.97           C  
ATOM   2609  CD1 LEU D 143     228.883 137.801 283.495  1.00142.97           C  
ATOM   2610  CD2 LEU D 143     228.376 139.883 282.194  1.00142.97           C  
ATOM   2611  N   LEU D 144     223.938 139.792 284.426  1.00135.12           N  
ATOM   2612  CA  LEU D 144     222.548 140.237 284.501  1.00135.12           C  
ATOM   2613  C   LEU D 144     221.817 140.031 283.182  1.00135.12           C  
ATOM   2614  O   LEU D 144     220.761 139.389 283.140  1.00135.12           O  
ATOM   2615  CB  LEU D 144     222.487 141.711 284.902  1.00135.12           C  
ATOM   2616  CG  LEU D 144     221.083 142.241 285.207  1.00135.12           C  
ATOM   2617  CD1 LEU D 144     220.651 141.909 286.616  1.00135.12           C  
ATOM   2618  CD2 LEU D 144     221.000 143.737 284.955  1.00135.12           C  
ATOM   2619  N   GLU D 145     222.353 140.597 282.100  1.00138.40           N  
ATOM   2620  CA  GLU D 145     221.689 140.512 280.800  1.00138.40           C  
ATOM   2621  C   GLU D 145     221.557 139.095 280.229  1.00138.40           C  
ATOM   2622  O   GLU D 145     220.459 138.773 279.741  1.00138.40           O  
ATOM   2623  CB  GLU D 145     222.390 141.460 279.813  1.00138.40           C  
ATOM   2624  CG  GLU D 145     221.937 141.330 278.368  1.00138.40           C  
ATOM   2625  CD  GLU D 145     220.485 141.713 278.175  1.00138.40           C  
ATOM   2626  OE1 GLU D 145     220.091 142.809 278.626  1.00138.40           O  
ATOM   2627  OE2 GLU D 145     219.736 140.917 277.572  1.00138.40           O  
ATOM   2628  N   PRO D 146     222.588 138.192 280.248  1.00138.80           N  
ATOM   2629  CA  PRO D 146     222.309 136.820 279.799  1.00138.80           C  
ATOM   2630  C   PRO D 146     221.416 136.018 280.734  1.00138.80           C  
ATOM   2631  O   PRO D 146     220.434 135.419 280.287  1.00138.80           O  
ATOM   2632  CB  PRO D 146     223.705 136.188 279.708  1.00138.80           C  
ATOM   2633  CG  PRO D 146     224.629 137.325 279.583  1.00138.80           C  
ATOM   2634  CD  PRO D 146     224.039 138.359 280.471  1.00138.80           C  
ATOM   2635  N   GLY D 147     221.734 135.998 282.026  1.00136.87           N  
ATOM   2636  CA  GLY D 147     221.115 135.027 282.907  1.00136.87           C  
ATOM   2637  C   GLY D 147     220.060 135.503 283.883  1.00136.87           C  
ATOM   2638  O   GLY D 147     219.062 134.806 284.093  1.00136.87           O  
ATOM   2639  N   LEU D 148     220.276 136.666 284.506  1.00134.75           N  
ATOM   2640  CA  LEU D 148     219.346 137.145 285.526  1.00134.75           C  
ATOM   2641  C   LEU D 148     218.011 137.553 284.924  1.00134.75           C  
ATOM   2642  O   LEU D 148     216.970 137.408 285.575  1.00134.75           O  
ATOM   2643  CB  LEU D 148     219.943 138.299 286.329  1.00134.75           C  
ATOM   2644  CG  LEU D 148     220.845 138.027 287.543  1.00134.75           C  
ATOM   2645  CD1 LEU D 148     220.042 137.319 288.616  1.00134.75           C  
ATOM   2646  CD2 LEU D 148     222.114 137.248 287.234  1.00134.75           C  
ATOM   2647  N   ASN D 149     218.028 138.078 283.697  1.00132.71           N  
ATOM   2648  CA  ASN D 149     216.786 138.377 282.995  1.00132.71           C  
ATOM   2649  C   ASN D 149     215.995 137.103 282.725  1.00132.71           C  
ATOM   2650  O   ASN D 149     214.769 137.081 282.887  1.00132.71           O  
ATOM   2651  CB  ASN D 149     217.095 139.105 281.689  1.00132.71           C  
ATOM   2652  CG  ASN D 149     217.195 140.603 281.870  1.00132.71           C  
ATOM   2653  OD1 ASN D 149     217.314 141.096 282.991  1.00132.71           O  
ATOM   2654  ND2 ASN D 149     217.150 141.338 280.766  1.00132.71           N  
ATOM   2655  N   GLU D 150     216.687 136.023 282.345  1.00133.41           N  
ATOM   2656  CA  GLU D 150     216.012 134.755 282.080  1.00133.41           C  
ATOM   2657  C   GLU D 150     215.463 134.134 283.358  1.00133.41           C  
ATOM   2658  O   GLU D 150     214.351 133.592 283.358  1.00133.41           O  
ATOM   2659  CB  GLU D 150     216.965 133.785 281.383  1.00133.41           C  
ATOM   2660  CG  GLU D 150     217.378 134.212 279.985  1.00133.41           C  
ATOM   2661  CD  GLU D 150     216.228 134.188 278.996  1.00133.41           C  
ATOM   2662  OE1 GLU D 150     215.328 133.334 279.143  1.00133.41           O  
ATOM   2663  OE2 GLU D 150     216.226 135.025 278.068  1.00133.41           O  
ATOM   2664  N   ILE D 151     216.215 134.208 284.460  1.00129.39           N  
ATOM   2665  CA  ILE D 151     215.734 133.615 285.704  1.00129.39           C  
ATOM   2666  C   ILE D 151     214.643 134.482 286.323  1.00129.39           C  
ATOM   2667  O   ILE D 151     213.820 133.981 287.097  1.00129.39           O  
ATOM   2668  CB  ILE D 151     216.906 133.363 286.678  1.00129.39           C  
ATOM   2669  CG1 ILE D 151     216.523 132.393 287.794  1.00129.39           C  
ATOM   2670  CG2 ILE D 151     217.373 134.630 287.349  1.00129.39           C  
ATOM   2671  CD1 ILE D 151     217.713 131.921 288.592  1.00129.39           C  
ATOM   2672  N   MET D 152     214.588 135.771 285.981  1.00124.49           N  
ATOM   2673  CA  MET D 152     213.507 136.604 286.481  1.00124.49           C  
ATOM   2674  C   MET D 152     212.248 136.456 285.639  1.00124.49           C  
ATOM   2675  O   MET D 152     211.138 136.554 286.170  1.00124.49           O  
ATOM   2676  CB  MET D 152     213.953 138.066 286.521  1.00124.49           C  
ATOM   2677  CG  MET D 152     214.664 138.512 287.808  1.00124.49           C  
ATOM   2678  SD  MET D 152     214.097 138.195 289.506  1.00124.49           S  
ATOM   2679  CE  MET D 152     212.310 138.307 289.435  1.00124.49           C  
ATOM   2680  N   ALA D 153     212.396 136.229 284.333  1.00121.81           N  
ATOM   2681  CA  ALA D 153     211.242 136.162 283.449  1.00121.81           C  
ATOM   2682  C   ALA D 153     210.658 134.765 283.310  1.00121.81           C  
ATOM   2683  O   ALA D 153     209.466 134.633 283.010  1.00121.81           O  
ATOM   2684  CB  ALA D 153     211.615 136.687 282.062  1.00121.81           C  
ATOM   2685  N   ASN D 154     211.453 133.713 283.514  1.00126.94           N  
ATOM   2686  CA  ASN D 154     210.994 132.366 283.211  1.00126.94           C  
ATOM   2687  C   ASN D 154     210.765 131.482 284.426  1.00126.94           C  
ATOM   2688  O   ASN D 154     209.985 130.531 284.330  1.00126.94           O  
ATOM   2689  CB  ASN D 154     211.988 131.665 282.275  1.00126.94           C  
ATOM   2690  CG  ASN D 154     212.102 132.352 280.930  1.00126.94           C  
ATOM   2691  OD1 ASN D 154     212.821 133.339 280.784  1.00126.94           O  
ATOM   2692  ND2 ASN D 154     211.383 131.838 279.941  1.00126.94           N  
ATOM   2693  N   SER D 155     211.415 131.756 285.553  1.00126.87           N  
ATOM   2694  CA  SER D 155     211.318 130.858 286.692  1.00126.87           C  
ATOM   2695  C   SER D 155     210.000 131.040 287.432  1.00126.87           C  
ATOM   2696  O   SER D 155     209.416 132.126 287.454  1.00126.87           O  
ATOM   2697  CB  SER D 155     212.477 131.073 287.661  1.00126.87           C  
ATOM   2698  OG  SER D 155     212.334 130.251 288.806  1.00126.87           O  
ATOM   2699  N   LEU D 156     209.539 129.951 288.043  1.00124.83           N  
ATOM   2700  CA  LEU D 156     208.322 129.948 288.845  1.00124.83           C  
ATOM   2701  C   LEU D 156     208.599 129.616 290.302  1.00124.83           C  
ATOM   2702  O   LEU D 156     207.660 129.328 291.052  1.00124.83           O  
ATOM   2703  CB  LEU D 156     207.293 128.961 288.281  1.00124.83           C  
ATOM   2704  CG  LEU D 156     206.365 129.382 287.137  1.00124.83           C  
ATOM   2705  CD1 LEU D 156     205.498 130.513 287.639  1.00124.83           C  
ATOM   2706  CD2 LEU D 156     207.059 129.759 285.832  1.00124.83           C  
ATOM   2707  N   ASP D 157     209.857 129.647 290.721  1.00128.16           N  
ATOM   2708  CA  ASP D 157     210.243 129.281 292.074  1.00128.16           C  
ATOM   2709  C   ASP D 157     210.388 130.537 292.920  1.00128.16           C  
ATOM   2710  O   ASP D 157     211.058 131.489 292.510  1.00128.16           O  
ATOM   2711  CB  ASP D 157     211.551 128.490 292.066  1.00128.16           C  
ATOM   2712  CG  ASP D 157     211.854 127.859 293.404  1.00128.16           C  
ATOM   2713  OD1 ASP D 157     210.899 127.613 294.170  1.00128.16           O  
ATOM   2714  OD2 ASP D 157     213.044 127.610 293.691  1.00128.16           O  
ATOM   2715  N   TYR D 158     209.747 130.538 294.090  1.00125.22           N  
ATOM   2716  CA  TYR D 158     209.689 131.742 294.914  1.00125.22           C  
ATOM   2717  C   TYR D 158     211.046 132.061 295.525  1.00125.22           C  
ATOM   2718  O   TYR D 158     211.512 133.204 295.456  1.00125.22           O  
ATOM   2719  CB  TYR D 158     208.639 131.572 296.009  1.00125.22           C  
ATOM   2720  CG  TYR D 158     208.335 132.829 296.793  1.00125.22           C  
ATOM   2721  CD1 TYR D 158     207.380 133.734 296.351  1.00125.22           C  
ATOM   2722  CD2 TYR D 158     208.977 133.088 298.001  1.00125.22           C  
ATOM   2723  CE1 TYR D 158     207.086 134.872 297.081  1.00125.22           C  
ATOM   2724  CE2 TYR D 158     208.696 134.224 298.731  1.00125.22           C  
ATOM   2725  CZ  TYR D 158     207.751 135.111 298.268  1.00125.22           C  
ATOM   2726  OH  TYR D 158     207.470 136.242 298.996  1.00125.22           O  
ATOM   2727  N   ASN D 159     211.693 131.066 296.132  1.00130.81           N  
ATOM   2728  CA  ASN D 159     212.949 131.331 296.824  1.00130.81           C  
ATOM   2729  C   ASN D 159     214.094 131.548 295.845  1.00130.81           C  
ATOM   2730  O   ASN D 159     215.050 132.254 296.171  1.00130.81           O  
ATOM   2731  CB  ASN D 159     213.277 130.197 297.795  1.00130.81           C  
ATOM   2732  CG  ASN D 159     213.421 128.860 297.103  1.00130.81           C  
ATOM   2733  OD1 ASN D 159     212.481 128.366 296.486  1.00130.81           O  
ATOM   2734  ND2 ASN D 159     214.605 128.266 297.203  1.00130.81           N  
ATOM   2735  N   GLU D 160     214.010 130.975 294.643  1.00130.63           N  
ATOM   2736  CA  GLU D 160     215.037 131.205 293.629  1.00130.63           C  
ATOM   2737  C   GLU D 160     214.996 132.642 293.117  1.00130.63           C  
ATOM   2738  O   GLU D 160     216.036 133.315 293.024  1.00130.63           O  
ATOM   2739  CB  GLU D 160     214.837 130.215 292.484  1.00130.63           C  
ATOM   2740  CG  GLU D 160     215.910 130.204 291.418  1.00130.63           C  
ATOM   2741  CD  GLU D 160     215.629 129.160 290.353  1.00130.63           C  
ATOM   2742  OE1 GLU D 160     214.585 128.481 290.451  1.00130.63           O  
ATOM   2743  OE2 GLU D 160     216.449 129.002 289.427  1.00130.63           O  
ATOM   2744  N   ARG D 161     213.792 133.133 292.803  1.00123.60           N  
ATOM   2745  CA  ARG D 161     213.619 134.530 292.417  1.00123.60           C  
ATOM   2746  C   ARG D 161     213.963 135.463 293.567  1.00123.60           C  
ATOM   2747  O   ARG D 161     214.529 136.540 293.351  1.00123.60           O  
ATOM   2748  CB  ARG D 161     212.189 134.774 291.938  1.00123.60           C  
ATOM   2749  CG  ARG D 161     211.843 134.066 290.643  1.00123.60           C  
ATOM   2750  CD  ARG D 161     210.344 134.062 290.401  1.00123.60           C  
ATOM   2751  NE  ARG D 161     209.826 135.389 290.098  1.00123.60           N  
ATOM   2752  CZ  ARG D 161     209.682 135.867 288.870  1.00123.60           C  
ATOM   2753  NH1 ARG D 161     210.000 135.147 287.808  1.00123.60           N  
ATOM   2754  NH2 ARG D 161     209.205 137.096 288.703  1.00123.60           N  
ATOM   2755  N   LEU D 162     213.634 135.057 294.798  1.00127.19           N  
ATOM   2756  CA  LEU D 162     214.005 135.831 295.978  1.00127.19           C  
ATOM   2757  C   LEU D 162     215.512 135.927 296.149  1.00127.19           C  
ATOM   2758  O   LEU D 162     216.033 137.002 296.470  1.00127.19           O  
ATOM   2759  CB  LEU D 162     213.381 135.211 297.226  1.00127.19           C  
ATOM   2760  CG  LEU D 162     213.379 136.114 298.456  1.00127.19           C  
ATOM   2761  CD1 LEU D 162     212.833 137.465 298.103  1.00127.19           C  
ATOM   2762  CD2 LEU D 162     212.577 135.489 299.583  1.00127.19           C  
ATOM   2763  N   TRP D 163     216.225 134.818 295.933  1.00135.11           N  
ATOM   2764  CA  TRP D 163     217.678 134.818 296.051  1.00135.11           C  
ATOM   2765  C   TRP D 163     218.308 135.718 295.003  1.00135.11           C  
ATOM   2766  O   TRP D 163     219.183 136.530 295.322  1.00135.11           O  
ATOM   2767  CB  TRP D 163     218.225 133.396 295.916  1.00135.11           C  
ATOM   2768  CG  TRP D 163     219.615 133.358 295.342  1.00135.11           C  
ATOM   2769  CD1 TRP D 163     220.779 133.604 296.008  1.00135.11           C  
ATOM   2770  CD2 TRP D 163     219.983 133.077 293.983  1.00135.11           C  
ATOM   2771  NE1 TRP D 163     221.848 133.486 295.154  1.00135.11           N  
ATOM   2772  CE2 TRP D 163     221.386 133.167 293.905  1.00135.11           C  
ATOM   2773  CE3 TRP D 163     219.261 132.765 292.828  1.00135.11           C  
ATOM   2774  CZ2 TRP D 163     222.081 132.948 292.719  1.00135.11           C  
ATOM   2775  CZ3 TRP D 163     219.954 132.549 291.651  1.00135.11           C  
ATOM   2776  CH2 TRP D 163     221.349 132.641 291.606  1.00135.11           C  
ATOM   2777  N   ALA D 164     217.853 135.602 293.749  1.00129.36           N  
ATOM   2778  CA  ALA D 164     218.410 136.428 292.679  1.00129.36           C  
ATOM   2779  C   ALA D 164     218.112 137.908 292.895  1.00129.36           C  
ATOM   2780  O   ALA D 164     219.012 138.752 292.774  1.00129.36           O  
ATOM   2781  CB  ALA D 164     217.862 135.966 291.330  1.00129.36           C  
ATOM   2782  N   TRP D 165     216.869 138.223 293.274  1.00123.67           N  
ATOM   2783  CA  TRP D 165     216.443 139.596 293.520  1.00123.67           C  
ATOM   2784  C   TRP D 165     217.217 140.231 294.668  1.00123.67           C  
ATOM   2785  O   TRP D 165     217.816 141.307 294.512  1.00123.67           O  
ATOM   2786  CB  TRP D 165     214.942 139.588 293.805  1.00123.67           C  
ATOM   2787  CG  TRP D 165     214.243 140.892 293.699  1.00123.67           C  
ATOM   2788  CD1 TRP D 165     213.662 141.422 292.587  1.00123.67           C  
ATOM   2789  CD2 TRP D 165     214.002 141.816 294.758  1.00123.67           C  
ATOM   2790  NE1 TRP D 165     213.090 142.634 292.886  1.00123.67           N  
ATOM   2791  CE2 TRP D 165     213.283 142.896 294.215  1.00123.67           C  
ATOM   2792  CE3 TRP D 165     214.334 141.840 296.114  1.00123.67           C  
ATOM   2793  CZ2 TRP D 165     212.894 143.986 294.980  1.00123.67           C  
ATOM   2794  CZ3 TRP D 165     213.949 142.923 296.866  1.00123.67           C  
ATOM   2795  CH2 TRP D 165     213.237 143.979 296.302  1.00123.67           C  
ATOM   2796  N   GLU D 166     217.251 139.552 295.820  1.00128.43           N  
ATOM   2797  CA  GLU D 166     217.910 140.099 296.997  1.00128.43           C  
ATOM   2798  C   GLU D 166     219.416 140.163 296.817  1.00128.43           C  
ATOM   2799  O   GLU D 166     220.046 141.122 297.264  1.00128.43           O  
ATOM   2800  CB  GLU D 166     217.559 139.272 298.229  1.00128.43           C  
ATOM   2801  CG  GLU D 166     216.159 139.520 298.723  1.00128.43           C  
ATOM   2802  CD  GLU D 166     216.071 140.776 299.553  1.00128.43           C  
ATOM   2803  OE1 GLU D 166     217.046 141.092 300.267  1.00128.43           O  
ATOM   2804  OE2 GLU D 166     215.029 141.456 299.478  1.00128.43           O  
ATOM   2805  N   SER D 167     220.005 139.174 296.138  1.00130.80           N  
ATOM   2806  CA  SER D 167     221.448 139.163 295.946  1.00130.80           C  
ATOM   2807  C   SER D 167     221.894 140.276 295.008  1.00130.80           C  
ATOM   2808  O   SER D 167     222.869 140.984 295.306  1.00130.80           O  
ATOM   2809  CB  SER D 167     221.883 137.796 295.427  1.00130.80           C  
ATOM   2810  OG  SER D 167     221.283 137.519 294.175  1.00130.80           O  
ATOM   2811  N   TRP D 168     221.185 140.463 293.883  1.00128.36           N  
ATOM   2812  CA  TRP D 168     221.551 141.530 292.956  1.00128.36           C  
ATOM   2813  C   TRP D 168     221.340 142.901 293.579  1.00128.36           C  
ATOM   2814  O   TRP D 168     222.214 143.769 293.478  1.00128.36           O  
ATOM   2815  CB  TRP D 168     220.763 141.417 291.654  1.00128.36           C  
ATOM   2816  CG  TRP D 168     220.885 142.635 290.755  1.00128.36           C  
ATOM   2817  CD1 TRP D 168     220.037 143.708 290.699  1.00128.36           C  
ATOM   2818  CD2 TRP D 168     221.910 142.893 289.791  1.00128.36           C  
ATOM   2819  NE1 TRP D 168     220.470 144.610 289.765  1.00128.36           N  
ATOM   2820  CE2 TRP D 168     221.618 144.134 289.191  1.00128.36           C  
ATOM   2821  CE3 TRP D 168     223.045 142.194 289.374  1.00128.36           C  
ATOM   2822  CZ2 TRP D 168     222.420 144.691 288.200  1.00128.36           C  
ATOM   2823  CZ3 TRP D 168     223.841 142.750 288.389  1.00128.36           C  
ATOM   2824  CH2 TRP D 168     223.524 143.986 287.814  1.00128.36           C  
ATOM   2825  N   ARG D 169     220.189 143.117 294.232  1.00121.57           N  
ATOM   2826  CA  ARG D 169     219.970 144.410 294.871  1.00121.57           C  
ATOM   2827  C   ARG D 169     220.922 144.657 296.028  1.00121.57           C  
ATOM   2828  O   ARG D 169     221.372 145.788 296.198  1.00121.57           O  
ATOM   2829  CB  ARG D 169     218.528 144.564 295.334  1.00121.57           C  
ATOM   2830  CG  ARG D 169     217.670 145.233 294.296  1.00121.57           C  
ATOM   2831  CD  ARG D 169     216.306 144.642 294.231  1.00121.57           C  
ATOM   2832  NE  ARG D 169     215.402 145.523 293.507  1.00121.57           N  
ATOM   2833  CZ  ARG D 169     215.000 145.325 292.262  1.00121.57           C  
ATOM   2834  NH1 ARG D 169     215.413 144.284 291.560  1.00121.57           N  
ATOM   2835  NH2 ARG D 169     214.173 146.202 291.702  1.00121.57           N  
ATOM   2836  N   SER D 170     221.297 143.619 296.778  1.00126.88           N  
ATOM   2837  CA  SER D 170     222.227 143.792 297.885  1.00126.88           C  
ATOM   2838  C   SER D 170     223.615 144.182 297.390  1.00126.88           C  
ATOM   2839  O   SER D 170     224.180 145.189 297.844  1.00126.88           O  
ATOM   2840  CB  SER D 170     222.279 142.507 298.711  1.00126.88           C  
ATOM   2841  OG  SER D 170     223.414 142.474 299.551  1.00126.88           O  
ATOM   2842  N   GLU D 171     224.154 143.428 296.422  1.00129.16           N  
ATOM   2843  CA  GLU D 171     225.495 143.714 295.918  1.00129.16           C  
ATOM   2844  C   GLU D 171     225.546 145.054 295.191  1.00129.16           C  
ATOM   2845  O   GLU D 171     226.405 145.898 295.489  1.00129.16           O  
ATOM   2846  CB  GLU D 171     225.955 142.588 294.991  1.00129.16           C  
ATOM   2847  CG  GLU D 171     226.152 141.245 295.675  1.00129.16           C  
ATOM   2848  CD  GLU D 171     227.202 141.287 296.768  1.00129.16           C  
ATOM   2849  OE1 GLU D 171     228.247 141.943 296.571  1.00129.16           O  
ATOM   2850  OE2 GLU D 171     226.981 140.663 297.827  1.00129.16           O  
ATOM   2851  N   VAL D 172     224.602 145.282 294.271  1.00124.25           N  
ATOM   2852  CA  VAL D 172     224.579 146.506 293.478  1.00124.25           C  
ATOM   2853  C   VAL D 172     224.272 147.723 294.349  1.00124.25           C  
ATOM   2854  O   VAL D 172     224.865 148.792 294.163  1.00124.25           O  
ATOM   2855  CB  VAL D 172     223.592 146.327 292.309  1.00124.25           C  
ATOM   2856  CG1 VAL D 172     223.345 147.614 291.576  1.00124.25           C  
ATOM   2857  CG2 VAL D 172     224.165 145.316 291.334  1.00124.25           C  
ATOM   2858  N   GLY D 173     223.392 147.574 295.345  1.00124.63           N  
ATOM   2859  CA  GLY D 173     223.102 148.676 296.243  1.00124.63           C  
ATOM   2860  C   GLY D 173     224.273 149.056 297.126  1.00124.63           C  
ATOM   2861  O   GLY D 173     224.557 150.245 297.302  1.00124.63           O  
ATOM   2862  N   LYS D 174     224.994 148.061 297.666  1.00126.63           N  
ATOM   2863  CA  LYS D 174     226.146 148.413 298.490  1.00126.63           C  
ATOM   2864  C   LYS D 174     227.289 148.976 297.658  1.00126.63           C  
ATOM   2865  O   LYS D 174     228.070 149.787 298.168  1.00126.63           O  
ATOM   2866  CB  LYS D 174     226.653 147.224 299.308  1.00126.63           C  
ATOM   2867  CG  LYS D 174     225.697 146.690 300.357  1.00126.63           C  
ATOM   2868  CD  LYS D 174     226.384 145.604 301.179  1.00126.63           C  
ATOM   2869  CE  LYS D 174     226.635 144.337 300.385  1.00126.63           C  
ATOM   2870  NZ  LYS D 174     225.377 143.665 300.007  1.00126.63           N  
ATOM   2871  N   GLN D 175     227.418 148.577 296.393  1.00125.25           N  
ATOM   2872  CA  GLN D 175     228.482 149.183 295.602  1.00125.25           C  
ATOM   2873  C   GLN D 175     228.061 150.485 294.926  1.00125.25           C  
ATOM   2874  O   GLN D 175     228.930 151.204 294.422  1.00125.25           O  
ATOM   2875  CB  GLN D 175     229.028 148.202 294.557  1.00125.25           C  
ATOM   2876  CG  GLN D 175     228.068 147.780 293.479  1.00125.25           C  
ATOM   2877  CD  GLN D 175     228.609 146.623 292.663  1.00125.25           C  
ATOM   2878  OE1 GLN D 175     229.788 146.281 292.760  1.00125.25           O  
ATOM   2879  NE2 GLN D 175     227.745 145.997 291.872  1.00125.25           N  
ATOM   2880  N   LEU D 176     226.766 150.813 294.897  1.00118.41           N  
ATOM   2881  CA  LEU D 176     226.312 152.000 294.189  1.00118.41           C  
ATOM   2882  C   LEU D 176     225.753 153.101 295.078  1.00118.41           C  
ATOM   2883  O   LEU D 176     225.479 154.190 294.562  1.00118.41           O  
ATOM   2884  CB  LEU D 176     225.233 151.638 293.157  1.00118.41           C  
ATOM   2885  CG  LEU D 176     225.691 151.062 291.819  1.00118.41           C  
ATOM   2886  CD1 LEU D 176     224.535 151.004 290.843  1.00118.41           C  
ATOM   2887  CD2 LEU D 176     226.821 151.859 291.254  1.00118.41           C  
ATOM   2888  N   ARG D 177     225.529 152.847 296.377  1.00117.62           N  
ATOM   2889  CA  ARG D 177     224.897 153.871 297.211  1.00117.62           C  
ATOM   2890  C   ARG D 177     225.750 155.127 297.425  1.00117.62           C  
ATOM   2891  O   ARG D 177     225.210 156.232 297.236  1.00117.62           O  
ATOM   2892  CB  ARG D 177     224.416 153.250 298.530  1.00117.62           C  
ATOM   2893  CG  ARG D 177     223.954 154.277 299.543  1.00117.62           C  
ATOM   2894  CD  ARG D 177     222.659 154.923 299.094  1.00117.62           C  
ATOM   2895  NE  ARG D 177     222.235 155.986 299.995  1.00117.62           N  
ATOM   2896  CZ  ARG D 177     221.174 155.921 300.785  1.00117.62           C  
ATOM   2897  NH1 ARG D 177     220.392 154.856 300.804  1.00117.62           N  
ATOM   2898  NH2 ARG D 177     220.882 156.960 301.561  1.00117.62           N  
ATOM   2899  N   PRO D 178     227.048 155.065 297.793  1.00114.69           N  
ATOM   2900  CA  PRO D 178     227.806 156.329 297.885  1.00114.69           C  
ATOM   2901  C   PRO D 178     228.050 156.991 296.541  1.00114.69           C  
ATOM   2902  O   PRO D 178     228.212 158.219 296.481  1.00114.69           O  
ATOM   2903  CB  PRO D 178     229.125 155.904 298.546  1.00114.69           C  
ATOM   2904  CG  PRO D 178     228.802 154.647 299.242  1.00114.69           C  
ATOM   2905  CD  PRO D 178     227.892 153.958 298.290  1.00114.69           C  
ATOM   2906  N   LEU D 179     228.064 156.207 295.462  1.00112.46           N  
ATOM   2907  CA  LEU D 179     228.162 156.768 294.121  1.00112.46           C  
ATOM   2908  C   LEU D 179     226.947 157.624 293.796  1.00112.46           C  
ATOM   2909  O   LEU D 179     227.085 158.743 293.290  1.00112.46           O  
ATOM   2910  CB  LEU D 179     228.315 155.644 293.103  1.00112.46           C  
ATOM   2911  CG  LEU D 179     229.720 155.167 292.744  1.00112.46           C  
ATOM   2912  CD1 LEU D 179     230.390 154.410 293.875  1.00112.46           C  
ATOM   2913  CD2 LEU D 179     229.594 154.274 291.547  1.00112.46           C  
ATOM   2914  N   TYR D 180     225.749 157.134 294.126  1.00107.82           N  
ATOM   2915  CA  TYR D 180     224.546 157.936 293.936  1.00107.82           C  
ATOM   2916  C   TYR D 180     224.493 159.098 294.918  1.00107.82           C  
ATOM   2917  O   TYR D 180     223.942 160.155 294.587  1.00107.82           O  
ATOM   2918  CB  TYR D 180     223.300 157.065 294.079  1.00107.82           C  
ATOM   2919  CG  TYR D 180     222.121 157.564 293.280  1.00107.82           C  
ATOM   2920  CD1 TYR D 180     222.067 157.390 291.905  1.00107.82           C  
ATOM   2921  CD2 TYR D 180     221.070 158.226 293.901  1.00107.82           C  
ATOM   2922  CE1 TYR D 180     220.994 157.850 291.171  1.00107.82           C  
ATOM   2923  CE2 TYR D 180     219.995 158.693 293.175  1.00107.82           C  
ATOM   2924  CZ  TYR D 180     219.963 158.503 291.811  1.00107.82           C  
ATOM   2925  OH  TYR D 180     218.893 158.966 291.085  1.00107.82           O  
ATOM   2926  N   GLU D 181     225.076 158.917 296.110  1.00112.60           N  
ATOM   2927  CA  GLU D 181     225.162 159.985 297.105  1.00112.60           C  
ATOM   2928  C   GLU D 181     225.960 161.171 296.581  1.00112.60           C  
ATOM   2929  O   GLU D 181     225.575 162.328 296.782  1.00112.60           O  
ATOM   2930  CB  GLU D 181     225.813 159.448 298.379  1.00112.60           C  
ATOM   2931  CG  GLU D 181     224.894 158.723 299.334  1.00112.60           C  
ATOM   2932  CD  GLU D 181     224.466 159.593 300.485  1.00112.60           C  
ATOM   2933  OE1 GLU D 181     224.793 160.798 300.470  1.00112.60           O  
ATOM   2934  OE2 GLU D 181     223.811 159.072 301.412  1.00112.60           O  
ATOM   2935  N   GLU D 182     227.087 160.904 295.925  1.00111.33           N  
ATOM   2936  CA  GLU D 182     227.837 161.990 295.303  1.00111.33           C  
ATOM   2937  C   GLU D 182     227.173 162.475 294.019  1.00111.33           C  
ATOM   2938  O   GLU D 182     227.287 163.660 293.676  1.00111.33           O  
ATOM   2939  CB  GLU D 182     229.276 161.554 295.039  1.00111.33           C  
ATOM   2940  CG  GLU D 182     230.196 161.818 296.219  1.00111.33           C  
ATOM   2941  CD  GLU D 182     231.600 161.318 295.983  1.00111.33           C  
ATOM   2942  OE1 GLU D 182     232.036 161.328 294.816  1.00111.33           O  
ATOM   2943  OE2 GLU D 182     232.267 160.916 296.959  1.00111.33           O  
ATOM   2944  N   TYR D 183     226.484 161.574 293.312  1.00104.67           N  
ATOM   2945  CA  TYR D 183     225.880 161.892 292.022  1.00104.67           C  
ATOM   2946  C   TYR D 183     224.757 162.909 292.159  1.00104.67           C  
ATOM   2947  O   TYR D 183     224.650 163.829 291.338  1.00104.67           O  
ATOM   2948  CB  TYR D 183     225.365 160.602 291.389  1.00104.67           C  
ATOM   2949  CG  TYR D 183     224.415 160.767 290.228  1.00104.67           C  
ATOM   2950  CD1 TYR D 183     224.872 161.093 288.961  1.00104.67           C  
ATOM   2951  CD2 TYR D 183     223.051 160.574 290.405  1.00104.67           C  
ATOM   2952  CE1 TYR D 183     223.990 161.227 287.905  1.00104.67           C  
ATOM   2953  CE2 TYR D 183     222.169 160.711 289.364  1.00104.67           C  
ATOM   2954  CZ  TYR D 183     222.640 161.035 288.118  1.00104.67           C  
ATOM   2955  OH  TYR D 183     221.745 161.165 287.088  1.00104.67           O  
ATOM   2956  N   VAL D 184     223.917 162.757 293.190  1.00103.73           N  
ATOM   2957  CA  VAL D 184     222.805 163.686 293.387  1.00103.73           C  
ATOM   2958  C   VAL D 184     223.327 165.079 293.731  1.00103.73           C  
ATOM   2959  O   VAL D 184     222.816 166.084 293.222  1.00103.73           O  
ATOM   2960  CB  VAL D 184     221.811 163.141 294.441  1.00103.73           C  
ATOM   2961  CG1 VAL D 184     222.476 162.816 295.765  1.00103.73           C  
ATOM   2962  CG2 VAL D 184     220.676 164.112 294.678  1.00103.73           C  
ATOM   2963  N   VAL D 185     224.409 165.157 294.513  1.00104.56           N  
ATOM   2964  CA  VAL D 185     224.977 166.445 294.897  1.00104.56           C  
ATOM   2965  C   VAL D 185     225.630 167.126 293.701  1.00104.56           C  
ATOM   2966  O   VAL D 185     225.439 168.329 293.480  1.00104.56           O  
ATOM   2967  CB  VAL D 185     225.972 166.254 296.057  1.00104.56           C  
ATOM   2968  CG1 VAL D 185     226.623 167.573 296.439  1.00104.56           C  
ATOM   2969  CG2 VAL D 185     225.267 165.647 297.255  1.00104.56           C  
ATOM   2970  N   LEU D 186     226.379 166.367 292.894  1.00103.92           N  
ATOM   2971  CA  LEU D 186     227.032 166.950 291.723  1.00103.92           C  
ATOM   2972  C   LEU D 186     226.022 167.405 290.676  1.00103.92           C  
ATOM   2973  O   LEU D 186     226.169 168.490 290.099  1.00103.92           O  
ATOM   2974  CB  LEU D 186     228.019 165.953 291.124  1.00103.92           C  
ATOM   2975  CG  LEU D 186     229.294 165.682 291.927  1.00103.92           C  
ATOM   2976  CD1 LEU D 186     230.343 165.043 291.044  1.00103.92           C  
ATOM   2977  CD2 LEU D 186     229.839 166.955 292.557  1.00103.92           C  
ATOM   2978  N   LYS D 187     224.971 166.615 290.439  1.00 99.15           N  
ATOM   2979  CA  LYS D 187     223.963 167.024 289.469  1.00 99.15           C  
ATOM   2980  C   LYS D 187     223.124 168.185 289.985  1.00 99.15           C  
ATOM   2981  O   LYS D 187     222.695 169.034 289.195  1.00 99.15           O  
ATOM   2982  CB  LYS D 187     223.075 165.841 289.109  1.00 99.15           C  
ATOM   2983  CG  LYS D 187     223.761 164.811 288.246  1.00 99.15           C  
ATOM   2984  CD  LYS D 187     224.080 165.367 286.878  1.00 99.15           C  
ATOM   2985  CE  LYS D 187     224.557 164.273 285.948  1.00 99.15           C  
ATOM   2986  NZ  LYS D 187     224.922 164.808 284.612  1.00 99.15           N  
ATOM   2987  N   ASN D 188     222.899 168.250 291.301  1.00102.20           N  
ATOM   2988  CA  ASN D 188     222.195 169.382 291.889  1.00102.20           C  
ATOM   2989  C   ASN D 188     223.014 170.661 291.739  1.00102.20           C  
ATOM   2990  O   ASN D 188     222.462 171.714 291.406  1.00102.20           O  
ATOM   2991  CB  ASN D 188     221.885 169.073 293.356  1.00102.20           C  
ATOM   2992  CG  ASN D 188     220.927 170.068 293.997  1.00102.20           C  
ATOM   2993  OD1 ASN D 188     220.467 171.022 293.372  1.00102.20           O  
ATOM   2994  ND2 ASN D 188     220.612 169.833 295.264  1.00102.20           N  
ATOM   2995  N   GLU D 189     224.333 170.583 291.962  1.00104.14           N  
ATOM   2996  CA  GLU D 189     225.196 171.745 291.749  1.00104.14           C  
ATOM   2997  C   GLU D 189     225.233 172.152 290.281  1.00104.14           C  
ATOM   2998  O   GLU D 189     225.277 173.349 289.967  1.00104.14           O  
ATOM   2999  CB  GLU D 189     226.615 171.467 292.249  1.00104.14           C  
ATOM   3000  CG  GLU D 189     226.750 171.300 293.752  1.00104.14           C  
ATOM   3001  CD  GLU D 189     226.464 172.579 294.512  1.00104.14           C  
ATOM   3002  OE1 GLU D 189     226.746 173.671 293.975  1.00104.14           O  
ATOM   3003  OE2 GLU D 189     225.954 172.493 295.649  1.00104.14           O  
ATOM   3004  N   MET D 190     225.211 171.168 289.375  1.00100.46           N  
ATOM   3005  CA  MET D 190     225.174 171.461 287.945  1.00100.46           C  
ATOM   3006  C   MET D 190     223.896 172.186 287.554  1.00100.46           C  
ATOM   3007  O   MET D 190     223.931 173.151 286.782  1.00100.46           O  
ATOM   3008  CB  MET D 190     225.294 170.166 287.142  1.00100.46           C  
ATOM   3009  CG  MET D 190     225.303 170.378 285.640  1.00100.46           C  
ATOM   3010  SD  MET D 190     223.746 169.947 284.840  1.00100.46           S  
ATOM   3011  CE  MET D 190     224.044 168.240 284.401  1.00100.46           C  
ATOM   3012  N   ALA D 191     222.758 171.735 288.076  1.00 98.38           N  
ATOM   3013  CA  ALA D 191     221.492 172.358 287.716  1.00 98.38           C  
ATOM   3014  C   ALA D 191     221.328 173.732 288.356  1.00 98.38           C  
ATOM   3015  O   ALA D 191     220.809 174.654 287.720  1.00 98.38           O  
ATOM   3016  CB  ALA D 191     220.340 171.442 288.100  1.00 98.38           C  
ATOM   3017  N   ARG D 192     221.772 173.899 289.604  1.00 99.81           N  
ATOM   3018  CA  ARG D 192     221.675 175.209 290.237  1.00 99.81           C  
ATOM   3019  C   ARG D 192     222.678 176.203 289.675  1.00 99.81           C  
ATOM   3020  O   ARG D 192     222.443 177.412 289.760  1.00 99.81           O  
ATOM   3021  CB  ARG D 192     221.841 175.090 291.750  1.00 99.81           C  
ATOM   3022  CG  ARG D 192     220.758 174.263 292.421  1.00 99.81           C  
ATOM   3023  CD  ARG D 192     220.606 174.501 293.928  1.00 99.81           C  
ATOM   3024  NE  ARG D 192     221.681 173.923 294.730  1.00 99.81           N  
ATOM   3025  CZ  ARG D 192     222.815 174.531 295.055  1.00 99.81           C  
ATOM   3026  NH1 ARG D 192     223.034 175.801 294.755  1.00 99.81           N  
ATOM   3027  NH2 ARG D 192     223.743 173.855 295.725  1.00 99.81           N  
ATOM   3028  N   ALA D 193     223.784 175.731 289.102  1.00 97.26           N  
ATOM   3029  CA  ALA D 193     224.638 176.638 288.352  1.00 97.26           C  
ATOM   3030  C   ALA D 193     224.030 177.000 287.005  1.00 97.26           C  
ATOM   3031  O   ALA D 193     224.357 178.054 286.454  1.00 97.26           O  
ATOM   3032  CB  ALA D 193     226.021 176.022 288.163  1.00 97.26           C  
ATOM   3033  N   ASN D 194     223.153 176.153 286.469  1.00 95.75           N  
ATOM   3034  CA  ASN D 194     222.492 176.388 285.194  1.00 95.75           C  
ATOM   3035  C   ASN D 194     221.149 177.094 285.342  1.00 95.75           C  
ATOM   3036  O   ASN D 194     220.317 177.000 284.432  1.00 95.75           O  
ATOM   3037  CB  ASN D 194     222.308 175.066 284.450  1.00 95.75           C  
ATOM   3038  CG  ASN D 194     223.491 174.725 283.578  1.00 95.75           C  
ATOM   3039  OD1 ASN D 194     224.199 175.610 283.105  1.00 95.75           O  
ATOM   3040  ND2 ASN D 194     223.718 173.437 283.364  1.00 95.75           N  
ATOM   3041  N   HIS D 195     220.933 177.787 286.469  1.00 94.33           N  
ATOM   3042  CA  HIS D 195     219.705 178.534 286.783  1.00 94.33           C  
ATOM   3043  C   HIS D 195     218.458 177.648 286.784  1.00 94.33           C  
ATOM   3044  O   HIS D 195     217.374 178.068 286.379  1.00 94.33           O  
ATOM   3045  CB  HIS D 195     219.527 179.734 285.851  1.00 94.33           C  
ATOM   3046  CG  HIS D 195     220.733 180.614 285.778  1.00 94.33           C  
ATOM   3047  ND1 HIS D 195     221.448 180.802 284.615  1.00 94.33           N  
ATOM   3048  CD2 HIS D 195     221.360 181.346 286.727  1.00 94.33           C  
ATOM   3049  CE1 HIS D 195     222.459 181.617 284.849  1.00 94.33           C  
ATOM   3050  NE2 HIS D 195     222.429 181.963 286.124  1.00 94.33           N  
ATOM   3051  N   TYR D 196     218.615 176.415 287.249  1.00 91.03           N  
ATOM   3052  CA  TYR D 196     217.508 175.513 287.519  1.00 91.03           C  
ATOM   3053  C   TYR D 196     217.410 175.293 289.021  1.00 91.03           C  
ATOM   3054  O   TYR D 196     218.378 175.484 289.759  1.00 91.03           O  
ATOM   3055  CB  TYR D 196     217.689 174.170 286.803  1.00 91.03           C  
ATOM   3056  CG  TYR D 196     217.433 174.214 285.319  1.00 91.03           C  
ATOM   3057  CD1 TYR D 196     216.150 174.085 284.817  1.00 91.03           C  
ATOM   3058  CD2 TYR D 196     218.473 174.384 284.421  1.00 91.03           C  
ATOM   3059  CE1 TYR D 196     215.907 174.127 283.462  1.00 91.03           C  
ATOM   3060  CE2 TYR D 196     218.241 174.432 283.063  1.00 91.03           C  
ATOM   3061  CZ  TYR D 196     216.957 174.298 282.590  1.00 91.03           C  
ATOM   3062  OH  TYR D 196     216.721 174.339 281.238  1.00 91.03           O  
ATOM   3063  N   GLU D 197     216.215 174.919 289.475  1.00 93.57           N  
ATOM   3064  CA  GLU D 197     216.013 174.683 290.901  1.00 93.57           C  
ATOM   3065  C   GLU D 197     216.733 173.422 291.363  1.00 93.57           C  
ATOM   3066  O   GLU D 197     217.420 173.428 292.391  1.00 93.57           O  
ATOM   3067  CB  GLU D 197     214.520 174.595 291.213  1.00 93.57           C  
ATOM   3068  CG  GLU D 197     214.204 174.374 292.687  1.00 93.57           C  
ATOM   3069  CD  GLU D 197     214.606 175.538 293.580  1.00 93.57           C  
ATOM   3070  OE1 GLU D 197     214.664 176.690 293.098  1.00 93.57           O  
ATOM   3071  OE2 GLU D 197     214.873 175.296 294.776  1.00 93.57           O  
ATOM   3072  N   ASP D 198     216.593 172.335 290.614  1.00 92.15           N  
ATOM   3073  CA  ASP D 198     217.247 171.075 290.928  1.00 92.15           C  
ATOM   3074  C   ASP D 198     217.448 170.308 289.630  1.00 92.15           C  
ATOM   3075  O   ASP D 198     217.083 170.779 288.550  1.00 92.15           O  
ATOM   3076  CB  ASP D 198     216.440 170.292 291.973  1.00 92.15           C  
ATOM   3077  CG  ASP D 198     214.950 170.213 291.647  1.00 92.15           C  
ATOM   3078  OD1 ASP D 198     214.567 169.959 290.488  1.00 92.15           O  
ATOM   3079  OD2 ASP D 198     214.141 170.438 292.568  1.00 92.15           O  
ATOM   3080  N   TYR D 199     218.058 169.126 289.735  1.00 89.96           N  
ATOM   3081  CA  TYR D 199     218.252 168.299 288.549  1.00 89.96           C  
ATOM   3082  C   TYR D 199     216.934 167.760 288.013  1.00 89.96           C  
ATOM   3083  O   TYR D 199     216.809 167.522 286.804  1.00 89.96           O  
ATOM   3084  CB  TYR D 199     219.197 167.143 288.854  1.00 89.96           C  
ATOM   3085  CG  TYR D 199     219.805 166.538 287.618  1.00 89.96           C  
ATOM   3086  CD1 TYR D 199     220.216 167.335 286.565  1.00 89.96           C  
ATOM   3087  CD2 TYR D 199     219.932 165.164 287.490  1.00 89.96           C  
ATOM   3088  CE1 TYR D 199     220.764 166.781 285.429  1.00 89.96           C  
ATOM   3089  CE2 TYR D 199     220.476 164.603 286.358  1.00 89.96           C  
ATOM   3090  CZ  TYR D 199     220.886 165.416 285.329  1.00 89.96           C  
ATOM   3091  OH  TYR D 199     221.431 164.861 284.197  1.00 89.96           O  
ATOM   3092  N   GLY D 200     215.948 167.560 288.889  1.00 86.68           N  
ATOM   3093  CA  GLY D 200     214.613 167.237 288.422  1.00 86.68           C  
ATOM   3094  C   GLY D 200     214.000 168.358 287.607  1.00 86.68           C  
ATOM   3095  O   GLY D 200     213.320 168.109 286.612  1.00 86.68           O  
ATOM   3096  N   ASP D 201     214.266 169.608 287.995  1.00 86.41           N  
ATOM   3097  CA  ASP D 201     213.835 170.745 287.189  1.00 86.41           C  
ATOM   3098  C   ASP D 201     214.582 170.805 285.863  1.00 86.41           C  
ATOM   3099  O   ASP D 201     213.998 171.188 284.842  1.00 86.41           O  
ATOM   3100  CB  ASP D 201     214.024 172.041 287.972  1.00 86.41           C  
ATOM   3101  CG  ASP D 201     213.154 173.161 287.460  1.00 86.41           C  
ATOM   3102  OD1 ASP D 201     211.918 173.051 287.575  1.00 86.41           O  
ATOM   3103  OD2 ASP D 201     213.703 174.158 286.950  1.00 86.41           O  
ATOM   3104  N   TYR D 202     215.855 170.401 285.856  1.00 88.08           N  
ATOM   3105  CA  TYR D 202     216.616 170.340 284.613  1.00 88.08           C  
ATOM   3106  C   TYR D 202     216.039 169.298 283.667  1.00 88.08           C  
ATOM   3107  O   TYR D 202     215.996 169.510 282.450  1.00 88.08           O  
ATOM   3108  CB  TYR D 202     218.082 170.023 284.912  1.00 88.08           C  
ATOM   3109  CG  TYR D 202     218.983 170.016 283.696  1.00 88.08           C  
ATOM   3110  CD1 TYR D 202     219.497 171.196 283.187  1.00 88.08           C  
ATOM   3111  CD2 TYR D 202     219.317 168.827 283.057  1.00 88.08           C  
ATOM   3112  CE1 TYR D 202     220.318 171.198 282.079  1.00 88.08           C  
ATOM   3113  CE2 TYR D 202     220.136 168.817 281.950  1.00 88.08           C  
ATOM   3114  CZ  TYR D 202     220.634 170.006 281.466  1.00 88.08           C  
ATOM   3115  OH  TYR D 202     221.453 170.002 280.362  1.00 88.08           O  
ATOM   3116  N   TRP D 203     215.592 168.164 284.208  1.00 86.41           N  
ATOM   3117  CA  TRP D 203     214.986 167.142 283.366  1.00 86.41           C  
ATOM   3118  C   TRP D 203     213.580 167.525 282.930  1.00 86.41           C  
ATOM   3119  O   TRP D 203     213.152 167.155 281.832  1.00 86.41           O  
ATOM   3120  CB  TRP D 203     214.961 165.806 284.091  1.00 86.41           C  
ATOM   3121  CG  TRP D 203     216.162 164.986 283.827  1.00 86.41           C  
ATOM   3122  CD1 TRP D 203     217.000 165.085 282.761  1.00 86.41           C  
ATOM   3123  CD2 TRP D 203     216.644 163.906 284.620  1.00 86.41           C  
ATOM   3124  NE1 TRP D 203     217.993 164.145 282.853  1.00 86.41           N  
ATOM   3125  CE2 TRP D 203     217.793 163.405 283.987  1.00 86.41           C  
ATOM   3126  CE3 TRP D 203     216.218 163.317 285.809  1.00 86.41           C  
ATOM   3127  CZ2 TRP D 203     218.519 162.342 284.502  1.00 86.41           C  
ATOM   3128  CZ3 TRP D 203     216.940 162.268 286.318  1.00 86.41           C  
ATOM   3129  CH2 TRP D 203     218.079 161.790 285.669  1.00 86.41           C  
ATOM   3130  N   ARG D 204     212.849 168.261 283.767  1.00 80.62           N  
ATOM   3131  CA  ARG D 204     211.538 168.765 283.381  1.00 80.62           C  
ATOM   3132  C   ARG D 204     211.623 169.924 282.403  1.00 80.62           C  
ATOM   3133  O   ARG D 204     210.605 170.276 281.801  1.00 80.62           O  
ATOM   3134  CB  ARG D 204     210.748 169.193 284.614  1.00 80.62           C  
ATOM   3135  CG  ARG D 204     210.260 168.044 285.462  1.00 80.62           C  
ATOM   3136  CD  ARG D 204     209.350 168.531 286.563  1.00 80.62           C  
ATOM   3137  NE  ARG D 204     209.985 169.518 287.426  1.00 80.62           N  
ATOM   3138  CZ  ARG D 204     210.637 169.232 288.542  1.00 80.62           C  
ATOM   3139  NH1 ARG D 204     210.778 167.986 288.960  1.00 80.62           N  
ATOM   3140  NH2 ARG D 204     211.152 170.221 289.264  1.00 80.62           N  
ATOM   3141  N   GLY D 205     212.799 170.525 282.237  1.00 79.20           N  
ATOM   3142  CA  GLY D 205     212.981 171.604 281.282  1.00 79.20           C  
ATOM   3143  C   GLY D 205     212.842 171.206 279.825  1.00 79.20           C  
ATOM   3144  O   GLY D 205     212.766 172.096 278.972  1.00 79.20           O  
ATOM   3145  N   ASP D 206     212.821 169.907 279.515  1.00 76.90           N  
ATOM   3146  CA  ASP D 206     212.577 169.480 278.142  1.00 76.90           C  
ATOM   3147  C   ASP D 206     211.146 169.755 277.700  1.00 76.90           C  
ATOM   3148  O   ASP D 206     210.895 169.931 276.504  1.00 76.90           O  
ATOM   3149  CB  ASP D 206     212.881 167.991 278.000  1.00 76.90           C  
ATOM   3150  CG  ASP D 206     212.995 167.554 276.556  1.00 76.90           C  
ATOM   3151  OD1 ASP D 206     213.988 167.916 275.893  1.00 76.90           O  
ATOM   3152  OD2 ASP D 206     212.083 166.849 276.081  1.00 76.90           O  
ATOM   3153  N   TYR D 207     210.203 169.798 278.633  1.00 72.38           N  
ATOM   3154  CA  TYR D 207     208.817 170.095 278.307  1.00 72.38           C  
ATOM   3155  C   TYR D 207     208.475 171.568 278.450  1.00 72.38           C  
ATOM   3156  O   TYR D 207     207.319 171.942 278.237  1.00 72.38           O  
ATOM   3157  CB  TYR D 207     207.881 169.270 279.194  1.00 72.38           C  
ATOM   3158  CG  TYR D 207     208.037 167.778 279.041  1.00 72.38           C  
ATOM   3159  CD1 TYR D 207     208.957 167.072 279.803  1.00 72.38           C  
ATOM   3160  CD2 TYR D 207     207.260 167.074 278.136  1.00 72.38           C  
ATOM   3161  CE1 TYR D 207     209.101 165.715 279.663  1.00 72.38           C  
ATOM   3162  CE2 TYR D 207     207.396 165.715 277.992  1.00 72.38           C  
ATOM   3163  CZ  TYR D 207     208.318 165.042 278.757  1.00 72.38           C  
ATOM   3164  OH  TYR D 207     208.456 163.685 278.612  1.00 72.38           O  
ATOM   3165  N   GLU D 208     209.443 172.407 278.800  1.00 77.88           N  
ATOM   3166  CA  GLU D 208     209.170 173.815 279.042  1.00 77.88           C  
ATOM   3167  C   GLU D 208     208.962 174.553 277.728  1.00 77.88           C  
ATOM   3168  O   GLU D 208     209.769 174.430 276.803  1.00 77.88           O  
ATOM   3169  CB  GLU D 208     210.317 174.449 279.821  1.00 77.88           C  
ATOM   3170  CG  GLU D 208     210.112 175.917 280.129  1.00 77.88           C  
ATOM   3171  CD  GLU D 208     211.413 176.649 280.363  1.00 77.88           C  
ATOM   3172  OE1 GLU D 208     212.295 176.094 281.047  1.00 77.88           O  
ATOM   3173  OE2 GLU D 208     211.555 177.784 279.863  1.00 77.88           O  
ATOM   3174  N   VAL D 209     207.878 175.316 277.640  1.00 77.35           N  
ATOM   3175  CA  VAL D 209     207.609 176.172 276.493  1.00 77.35           C  
ATOM   3176  C   VAL D 209     207.429 177.587 277.017  1.00 77.35           C  
ATOM   3177  O   VAL D 209     206.561 177.832 277.861  1.00 77.35           O  
ATOM   3178  CB  VAL D 209     206.370 175.720 275.709  1.00 77.35           C  
ATOM   3179  CG1 VAL D 209     205.999 176.771 274.693  1.00 77.35           C  
ATOM   3180  CG2 VAL D 209     206.630 174.395 275.029  1.00 77.35           C  
ATOM   3181  N   ASN D 210     208.242 178.513 276.519  1.00 81.95           N  
ATOM   3182  CA  ASN D 210     208.218 179.899 276.957  1.00 81.95           C  
ATOM   3183  C   ASN D 210     208.134 180.827 275.757  1.00 81.95           C  
ATOM   3184  O   ASN D 210     208.788 180.596 274.736  1.00 81.95           O  
ATOM   3185  CB  ASN D 210     209.457 180.234 277.783  1.00 81.95           C  
ATOM   3186  CG  ASN D 210     209.280 179.915 279.249  1.00 81.95           C  
ATOM   3187  OD1 ASN D 210     208.236 179.415 279.665  1.00 81.95           O  
ATOM   3188  ND2 ASN D 210     210.305 180.196 280.043  1.00 81.95           N  
ATOM   3189  N   GLY D 211     207.328 181.877 275.884  1.00 87.24           N  
ATOM   3190  CA  GLY D 211     207.289 182.942 274.907  1.00 87.24           C  
ATOM   3191  C   GLY D 211     206.170 182.856 273.893  1.00 87.24           C  
ATOM   3192  O   GLY D 211     205.953 183.825 273.158  1.00 87.24           O  
ATOM   3193  N   VAL D 212     205.458 181.738 273.828  1.00 87.51           N  
ATOM   3194  CA  VAL D 212     204.375 181.552 272.872  1.00 87.51           C  
ATOM   3195  C   VAL D 212     203.063 181.709 273.625  1.00 87.51           C  
ATOM   3196  O   VAL D 212     202.830 181.023 274.627  1.00 87.51           O  
ATOM   3197  CB  VAL D 212     204.462 180.184 272.181  1.00 87.51           C  
ATOM   3198  CG1 VAL D 212     203.446 180.096 271.061  1.00 87.51           C  
ATOM   3199  CG2 VAL D 212     205.862 179.958 271.650  1.00 87.51           C  
ATOM   3200  N   ASP D 213     202.214 182.620 273.159  1.00 92.25           N  
ATOM   3201  CA  ASP D 213     200.967 182.903 273.856  1.00 92.25           C  
ATOM   3202  C   ASP D 213     199.965 181.779 273.640  1.00 92.25           C  
ATOM   3203  O   ASP D 213     199.766 181.318 272.513  1.00 92.25           O  
ATOM   3204  CB  ASP D 213     200.382 184.229 273.377  1.00 92.25           C  
ATOM   3205  CG  ASP D 213     201.269 185.408 273.711  1.00 92.25           C  
ATOM   3206  OD1 ASP D 213     201.948 185.363 274.759  1.00 92.25           O  
ATOM   3207  OD2 ASP D 213     201.287 186.380 272.928  1.00 92.25           O  
ATOM   3208  N   GLY D 214     199.338 181.333 274.728  1.00 84.58           N  
ATOM   3209  CA  GLY D 214     198.365 180.267 274.691  1.00 84.58           C  
ATOM   3210  C   GLY D 214     198.949 178.871 274.763  1.00 84.58           C  
ATOM   3211  O   GLY D 214     198.296 177.962 275.282  1.00 84.58           O  
ATOM   3212  N   TYR D 215     200.163 178.679 274.251  1.00 82.78           N  
ATOM   3213  CA  TYR D 215     200.829 177.387 274.246  1.00 82.78           C  
ATOM   3214  C   TYR D 215     201.926 177.287 275.296  1.00 82.78           C  
ATOM   3215  O   TYR D 215     202.770 176.391 275.214  1.00 82.78           O  
ATOM   3216  CB  TYR D 215     201.387 177.105 272.854  1.00 82.78           C  
ATOM   3217  CG  TYR D 215     200.320 177.078 271.795  1.00 82.78           C  
ATOM   3218  CD1 TYR D 215     199.338 176.100 271.806  1.00 82.78           C  
ATOM   3219  CD2 TYR D 215     200.283 178.036 270.794  1.00 82.78           C  
ATOM   3220  CE1 TYR D 215     198.353 176.068 270.845  1.00 82.78           C  
ATOM   3221  CE2 TYR D 215     199.300 178.015 269.826  1.00 82.78           C  
ATOM   3222  CZ  TYR D 215     198.336 177.030 269.860  1.00 82.78           C  
ATOM   3223  OH  TYR D 215     197.355 177.000 268.898  1.00 82.78           O  
ATOM   3224  N   ASP D 216     201.926 178.187 276.274  1.00 83.13           N  
ATOM   3225  CA  ASP D 216     202.980 178.236 277.276  1.00 83.13           C  
ATOM   3226  C   ASP D 216     202.885 177.041 278.217  1.00 83.13           C  
ATOM   3227  O   ASP D 216     201.801 176.705 278.702  1.00 83.13           O  
ATOM   3228  CB  ASP D 216     202.869 179.539 278.063  1.00 83.13           C  
ATOM   3229  CG  ASP D 216     204.035 179.763 278.993  1.00 83.13           C  
ATOM   3230  OD1 ASP D 216     205.091 180.227 278.515  1.00 83.13           O  
ATOM   3231  OD2 ASP D 216     203.896 179.478 280.201  1.00 83.13           O  
ATOM   3232  N   TYR D 217     204.021 176.392 278.465  1.00 76.80           N  
ATOM   3233  CA  TYR D 217     204.101 175.242 279.355  1.00 76.80           C  
ATOM   3234  C   TYR D 217     205.286 175.412 280.292  1.00 76.80           C  
ATOM   3235  O   TYR D 217     206.409 175.633 279.835  1.00 76.80           O  
ATOM   3236  CB  TYR D 217     204.237 173.943 278.566  1.00 76.80           C  
ATOM   3237  CG  TYR D 217     203.785 172.727 279.328  1.00 76.80           C  
ATOM   3238  CD1 TYR D 217     202.458 172.330 279.307  1.00 76.80           C  
ATOM   3239  CD2 TYR D 217     204.682 171.981 280.074  1.00 76.80           C  
ATOM   3240  CE1 TYR D 217     202.039 171.223 280.000  1.00 76.80           C  
ATOM   3241  CE2 TYR D 217     204.273 170.871 280.773  1.00 76.80           C  
ATOM   3242  CZ  TYR D 217     202.951 170.498 280.730  1.00 76.80           C  
ATOM   3243  OH  TYR D 217     202.529 169.392 281.425  1.00 76.80           O  
ATOM   3244  N   SER D 218     205.043 175.295 281.591  1.00 79.02           N  
ATOM   3245  CA  SER D 218     206.091 175.519 282.574  1.00 79.02           C  
ATOM   3246  C   SER D 218     206.786 174.216 282.955  1.00 79.02           C  
ATOM   3247  O   SER D 218     206.278 173.119 282.716  1.00 79.02           O  
ATOM   3248  CB  SER D 218     205.510 176.173 283.824  1.00 79.02           C  
ATOM   3249  OG  SER D 218     206.445 176.150 284.885  1.00 79.02           O  
ATOM   3250  N   ARG D 219     207.972 174.354 283.556  1.00 81.86           N  
ATOM   3251  CA  ARG D 219     208.668 173.195 284.107  1.00 81.86           C  
ATOM   3252  C   ARG D 219     207.919 172.630 285.299  1.00 81.86           C  
ATOM   3253  O   ARG D 219     207.871 171.412 285.496  1.00 81.86           O  
ATOM   3254  CB  ARG D 219     210.084 173.567 284.537  1.00 81.86           C  
ATOM   3255  CG  ARG D 219     211.046 173.874 283.426  1.00 81.86           C  
ATOM   3256  CD  ARG D 219     212.254 174.599 283.979  1.00 81.86           C  
ATOM   3257  NE  ARG D 219     211.900 175.948 284.400  1.00 81.86           N  
ATOM   3258  CZ  ARG D 219     212.737 176.806 284.964  1.00 81.86           C  
ATOM   3259  NH1 ARG D 219     213.998 176.491 285.192  1.00 81.86           N  
ATOM   3260  NH2 ARG D 219     212.295 178.012 285.309  1.00 81.86           N  
ATOM   3261  N   GLY D 220     207.336 173.509 286.112  1.00 82.51           N  
ATOM   3262  CA  GLY D 220     206.666 173.080 287.319  1.00 82.51           C  
ATOM   3263  C   GLY D 220     205.321 172.441 287.090  1.00 82.51           C  
ATOM   3264  O   GLY D 220     204.864 171.685 287.947  1.00 82.51           O  
ATOM   3265  N   GLN D 221     204.674 172.729 285.958  1.00 82.49           N  
ATOM   3266  CA  GLN D 221     203.315 172.252 285.742  1.00 82.49           C  
ATOM   3267  C   GLN D 221     203.255 170.762 285.460  1.00 82.49           C  
ATOM   3268  O   GLN D 221     202.250 170.123 285.816  1.00 82.49           O  
ATOM   3269  CB  GLN D 221     202.696 172.992 284.560  1.00 82.49           C  
ATOM   3270  CG  GLN D 221     201.191 172.990 284.525  1.00 82.49           C  
ATOM   3271  CD  GLN D 221     200.645 174.009 283.555  1.00 82.49           C  
ATOM   3272  OE1 GLN D 221     201.402 174.715 282.890  1.00 82.49           O  
ATOM   3273  NE2 GLN D 221     199.324 174.090 283.463  1.00 82.49           N  
ATOM   3274  N   LEU D 222     204.371 170.180 285.000  1.00 77.63           N  
ATOM   3275  CA  LEU D 222     204.365 168.819 284.478  1.00 77.63           C  
ATOM   3276  C   LEU D 222     204.025 167.807 285.545  1.00 77.63           C  
ATOM   3277  O   LEU D 222     203.226 166.896 285.282  1.00 77.63           O  
ATOM   3278  CB  LEU D 222     205.731 168.466 283.899  1.00 77.63           C  
ATOM   3279  CG  LEU D 222     205.796 167.181 283.071  1.00 77.63           C  
ATOM   3280  CD1 LEU D 222     205.135 167.322 281.715  1.00 77.63           C  
ATOM   3281  CD2 LEU D 222     207.226 166.706 282.949  1.00 77.63           C  
ATOM   3282  N   ILE D 223     204.449 168.074 286.782  1.00 80.67           N  
ATOM   3283  CA  ILE D 223     204.234 167.111 287.845  1.00 80.67           C  
ATOM   3284  C   ILE D 223     202.753 167.016 288.179  1.00 80.67           C  
ATOM   3285  O   ILE D 223     202.211 165.902 288.209  1.00 80.67           O  
ATOM   3286  CB  ILE D 223     205.106 167.438 289.077  1.00 80.67           C  
ATOM   3287  CG1 ILE D 223     204.898 168.851 289.603  1.00 80.67           C  
ATOM   3288  CG2 ILE D 223     206.558 167.347 288.724  1.00 80.67           C  
ATOM   3289  CD1 ILE D 223     205.504 169.082 290.967  1.00 80.67           C  
ATOM   3290  N   GLU D 224     202.031 168.158 288.223  1.00 83.95           N  
ATOM   3291  CA  GLU D 224     200.613 167.994 288.526  1.00 83.95           C  
ATOM   3292  C   GLU D 224     199.862 167.456 287.330  1.00 83.95           C  
ATOM   3293  O   GLU D 224     198.921 166.675 287.525  1.00 83.95           O  
ATOM   3294  CB  GLU D 224     199.932 169.279 289.023  1.00 83.95           C  
ATOM   3295  CG  GLU D 224     200.081 170.545 288.211  1.00 83.95           C  
ATOM   3296  CD  GLU D 224     201.307 171.339 288.580  1.00 83.95           C  
ATOM   3297  OE1 GLU D 224     202.357 170.731 288.839  1.00 83.95           O  
ATOM   3298  OE2 GLU D 224     201.216 172.584 288.618  1.00 83.95           O  
ATOM   3299  N   ASP D 225     200.362 167.731 286.114  1.00 81.43           N  
ATOM   3300  CA  ASP D 225     199.755 167.130 284.936  1.00 81.43           C  
ATOM   3301  C   ASP D 225     199.919 165.630 284.980  1.00 81.43           C  
ATOM   3302  O   ASP D 225     198.941 164.895 284.785  1.00 81.43           O  
ATOM   3303  CB  ASP D 225     200.348 167.708 283.655  1.00 81.43           C  
ATOM   3304  CG  ASP D 225     199.946 169.143 283.432  1.00 81.43           C  
ATOM   3305  OD1 ASP D 225     198.848 169.525 283.886  1.00 81.43           O  
ATOM   3306  OD2 ASP D 225     200.714 169.889 282.798  1.00 81.43           O  
ATOM   3307  N   VAL D 226     201.104 165.172 285.402  1.00 77.81           N  
ATOM   3308  CA  VAL D 226     201.333 163.742 285.514  1.00 77.81           C  
ATOM   3309  C   VAL D 226     200.450 163.177 286.612  1.00 77.81           C  
ATOM   3310  O   VAL D 226     199.747 162.178 286.398  1.00 77.81           O  
ATOM   3311  CB  VAL D 226     202.828 163.464 285.748  1.00 77.81           C  
ATOM   3312  CG1 VAL D 226     203.038 162.067 286.235  1.00 77.81           C  
ATOM   3313  CG2 VAL D 226     203.601 163.680 284.467  1.00 77.81           C  
ATOM   3314  N   GLU D 227     200.319 163.932 287.717  1.00 83.12           N  
ATOM   3315  CA  GLU D 227     199.441 163.525 288.807  1.00 83.12           C  
ATOM   3316  C   GLU D 227     197.999 163.497 288.344  1.00 83.12           C  
ATOM   3317  O   GLU D 227     197.287 162.512 288.585  1.00 83.12           O  
ATOM   3318  CB  GLU D 227     199.595 164.477 289.991  1.00 83.12           C  
ATOM   3319  CG  GLU D 227     200.898 164.359 290.748  1.00 83.12           C  
ATOM   3320  CD  GLU D 227     200.777 163.475 291.964  1.00 83.12           C  
ATOM   3321  OE1 GLU D 227     199.696 162.883 292.163  1.00 83.12           O  
ATOM   3322  OE2 GLU D 227     201.765 163.366 292.721  1.00 83.12           O  
ATOM   3323  N   HIS D 228     197.609 164.496 287.541  1.00 81.91           N  
ATOM   3324  CA  HIS D 228     196.236 164.564 287.071  1.00 81.91           C  
ATOM   3325  C   HIS D 228     195.945 163.434 286.108  1.00 81.91           C  
ATOM   3326  O   HIS D 228     194.811 162.948 286.050  1.00 81.91           O  
ATOM   3327  CB  HIS D 228     195.948 165.911 286.416  1.00 81.91           C  
ATOM   3328  CG  HIS D 228     194.512 166.103 286.049  1.00 81.91           C  
ATOM   3329  ND1 HIS D 228     193.988 165.679 284.847  1.00 81.91           N  
ATOM   3330  CD2 HIS D 228     193.484 166.655 286.733  1.00 81.91           C  
ATOM   3331  CE1 HIS D 228     192.701 165.973 284.802  1.00 81.91           C  
ATOM   3332  NE2 HIS D 228     192.370 166.565 285.935  1.00 81.91           N  
ATOM   3333  N   THR D 229     196.946 163.013 285.339  1.00 77.15           N  
ATOM   3334  CA  THR D 229     196.695 161.861 284.497  1.00 77.15           C  
ATOM   3335  C   THR D 229     196.695 160.578 285.312  1.00 77.15           C  
ATOM   3336  O   THR D 229     195.821 159.721 285.117  1.00 77.15           O  
ATOM   3337  CB  THR D 229     197.720 161.812 283.376  1.00 77.15           C  
ATOM   3338  OG1 THR D 229     199.032 161.897 283.935  1.00 77.15           O  
ATOM   3339  CG2 THR D 229     197.503 163.004 282.474  1.00 77.15           C  
ATOM   3340  N   PHE D 230     197.588 160.484 286.308  1.00 77.25           N  
ATOM   3341  CA  PHE D 230     197.710 159.231 287.045  1.00 77.25           C  
ATOM   3342  C   PHE D 230     196.509 158.978 287.934  1.00 77.25           C  
ATOM   3343  O   PHE D 230     196.139 157.816 288.149  1.00 77.25           O  
ATOM   3344  CB  PHE D 230     198.981 159.214 287.880  1.00 77.25           C  
ATOM   3345  CG  PHE D 230     199.244 157.891 288.512  1.00 77.25           C  
ATOM   3346  CD1 PHE D 230     199.580 156.803 287.731  1.00 77.25           C  
ATOM   3347  CD2 PHE D 230     199.105 157.720 289.876  1.00 77.25           C  
ATOM   3348  CE1 PHE D 230     199.803 155.576 288.298  1.00 77.25           C  
ATOM   3349  CE2 PHE D 230     199.329 156.491 290.452  1.00 77.25           C  
ATOM   3350  CZ  PHE D 230     199.679 155.417 289.660  1.00 77.25           C  
ATOM   3351  N   GLU D 231     195.833 160.049 288.356  1.00 82.02           N  
ATOM   3352  CA  GLU D 231     194.625 159.922 289.158  1.00 82.02           C  
ATOM   3353  C   GLU D 231     193.521 159.236 288.376  1.00 82.02           C  
ATOM   3354  O   GLU D 231     192.671 158.561 288.966  1.00 82.02           O  
ATOM   3355  CB  GLU D 231     194.167 161.296 289.639  1.00 82.02           C  
ATOM   3356  CG  GLU D 231     194.706 161.666 290.999  1.00 82.02           C  
ATOM   3357  CD  GLU D 231     194.333 160.652 292.056  1.00 82.02           C  
ATOM   3358  OE1 GLU D 231     193.132 160.543 292.377  1.00 82.02           O  
ATOM   3359  OE2 GLU D 231     195.240 159.960 292.563  1.00 82.02           O  
ATOM   3360  N   GLU D 232     193.509 159.397 287.056  1.00 80.30           N  
ATOM   3361  CA  GLU D 232     192.540 158.660 286.269  1.00 80.30           C  
ATOM   3362  C   GLU D 232     193.109 157.343 285.750  1.00 80.30           C  
ATOM   3363  O   GLU D 232     192.337 156.460 285.362  1.00 80.30           O  
ATOM   3364  CB  GLU D 232     192.029 159.548 285.134  1.00 80.30           C  
ATOM   3365  CG  GLU D 232     190.697 159.127 284.540  1.00 80.30           C  
ATOM   3366  CD  GLU D 232     190.081 160.205 283.672  1.00 80.30           C  
ATOM   3367  OE1 GLU D 232     190.696 161.284 283.534  1.00 80.30           O  
ATOM   3368  OE2 GLU D 232     188.976 159.975 283.137  1.00 80.30           O  
ATOM   3369  N   ILE D 233     194.438 157.189 285.746  1.00 76.14           N  
ATOM   3370  CA  ILE D 233     195.047 155.882 285.492  1.00 76.14           C  
ATOM   3371  C   ILE D 233     194.699 154.908 286.606  1.00 76.14           C  
ATOM   3372  O   ILE D 233     194.386 153.737 286.352  1.00 76.14           O  
ATOM   3373  CB  ILE D 233     196.572 156.032 285.311  1.00 76.14           C  
ATOM   3374  CG1 ILE D 233     196.887 156.499 283.901  1.00 76.14           C  
ATOM   3375  CG2 ILE D 233     197.331 154.740 285.593  1.00 76.14           C  
ATOM   3376  CD1 ILE D 233     196.476 155.491 282.871  1.00 76.14           C  
ATOM   3377  N   LYS D 234     194.688 155.404 287.843  1.00 80.10           N  
ATOM   3378  CA  LYS D 234     194.682 154.559 289.036  1.00 80.10           C  
ATOM   3379  C   LYS D 234     193.522 153.567 289.182  1.00 80.10           C  
ATOM   3380  O   LYS D 234     193.780 152.475 289.714  1.00 80.10           O  
ATOM   3381  CB  LYS D 234     194.780 155.462 290.273  1.00 80.10           C  
ATOM   3382  CG  LYS D 234     195.453 154.814 291.464  1.00 80.10           C  
ATOM   3383  CD  LYS D 234     195.334 155.684 292.701  1.00 80.10           C  
ATOM   3384  CE  LYS D 234     195.800 154.940 293.940  1.00 80.10           C  
ATOM   3385  NZ  LYS D 234     195.402 155.639 295.191  1.00 80.10           N  
ATOM   3386  N   PRO D 235     192.258 153.858 288.812  1.00 79.07           N  
ATOM   3387  CA  PRO D 235     191.246 152.790 288.932  1.00 79.07           C  
ATOM   3388  C   PRO D 235     191.471 151.604 288.009  1.00 79.07           C  
ATOM   3389  O   PRO D 235     191.433 150.461 288.490  1.00 79.07           O  
ATOM   3390  CB  PRO D 235     189.936 153.513 288.601  1.00 79.07           C  
ATOM   3391  CG  PRO D 235     190.176 154.886 288.991  1.00 79.07           C  
ATOM   3392  CD  PRO D 235     191.585 155.155 288.590  1.00 79.07           C  
ATOM   3393  N   LEU D 236     191.815 151.850 286.735  1.00 76.07           N  
ATOM   3394  CA  LEU D 236     192.066 150.767 285.784  1.00 76.07           C  
ATOM   3395  C   LEU D 236     193.230 149.900 286.214  1.00 76.07           C  
ATOM   3396  O   LEU D 236     193.092 148.669 286.292  1.00 76.07           O  
ATOM   3397  CB  LEU D 236     192.359 151.344 284.400  1.00 76.07           C  
ATOM   3398  CG  LEU D 236     192.888 150.390 283.319  1.00 76.07           C  
ATOM   3399  CD1 LEU D 236     191.947 149.249 282.993  1.00 76.07           C  
ATOM   3400  CD2 LEU D 236     193.246 151.159 282.061  1.00 76.07           C  
ATOM   3401  N   TYR D 237     194.303 150.542 286.679  1.00 78.91           N  
ATOM   3402  CA  TYR D 237     195.466 149.818 287.161  1.00 78.91           C  
ATOM   3403  C   TYR D 237     195.126 149.000 288.389  1.00 78.91           C  
ATOM   3404  O   TYR D 237     195.541 147.836 288.477  1.00 78.91           O  
ATOM   3405  CB  TYR D 237     196.590 150.795 287.482  1.00 78.91           C  
ATOM   3406  CG  TYR D 237     197.787 150.137 288.109  1.00 78.91           C  
ATOM   3407  CD1 TYR D 237     198.585 149.261 287.391  1.00 78.91           C  
ATOM   3408  CD2 TYR D 237     198.093 150.363 289.441  1.00 78.91           C  
ATOM   3409  CE1 TYR D 237     199.671 148.651 287.977  1.00 78.91           C  
ATOM   3410  CE2 TYR D 237     199.169 149.759 290.033  1.00 78.91           C  
ATOM   3411  CZ  TYR D 237     199.956 148.906 289.299  1.00 78.91           C  
ATOM   3412  OH  TYR D 237     201.034 148.307 289.900  1.00 78.91           O  
ATOM   3413  N   GLU D 238     194.233 149.529 289.241  1.00 83.93           N  
ATOM   3414  CA  GLU D 238     193.835 148.806 290.442  1.00 83.93           C  
ATOM   3415  C   GLU D 238     193.133 147.515 290.078  1.00 83.93           C  
ATOM   3416  O   GLU D 238     193.500 146.448 290.592  1.00 83.93           O  
ATOM   3417  CB  GLU D 238     192.932 149.669 291.319  1.00 83.93           C  
ATOM   3418  CG  GLU D 238     193.674 150.504 292.339  1.00 83.93           C  
ATOM   3419  CD  GLU D 238     192.776 151.502 293.036  1.00 83.93           C  
ATOM   3420  OE1 GLU D 238     191.679 151.784 292.510  1.00 83.93           O  
ATOM   3421  OE2 GLU D 238     193.167 152.009 294.108  1.00 83.93           O  
ATOM   3422  N   HIS D 239     192.243 147.575 289.076  1.00 82.60           N  
ATOM   3423  CA  HIS D 239     191.548 146.369 288.653  1.00 82.60           C  
ATOM   3424  C   HIS D 239     192.524 145.386 288.043  1.00 82.60           C  
ATOM   3425  O   HIS D 239     192.525 144.204 288.419  1.00 82.60           O  
ATOM   3426  CB  HIS D 239     190.426 146.713 287.683  1.00 82.60           C  
ATOM   3427  CG  HIS D 239     189.194 147.219 288.358  1.00 82.60           C  
ATOM   3428  ND1 HIS D 239     188.359 146.400 289.085  1.00 82.60           N  
ATOM   3429  CD2 HIS D 239     188.665 148.461 288.438  1.00 82.60           C  
ATOM   3430  CE1 HIS D 239     187.361 147.113 289.573  1.00 82.60           C  
ATOM   3431  NE2 HIS D 239     187.523 148.368 289.194  1.00 82.60           N  
ATOM   3432  N   LEU D 240     193.465 145.902 287.239  1.00 81.21           N  
ATOM   3433  CA  LEU D 240     194.470 145.042 286.636  1.00 81.21           C  
ATOM   3434  C   LEU D 240     195.356 144.441 287.707  1.00 81.21           C  
ATOM   3435  O   LEU D 240     195.587 143.221 287.703  1.00 81.21           O  
ATOM   3436  CB  LEU D 240     195.293 145.837 285.627  1.00 81.21           C  
ATOM   3437  CG  LEU D 240     196.511 145.145 285.028  1.00 81.21           C  
ATOM   3438  CD1 LEU D 240     196.076 144.135 284.003  1.00 81.21           C  
ATOM   3439  CD2 LEU D 240     197.424 146.171 284.401  1.00 81.21           C  
ATOM   3440  N   HIS D 241     195.666 145.244 288.736  1.00 87.25           N  
ATOM   3441  CA  HIS D 241     196.494 144.770 289.834  1.00 87.25           C  
ATOM   3442  C   HIS D 241     195.791 143.663 290.586  1.00 87.25           C  
ATOM   3443  O   HIS D 241     196.373 142.585 290.782  1.00 87.25           O  
ATOM   3444  CB  HIS D 241     196.812 145.931 290.776  1.00 87.25           C  
ATOM   3445  CG  HIS D 241     197.730 145.578 291.900  1.00 87.25           C  
ATOM   3446  ND1 HIS D 241     197.280 145.375 293.186  1.00 87.25           N  
ATOM   3447  CD2 HIS D 241     199.074 145.431 291.945  1.00 87.25           C  
ATOM   3448  CE1 HIS D 241     198.304 145.095 293.970  1.00 87.25           C  
ATOM   3449  NE2 HIS D 241     199.405 145.125 293.242  1.00 87.25           N  
ATOM   3450  N   ALA D 242     194.478 143.838 290.805  1.00 87.84           N  
ATOM   3451  CA  ALA D 242     193.704 142.832 291.518  1.00 87.84           C  
ATOM   3452  C   ALA D 242     193.654 141.541 290.732  1.00 87.84           C  
ATOM   3453  O   ALA D 242     193.945 140.469 291.285  1.00 87.84           O  
ATOM   3454  CB  ALA D 242     192.295 143.349 291.797  1.00 87.84           C  
ATOM   3455  N   TYR D 243     193.484 141.656 289.408  1.00 88.98           N  
ATOM   3456  CA  TYR D 243     193.420 140.464 288.579  1.00 88.98           C  
ATOM   3457  C   TYR D 243     194.753 139.751 288.562  1.00 88.98           C  
ATOM   3458  O   TYR D 243     194.803 138.530 288.775  1.00 88.98           O  
ATOM   3459  CB  TYR D 243     193.000 140.829 287.162  1.00 88.98           C  
ATOM   3460  CG  TYR D 243     192.941 139.647 286.231  1.00 88.98           C  
ATOM   3461  CD1 TYR D 243     191.924 138.711 286.337  1.00 88.98           C  
ATOM   3462  CD2 TYR D 243     193.905 139.462 285.251  1.00 88.98           C  
ATOM   3463  CE1 TYR D 243     191.867 137.624 285.492  1.00 88.98           C  
ATOM   3464  CE2 TYR D 243     193.857 138.379 284.406  1.00 88.98           C  
ATOM   3465  CZ  TYR D 243     192.837 137.466 284.528  1.00 88.98           C  
ATOM   3466  OH  TYR D 243     192.786 136.386 283.683  1.00 88.98           O  
ATOM   3467  N   VAL D 244     195.841 140.528 288.476  1.00 89.46           N  
ATOM   3468  CA  VAL D 244     197.172 139.937 288.469  1.00 89.46           C  
ATOM   3469  C   VAL D 244     197.445 139.265 289.798  1.00 89.46           C  
ATOM   3470  O   VAL D 244     197.901 138.111 289.835  1.00 89.46           O  
ATOM   3471  CB  VAL D 244     198.221 141.010 288.126  1.00 89.46           C  
ATOM   3472  CG1 VAL D 244     199.609 140.584 288.555  1.00 89.46           C  
ATOM   3473  CG2 VAL D 244     198.195 141.295 286.642  1.00 89.46           C  
ATOM   3474  N   ARG D 245     196.975 139.893 290.886  1.00 96.57           N  
ATOM   3475  CA  ARG D 245     197.160 139.325 292.212  1.00 96.57           C  
ATOM   3476  C   ARG D 245     196.422 138.008 292.344  1.00 96.57           C  
ATOM   3477  O   ARG D 245     197.014 137.011 292.784  1.00 96.57           O  
ATOM   3478  CB  ARG D 245     196.693 140.328 293.263  1.00 96.57           C  
ATOM   3479  CG  ARG D 245     196.934 139.926 294.695  1.00 96.57           C  
ATOM   3480  CD  ARG D 245     195.804 140.443 295.556  1.00 96.57           C  
ATOM   3481  NE  ARG D 245     195.922 141.877 295.787  1.00 96.57           N  
ATOM   3482  CZ  ARG D 245     194.892 142.697 295.929  1.00 96.57           C  
ATOM   3483  NH1 ARG D 245     193.647 142.259 295.862  1.00 96.57           N  
ATOM   3484  NH2 ARG D 245     195.116 143.990 296.136  1.00 96.57           N  
ATOM   3485  N   ALA D 246     195.204 137.946 291.783  1.00 97.98           N  
ATOM   3486  CA  ALA D 246     194.427 136.714 291.822  1.00 97.98           C  
ATOM   3487  C   ALA D 246     195.125 135.617 291.042  1.00 97.98           C  
ATOM   3488  O   ALA D 246     195.281 134.495 291.543  1.00 97.98           O  
ATOM   3489  CB  ALA D 246     193.022 136.958 291.275  1.00 97.98           C  
ATOM   3490  N   LYS D 247     195.674 135.967 289.876  1.00 98.86           N  
ATOM   3491  CA  LYS D 247     196.350 134.960 289.079  1.00 98.86           C  
ATOM   3492  C   LYS D 247     197.661 134.551 289.722  1.00 98.86           C  
ATOM   3493  O   LYS D 247     198.024 133.369 289.680  1.00 98.86           O  
ATOM   3494  CB  LYS D 247     196.557 135.464 287.659  1.00 98.86           C  
ATOM   3495  CG  LYS D 247     195.303 135.386 286.816  1.00 98.86           C  
ATOM   3496  CD  LYS D 247     194.855 133.949 286.657  1.00 98.86           C  
ATOM   3497  CE  LYS D 247     193.684 133.838 285.706  1.00 98.86           C  
ATOM   3498  NZ  LYS D 247     193.291 132.419 285.496  1.00 98.86           N  
ATOM   3499  N   LEU D 248     198.326 135.485 290.410  1.00104.54           N  
ATOM   3500  CA  LEU D 248     199.537 135.099 291.114  1.00104.54           C  
ATOM   3501  C   LEU D 248     199.213 134.264 292.337  1.00104.54           C  
ATOM   3502  O   LEU D 248     200.038 133.436 292.741  1.00104.54           O  
ATOM   3503  CB  LEU D 248     200.360 136.329 291.484  1.00104.54           C  
ATOM   3504  CG  LEU D 248     201.031 137.025 290.299  1.00104.54           C  
ATOM   3505  CD1 LEU D 248     201.759 138.276 290.749  1.00104.54           C  
ATOM   3506  CD2 LEU D 248     201.979 136.076 289.590  1.00104.54           C  
ATOM   3507  N   MET D 249     197.998 134.414 292.874  1.00111.70           N  
ATOM   3508  CA  MET D 249     197.525 133.507 293.910  1.00111.70           C  
ATOM   3509  C   MET D 249     197.404 132.090 293.370  1.00111.70           C  
ATOM   3510  O   MET D 249     197.657 131.119 294.093  1.00111.70           O  
ATOM   3511  CB  MET D 249     196.190 134.000 294.449  1.00111.70           C  
ATOM   3512  CG  MET D 249     195.955 133.670 295.893  1.00111.70           C  
ATOM   3513  SD  MET D 249     194.422 134.428 296.425  1.00111.70           S  
ATOM   3514  CE  MET D 249     195.109 135.835 297.277  1.00111.70           C  
ATOM   3515  N   ASN D 250     196.985 131.954 292.109  1.00109.80           N  
ATOM   3516  CA  ASN D 250     197.041 130.653 291.454  1.00109.80           C  
ATOM   3517  C   ASN D 250     198.478 130.173 291.292  1.00109.80           C  
ATOM   3518  O   ASN D 250     198.754 128.974 291.416  1.00109.80           O  
ATOM   3519  CB  ASN D 250     196.337 130.714 290.100  1.00109.80           C  
ATOM   3520  CG  ASN D 250     194.836 130.842 290.235  1.00109.80           C  
ATOM   3521  OD1 ASN D 250     194.213 131.693 289.600  1.00109.80           O  
ATOM   3522  ND2 ASN D 250     194.244 130.001 291.074  1.00109.80           N  
ATOM   3523  N   ALA D 251     199.409 131.090 291.015  1.00113.87           N  
ATOM   3524  CA  ALA D 251     200.808 130.691 290.892  1.00113.87           C  
ATOM   3525  C   ALA D 251     201.429 130.390 292.251  1.00113.87           C  
ATOM   3526  O   ALA D 251     202.081 129.356 292.431  1.00113.87           O  
ATOM   3527  CB  ALA D 251     201.599 131.777 290.166  1.00113.87           C  
ATOM   3528  N   TYR D 252     201.241 131.280 293.214  1.00118.75           N  
ATOM   3529  CA  TYR D 252     201.835 131.122 294.540  1.00118.75           C  
ATOM   3530  C   TYR D 252     200.723 131.054 295.574  1.00118.75           C  
ATOM   3531  O   TYR D 252     200.037 132.068 295.805  1.00118.75           O  
ATOM   3532  CB  TYR D 252     202.788 132.279 294.833  1.00118.75           C  
ATOM   3533  CG  TYR D 252     203.823 132.465 293.746  1.00118.75           C  
ATOM   3534  CD1 TYR D 252     204.965 131.676 293.703  1.00118.75           C  
ATOM   3535  CD2 TYR D 252     203.648 133.422 292.753  1.00118.75           C  
ATOM   3536  CE1 TYR D 252     205.908 131.843 292.705  1.00118.75           C  
ATOM   3537  CE2 TYR D 252     204.582 133.593 291.753  1.00118.75           C  
ATOM   3538  CZ  TYR D 252     205.708 132.801 291.733  1.00118.75           C  
ATOM   3539  OH  TYR D 252     206.638 132.976 290.736  1.00118.75           O  
ATOM   3540  N   PRO D 253     200.500 129.905 296.212  1.00121.62           N  
ATOM   3541  CA  PRO D 253     199.247 129.698 296.953  1.00121.62           C  
ATOM   3542  C   PRO D 253     199.160 130.443 298.277  1.00121.62           C  
ATOM   3543  O   PRO D 253     198.147 131.089 298.560  1.00121.62           O  
ATOM   3544  CB  PRO D 253     199.212 128.176 297.164  1.00121.62           C  
ATOM   3545  CG  PRO D 253     200.543 127.639 296.663  1.00121.62           C  
ATOM   3546  CD  PRO D 253     201.443 128.793 296.392  1.00121.62           C  
ATOM   3547  N   SER D 254     200.210 130.367 299.095  1.00122.86           N  
ATOM   3548  CA  SER D 254     200.155 130.841 300.469  1.00122.86           C  
ATOM   3549  C   SER D 254     200.908 132.140 300.701  1.00122.86           C  
ATOM   3550  O   SER D 254     200.674 132.797 301.719  1.00122.86           O  
ATOM   3551  CB  SER D 254     200.715 129.776 301.422  1.00122.86           C  
ATOM   3552  OG  SER D 254     202.090 129.549 301.169  1.00122.86           O  
ATOM   3553  N   TYR D 255     201.804 132.516 299.794  1.00124.17           N  
ATOM   3554  CA  TYR D 255     202.730 133.611 300.054  1.00124.17           C  
ATOM   3555  C   TYR D 255     202.105 134.982 299.824  1.00124.17           C  
ATOM   3556  O   TYR D 255     202.530 135.960 300.448  1.00124.17           O  
ATOM   3557  CB  TYR D 255     203.976 133.432 299.187  1.00124.17           C  
ATOM   3558  CG  TYR D 255     204.845 132.252 299.583  1.00124.17           C  
ATOM   3559  CD1 TYR D 255     204.704 131.629 300.822  1.00124.17           C  
ATOM   3560  CD2 TYR D 255     205.778 131.736 298.701  1.00124.17           C  
ATOM   3561  CE1 TYR D 255     205.490 130.548 301.173  1.00124.17           C  
ATOM   3562  CE2 TYR D 255     206.571 130.659 299.042  1.00124.17           C  
ATOM   3563  CZ  TYR D 255     206.422 130.067 300.278  1.00124.17           C  
ATOM   3564  OH  TYR D 255     207.209 128.991 300.617  1.00124.17           O  
ATOM   3565  N   ILE D 256     201.120 135.082 298.940  1.00118.52           N  
ATOM   3566  CA  ILE D 256     200.482 136.350 298.603  1.00118.52           C  
ATOM   3567  C   ILE D 256     199.163 136.472 299.352  1.00118.52           C  
ATOM   3568  O   ILE D 256     198.375 135.520 299.408  1.00118.52           O  
ATOM   3569  CB  ILE D 256     200.285 136.466 297.082  1.00118.52           C  
ATOM   3570  CG1 ILE D 256     201.592 136.109 296.382  1.00118.52           C  
ATOM   3571  CG2 ILE D 256     199.854 137.866 296.694  1.00118.52           C  
ATOM   3572  CD1 ILE D 256     201.433 135.778 294.943  1.00118.52           C  
ATOM   3573  N   SER D 257     198.919 137.650 299.928  1.00115.95           N  
ATOM   3574  CA  SER D 257     197.724 137.970 300.700  1.00115.95           C  
ATOM   3575  C   SER D 257     196.654 138.590 299.805  1.00115.95           C  
ATOM   3576  O   SER D 257     196.981 139.321 298.866  1.00115.95           O  
ATOM   3577  CB  SER D 257     198.062 138.937 301.829  1.00115.95           C  
ATOM   3578  OG  SER D 257     196.896 139.358 302.515  1.00115.95           O  
ATOM   3579  N   PRO D 258     195.378 138.284 300.069  1.00112.45           N  
ATOM   3580  CA  PRO D 258     194.298 138.908 299.286  1.00112.45           C  
ATOM   3581  C   PRO D 258     194.179 140.405 299.495  1.00112.45           C  
ATOM   3582  O   PRO D 258     193.780 141.120 298.569  1.00112.45           O  
ATOM   3583  CB  PRO D 258     193.041 138.188 299.794  1.00112.45           C  
ATOM   3584  CG  PRO D 258     193.532 136.916 300.384  1.00112.45           C  
ATOM   3585  CD  PRO D 258     194.860 137.253 300.984  1.00112.45           C  
ATOM   3586  N   ILE D 259     194.524 140.900 300.685  1.00112.24           N  
ATOM   3587  CA  ILE D 259     194.357 142.313 301.012  1.00112.24           C  
ATOM   3588  C   ILE D 259     195.617 143.133 300.772  1.00112.24           C  
ATOM   3589  O   ILE D 259     195.547 144.372 300.760  1.00112.24           O  
ATOM   3590  CB  ILE D 259     193.887 142.432 302.480  1.00112.24           C  
ATOM   3591  CG1 ILE D 259     193.001 143.661 302.686  1.00112.24           C  
ATOM   3592  CG2 ILE D 259     195.068 142.430 303.450  1.00112.24           C  
ATOM   3593  CD1 ILE D 259     191.645 143.535 302.048  1.00112.24           C  
ATOM   3594  N   GLY D 260     196.760 142.489 300.542  1.00110.46           N  
ATOM   3595  CA  GLY D 260     198.035 143.167 300.499  1.00110.46           C  
ATOM   3596  C   GLY D 260     198.532 143.418 299.088  1.00110.46           C  
ATOM   3597  O   GLY D 260     197.825 143.240 298.095  1.00110.46           O  
ATOM   3598  N   CYS D 261     199.785 143.851 299.013  1.00107.89           N  
ATOM   3599  CA  CYS D 261     200.398 144.216 297.752  1.00107.89           C  
ATOM   3600  C   CYS D 261     201.071 142.997 297.131  1.00107.89           C  
ATOM   3601  O   CYS D 261     201.119 141.914 297.717  1.00107.89           O  
ATOM   3602  CB  CYS D 261     201.413 145.337 297.964  1.00107.89           C  
ATOM   3603  SG  CYS D 261     200.722 146.908 298.508  1.00107.89           S  
ATOM   3604  N   LEU D 262     201.580 143.167 295.930  1.00102.44           N  
ATOM   3605  CA  LEU D 262     202.311 142.081 295.303  1.00102.44           C  
ATOM   3606  C   LEU D 262     203.719 141.997 295.887  1.00102.44           C  
ATOM   3607  O   LEU D 262     204.328 143.030 296.176  1.00102.44           O  
ATOM   3608  CB  LEU D 262     202.384 142.287 293.796  1.00102.44           C  
ATOM   3609  CG  LEU D 262     201.041 142.141 293.085  1.00102.44           C  
ATOM   3610  CD1 LEU D 262     201.157 142.494 291.613  1.00102.44           C  
ATOM   3611  CD2 LEU D 262     200.503 140.742 293.270  1.00102.44           C  
ATOM   3612  N   PRO D 263     204.244 140.791 296.101  1.00109.50           N  
ATOM   3613  CA  PRO D 263     205.674 140.661 296.401  1.00109.50           C  
ATOM   3614  C   PRO D 263     206.499 141.104 295.205  1.00109.50           C  
ATOM   3615  O   PRO D 263     206.130 140.861 294.057  1.00109.50           O  
ATOM   3616  CB  PRO D 263     205.844 139.166 296.689  1.00109.50           C  
ATOM   3617  CG  PRO D 263     204.473 138.687 297.030  1.00109.50           C  
ATOM   3618  CD  PRO D 263     203.547 139.500 296.187  1.00109.50           C  
ATOM   3619  N   ALA D 264     207.646 141.724 295.489  1.00112.74           N  
ATOM   3620  CA  ALA D 264     208.349 142.506 294.476  1.00112.74           C  
ATOM   3621  C   ALA D 264     209.060 141.642 293.447  1.00112.74           C  
ATOM   3622  O   ALA D 264     209.196 142.051 292.289  1.00112.74           O  
ATOM   3623  CB  ALA D 264     209.344 143.448 295.146  1.00112.74           C  
ATOM   3624  N   HIS D 265     209.524 140.462 293.839  1.00119.12           N  
ATOM   3625  CA  HIS D 265     210.286 139.600 292.951  1.00119.12           C  
ATOM   3626  C   HIS D 265     209.404 138.661 292.144  1.00119.12           C  
ATOM   3627  O   HIS D 265     209.897 137.652 291.630  1.00119.12           O  
ATOM   3628  CB  HIS D 265     211.289 138.788 293.765  1.00119.12           C  
ATOM   3629  CG  HIS D 265     210.648 137.901 294.783  1.00119.12           C  
ATOM   3630  ND1 HIS D 265     210.127 138.380 295.965  1.00119.12           N  
ATOM   3631  CD2 HIS D 265     210.442 136.565 294.795  1.00119.12           C  
ATOM   3632  CE1 HIS D 265     209.620 137.377 296.658  1.00119.12           C  
ATOM   3633  NE2 HIS D 265     209.806 136.264 295.974  1.00119.12           N  
ATOM   3634  N   LEU D 266     208.112 138.964 292.023  1.00113.88           N  
ATOM   3635  CA  LEU D 266     207.192 138.128 291.265  1.00113.88           C  
ATOM   3636  C   LEU D 266     206.607 138.869 290.072  1.00113.88           C  
ATOM   3637  O   LEU D 266     205.606 138.427 289.503  1.00113.88           O  
ATOM   3638  CB  LEU D 266     206.071 137.630 292.176  1.00113.88           C  
ATOM   3639  CG  LEU D 266     206.536 136.809 293.377  1.00113.88           C  
ATOM   3640  CD1 LEU D 266     205.351 136.337 294.198  1.00113.88           C  
ATOM   3641  CD2 LEU D 266     207.408 135.646 292.945  1.00113.88           C  
ATOM   3642  N   LEU D 267     207.214 139.982 289.673  1.00105.62           N  
ATOM   3643  CA  LEU D 267     206.640 140.838 288.646  1.00105.62           C  
ATOM   3644  C   LEU D 267     207.146 140.523 287.248  1.00105.62           C  
ATOM   3645  O   LEU D 267     206.825 141.259 286.311  1.00105.62           O  
ATOM   3646  CB  LEU D 267     206.898 142.314 288.952  1.00105.62           C  
ATOM   3647  CG  LEU D 267     205.990 143.074 289.929  1.00105.62           C  
ATOM   3648  CD1 LEU D 267     204.572 143.092 289.423  1.00105.62           C  
ATOM   3649  CD2 LEU D 267     206.037 142.608 291.352  1.00105.62           C  
ATOM   3650  N   GLY D 268     207.942 139.473 287.079  1.00109.42           N  
ATOM   3651  CA  GLY D 268     208.350 139.030 285.767  1.00109.42           C  
ATOM   3652  C   GLY D 268     209.584 139.709 285.216  1.00109.42           C  
ATOM   3653  O   GLY D 268     210.168 139.211 284.250  1.00109.42           O  
ATOM   3654  N   ASP D 269     209.985 140.835 285.785  1.00107.51           N  
ATOM   3655  CA  ASP D 269     211.233 141.501 285.454  1.00107.51           C  
ATOM   3656  C   ASP D 269     212.074 141.634 286.713  1.00107.51           C  
ATOM   3657  O   ASP D 269     211.685 141.196 287.798  1.00107.51           O  
ATOM   3658  CB  ASP D 269     210.992 142.873 284.823  1.00107.51           C  
ATOM   3659  CG  ASP D 269     210.919 142.812 283.318  1.00107.51           C  
ATOM   3660  OD1 ASP D 269     211.525 141.893 282.730  1.00107.51           O  
ATOM   3661  OD2 ASP D 269     210.273 143.693 282.719  1.00107.51           O  
ATOM   3662  N   MET D 270     213.248 142.238 286.550  1.00113.77           N  
ATOM   3663  CA  MET D 270     214.127 142.444 287.691  1.00113.77           C  
ATOM   3664  C   MET D 270     213.567 143.501 288.631  1.00113.77           C  
ATOM   3665  O   MET D 270     213.734 143.404 289.852  1.00113.77           O  
ATOM   3666  CB  MET D 270     215.520 142.840 287.200  1.00113.77           C  
ATOM   3667  CG  MET D 270     216.527 142.900 288.305  1.00113.77           C  
ATOM   3668  SD  MET D 270     216.734 141.238 288.931  1.00113.77           S  
ATOM   3669  CE  MET D 270     217.280 141.598 290.573  1.00113.77           C  
ATOM   3670  N   TRP D 271     212.857 144.483 288.085  1.00105.36           N  
ATOM   3671  CA  TRP D 271     212.440 145.656 288.829  1.00105.36           C  
ATOM   3672  C   TRP D 271     210.935 145.842 288.883  1.00105.36           C  
ATOM   3673  O   TRP D 271     210.464 146.675 289.664  1.00105.36           O  
ATOM   3674  CB  TRP D 271     213.071 146.915 288.220  1.00105.36           C  
ATOM   3675  CG  TRP D 271     214.500 146.723 287.861  1.00105.36           C  
ATOM   3676  CD1 TRP D 271     215.575 146.847 288.686  1.00105.36           C  
ATOM   3677  CD2 TRP D 271     215.016 146.329 286.585  1.00105.36           C  
ATOM   3678  NE1 TRP D 271     216.731 146.576 288.000  1.00105.36           N  
ATOM   3679  CE2 TRP D 271     216.414 146.254 286.707  1.00105.36           C  
ATOM   3680  CE3 TRP D 271     214.430 146.040 285.351  1.00105.36           C  
ATOM   3681  CZ2 TRP D 271     217.236 145.906 285.642  1.00105.36           C  
ATOM   3682  CZ3 TRP D 271     215.249 145.697 284.294  1.00105.36           C  
ATOM   3683  CH2 TRP D 271     216.636 145.632 284.447  1.00105.36           C  
ATOM   3684  N   GLY D 272     210.170 145.092 288.101  1.00 92.96           N  
ATOM   3685  CA  GLY D 272     208.751 145.338 288.008  1.00 92.96           C  
ATOM   3686  C   GLY D 272     208.375 146.392 287.000  1.00 92.96           C  
ATOM   3687  O   GLY D 272     207.263 146.924 287.070  1.00 92.96           O  
ATOM   3688  N   ARG D 273     209.277 146.722 286.074  1.00 85.55           N  
ATOM   3689  CA  ARG D 273     208.992 147.750 285.081  1.00 85.55           C  
ATOM   3690  C   ARG D 273     207.942 147.284 284.087  1.00 85.55           C  
ATOM   3691  O   ARG D 273     206.991 148.011 283.796  1.00 85.55           O  
ATOM   3692  CB  ARG D 273     210.285 148.153 284.373  1.00 85.55           C  
ATOM   3693  CG  ARG D 273     210.109 148.993 283.122  1.00 85.55           C  
ATOM   3694  CD  ARG D 273     211.464 149.338 282.533  1.00 85.55           C  
ATOM   3695  NE  ARG D 273     211.406 149.660 281.112  1.00 85.55           N  
ATOM   3696  CZ  ARG D 273     211.153 150.858 280.607  1.00 85.55           C  
ATOM   3697  NH1 ARG D 273     210.871 151.888 281.380  1.00 85.55           N  
ATOM   3698  NH2 ARG D 273     211.178 151.024 279.288  1.00 85.55           N  
ATOM   3699  N   PHE D 274     208.076 146.072 283.571  1.00 86.87           N  
ATOM   3700  CA  PHE D 274     207.088 145.526 282.659  1.00 86.87           C  
ATOM   3701  C   PHE D 274     206.457 144.288 283.272  1.00 86.87           C  
ATOM   3702  O   PHE D 274     207.113 143.524 283.983  1.00 86.87           O  
ATOM   3703  CB  PHE D 274     207.697 145.183 281.304  1.00 86.87           C  
ATOM   3704  CG  PHE D 274     208.104 146.380 280.509  1.00 86.87           C  
ATOM   3705  CD1 PHE D 274     207.208 147.407 280.277  1.00 86.87           C  
ATOM   3706  CD2 PHE D 274     209.379 146.474 279.983  1.00 86.87           C  
ATOM   3707  CE1 PHE D 274     207.579 148.512 279.538  1.00 86.87           C  
ATOM   3708  CE2 PHE D 274     209.754 147.574 279.240  1.00 86.87           C  
ATOM   3709  CZ  PHE D 274     208.854 148.595 279.021  1.00 86.87           C  
ATOM   3710  N   TRP D 275     205.171 144.099 282.998  1.00 84.05           N  
ATOM   3711  CA  TRP D 275     204.448 142.934 283.483  1.00 84.05           C  
ATOM   3712  C   TRP D 275     204.191 141.936 282.369  1.00 84.05           C  
ATOM   3713  O   TRP D 275     203.411 140.998 282.557  1.00 84.05           O  
ATOM   3714  CB  TRP D 275     203.119 143.329 284.127  1.00 84.05           C  
ATOM   3715  CG  TRP D 275     203.196 144.126 285.389  1.00 84.05           C  
ATOM   3716  CD1 TRP D 275     204.283 144.761 285.905  1.00 84.05           C  
ATOM   3717  CD2 TRP D 275     202.128 144.351 286.312  1.00 84.05           C  
ATOM   3718  NE1 TRP D 275     203.955 145.386 287.078  1.00 84.05           N  
ATOM   3719  CE2 TRP D 275     202.636 145.143 287.353  1.00 84.05           C  
ATOM   3720  CE3 TRP D 275     200.787 143.965 286.352  1.00 84.05           C  
ATOM   3721  CZ2 TRP D 275     201.856 145.549 288.426  1.00 84.05           C  
ATOM   3722  CZ3 TRP D 275     200.015 144.372 287.415  1.00 84.05           C  
ATOM   3723  CH2 TRP D 275     200.550 145.156 288.438  1.00 84.05           C  
ATOM   3724  N   THR D 276     204.831 142.116 281.212  1.00 86.85           N  
ATOM   3725  CA  THR D 276     204.511 141.337 280.025  1.00 86.85           C  
ATOM   3726  C   THR D 276     205.000 139.898 280.107  1.00 86.85           C  
ATOM   3727  O   THR D 276     204.608 139.084 279.266  1.00 86.85           O  
ATOM   3728  CB  THR D 276     205.100 142.012 278.788  1.00 86.85           C  
ATOM   3729  OG1 THR D 276     204.710 141.287 277.616  1.00 86.85           O  
ATOM   3730  CG2 THR D 276     206.612 142.054 278.873  1.00 86.85           C  
ATOM   3731  N   ASN D 277     205.828 139.563 281.093  1.00 93.96           N  
ATOM   3732  CA  ASN D 277     206.280 138.195 281.284  1.00 93.96           C  
ATOM   3733  C   ASN D 277     205.279 137.355 282.059  1.00 93.96           C  
ATOM   3734  O   ASN D 277     205.537 136.170 282.291  1.00 93.96           O  
ATOM   3735  CB  ASN D 277     207.632 138.181 281.996  1.00 93.96           C  
ATOM   3736  CG  ASN D 277     208.753 138.693 281.118  1.00 93.96           C  
ATOM   3737  OD1 ASN D 277     208.810 138.390 279.927  1.00 93.96           O  
ATOM   3738  ND2 ASN D 277     209.650 139.477 281.700  1.00 93.96           N  
ATOM   3739  N   LEU D 278     204.158 137.940 282.472  1.00 91.39           N  
ATOM   3740  CA  LEU D 278     203.126 137.240 283.220  1.00 91.39           C  
ATOM   3741  C   LEU D 278     201.969 136.807 282.345  1.00 91.39           C  
ATOM   3742  O   LEU D 278     200.922 136.441 282.879  1.00 91.39           O  
ATOM   3743  CB  LEU D 278     202.583 138.095 284.366  1.00 91.39           C  
ATOM   3744  CG  LEU D 278     203.306 138.166 285.710  1.00 91.39           C  
ATOM   3745  CD1 LEU D 278     204.558 138.953 285.596  1.00 91.39           C  
ATOM   3746  CD2 LEU D 278     202.406 138.781 286.761  1.00 91.39           C  
ATOM   3747  N   TYR D 279     202.123 136.861 281.019  1.00 93.55           N  
ATOM   3748  CA  TYR D 279     201.021 136.500 280.135  1.00 93.55           C  
ATOM   3749  C   TYR D 279     200.728 135.007 280.244  1.00 93.55           C  
ATOM   3750  O   TYR D 279     199.569 134.595 280.161  1.00 93.55           O  
ATOM   3751  CB  TYR D 279     201.370 136.875 278.691  1.00 93.55           C  
ATOM   3752  CG  TYR D 279     200.245 136.791 277.665  1.00 93.55           C  
ATOM   3753  CD1 TYR D 279     198.907 136.738 278.046  1.00 93.55           C  
ATOM   3754  CD2 TYR D 279     200.535 136.709 276.310  1.00 93.55           C  
ATOM   3755  CE1 TYR D 279     197.898 136.646 277.114  1.00 93.55           C  
ATOM   3756  CE2 TYR D 279     199.527 136.609 275.368  1.00 93.55           C  
ATOM   3757  CZ  TYR D 279     198.212 136.581 275.778  1.00 93.55           C  
ATOM   3758  OH  TYR D 279     197.207 136.485 274.845  1.00 93.55           O  
ATOM   3759  N   SER D 280     201.760 134.193 280.471  1.00 96.53           N  
ATOM   3760  CA  SER D 280     201.551 132.765 280.684  1.00 96.53           C  
ATOM   3761  C   SER D 280     200.795 132.499 281.980  1.00 96.53           C  
ATOM   3762  O   SER D 280     199.924 131.624 282.027  1.00 96.53           O  
ATOM   3763  CB  SER D 280     202.894 132.040 280.689  1.00 96.53           C  
ATOM   3764  OG  SER D 280     203.696 132.474 281.772  1.00 96.53           O  
ATOM   3765  N   LEU D 281     201.106 133.247 283.038  1.00 97.92           N  
ATOM   3766  CA  LEU D 281     200.436 133.030 284.315  1.00 97.92           C  
ATOM   3767  C   LEU D 281     199.063 133.685 284.366  1.00 97.92           C  
ATOM   3768  O   LEU D 281     198.134 133.133 284.965  1.00 97.92           O  
ATOM   3769  CB  LEU D 281     201.297 133.561 285.456  1.00 97.92           C  
ATOM   3770  CG  LEU D 281     202.589 132.801 285.709  1.00 97.92           C  
ATOM   3771  CD1 LEU D 281     203.361 133.468 286.828  1.00 97.92           C  
ATOM   3772  CD2 LEU D 281     202.254 131.363 286.051  1.00 97.92           C  
ATOM   3773  N   THR D 282     198.913 134.857 283.755  1.00 94.83           N  
ATOM   3774  CA  THR D 282     197.704 135.653 283.906  1.00 94.83           C  
ATOM   3775  C   THR D 282     196.844 135.627 282.651  1.00 94.83           C  
ATOM   3776  O   THR D 282     196.181 136.615 282.347  1.00 94.83           O  
ATOM   3777  CB  THR D 282     198.040 137.103 284.247  1.00 94.83           C  
ATOM   3778  OG1 THR D 282     198.775 137.678 283.162  1.00 94.83           O  
ATOM   3779  CG2 THR D 282     198.916 137.173 285.476  1.00 94.83           C  
ATOM   3780  N   VAL D 283     196.859 134.531 281.902  1.00 95.03           N  
ATOM   3781  CA  VAL D 283     196.110 134.508 280.638  1.00 95.03           C  
ATOM   3782  C   VAL D 283     194.615 134.453 280.937  1.00 95.03           C  
ATOM   3783  O   VAL D 283     194.199 133.785 281.903  1.00 95.03           O  
ATOM   3784  CB  VAL D 283     196.575 133.337 279.751  1.00 95.03           C  
ATOM   3785  CG1 VAL D 283     196.295 131.959 280.364  1.00 95.03           C  
ATOM   3786  CG2 VAL D 283     195.996 133.446 278.347  1.00 95.03           C  
ATOM   3787  N   PRO D 284     193.790 135.225 280.237  1.00 92.29           N  
ATOM   3788  CA  PRO D 284     192.342 135.119 280.437  1.00 92.29           C  
ATOM   3789  C   PRO D 284     191.774 133.819 279.909  1.00 92.29           C  
ATOM   3790  O   PRO D 284     191.021 133.125 280.598  1.00 92.29           O  
ATOM   3791  CB  PRO D 284     191.800 136.314 279.646  1.00 92.29           C  
ATOM   3792  CG  PRO D 284     192.914 137.269 279.627  1.00 92.29           C  
ATOM   3793  CD  PRO D 284     194.133 136.426 279.462  1.00 92.29           C  
ATOM   3794  N   PHE D 285     192.143 133.482 278.677  1.00 98.66           N  
ATOM   3795  CA  PHE D 285     191.611 132.320 277.974  1.00 98.66           C  
ATOM   3796  C   PHE D 285     192.794 131.599 277.342  1.00 98.66           C  
ATOM   3797  O   PHE D 285     193.200 131.920 276.223  1.00 98.66           O  
ATOM   3798  CB  PHE D 285     190.579 132.740 276.940  1.00 98.66           C  
ATOM   3799  CG  PHE D 285     189.452 133.545 277.510  1.00 98.66           C  
ATOM   3800  CD1 PHE D 285     188.452 132.935 278.246  1.00 98.66           C  
ATOM   3801  CD2 PHE D 285     189.399 134.914 277.319  1.00 98.66           C  
ATOM   3802  CE1 PHE D 285     187.415 133.677 278.776  1.00 98.66           C  
ATOM   3803  CE2 PHE D 285     188.366 135.661 277.846  1.00 98.66           C  
ATOM   3804  CZ  PHE D 285     187.373 135.041 278.575  1.00 98.66           C  
ATOM   3805  N   GLY D 286     193.351 130.627 278.067  1.00103.60           N  
ATOM   3806  CA  GLY D 286     194.505 129.909 277.564  1.00103.60           C  
ATOM   3807  C   GLY D 286     194.179 128.949 276.443  1.00103.60           C  
ATOM   3808  O   GLY D 286     195.070 128.594 275.666  1.00103.60           O  
ATOM   3809  N   GLN D 287     192.920 128.520 276.344  1.00107.87           N  
ATOM   3810  CA  GLN D 287     192.533 127.599 275.285  1.00107.87           C  
ATOM   3811  C   GLN D 287     192.485 128.290 273.931  1.00107.87           C  
ATOM   3812  O   GLN D 287     192.702 127.643 272.900  1.00107.87           O  
ATOM   3813  CB  GLN D 287     191.181 126.970 275.608  1.00107.87           C  
ATOM   3814  CG  GLN D 287     191.206 126.093 276.840  1.00107.87           C  
ATOM   3815  CD  GLN D 287     192.136 124.911 276.681  1.00107.87           C  
ATOM   3816  OE1 GLN D 287     193.193 124.851 277.307  1.00107.87           O  
ATOM   3817  NE2 GLN D 287     191.750 123.962 275.836  1.00107.87           N  
ATOM   3818  N   LYS D 288     192.194 129.587 273.909  1.00106.19           N  
ATOM   3819  CA  LYS D 288     192.164 130.310 272.650  1.00106.19           C  
ATOM   3820  C   LYS D 288     193.588 130.518 272.139  1.00106.19           C  
ATOM   3821  O   LYS D 288     194.502 130.764 272.932  1.00106.19           O  
ATOM   3822  CB  LYS D 288     191.469 131.665 272.820  1.00106.19           C  
ATOM   3823  CG  LYS D 288     189.933 131.652 272.966  1.00106.19           C  
ATOM   3824  CD  LYS D 288     189.149 130.656 272.093  1.00106.19           C  
ATOM   3825  CE  LYS D 288     189.280 130.906 270.583  1.00106.19           C  
ATOM   3826  NZ  LYS D 288     188.645 129.816 269.789  1.00106.19           N  
ATOM   3827  N   PRO D 289     193.810 130.423 270.832  1.00107.68           N  
ATOM   3828  CA  PRO D 289     195.151 130.662 270.294  1.00107.68           C  
ATOM   3829  C   PRO D 289     195.480 132.146 270.283  1.00107.68           C  
ATOM   3830  O   PRO D 289     194.621 133.011 270.457  1.00107.68           O  
ATOM   3831  CB  PRO D 289     195.065 130.098 268.874  1.00107.68           C  
ATOM   3832  CG  PRO D 289     193.629 130.261 268.512  1.00107.68           C  
ATOM   3833  CD  PRO D 289     192.864 130.004 269.783  1.00107.68           C  
ATOM   3834  N   ASN D 290     196.759 132.433 270.072  1.00108.04           N  
ATOM   3835  CA  ASN D 290     197.213 133.808 269.973  1.00108.04           C  
ATOM   3836  C   ASN D 290     197.188 134.237 268.507  1.00108.04           C  
ATOM   3837  O   ASN D 290     196.745 133.499 267.625  1.00108.04           O  
ATOM   3838  CB  ASN D 290     198.602 133.957 270.586  1.00108.04           C  
ATOM   3839  CG  ASN D 290     198.783 135.282 271.296  1.00108.04           C  
ATOM   3840  OD1 ASN D 290     197.896 136.135 271.275  1.00108.04           O  
ATOM   3841  ND2 ASN D 290     199.932 135.460 271.934  1.00108.04           N  
ATOM   3842  N   ILE D 291     197.662 135.451 268.237  1.00104.30           N  
ATOM   3843  CA  ILE D 291     197.620 135.991 266.884  1.00104.30           C  
ATOM   3844  C   ILE D 291     199.050 135.992 266.351  1.00104.30           C  
ATOM   3845  O   ILE D 291     199.427 136.832 265.528  1.00104.30           O  
ATOM   3846  CB  ILE D 291     196.982 137.393 266.866  1.00104.30           C  
ATOM   3847  CG1 ILE D 291     195.826 137.451 267.862  1.00104.30           C  
ATOM   3848  CG2 ILE D 291     196.349 137.685 265.509  1.00104.30           C  
ATOM   3849  CD1 ILE D 291     195.173 138.819 267.983  1.00104.30           C  
ATOM   3850  N   ASP D 292     199.864 135.057 266.833  1.00102.04           N  
ATOM   3851  CA  ASP D 292     201.244 134.936 266.375  1.00102.04           C  
ATOM   3852  C   ASP D 292     201.294 134.417 264.942  1.00102.04           C  
ATOM   3853  O   ASP D 292     200.759 133.345 264.643  1.00102.04           O  
ATOM   3854  CB  ASP D 292     202.022 134.010 267.303  1.00102.04           C  
ATOM   3855  CG  ASP D 292     203.504 133.983 266.991  1.00102.04           C  
ATOM   3856  OD1 ASP D 292     204.092 135.065 266.792  1.00102.04           O  
ATOM   3857  OD2 ASP D 292     204.081 132.877 266.947  1.00102.04           O  
ATOM   3858  N   VAL D 293     201.930 135.179 264.058  1.00 95.23           N  
ATOM   3859  CA  VAL D 293     201.958 134.868 262.636  1.00 95.23           C  
ATOM   3860  C   VAL D 293     203.354 134.441 262.186  1.00 95.23           C  
ATOM   3861  O   VAL D 293     203.672 134.537 261.007  1.00 95.23           O  
ATOM   3862  CB  VAL D 293     201.440 136.045 261.794  1.00 95.23           C  
ATOM   3863  CG1 VAL D 293     199.965 136.265 262.046  1.00 95.23           C  
ATOM   3864  CG2 VAL D 293     202.223 137.304 262.100  1.00 95.23           C  
ATOM   3865  N   THR D 294     204.183 133.956 263.117  1.00 95.61           N  
ATOM   3866  CA  THR D 294     205.545 133.540 262.789  1.00 95.61           C  
ATOM   3867  C   THR D 294     205.547 132.322 261.871  1.00 95.61           C  
ATOM   3868  O   THR D 294     206.370 132.227 260.946  1.00 95.61           O  
ATOM   3869  CB  THR D 294     206.304 133.251 264.085  1.00 95.61           C  
ATOM   3870  OG1 THR D 294     206.277 134.416 264.918  1.00 95.61           O  
ATOM   3871  CG2 THR D 294     207.749 132.885 263.815  1.00 95.61           C  
ATOM   3872  N   ASP D 295     204.607 131.399 262.100  1.00 98.46           N  
ATOM   3873  CA  ASP D 295     204.503 130.193 261.287  1.00 98.46           C  
ATOM   3874  C   ASP D 295     204.146 130.533 259.846  1.00 98.46           C  
ATOM   3875  O   ASP D 295     204.641 129.899 258.907  1.00 98.46           O  
ATOM   3876  CB  ASP D 295     203.468 129.250 261.897  1.00 98.46           C  
ATOM   3877  CG  ASP D 295     203.363 127.939 261.152  1.00 98.46           C  
ATOM   3878  OD1 ASP D 295     204.314 127.132 261.227  1.00 98.46           O  
ATOM   3879  OD2 ASP D 295     202.324 127.709 260.499  1.00 98.46           O  
ATOM   3880  N   ALA D 296     203.315 131.558 259.656  1.00 95.17           N  
ATOM   3881  CA  ALA D 296     202.963 132.004 258.314  1.00 95.17           C  
ATOM   3882  C   ALA D 296     204.146 132.642 257.599  1.00 95.17           C  
ATOM   3883  O   ALA D 296     204.263 132.516 256.377  1.00 95.17           O  
ATOM   3884  CB  ALA D 296     201.799 132.981 258.376  1.00 95.17           C  
ATOM   3885  N   MET D 297     205.018 133.340 258.331  1.00 94.61           N  
ATOM   3886  CA  MET D 297     206.208 133.902 257.703  1.00 94.61           C  
ATOM   3887  C   MET D 297     207.186 132.810 257.307  1.00 94.61           C  
ATOM   3888  O   MET D 297     207.793 132.878 256.232  1.00 94.61           O  
ATOM   3889  CB  MET D 297     206.899 134.896 258.629  1.00 94.61           C  
ATOM   3890  CG  MET D 297     206.004 135.922 259.232  1.00 94.61           C  
ATOM   3891  SD  MET D 297     206.900 136.941 260.399  1.00 94.61           S  
ATOM   3892  CE  MET D 297     205.835 138.358 260.402  1.00 94.61           C  
ATOM   3893  N   VAL D 298     207.368 131.802 258.163  1.00 97.42           N  
ATOM   3894  CA  VAL D 298     208.394 130.817 257.844  1.00 97.42           C  
ATOM   3895  C   VAL D 298     207.884 129.843 256.782  1.00 97.42           C  
ATOM   3896  O   VAL D 298     208.682 129.297 256.012  1.00 97.42           O  
ATOM   3897  CB  VAL D 298     208.902 130.094 259.106  1.00 97.42           C  
ATOM   3898  CG1 VAL D 298     209.537 131.091 260.060  1.00 97.42           C  
ATOM   3899  CG2 VAL D 298     207.799 129.324 259.801  1.00 97.42           C  
ATOM   3900  N   ASP D 299     206.569 129.598 256.722  1.00 98.59           N  
ATOM   3901  CA  ASP D 299     206.030 128.752 255.661  1.00 98.59           C  
ATOM   3902  C   ASP D 299     206.093 129.446 254.306  1.00 98.59           C  
ATOM   3903  O   ASP D 299     206.352 128.800 253.285  1.00 98.59           O  
ATOM   3904  CB  ASP D 299     204.599 128.333 255.983  1.00 98.59           C  
ATOM   3905  CG  ASP D 299     204.527 127.363 257.139  1.00 98.59           C  
ATOM   3906  OD1 ASP D 299     205.499 126.606 257.338  1.00 98.59           O  
ATOM   3907  OD2 ASP D 299     203.498 127.352 257.845  1.00 98.59           O  
ATOM   3908  N   GLN D 300     205.857 130.755 254.271  1.00 94.00           N  
ATOM   3909  CA  GLN D 300     205.886 131.500 253.021  1.00 94.00           C  
ATOM   3910  C   GLN D 300     207.250 132.102 252.725  1.00 94.00           C  
ATOM   3911  O   GLN D 300     207.384 132.808 251.718  1.00 94.00           O  
ATOM   3912  CB  GLN D 300     204.836 132.614 253.041  1.00 94.00           C  
ATOM   3913  CG  GLN D 300     203.406 132.145 253.212  1.00 94.00           C  
ATOM   3914  CD  GLN D 300     202.442 133.301 253.385  1.00 94.00           C  
ATOM   3915  OE1 GLN D 300     202.641 134.379 252.827  1.00 94.00           O  
ATOM   3916  NE2 GLN D 300     201.393 133.083 254.165  1.00 94.00           N  
ATOM   3917  N   ALA D 301     208.244 131.839 253.582  1.00 92.86           N  
ATOM   3918  CA  ALA D 301     209.638 132.277 253.449  1.00 92.86           C  
ATOM   3919  C   ALA D 301     209.741 133.801 253.334  1.00 92.86           C  
ATOM   3920  O   ALA D 301     210.141 134.356 252.310  1.00 92.86           O  
ATOM   3921  CB  ALA D 301     210.325 131.582 252.266  1.00 92.86           C  
ATOM   3922  N   TRP D 302     209.356 134.468 254.418  1.00 92.65           N  
ATOM   3923  CA  TRP D 302     209.385 135.927 254.462  1.00 92.65           C  
ATOM   3924  C   TRP D 302     210.754 136.349 254.977  1.00 92.65           C  
ATOM   3925  O   TRP D 302     211.014 136.315 256.180  1.00 92.65           O  
ATOM   3926  CB  TRP D 302     208.277 136.484 255.349  1.00 92.65           C  
ATOM   3927  CG  TRP D 302     206.934 136.549 254.693  1.00 92.65           C  
ATOM   3928  CD1 TRP D 302     206.398 135.630 253.848  1.00 92.65           C  
ATOM   3929  CD2 TRP D 302     205.968 137.601 254.805  1.00 92.65           C  
ATOM   3930  NE1 TRP D 302     205.148 136.026 253.444  1.00 92.65           N  
ATOM   3931  CE2 TRP D 302     204.861 137.235 254.016  1.00 92.65           C  
ATOM   3932  CE3 TRP D 302     205.929 138.810 255.501  1.00 92.65           C  
ATOM   3933  CZ2 TRP D 302     203.727 138.034 253.907  1.00 92.65           C  
ATOM   3934  CZ3 TRP D 302     204.806 139.604 255.388  1.00 92.65           C  
ATOM   3935  CH2 TRP D 302     203.723 139.218 254.592  1.00 92.65           C  
ATOM   3936  N   ASP D 303     211.637 136.750 254.070  1.00 91.80           N  
ATOM   3937  CA  ASP D 303     212.951 137.203 254.490  1.00 91.80           C  
ATOM   3938  C   ASP D 303     212.864 138.647 254.978  1.00 91.80           C  
ATOM   3939  O   ASP D 303     211.855 139.329 254.787  1.00 91.80           O  
ATOM   3940  CB  ASP D 303     213.968 137.052 253.360  1.00 91.80           C  
ATOM   3941  CG  ASP D 303     213.498 137.666 252.059  1.00 91.80           C  
ATOM   3942  OD1 ASP D 303     212.324 138.073 251.973  1.00 91.80           O  
ATOM   3943  OD2 ASP D 303     214.309 137.742 251.114  1.00 91.80           O  
ATOM   3944  N   ALA D 304     213.947 139.103 255.618  1.00 89.62           N  
ATOM   3945  CA  ALA D 304     213.956 140.384 256.322  1.00 89.62           C  
ATOM   3946  C   ALA D 304     213.784 141.566 255.380  1.00 89.62           C  
ATOM   3947  O   ALA D 304     213.152 142.571 255.748  1.00 89.62           O  
ATOM   3948  CB  ALA D 304     215.263 140.532 257.086  1.00 89.62           C  
ATOM   3949  N   GLN D 305     214.336 141.449 254.170  1.00 90.88           N  
ATOM   3950  CA  GLN D 305     214.196 142.485 253.157  1.00 90.88           C  
ATOM   3951  C   GLN D 305     212.735 142.700 252.800  1.00 90.88           C  
ATOM   3952  O   GLN D 305     212.272 143.841 252.690  1.00 90.88           O  
ATOM   3953  CB  GLN D 305     215.000 142.096 251.917  1.00 90.88           C  
ATOM   3954  CG  GLN D 305     214.898 143.058 250.752  1.00 90.88           C  
ATOM   3955  CD  GLN D 305     215.821 144.246 250.898  1.00 90.88           C  
ATOM   3956  OE1 GLN D 305     216.720 144.249 251.737  1.00 90.88           O  
ATOM   3957  NE2 GLN D 305     215.617 145.256 250.063  1.00 90.88           N  
ATOM   3958  N   ARG D 306     211.972 141.619 252.690  1.00 90.75           N  
ATOM   3959  CA  ARG D 306     210.588 141.779 252.290  1.00 90.75           C  
ATOM   3960  C   ARG D 306     209.715 142.158 253.489  1.00 90.75           C  
ATOM   3961  O   ARG D 306     208.652 142.757 253.301  1.00 90.75           O  
ATOM   3962  CB  ARG D 306     210.113 140.498 251.599  1.00 90.75           C  
ATOM   3963  CG  ARG D 306     208.746 140.580 250.973  1.00 90.75           C  
ATOM   3964  CD  ARG D 306     208.189 139.231 250.588  1.00 90.75           C  
ATOM   3965  NE  ARG D 306     206.810 139.349 250.130  1.00 90.75           N  
ATOM   3966  CZ  ARG D 306     205.760 139.496 250.923  1.00 90.75           C  
ATOM   3967  NH1 ARG D 306     205.897 139.630 252.228  1.00 90.75           N  
ATOM   3968  NH2 ARG D 306     204.543 139.536 250.389  1.00 90.75           N  
ATOM   3969  N   ILE D 307     210.167 141.866 254.716  1.00 86.89           N  
ATOM   3970  CA  ILE D 307     209.530 142.414 255.918  1.00 86.89           C  
ATOM   3971  C   ILE D 307     209.606 143.935 255.912  1.00 86.89           C  
ATOM   3972  O   ILE D 307     208.604 144.635 256.132  1.00 86.89           O  
ATOM   3973  CB  ILE D 307     210.196 141.846 257.187  1.00 86.89           C  
ATOM   3974  CG1 ILE D 307     210.027 140.333 257.297  1.00 86.89           C  
ATOM   3975  CG2 ILE D 307     209.685 142.546 258.437  1.00 86.89           C  
ATOM   3976  CD1 ILE D 307     208.624 139.901 257.575  1.00 86.89           C  
ATOM   3977  N   PHE D 308     210.795 144.470 255.628  1.00 81.67           N  
ATOM   3978  CA  PHE D 308     210.927 145.919 255.540  1.00 81.67           C  
ATOM   3979  C   PHE D 308     210.214 146.486 254.319  1.00 81.67           C  
ATOM   3980  O   PHE D 308     209.735 147.625 254.361  1.00 81.67           O  
ATOM   3981  CB  PHE D 308     212.398 146.302 255.554  1.00 81.67           C  
ATOM   3982  CG  PHE D 308     212.968 146.368 256.929  1.00 81.67           C  
ATOM   3983  CD1 PHE D 308     212.885 147.534 257.666  1.00 81.67           C  
ATOM   3984  CD2 PHE D 308     213.549 145.255 257.504  1.00 81.67           C  
ATOM   3985  CE1 PHE D 308     213.391 147.593 258.940  1.00 81.67           C  
ATOM   3986  CE2 PHE D 308     214.058 145.310 258.778  1.00 81.67           C  
ATOM   3987  CZ  PHE D 308     213.982 146.482 259.493  1.00 81.67           C  
ATOM   3988  N   LYS D 309     210.101 145.703 253.246  1.00 82.51           N  
ATOM   3989  CA  LYS D 309     209.304 146.127 252.099  1.00 82.51           C  
ATOM   3990  C   LYS D 309     207.821 146.210 252.449  1.00 82.51           C  
ATOM   3991  O   LYS D 309     207.117 147.105 251.973  1.00 82.51           O  
ATOM   3992  CB  LYS D 309     209.533 145.181 250.923  1.00 82.51           C  
ATOM   3993  CG  LYS D 309     210.846 145.425 250.201  1.00 82.51           C  
ATOM   3994  CD  LYS D 309     210.752 146.601 249.252  1.00 82.51           C  
ATOM   3995  CE  LYS D 309     212.009 146.725 248.414  1.00 82.51           C  
ATOM   3996  NZ  LYS D 309     211.944 147.897 247.500  1.00 82.51           N  
ATOM   3997  N   GLU D 310     207.330 145.287 253.278  1.00 83.62           N  
ATOM   3998  CA  GLU D 310     205.937 145.337 253.715  1.00 83.62           C  
ATOM   3999  C   GLU D 310     205.687 146.525 254.634  1.00 83.62           C  
ATOM   4000  O   GLU D 310     204.622 147.157 254.570  1.00 83.62           O  
ATOM   4001  CB  GLU D 310     205.556 144.035 254.415  1.00 83.62           C  
ATOM   4002  CG  GLU D 310     205.325 142.871 253.473  1.00 83.62           C  
ATOM   4003  CD  GLU D 310     204.089 143.041 252.615  1.00 83.62           C  
ATOM   4004  OE1 GLU D 310     203.120 143.676 253.078  1.00 83.62           O  
ATOM   4005  OE2 GLU D 310     204.088 142.542 251.472  1.00 83.62           O  
ATOM   4006  N   ALA D 311     206.659 146.845 255.493  1.00 76.84           N  
ATOM   4007  CA  ALA D 311     206.534 148.042 256.322  1.00 76.84           C  
ATOM   4008  C   ALA D 311     206.541 149.311 255.472  1.00 76.84           C  
ATOM   4009  O   ALA D 311     205.774 150.249 255.731  1.00 76.84           O  
ATOM   4010  CB  ALA D 311     207.655 148.076 257.357  1.00 76.84           C  
ATOM   4011  N   GLU D 312     207.363 149.331 254.420  1.00 81.11           N  
ATOM   4012  CA  GLU D 312     207.360 150.443 253.474  1.00 81.11           C  
ATOM   4013  C   GLU D 312     206.036 150.542 252.721  1.00 81.11           C  
ATOM   4014  O   GLU D 312     205.568 151.647 252.422  1.00 81.11           O  
ATOM   4015  CB  GLU D 312     208.523 150.281 252.500  1.00 81.11           C  
ATOM   4016  CG  GLU D 312     208.793 151.483 251.632  1.00 81.11           C  
ATOM   4017  CD  GLU D 312     209.647 151.137 250.436  1.00 81.11           C  
ATOM   4018  OE1 GLU D 312     209.573 149.981 249.971  1.00 81.11           O  
ATOM   4019  OE2 GLU D 312     210.392 152.017 249.960  1.00 81.11           O  
ATOM   4020  N   LYS D 313     205.429 149.397 252.393  1.00 79.39           N  
ATOM   4021  CA  LYS D 313     204.112 149.400 251.759  1.00 79.39           C  
ATOM   4022  C   LYS D 313     203.045 149.964 252.684  1.00 79.39           C  
ATOM   4023  O   LYS D 313     202.136 150.667 252.232  1.00 79.39           O  
ATOM   4024  CB  LYS D 313     203.724 147.991 251.316  1.00 79.39           C  
ATOM   4025  CG  LYS D 313     204.244 147.592 249.949  1.00 79.39           C  
ATOM   4026  CD  LYS D 313     204.176 146.086 249.741  1.00 79.39           C  
ATOM   4027  CE  LYS D 313     202.801 145.531 250.082  1.00 79.39           C  
ATOM   4028  NZ  LYS D 313     202.680 144.088 249.743  1.00 79.39           N  
ATOM   4029  N   PHE D 314     203.145 149.674 253.983  1.00 73.80           N  
ATOM   4030  CA  PHE D 314     202.243 150.291 254.955  1.00 73.80           C  
ATOM   4031  C   PHE D 314     202.429 151.803 255.000  1.00 73.80           C  
ATOM   4032  O   PHE D 314     201.449 152.567 255.022  1.00 73.80           O  
ATOM   4033  CB  PHE D 314     202.489 149.678 256.334  1.00 73.80           C  
ATOM   4034  CG  PHE D 314     201.932 150.480 257.473  1.00 73.80           C  
ATOM   4035  CD1 PHE D 314     200.574 150.512 257.713  1.00 73.80           C  
ATOM   4036  CD2 PHE D 314     202.772 151.184 258.320  1.00 73.80           C  
ATOM   4037  CE1 PHE D 314     200.057 151.242 258.763  1.00 73.80           C  
ATOM   4038  CE2 PHE D 314     202.260 151.921 259.369  1.00 73.80           C  
ATOM   4039  CZ  PHE D 314     200.902 151.948 259.591  1.00 73.80           C  
ATOM   4040  N   PHE D 315     203.679 152.254 254.940  1.00 72.19           N  
ATOM   4041  CA  PHE D 315     203.932 153.684 255.048  1.00 72.19           C  
ATOM   4042  C   PHE D 315     203.570 154.440 253.777  1.00 72.19           C  
ATOM   4043  O   PHE D 315     203.287 155.639 253.842  1.00 72.19           O  
ATOM   4044  CB  PHE D 315     205.385 153.925 255.428  1.00 72.19           C  
ATOM   4045  CG  PHE D 315     205.602 153.919 256.896  1.00 72.19           C  
ATOM   4046  CD1 PHE D 315     205.249 155.005 257.661  1.00 72.19           C  
ATOM   4047  CD2 PHE D 315     206.130 152.806 257.519  1.00 72.19           C  
ATOM   4048  CE1 PHE D 315     205.432 154.988 259.016  1.00 72.19           C  
ATOM   4049  CE2 PHE D 315     206.315 152.783 258.869  1.00 72.19           C  
ATOM   4050  CZ  PHE D 315     205.965 153.872 259.615  1.00 72.19           C  
ATOM   4051  N   VAL D 316     203.596 153.788 252.616  1.00 73.72           N  
ATOM   4052  CA  VAL D 316     203.074 154.450 251.427  1.00 73.72           C  
ATOM   4053  C   VAL D 316     201.570 154.259 251.296  1.00 73.72           C  
ATOM   4054  O   VAL D 316     200.929 154.988 250.526  1.00 73.72           O  
ATOM   4055  CB  VAL D 316     203.761 153.978 250.135  1.00 73.72           C  
ATOM   4056  CG1 VAL D 316     205.233 154.147 250.257  1.00 73.72           C  
ATOM   4057  CG2 VAL D 316     203.411 152.543 249.815  1.00 73.72           C  
ATOM   4058  N   SER D 317     200.987 153.307 252.029  1.00 74.20           N  
ATOM   4059  CA  SER D 317     199.537 153.214 252.093  1.00 74.20           C  
ATOM   4060  C   SER D 317     198.968 154.375 252.885  1.00 74.20           C  
ATOM   4061  O   SER D 317     197.902 154.900 252.550  1.00 74.20           O  
ATOM   4062  CB  SER D 317     199.111 151.890 252.716  1.00 74.20           C  
ATOM   4063  OG  SER D 317     199.087 151.988 254.127  1.00 74.20           O  
ATOM   4064  N   VAL D 318     199.671 154.800 253.937  1.00 74.36           N  
ATOM   4065  CA  VAL D 318     199.143 155.903 254.738  1.00 74.36           C  
ATOM   4066  C   VAL D 318     199.473 157.252 254.112  1.00 74.36           C  
ATOM   4067  O   VAL D 318     198.863 158.265 254.472  1.00 74.36           O  
ATOM   4068  CB  VAL D 318     199.667 155.775 256.184  1.00 74.36           C  
ATOM   4069  CG1 VAL D 318     201.135 156.137 256.274  1.00 74.36           C  
ATOM   4070  CG2 VAL D 318     198.813 156.547 257.180  1.00 74.36           C  
ATOM   4071  N   GLY D 319     200.383 157.294 253.142  1.00 72.00           N  
ATOM   4072  CA  GLY D 319     200.681 158.512 252.413  1.00 72.00           C  
ATOM   4073  C   GLY D 319     202.047 159.105 252.670  1.00 72.00           C  
ATOM   4074  O   GLY D 319     202.399 160.100 252.027  1.00 72.00           O  
ATOM   4075  N   LEU D 320     202.824 158.532 253.566  1.00 72.57           N  
ATOM   4076  CA  LEU D 320     204.166 159.000 253.861  1.00 72.57           C  
ATOM   4077  C   LEU D 320     205.121 158.578 252.745  1.00 72.57           C  
ATOM   4078  O   LEU D 320     204.849 157.611 252.030  1.00 72.57           O  
ATOM   4079  CB  LEU D 320     204.624 158.449 255.210  1.00 72.57           C  
ATOM   4080  CG  LEU D 320     203.805 159.020 256.369  1.00 72.57           C  
ATOM   4081  CD1 LEU D 320     204.220 158.435 257.693  1.00 72.57           C  
ATOM   4082  CD2 LEU D 320     203.926 160.528 256.405  1.00 72.57           C  
ATOM   4083  N   PRO D 321     206.215 159.317 252.541  1.00 77.05           N  
ATOM   4084  CA  PRO D 321     207.156 158.962 251.472  1.00 77.05           C  
ATOM   4085  C   PRO D 321     207.860 157.641 251.717  1.00 77.05           C  
ATOM   4086  O   PRO D 321     208.062 157.215 252.855  1.00 77.05           O  
ATOM   4087  CB  PRO D 321     208.160 160.118 251.495  1.00 77.05           C  
ATOM   4088  CG  PRO D 321     207.394 161.249 252.041  1.00 77.05           C  
ATOM   4089  CD  PRO D 321     206.537 160.642 253.101  1.00 77.05           C  
ATOM   4090  N   ASN D 322     208.222 156.982 250.621  1.00 88.07           N  
ATOM   4091  CA  ASN D 322     208.849 155.678 250.720  1.00 88.07           C  
ATOM   4092  C   ASN D 322     210.324 155.828 251.060  1.00 88.07           C  
ATOM   4093  O   ASN D 322     210.845 156.928 251.253  1.00 88.07           O  
ATOM   4094  CB  ASN D 322     208.677 154.883 249.430  1.00 88.07           C  
ATOM   4095  CG  ASN D 322     209.025 155.678 248.204  1.00 88.07           C  
ATOM   4096  OD1 ASN D 322     209.230 156.888 248.269  1.00 88.07           O  
ATOM   4097  ND2 ASN D 322     209.093 155.000 247.070  1.00 88.07           N  
ATOM   4098  N   MET D 323     211.001 154.693 251.130  1.00 83.45           N  
ATOM   4099  CA  MET D 323     212.367 154.666 251.610  1.00 83.45           C  
ATOM   4100  C   MET D 323     213.312 155.214 250.551  1.00 83.45           C  
ATOM   4101  O   MET D 323     213.033 155.163 249.352  1.00 83.45           O  
ATOM   4102  CB  MET D 323     212.753 153.238 251.990  1.00 83.45           C  
ATOM   4103  CG  MET D 323     212.007 152.643 253.203  1.00 83.45           C  
ATOM   4104  SD  MET D 323     211.775 153.478 254.798  1.00 83.45           S  
ATOM   4105  CE  MET D 323     213.288 154.385 255.050  1.00 83.45           C  
ATOM   4106  N   THR D 324     214.437 155.750 251.003  1.00 82.15           N  
ATOM   4107  CA  THR D 324     215.453 156.198 250.070  1.00 82.15           C  
ATOM   4108  C   THR D 324     216.217 155.002 249.517  1.00 82.15           C  
ATOM   4109  O   THR D 324     216.160 153.895 250.054  1.00 82.15           O  
ATOM   4110  CB  THR D 324     216.414 157.176 250.745  1.00 82.15           C  
ATOM   4111  OG1 THR D 324     217.340 156.452 251.562  1.00 82.15           O  
ATOM   4112  CG2 THR D 324     215.650 158.158 251.610  1.00 82.15           C  
ATOM   4113  N   GLN D 325     216.921 155.234 248.408  1.00 86.41           N  
ATOM   4114  CA  GLN D 325     217.733 154.173 247.822  1.00 86.41           C  
ATOM   4115  C   GLN D 325     218.935 153.869 248.703  1.00 86.41           C  
ATOM   4116  O   GLN D 325     219.330 152.706 248.853  1.00 86.41           O  
ATOM   4117  CB  GLN D 325     218.174 154.572 246.416  1.00 86.41           C  
ATOM   4118  CG  GLN D 325     218.942 153.497 245.671  1.00 86.41           C  
ATOM   4119  CD  GLN D 325     218.145 152.218 245.520  1.00 86.41           C  
ATOM   4120  OE1 GLN D 325     218.394 151.233 246.213  1.00 86.41           O  
ATOM   4121  NE2 GLN D 325     217.174 152.230 244.614  1.00 86.41           N  
ATOM   4122  N   GLY D 326     219.507 154.904 249.317  1.00 82.92           N  
ATOM   4123  CA  GLY D 326     220.606 154.713 250.240  1.00 82.92           C  
ATOM   4124  C   GLY D 326     220.208 154.002 251.513  1.00 82.92           C  
ATOM   4125  O   GLY D 326     221.069 153.407 252.167  1.00 82.92           O  
ATOM   4126  N   PHE D 327     218.926 154.064 251.883  1.00 79.18           N  
ATOM   4127  CA  PHE D 327     218.424 153.247 252.981  1.00 79.18           C  
ATOM   4128  C   PHE D 327     218.549 151.766 252.660  1.00 79.18           C  
ATOM   4129  O   PHE D 327     219.014 150.980 253.487  1.00 79.18           O  
ATOM   4130  CB  PHE D 327     216.968 153.605 253.278  1.00 79.18           C  
ATOM   4131  CG  PHE D 327     216.306 152.687 254.265  1.00 79.18           C  
ATOM   4132  CD1 PHE D 327     216.541 152.832 255.616  1.00 79.18           C  
ATOM   4133  CD2 PHE D 327     215.434 151.694 253.844  1.00 79.18           C  
ATOM   4134  CE1 PHE D 327     215.935 152.000 256.524  1.00 79.18           C  
ATOM   4135  CE2 PHE D 327     214.830 150.856 254.751  1.00 79.18           C  
ATOM   4136  CZ  PHE D 327     215.079 151.010 256.091  1.00 79.18           C  
ATOM   4137  N   TRP D 328     218.124 151.364 251.464  1.00 80.60           N  
ATOM   4138  CA  TRP D 328     218.206 149.955 251.103  1.00 80.60           C  
ATOM   4139  C   TRP D 328     219.643 149.528 250.848  1.00 80.60           C  
ATOM   4140  O   TRP D 328     219.990 148.364 251.072  1.00 80.60           O  
ATOM   4141  CB  TRP D 328     217.345 149.671 249.879  1.00 80.60           C  
ATOM   4142  CG  TRP D 328     215.891 149.874 250.119  1.00 80.60           C  
ATOM   4143  CD1 TRP D 328     215.105 150.840 249.575  1.00 80.60           C  
ATOM   4144  CD2 TRP D 328     215.045 149.108 250.983  1.00 80.60           C  
ATOM   4145  NE1 TRP D 328     213.819 150.716 250.030  1.00 80.60           N  
ATOM   4146  CE2 TRP D 328     213.757 149.663 250.901  1.00 80.60           C  
ATOM   4147  CE3 TRP D 328     215.251 148.005 251.814  1.00 80.60           C  
ATOM   4148  CZ2 TRP D 328     212.682 149.153 251.616  1.00 80.60           C  
ATOM   4149  CZ3 TRP D 328     214.184 147.502 252.521  1.00 80.60           C  
ATOM   4150  CH2 TRP D 328     212.915 148.074 252.418  1.00 80.60           C  
ATOM   4151  N   GLU D 329     220.483 150.448 250.371  1.00 85.09           N  
ATOM   4152  CA  GLU D 329     221.877 150.106 250.118  1.00 85.09           C  
ATOM   4153  C   GLU D 329     222.673 149.974 251.411  1.00 85.09           C  
ATOM   4154  O   GLU D 329     223.481 149.050 251.554  1.00 85.09           O  
ATOM   4155  CB  GLU D 329     222.509 151.154 249.206  1.00 85.09           C  
ATOM   4156  CG  GLU D 329     222.000 151.112 247.779  1.00 85.09           C  
ATOM   4157  CD  GLU D 329     222.648 152.161 246.901  1.00 85.09           C  
ATOM   4158  OE1 GLU D 329     223.189 153.143 247.450  1.00 85.09           O  
ATOM   4159  OE2 GLU D 329     222.614 152.006 245.663  1.00 85.09           O  
ATOM   4160  N   ASN D 330     222.460 150.878 252.368  1.00 80.88           N  
ATOM   4161  CA  ASN D 330     223.386 151.023 253.484  1.00 80.88           C  
ATOM   4162  C   ASN D 330     222.910 150.396 254.785  1.00 80.88           C  
ATOM   4163  O   ASN D 330     223.738 150.165 255.670  1.00 80.88           O  
ATOM   4164  CB  ASN D 330     223.682 152.503 253.737  1.00 80.88           C  
ATOM   4165  CG  ASN D 330     224.185 153.213 252.505  1.00 80.88           C  
ATOM   4166  OD1 ASN D 330     225.237 152.875 251.965  1.00 80.88           O  
ATOM   4167  ND2 ASN D 330     223.438 154.208 252.052  1.00 80.88           N  
ATOM   4168  N   SER D 331     221.619 150.120 254.935  1.00 82.59           N  
ATOM   4169  CA  SER D 331     221.151 149.494 256.162  1.00 82.59           C  
ATOM   4170  C   SER D 331     221.537 148.027 256.180  1.00 82.59           C  
ATOM   4171  O   SER D 331     221.567 147.356 255.146  1.00 82.59           O  
ATOM   4172  CB  SER D 331     219.638 149.607 256.303  1.00 82.59           C  
ATOM   4173  OG  SER D 331     219.221 150.955 256.279  1.00 82.59           O  
ATOM   4174  N   MET D 332     221.832 147.528 257.365  1.00 89.12           N  
ATOM   4175  CA  MET D 332     222.158 146.122 257.535  1.00 89.12           C  
ATOM   4176  C   MET D 332     220.976 145.529 258.288  1.00 89.12           C  
ATOM   4177  O   MET D 332     220.873 145.664 259.509  1.00 89.12           O  
ATOM   4178  CB  MET D 332     223.471 145.927 258.279  1.00 89.12           C  
ATOM   4179  CG  MET D 332     223.872 144.470 258.389  1.00 89.12           C  
ATOM   4180  SD  MET D 332     224.934 144.084 259.780  1.00 89.12           S  
ATOM   4181  CE  MET D 332     224.031 144.889 261.083  1.00 89.12           C  
ATOM   4182  N   LEU D 333     220.077 144.889 257.546  1.00 88.80           N  
ATOM   4183  CA  LEU D 333     218.822 144.385 258.076  1.00 88.80           C  
ATOM   4184  C   LEU D 333     218.909 142.925 258.480  1.00 88.80           C  
ATOM   4185  O   LEU D 333     217.892 142.332 258.840  1.00 88.80           O  
ATOM   4186  CB  LEU D 333     217.706 144.577 257.050  1.00 88.80           C  
ATOM   4187  CG  LEU D 333     217.570 145.978 256.461  1.00 88.80           C  
ATOM   4188  CD1 LEU D 333     216.506 146.000 255.391  1.00 88.80           C  
ATOM   4189  CD2 LEU D 333     217.225 146.964 257.556  1.00 88.80           C  
ATOM   4190  N   THR D 334     220.095 142.332 258.413  1.00 95.57           N  
ATOM   4191  CA  THR D 334     220.291 140.929 258.735  1.00 95.57           C  
ATOM   4192  C   THR D 334     221.597 140.826 259.511  1.00 95.57           C  
ATOM   4193  O   THR D 334     222.513 141.621 259.292  1.00 95.57           O  
ATOM   4194  CB  THR D 334     220.317 140.080 257.445  1.00 95.57           C  
ATOM   4195  OG1 THR D 334     219.128 140.336 256.689  1.00 95.57           O  
ATOM   4196  CG2 THR D 334     220.362 138.585 257.737  1.00 95.57           C  
ATOM   4197  N   ASP D 335     221.658 139.884 260.452  1.00103.78           N  
ATOM   4198  CA  ASP D 335     222.895 139.618 261.175  1.00103.78           C  
ATOM   4199  C   ASP D 335     223.961 139.131 260.197  1.00103.78           C  
ATOM   4200  O   ASP D 335     223.704 138.198 259.424  1.00103.78           O  
ATOM   4201  CB  ASP D 335     222.670 138.582 262.272  1.00103.78           C  
ATOM   4202  CG  ASP D 335     223.879 138.410 263.163  1.00103.78           C  
ATOM   4203  OD1 ASP D 335     223.983 139.142 264.169  1.00103.78           O  
ATOM   4204  OD2 ASP D 335     224.729 137.548 262.860  1.00103.78           O  
ATOM   4205  N   PRO D 336     225.152 139.736 260.184  1.00106.37           N  
ATOM   4206  CA  PRO D 336     226.099 139.478 259.090  1.00106.37           C  
ATOM   4207  C   PRO D 336     226.790 138.124 259.160  1.00106.37           C  
ATOM   4208  O   PRO D 336     227.079 137.530 258.118  1.00106.37           O  
ATOM   4209  CB  PRO D 336     227.107 140.624 259.234  1.00106.37           C  
ATOM   4210  CG  PRO D 336     227.065 140.974 260.680  1.00106.37           C  
ATOM   4211  CD  PRO D 336     225.648 140.756 261.123  1.00106.37           C  
ATOM   4212  N   GLY D 337     227.064 137.626 260.352  1.00112.46           N  
ATOM   4213  CA  GLY D 337     227.714 136.342 260.493  1.00112.46           C  
ATOM   4214  C   GLY D 337     228.528 136.283 261.768  1.00112.46           C  
ATOM   4215  O   GLY D 337     228.499 137.193 262.591  1.00112.46           O  
ATOM   4216  N   ASN D 338     229.249 135.171 261.917  1.00121.82           N  
ATOM   4217  CA  ASN D 338     230.072 134.964 263.102  1.00121.82           C  
ATOM   4218  C   ASN D 338     231.377 135.750 263.045  1.00121.82           C  
ATOM   4219  O   ASN D 338     231.868 136.201 264.087  1.00121.82           O  
ATOM   4220  CB  ASN D 338     230.360 133.471 263.275  1.00121.82           C  
ATOM   4221  CG  ASN D 338     231.239 133.179 264.474  1.00121.82           C  
ATOM   4222  OD1 ASN D 338     230.939 133.595 265.593  1.00121.82           O  
ATOM   4223  ND2 ASN D 338     232.334 132.463 264.245  1.00121.82           N  
ATOM   4224  N   VAL D 339     231.939 135.932 261.847  1.00119.71           N  
ATOM   4225  CA  VAL D 339     233.247 136.570 261.719  1.00119.71           C  
ATOM   4226  C   VAL D 339     233.161 138.069 262.007  1.00119.71           C  
ATOM   4227  O   VAL D 339     234.106 138.660 262.546  1.00119.71           O  
ATOM   4228  CB  VAL D 339     233.849 136.248 260.330  1.00119.71           C  
ATOM   4229  CG1 VAL D 339     232.998 136.807 259.185  1.00119.71           C  
ATOM   4230  CG2 VAL D 339     235.301 136.714 260.224  1.00119.71           C  
ATOM   4231  N   GLN D 340     232.030 138.699 261.708  1.00113.80           N  
ATOM   4232  CA  GLN D 340     231.833 140.122 261.943  1.00113.80           C  
ATOM   4233  C   GLN D 340     230.819 140.283 263.064  1.00113.80           C  
ATOM   4234  O   GLN D 340     229.678 139.824 262.943  1.00113.80           O  
ATOM   4235  CB  GLN D 340     231.361 140.828 260.673  1.00113.80           C  
ATOM   4236  CG  GLN D 340     230.827 142.225 260.902  1.00113.80           C  
ATOM   4237  CD  GLN D 340     230.738 143.025 259.620  1.00113.80           C  
ATOM   4238  OE1 GLN D 340     231.567 142.874 258.724  1.00113.80           O  
ATOM   4239  NE2 GLN D 340     229.726 143.878 259.523  1.00113.80           N  
ATOM   4240  N   LYS D 341     231.227 140.937 264.142  1.00108.44           N  
ATOM   4241  CA  LYS D 341     230.368 141.135 265.297  1.00108.44           C  
ATOM   4242  C   LYS D 341     229.709 142.502 265.224  1.00108.44           C  
ATOM   4243  O   LYS D 341     230.351 143.497 264.879  1.00108.44           O  
ATOM   4244  CB  LYS D 341     231.157 141.000 266.598  1.00108.44           C  
ATOM   4245  CG  LYS D 341     231.618 139.583 266.877  1.00108.44           C  
ATOM   4246  CD  LYS D 341     230.573 138.812 267.664  1.00108.44           C  
ATOM   4247  CE  LYS D 341     230.976 137.357 267.837  1.00108.44           C  
ATOM   4248  NZ  LYS D 341     229.853 136.530 268.358  1.00108.44           N  
ATOM   4249  N   ALA D 342     228.420 142.541 265.542  1.00100.84           N  
ATOM   4250  CA  ALA D 342     227.646 143.767 265.473  1.00100.84           C  
ATOM   4251  C   ALA D 342     226.696 143.818 266.656  1.00100.84           C  
ATOM   4252  O   ALA D 342     226.350 142.792 267.244  1.00100.84           O  
ATOM   4253  CB  ALA D 342     226.859 143.861 264.163  1.00100.84           C  
ATOM   4254  N   VAL D 343     226.287 145.029 267.008  1.00101.03           N  
ATOM   4255  CA  VAL D 343     225.341 145.215 268.100  1.00101.03           C  
ATOM   4256  C   VAL D 343     223.957 144.818 267.609  1.00101.03           C  
ATOM   4257  O   VAL D 343     223.472 145.334 266.596  1.00101.03           O  
ATOM   4258  CB  VAL D 343     225.368 146.667 268.600  1.00101.03           C  
ATOM   4259  CG1 VAL D 343     224.223 146.925 269.564  1.00101.03           C  
ATOM   4260  CG2 VAL D 343     226.700 146.966 269.261  1.00101.03           C  
ATOM   4261  N   CYS D 344     223.316 143.901 268.328  1.00104.05           N  
ATOM   4262  CA  CYS D 344     222.031 143.354 267.916  1.00104.05           C  
ATOM   4263  C   CYS D 344     220.847 144.212 268.337  1.00104.05           C  
ATOM   4264  O   CYS D 344     219.705 143.832 268.058  1.00104.05           O  
ATOM   4265  CB  CYS D 344     221.865 141.940 268.477  1.00104.05           C  
ATOM   4266  SG  CYS D 344     221.899 141.854 270.283  1.00104.05           S  
ATOM   4267  N   HIS D 345     221.085 145.336 269.000  1.00 96.81           N  
ATOM   4268  CA  HIS D 345     219.991 146.187 269.449  1.00 96.81           C  
ATOM   4269  C   HIS D 345     219.345 146.892 268.261  1.00 96.81           C  
ATOM   4270  O   HIS D 345     220.056 147.432 267.407  1.00 96.81           O  
ATOM   4271  CB  HIS D 345     220.496 147.209 270.461  1.00 96.81           C  
ATOM   4272  CG  HIS D 345     219.408 148.017 271.095  1.00 96.81           C  
ATOM   4273  ND1 HIS D 345     218.936 149.190 270.547  1.00 96.81           N  
ATOM   4274  CD2 HIS D 345     218.696 147.818 272.228  1.00 96.81           C  
ATOM   4275  CE1 HIS D 345     217.982 149.680 271.317  1.00 96.81           C  
ATOM   4276  NE2 HIS D 345     217.816 148.867 272.344  1.00 96.81           N  
ATOM   4277  N   PRO D 346     218.014 146.901 268.166  1.00 91.19           N  
ATOM   4278  CA  PRO D 346     217.339 147.598 267.061  1.00 91.19           C  
ATOM   4279  C   PRO D 346     217.438 149.104 267.239  1.00 91.19           C  
ATOM   4280  O   PRO D 346     216.989 149.654 268.246  1.00 91.19           O  
ATOM   4281  CB  PRO D 346     215.889 147.113 267.172  1.00 91.19           C  
ATOM   4282  CG  PRO D 346     215.956 145.880 268.013  1.00 91.19           C  
ATOM   4283  CD  PRO D 346     217.060 146.137 268.982  1.00 91.19           C  
ATOM   4284  N   THR D 347     218.031 149.771 266.254  1.00 85.69           N  
ATOM   4285  CA  THR D 347     218.272 151.201 266.334  1.00 85.69           C  
ATOM   4286  C   THR D 347     218.000 151.835 264.980  1.00 85.69           C  
ATOM   4287  O   THR D 347     218.385 151.292 263.944  1.00 85.69           O  
ATOM   4288  CB  THR D 347     219.715 151.496 266.773  1.00 85.69           C  
ATOM   4289  OG1 THR D 347     220.022 150.738 267.949  1.00 85.69           O  
ATOM   4290  CG2 THR D 347     219.893 152.969 267.100  1.00 85.69           C  
ATOM   4291  N   ALA D 348     217.297 152.959 264.984  1.00 78.67           N  
ATOM   4292  CA  ALA D 348     217.112 153.749 263.780  1.00 78.67           C  
ATOM   4293  C   ALA D 348     218.112 154.895 263.787  1.00 78.67           C  
ATOM   4294  O   ALA D 348     218.220 155.621 264.779  1.00 78.67           O  
ATOM   4295  CB  ALA D 348     215.690 154.288 263.699  1.00 78.67           C  
ATOM   4296  N   TRP D 349     218.831 155.061 262.683  1.00 77.80           N  
ATOM   4297  CA  TRP D 349     219.944 155.989 262.596  1.00 77.80           C  
ATOM   4298  C   TRP D 349     219.592 157.097 261.618  1.00 77.80           C  
ATOM   4299  O   TRP D 349     219.258 156.826 260.459  1.00 77.80           O  
ATOM   4300  CB  TRP D 349     221.213 155.272 262.138  1.00 77.80           C  
ATOM   4301  CG  TRP D 349     221.793 154.356 263.162  1.00 77.80           C  
ATOM   4302  CD1 TRP D 349     221.292 153.155 263.556  1.00 77.80           C  
ATOM   4303  CD2 TRP D 349     222.986 154.562 263.924  1.00 77.80           C  
ATOM   4304  NE1 TRP D 349     222.098 152.596 264.513  1.00 77.80           N  
ATOM   4305  CE2 TRP D 349     223.145 153.442 264.758  1.00 77.80           C  
ATOM   4306  CE3 TRP D 349     223.934 155.585 263.983  1.00 77.80           C  
ATOM   4307  CZ2 TRP D 349     224.212 153.315 265.638  1.00 77.80           C  
ATOM   4308  CZ3 TRP D 349     224.992 155.457 264.855  1.00 77.80           C  
ATOM   4309  CH2 TRP D 349     225.123 154.332 265.672  1.00 77.80           C  
ATOM   4310  N   ASP D 350     219.695 158.332 262.081  1.00 75.41           N  
ATOM   4311  CA  ASP D 350     219.608 159.522 261.246  1.00 75.41           C  
ATOM   4312  C   ASP D 350     221.019 160.086 261.187  1.00 75.41           C  
ATOM   4313  O   ASP D 350     221.440 160.813 262.090  1.00 75.41           O  
ATOM   4314  CB  ASP D 350     218.618 160.523 261.836  1.00 75.41           C  
ATOM   4315  CG  ASP D 350     218.390 161.736 260.948  1.00 75.41           C  
ATOM   4316  OD1 ASP D 350     218.902 161.776 259.811  1.00 75.41           O  
ATOM   4317  OD2 ASP D 350     217.690 162.666 261.397  1.00 75.41           O  
ATOM   4318  N   LEU D 351     221.751 159.756 260.126  1.00 71.09           N  
ATOM   4319  CA  LEU D 351     223.156 160.124 260.092  1.00 71.09           C  
ATOM   4320  C   LEU D 351     223.341 161.564 259.658  1.00 71.09           C  
ATOM   4321  O   LEU D 351     224.406 162.143 259.888  1.00 71.09           O  
ATOM   4322  CB  LEU D 351     223.927 159.212 259.134  1.00 71.09           C  
ATOM   4323  CG  LEU D 351     224.003 157.707 259.399  1.00 71.09           C  
ATOM   4324  CD1 LEU D 351     225.192 157.105 258.684  1.00 71.09           C  
ATOM   4325  CD2 LEU D 351     224.049 157.377 260.864  1.00 71.09           C  
ATOM   4326  N   GLY D 352     222.317 162.148 259.054  1.00 67.92           N  
ATOM   4327  CA  GLY D 352     222.373 163.490 258.529  1.00 67.92           C  
ATOM   4328  C   GLY D 352     222.746 163.422 257.066  1.00 67.92           C  
ATOM   4329  O   GLY D 352     223.139 162.374 256.548  1.00 67.92           O  
ATOM   4330  N   LYS D 353     222.573 164.562 256.384  1.00 63.82           N  
ATOM   4331  CA  LYS D 353     222.822 164.699 254.944  1.00 63.82           C  
ATOM   4332  C   LYS D 353     221.955 163.718 254.160  1.00 63.82           C  
ATOM   4333  O   LYS D 353     222.414 163.074 253.217  1.00 63.82           O  
ATOM   4334  CB  LYS D 353     224.303 164.540 254.586  1.00 63.82           C  
ATOM   4335  CG  LYS D 353     225.227 165.535 255.247  1.00 63.82           C  
ATOM   4336  CD  LYS D 353     225.176 166.872 254.543  1.00 63.82           C  
ATOM   4337  CE  LYS D 353     226.293 167.777 255.009  1.00 63.82           C  
ATOM   4338  NZ  LYS D 353     227.616 167.122 254.852  1.00 63.82           N  
ATOM   4339  N   GLY D 354     220.685 163.619 254.551  1.00 66.13           N  
ATOM   4340  CA  GLY D 354     219.743 162.743 253.883  1.00 66.13           C  
ATOM   4341  C   GLY D 354     220.041 161.263 253.986  1.00 66.13           C  
ATOM   4342  O   GLY D 354     219.507 160.481 253.198  1.00 66.13           O  
ATOM   4343  N   ASP D 355     220.878 160.847 254.934  1.00 69.83           N  
ATOM   4344  CA  ASP D 355     221.227 159.442 255.109  1.00 69.83           C  
ATOM   4345  C   ASP D 355     220.459 158.866 256.293  1.00 69.83           C  
ATOM   4346  O   ASP D 355     220.604 159.334 257.430  1.00 69.83           O  
ATOM   4347  CB  ASP D 355     222.731 159.284 255.314  1.00 69.83           C  
ATOM   4348  CG  ASP D 355     223.192 157.857 255.155  1.00 69.83           C  
ATOM   4349  OD1 ASP D 355     222.396 157.018 254.694  1.00 69.83           O  
ATOM   4350  OD2 ASP D 355     224.361 157.572 255.480  1.00 69.83           O  
ATOM   4351  N   PHE D 356     219.654 157.841 256.019  1.00 70.13           N  
ATOM   4352  CA  PHE D 356     218.797 157.198 257.004  1.00 70.13           C  
ATOM   4353  C   PHE D 356     219.035 155.700 256.942  1.00 70.13           C  
ATOM   4354  O   PHE D 356     218.982 155.112 255.859  1.00 70.13           O  
ATOM   4355  CB  PHE D 356     217.331 157.520 256.722  1.00 70.13           C  
ATOM   4356  CG  PHE D 356     217.038 158.986 256.685  1.00 70.13           C  
ATOM   4357  CD1 PHE D 356     216.836 159.697 257.850  1.00 70.13           C  
ATOM   4358  CD2 PHE D 356     217.000 159.661 255.478  1.00 70.13           C  
ATOM   4359  CE1 PHE D 356     216.572 161.047 257.809  1.00 70.13           C  
ATOM   4360  CE2 PHE D 356     216.750 161.012 255.434  1.00 70.13           C  
ATOM   4361  CZ  PHE D 356     216.534 161.704 256.601  1.00 70.13           C  
ATOM   4362  N   ARG D 357     219.309 155.081 258.089  1.00 74.49           N  
ATOM   4363  CA  ARG D 357     219.637 153.661 258.128  1.00 74.49           C  
ATOM   4364  C   ARG D 357     218.927 153.001 259.300  1.00 74.49           C  
ATOM   4365  O   ARG D 357     218.507 153.666 260.244  1.00 74.49           O  
ATOM   4366  CB  ARG D 357     221.152 153.426 258.238  1.00 74.49           C  
ATOM   4367  CG  ARG D 357     221.961 153.903 257.043  1.00 74.49           C  
ATOM   4368  CD  ARG D 357     223.447 153.750 257.258  1.00 74.49           C  
ATOM   4369  NE  ARG D 357     224.193 154.612 256.353  1.00 74.49           N  
ATOM   4370  CZ  ARG D 357     225.494 154.518 256.130  1.00 74.49           C  
ATOM   4371  NH1 ARG D 357     226.230 153.593 256.717  1.00 74.49           N  
ATOM   4372  NH2 ARG D 357     226.071 155.371 255.289  1.00 74.49           N  
ATOM   4373  N   ILE D 358     218.740 151.688 259.212  1.00 77.72           N  
ATOM   4374  CA  ILE D 358     218.246 150.895 260.334  1.00 77.72           C  
ATOM   4375  C   ILE D 358     219.256 149.803 260.650  1.00 77.72           C  
ATOM   4376  O   ILE D 358     219.617 149.008 259.775  1.00 77.72           O  
ATOM   4377  CB  ILE D 358     216.851 150.306 260.066  1.00 77.72           C  
ATOM   4378  CG1 ILE D 358     215.809 151.420 260.063  1.00 77.72           C  
ATOM   4379  CG2 ILE D 358     216.486 149.262 261.098  1.00 77.72           C  
ATOM   4380  CD1 ILE D 358     214.437 150.979 259.665  1.00 77.72           C  
ATOM   4381  N   LEU D 359     219.717 149.775 261.898  1.00 84.77           N  
ATOM   4382  CA  LEU D 359     220.556 148.712 262.431  1.00 84.77           C  
ATOM   4383  C   LEU D 359     219.632 147.723 263.130  1.00 84.77           C  
ATOM   4384  O   LEU D 359     219.089 148.021 264.198  1.00 84.77           O  
ATOM   4385  CB  LEU D 359     221.587 149.291 263.398  1.00 84.77           C  
ATOM   4386  CG  LEU D 359     222.370 148.410 264.371  1.00 84.77           C  
ATOM   4387  CD1 LEU D 359     223.125 147.331 263.654  1.00 84.77           C  
ATOM   4388  CD2 LEU D 359     223.307 149.255 265.209  1.00 84.77           C  
ATOM   4389  N   MET D 360     219.430 146.561 262.521  1.00 89.60           N  
ATOM   4390  CA  MET D 360     218.502 145.581 263.070  1.00 89.60           C  
ATOM   4391  C   MET D 360     218.949 144.199 262.629  1.00 89.60           C  
ATOM   4392  O   MET D 360     219.087 143.951 261.429  1.00 89.60           O  
ATOM   4393  CB  MET D 360     217.075 145.846 262.598  1.00 89.60           C  
ATOM   4394  CG  MET D 360     216.149 144.666 262.804  1.00 89.60           C  
ATOM   4395  SD  MET D 360     214.396 145.045 262.676  1.00 89.60           S  
ATOM   4396  CE  MET D 360     214.131 145.967 264.166  1.00 89.60           C  
ATOM   4397  N   CYS D 361     219.174 143.304 263.586  1.00 96.00           N  
ATOM   4398  CA  CYS D 361     219.462 141.907 263.271  1.00 96.00           C  
ATOM   4399  C   CYS D 361     218.127 141.178 263.279  1.00 96.00           C  
ATOM   4400  O   CYS D 361     217.669 140.685 264.309  1.00 96.00           O  
ATOM   4401  CB  CYS D 361     220.448 141.313 264.267  1.00 96.00           C  
ATOM   4402  SG  CYS D 361     222.129 141.952 264.116  1.00 96.00           S  
ATOM   4403  N   THR D 362     217.491 141.123 262.112  1.00 90.96           N  
ATOM   4404  CA  THR D 362     216.125 140.634 262.008  1.00 90.96           C  
ATOM   4405  C   THR D 362     216.087 139.117 262.090  1.00 90.96           C  
ATOM   4406  O   THR D 362     216.820 138.427 261.376  1.00 90.96           O  
ATOM   4407  CB  THR D 362     215.488 141.075 260.694  1.00 90.96           C  
ATOM   4408  OG1 THR D 362     215.716 142.468 260.480  1.00 90.96           O  
ATOM   4409  CG2 THR D 362     213.994 140.824 260.712  1.00 90.96           C  
ATOM   4410  N   LYS D 363     215.226 138.603 262.955  1.00 93.14           N  
ATOM   4411  CA  LYS D 363     214.797 137.218 262.890  1.00 93.14           C  
ATOM   4412  C   LYS D 363     213.399 137.167 262.293  1.00 93.14           C  
ATOM   4413  O   LYS D 363     212.669 138.158 262.281  1.00 93.14           O  
ATOM   4414  CB  LYS D 363     214.812 136.579 264.278  1.00 93.14           C  
ATOM   4415  CG  LYS D 363     216.180 136.565 264.931  1.00 93.14           C  
ATOM   4416  CD  LYS D 363     217.194 135.845 264.060  1.00 93.14           C  
ATOM   4417  CE  LYS D 363     218.564 135.827 264.712  1.00 93.14           C  
ATOM   4418  NZ  LYS D 363     219.102 137.199 264.909  1.00 93.14           N  
ATOM   4419  N   VAL D 364     213.032 136.000 261.776  1.00 92.02           N  
ATOM   4420  CA  VAL D 364     211.750 135.850 261.075  1.00 92.02           C  
ATOM   4421  C   VAL D 364     210.718 135.535 262.150  1.00 92.02           C  
ATOM   4422  O   VAL D 364     210.369 134.385 262.421  1.00 92.02           O  
ATOM   4423  CB  VAL D 364     211.817 134.786 259.978  1.00 92.02           C  
ATOM   4424  CG1 VAL D 364     210.579 134.839 259.121  1.00 92.02           C  
ATOM   4425  CG2 VAL D 364     213.056 134.993 259.130  1.00 92.02           C  
ATOM   4426  N   THR D 365     210.215 136.595 262.784  1.00 92.09           N  
ATOM   4427  CA  THR D 365     209.193 136.504 263.819  1.00 92.09           C  
ATOM   4428  C   THR D 365     208.216 137.659 263.654  1.00 92.09           C  
ATOM   4429  O   THR D 365     208.467 138.613 262.914  1.00 92.09           O  
ATOM   4430  CB  THR D 365     209.789 136.543 265.234  1.00 92.09           C  
ATOM   4431  OG1 THR D 365     210.771 137.582 265.315  1.00 92.09           O  
ATOM   4432  CG2 THR D 365     210.414 135.211 265.624  1.00 92.09           C  
ATOM   4433  N   MET D 366     207.081 137.559 264.351  1.00 89.94           N  
ATOM   4434  CA  MET D 366     206.124 138.661 264.373  1.00 89.94           C  
ATOM   4435  C   MET D 366     206.654 139.838 265.182  1.00 89.94           C  
ATOM   4436  O   MET D 366     206.364 140.997 264.857  1.00 89.94           O  
ATOM   4437  CB  MET D 366     204.785 138.179 264.938  1.00 89.94           C  
ATOM   4438  CG  MET D 366     203.682 139.228 264.953  1.00 89.94           C  
ATOM   4439  SD  MET D 366     202.119 138.631 265.603  1.00 89.94           S  
ATOM   4440  CE  MET D 366     202.516 138.484 267.340  1.00 89.94           C  
ATOM   4441  N   ASP D 367     207.438 139.557 266.226  1.00 87.87           N  
ATOM   4442  CA  ASP D 367     207.977 140.614 267.076  1.00 87.87           C  
ATOM   4443  C   ASP D 367     208.968 141.486 266.318  1.00 87.87           C  
ATOM   4444  O   ASP D 367     208.951 142.713 266.456  1.00 87.87           O  
ATOM   4445  CB  ASP D 367     208.628 140.006 268.313  1.00 87.87           C  
ATOM   4446  CG  ASP D 367     207.618 139.382 269.248  1.00 87.87           C  
ATOM   4447  OD1 ASP D 367     206.457 139.841 269.256  1.00 87.87           O  
ATOM   4448  OD2 ASP D 367     207.981 138.430 269.971  1.00 87.87           O  
ATOM   4449  N   ASP D 368     209.824 140.874 265.498  1.00 88.03           N  
ATOM   4450  CA  ASP D 368     210.738 141.656 264.674  1.00 88.03           C  
ATOM   4451  C   ASP D 368     210.004 142.391 263.564  1.00 88.03           C  
ATOM   4452  O   ASP D 368     210.458 143.448 263.128  1.00 88.03           O  
ATOM   4453  CB  ASP D 368     211.822 140.760 264.085  1.00 88.03           C  
ATOM   4454  CG  ASP D 368     212.916 140.444 265.079  1.00 88.03           C  
ATOM   4455  OD1 ASP D 368     212.639 140.474 266.295  1.00 88.03           O  
ATOM   4456  OD2 ASP D 368     214.053 140.164 264.646  1.00 88.03           O  
ATOM   4457  N   PHE D 369     208.870 141.858 263.110  1.00 81.47           N  
ATOM   4458  CA  PHE D 369     208.027 142.557 262.142  1.00 81.47           C  
ATOM   4459  C   PHE D 369     207.452 143.838 262.742  1.00 81.47           C  
ATOM   4460  O   PHE D 369     207.518 144.918 262.134  1.00 81.47           O  
ATOM   4461  CB  PHE D 369     206.932 141.592 261.685  1.00 81.47           C  
ATOM   4462  CG  PHE D 369     205.834 142.212 260.880  1.00 81.47           C  
ATOM   4463  CD1 PHE D 369     206.015 142.489 259.538  1.00 81.47           C  
ATOM   4464  CD2 PHE D 369     204.595 142.454 261.451  1.00 81.47           C  
ATOM   4465  CE1 PHE D 369     204.994 143.037 258.788  1.00 81.47           C  
ATOM   4466  CE2 PHE D 369     203.573 143.003 260.708  1.00 81.47           C  
ATOM   4467  CZ  PHE D 369     203.773 143.295 259.377  1.00 81.47           C  
ATOM   4468  N   LEU D 370     206.920 143.738 263.963  1.00 77.64           N  
ATOM   4469  CA  LEU D 370     206.395 144.911 264.655  1.00 77.64           C  
ATOM   4470  C   LEU D 370     207.505 145.892 265.011  1.00 77.64           C  
ATOM   4471  O   LEU D 370     207.314 147.112 264.942  1.00 77.64           O  
ATOM   4472  CB  LEU D 370     205.656 144.473 265.916  1.00 77.64           C  
ATOM   4473  CG  LEU D 370     204.384 143.648 265.736  1.00 77.64           C  
ATOM   4474  CD1 LEU D 370     203.631 143.574 267.047  1.00 77.64           C  
ATOM   4475  CD2 LEU D 370     203.506 144.229 264.647  1.00 77.64           C  
ATOM   4476  N   THR D 371     208.682 145.377 265.369  1.00 77.93           N  
ATOM   4477  CA  THR D 371     209.810 146.244 265.680  1.00 77.93           C  
ATOM   4478  C   THR D 371     210.336 146.935 264.428  1.00 77.93           C  
ATOM   4479  O   THR D 371     210.799 148.076 264.502  1.00 77.93           O  
ATOM   4480  CB  THR D 371     210.909 145.438 266.368  1.00 77.93           C  
ATOM   4481  OG1 THR D 371     210.317 144.606 267.371  1.00 77.93           O  
ATOM   4482  CG2 THR D 371     211.880 146.363 267.072  1.00 77.93           C  
ATOM   4483  N   ALA D 372     210.266 146.266 263.276  1.00 77.40           N  
ATOM   4484  CA  ALA D 372     210.635 146.894 262.014  1.00 77.40           C  
ATOM   4485  C   ALA D 372     209.677 148.018 261.662  1.00 77.40           C  
ATOM   4486  O   ALA D 372     210.102 149.066 261.163  1.00 77.40           O  
ATOM   4487  CB  ALA D 372     210.662 145.851 260.900  1.00 77.40           C  
ATOM   4488  N   HIS D 373     208.383 147.820 261.934  1.00 73.75           N  
ATOM   4489  CA  HIS D 373     207.416 148.906 261.775  1.00 73.75           C  
ATOM   4490  C   HIS D 373     207.719 150.066 262.721  1.00 73.75           C  
ATOM   4491  O   HIS D 373     207.618 151.235 262.333  1.00 73.75           O  
ATOM   4492  CB  HIS D 373     206.002 148.381 262.001  1.00 73.75           C  
ATOM   4493  CG  HIS D 373     205.404 147.730 260.796  1.00 73.75           C  
ATOM   4494  ND1 HIS D 373     204.418 148.323 260.040  1.00 73.75           N  
ATOM   4495  CD2 HIS D 373     205.655 146.534 260.215  1.00 73.75           C  
ATOM   4496  CE1 HIS D 373     204.086 147.520 259.045  1.00 73.75           C  
ATOM   4497  NE2 HIS D 373     204.823 146.428 259.128  1.00 73.75           N  
ATOM   4498  N   HIS D 374     208.119 149.752 263.955  1.00 72.36           N  
ATOM   4499  CA  HIS D 374     208.472 150.771 264.945  1.00 72.36           C  
ATOM   4500  C   HIS D 374     209.687 151.592 264.512  1.00 72.36           C  
ATOM   4501  O   HIS D 374     209.673 152.830 264.564  1.00 72.36           O  
ATOM   4502  CB  HIS D 374     208.733 150.075 266.281  1.00 72.36           C  
ATOM   4503  CG  HIS D 374     208.970 151.000 267.432  1.00 72.36           C  
ATOM   4504  ND1 HIS D 374     210.192 151.585 267.680  1.00 72.36           N  
ATOM   4505  CD2 HIS D 374     208.148 151.414 268.422  1.00 72.36           C  
ATOM   4506  CE1 HIS D 374     210.108 152.329 268.767  1.00 72.36           C  
ATOM   4507  NE2 HIS D 374     208.878 152.246 269.234  1.00 72.36           N  
ATOM   4508  N   GLU D 375     210.740 150.919 264.050  1.00 75.69           N  
ATOM   4509  CA  GLU D 375     211.948 151.638 263.659  1.00 75.69           C  
ATOM   4510  C   GLU D 375     211.779 152.356 262.330  1.00 75.69           C  
ATOM   4511  O   GLU D 375     212.409 153.394 262.107  1.00 75.69           O  
ATOM   4512  CB  GLU D 375     213.146 150.692 263.615  1.00 75.69           C  
ATOM   4513  CG  GLU D 375     213.395 149.959 264.920  1.00 75.69           C  
ATOM   4514  CD  GLU D 375     213.930 150.847 266.026  1.00 75.69           C  
ATOM   4515  OE1 GLU D 375     214.468 151.933 265.733  1.00 75.69           O  
ATOM   4516  OE2 GLU D 375     213.801 150.459 267.204  1.00 75.69           O  
ATOM   4517  N   MET D 376     210.916 151.858 261.447  1.00 73.85           N  
ATOM   4518  CA  MET D 376     210.652 152.621 260.238  1.00 73.85           C  
ATOM   4519  C   MET D 376     209.767 153.824 260.543  1.00 73.85           C  
ATOM   4520  O   MET D 376     209.864 154.844 259.859  1.00 73.85           O  
ATOM   4521  CB  MET D 376     210.057 151.714 259.162  1.00 73.85           C  
ATOM   4522  CG  MET D 376     209.899 152.377 257.809  1.00 73.85           C  
ATOM   4523  SD  MET D 376     209.255 151.284 256.549  1.00 73.85           S  
ATOM   4524  CE  MET D 376     210.675 150.230 256.295  1.00 73.85           C  
ATOM   4525  N   GLY D 377     208.933 153.746 261.584  1.00 70.03           N  
ATOM   4526  CA  GLY D 377     208.250 154.941 262.062  1.00 70.03           C  
ATOM   4527  C   GLY D 377     209.208 155.974 262.620  1.00 70.03           C  
ATOM   4528  O   GLY D 377     209.036 157.179 262.398  1.00 70.03           O  
ATOM   4529  N   HIS D 378     210.232 155.509 263.346  1.00 69.65           N  
ATOM   4530  CA  HIS D 378     211.328 156.380 263.774  1.00 69.65           C  
ATOM   4531  C   HIS D 378     212.011 157.047 262.584  1.00 69.65           C  
ATOM   4532  O   HIS D 378     212.283 158.254 262.606  1.00 69.65           O  
ATOM   4533  CB  HIS D 378     212.374 155.574 264.540  1.00 69.65           C  
ATOM   4534  CG  HIS D 378     212.114 155.427 266.003  1.00 69.65           C  
ATOM   4535  ND1 HIS D 378     211.654 156.456 266.791  1.00 69.65           N  
ATOM   4536  CD2 HIS D 378     212.311 154.377 266.833  1.00 69.65           C  
ATOM   4537  CE1 HIS D 378     211.556 156.040 268.040  1.00 69.65           C  
ATOM   4538  NE2 HIS D 378     211.949 154.782 268.093  1.00 69.65           N  
ATOM   4539  N   ILE D 379     212.287 156.271 261.534  1.00 70.01           N  
ATOM   4540  CA  ILE D 379     212.989 156.795 260.365  1.00 70.01           C  
ATOM   4541  C   ILE D 379     212.110 157.774 259.590  1.00 70.01           C  
ATOM   4542  O   ILE D 379     212.599 158.783 259.078  1.00 70.01           O  
ATOM   4543  CB  ILE D 379     213.495 155.631 259.492  1.00 70.01           C  
ATOM   4544  CG1 ILE D 379     214.662 154.939 260.184  1.00 70.01           C  
ATOM   4545  CG2 ILE D 379     213.999 156.103 258.157  1.00 70.01           C  
ATOM   4546  CD1 ILE D 379     215.903 155.805 260.318  1.00 70.01           C  
ATOM   4547  N   GLN D 380     210.804 157.512 259.508  1.00 70.02           N  
ATOM   4548  CA  GLN D 380     209.895 158.448 258.848  1.00 70.02           C  
ATOM   4549  C   GLN D 380     209.799 159.761 259.613  1.00 70.02           C  
ATOM   4550  O   GLN D 380     209.752 160.841 259.004  1.00 70.02           O  
ATOM   4551  CB  GLN D 380     208.511 157.824 258.692  1.00 70.02           C  
ATOM   4552  CG  GLN D 380     208.432 156.757 257.623  1.00 70.02           C  
ATOM   4553  CD  GLN D 380     208.126 157.314 256.256  1.00 70.02           C  
ATOM   4554  OE1 GLN D 380     207.990 158.520 256.083  1.00 70.02           O  
ATOM   4555  NE2 GLN D 380     208.020 156.434 255.272  1.00 70.02           N  
ATOM   4556  N   TYR D 381     209.783 159.682 260.949  1.00 68.87           N  
ATOM   4557  CA  TYR D 381     209.818 160.887 261.771  1.00 68.87           C  
ATOM   4558  C   TYR D 381     211.112 161.661 261.553  1.00 68.87           C  
ATOM   4559  O   TYR D 381     211.092 162.890 261.454  1.00 68.87           O  
ATOM   4560  CB  TYR D 381     209.650 160.509 263.242  1.00 68.87           C  
ATOM   4561  CG  TYR D 381     209.302 161.657 264.158  1.00 68.87           C  
ATOM   4562  CD1 TYR D 381     208.040 162.199 264.166  1.00 68.87           C  
ATOM   4563  CD2 TYR D 381     210.225 162.176 265.029  1.00 68.87           C  
ATOM   4564  CE1 TYR D 381     207.705 163.243 264.992  1.00 68.87           C  
ATOM   4565  CE2 TYR D 381     209.902 163.221 265.870  1.00 68.87           C  
ATOM   4566  CZ  TYR D 381     208.637 163.750 265.843  1.00 68.87           C  
ATOM   4567  OH  TYR D 381     208.292 164.790 266.667  1.00 68.87           O  
ATOM   4568  N   ASP D 382     212.240 160.953 261.432  1.00 70.86           N  
ATOM   4569  CA  ASP D 382     213.512 161.614 261.142  1.00 70.86           C  
ATOM   4570  C   ASP D 382     213.556 162.178 259.729  1.00 70.86           C  
ATOM   4571  O   ASP D 382     214.218 163.192 259.488  1.00 70.86           O  
ATOM   4572  CB  ASP D 382     214.667 160.635 261.331  1.00 70.86           C  
ATOM   4573  CG  ASP D 382     214.928 160.316 262.779  1.00 70.86           C  
ATOM   4574  OD1 ASP D 382     214.502 161.105 263.643  1.00 70.86           O  
ATOM   4575  OD2 ASP D 382     215.554 159.273 263.055  1.00 70.86           O  
ATOM   4576  N   MET D 383     212.871 161.531 258.789  1.00 67.19           N  
ATOM   4577  CA  MET D 383     212.889 161.956 257.398  1.00 67.19           C  
ATOM   4578  C   MET D 383     212.076 163.217 257.206  1.00 67.19           C  
ATOM   4579  O   MET D 383     212.392 164.031 256.334  1.00 67.19           O  
ATOM   4580  CB  MET D 383     212.337 160.848 256.503  1.00 67.19           C  
ATOM   4581  CG  MET D 383     213.383 159.935 255.919  1.00 67.19           C  
ATOM   4582  SD  MET D 383     212.700 158.506 255.070  1.00 67.19           S  
ATOM   4583  CE  MET D 383     211.480 159.292 254.033  1.00 67.19           C  
ATOM   4584  N   ALA D 384     211.012 163.377 257.991  1.00 67.61           N  
ATOM   4585  CA  ALA D 384     210.090 164.474 257.739  1.00 67.61           C  
ATOM   4586  C   ALA D 384     210.671 165.819 258.156  1.00 67.61           C  
ATOM   4587  O   ALA D 384     210.423 166.830 257.491  1.00 67.61           O  
ATOM   4588  CB  ALA D 384     208.779 164.216 258.450  1.00 67.61           C  
ATOM   4589  N   TYR D 385     211.434 165.871 259.253  1.00 66.44           N  
ATOM   4590  CA  TYR D 385     212.000 167.148 259.672  1.00 66.44           C  
ATOM   4591  C   TYR D 385     213.396 167.381 259.114  1.00 66.44           C  
ATOM   4592  O   TYR D 385     214.194 168.091 259.736  1.00 66.44           O  
ATOM   4593  CB  TYR D 385     212.000 167.298 261.200  1.00 66.44           C  
ATOM   4594  CG  TYR D 385     212.612 166.200 262.060  1.00 66.44           C  
ATOM   4595  CD1 TYR D 385     213.968 165.889 262.001  1.00 66.44           C  
ATOM   4596  CD2 TYR D 385     211.845 165.548 263.008  1.00 66.44           C  
ATOM   4597  CE1 TYR D 385     214.516 164.919 262.804  1.00 66.44           C  
ATOM   4598  CE2 TYR D 385     212.391 164.581 263.820  1.00 66.44           C  
ATOM   4599  CZ  TYR D 385     213.722 164.269 263.712  1.00 66.44           C  
ATOM   4600  OH  TYR D 385     214.264 163.302 264.521  1.00 66.44           O  
ATOM   4601  N   ALA D 386     213.711 166.813 257.952  1.00 67.10           N  
ATOM   4602  CA  ALA D 386     215.008 167.051 257.338  1.00 67.10           C  
ATOM   4603  C   ALA D 386     215.133 168.471 256.806  1.00 67.10           C  
ATOM   4604  O   ALA D 386     216.252 168.979 256.684  1.00 67.10           O  
ATOM   4605  CB  ALA D 386     215.253 166.041 256.220  1.00 67.10           C  
ATOM   4606  N   ALA D 387     214.013 169.123 256.499  1.00 68.81           N  
ATOM   4607  CA  ALA D 387     214.025 170.502 256.037  1.00 68.81           C  
ATOM   4608  C   ALA D 387     214.270 171.494 257.162  1.00 68.81           C  
ATOM   4609  O   ALA D 387     214.553 172.663 256.884  1.00 68.81           O  
ATOM   4610  CB  ALA D 387     212.706 170.834 255.340  1.00 68.81           C  
ATOM   4611  N   GLN D 388     214.156 171.061 258.413  1.00 67.60           N  
ATOM   4612  CA  GLN D 388     214.393 171.930 259.547  1.00 67.60           C  
ATOM   4613  C   GLN D 388     215.884 172.230 259.678  1.00 67.60           C  
ATOM   4614  O   GLN D 388     216.718 171.514 259.120  1.00 67.60           O  
ATOM   4615  CB  GLN D 388     213.875 171.274 260.825  1.00 67.60           C  
ATOM   4616  CG  GLN D 388     212.391 171.022 260.829  1.00 67.60           C  
ATOM   4617  CD  GLN D 388     211.597 172.302 260.854  1.00 67.60           C  
ATOM   4618  OE1 GLN D 388     211.992 173.274 261.487  1.00 67.60           O  
ATOM   4619  NE2 GLN D 388     210.463 172.308 260.171  1.00 67.60           N  
ATOM   4620  N   PRO D 389     216.244 173.300 260.391  1.00 68.26           N  
ATOM   4621  CA  PRO D 389     217.648 173.492 260.767  1.00 68.26           C  
ATOM   4622  C   PRO D 389     218.124 172.377 261.684  1.00 68.26           C  
ATOM   4623  O   PRO D 389     217.326 171.682 262.315  1.00 68.26           O  
ATOM   4624  CB  PRO D 389     217.647 174.847 261.484  1.00 68.26           C  
ATOM   4625  CG  PRO D 389     216.214 175.147 261.759  1.00 68.26           C  
ATOM   4626  CD  PRO D 389     215.459 174.516 260.652  1.00 68.26           C  
ATOM   4627  N   PHE D 390     219.453 172.222 261.745  1.00 69.54           N  
ATOM   4628  CA  PHE D 390     220.068 171.035 262.339  1.00 69.54           C  
ATOM   4629  C   PHE D 390     219.753 170.909 263.820  1.00 69.54           C  
ATOM   4630  O   PHE D 390     219.482 169.809 264.315  1.00 69.54           O  
ATOM   4631  CB  PHE D 390     221.582 171.077 262.145  1.00 69.54           C  
ATOM   4632  CG  PHE D 390     222.323 170.048 262.950  1.00 69.54           C  
ATOM   4633  CD1 PHE D 390     222.266 168.711 262.602  1.00 69.54           C  
ATOM   4634  CD2 PHE D 390     223.048 170.411 264.072  1.00 69.54           C  
ATOM   4635  CE1 PHE D 390     222.937 167.762 263.342  1.00 69.54           C  
ATOM   4636  CE2 PHE D 390     223.716 169.466 264.817  1.00 69.54           C  
ATOM   4637  CZ  PHE D 390     223.660 168.141 264.451  1.00 69.54           C  
ATOM   4638  N   LEU D 391     219.771 172.020 264.540  1.00 69.79           N  
ATOM   4639  CA  LEU D 391     219.555 171.975 265.974  1.00 69.79           C  
ATOM   4640  C   LEU D 391     218.086 171.826 266.344  1.00 69.79           C  
ATOM   4641  O   LEU D 391     217.777 171.625 267.521  1.00 69.79           O  
ATOM   4642  CB  LEU D 391     220.152 173.231 266.599  1.00 69.79           C  
ATOM   4643  CG  LEU D 391     220.804 173.064 267.963  1.00 69.79           C  
ATOM   4644  CD1 LEU D 391     221.767 171.895 267.951  1.00 69.79           C  
ATOM   4645  CD2 LEU D 391     221.553 174.321 268.252  1.00 69.79           C  
ATOM   4646  N   LEU D 392     217.180 171.915 265.373  1.00 69.87           N  
ATOM   4647  CA  LEU D 392     215.763 171.670 265.580  1.00 69.87           C  
ATOM   4648  C   LEU D 392     215.324 170.315 265.041  1.00 69.87           C  
ATOM   4649  O   LEU D 392     214.125 170.032 265.000  1.00 69.87           O  
ATOM   4650  CB  LEU D 392     214.947 172.782 264.926  1.00 69.87           C  
ATOM   4651  CG  LEU D 392     215.022 174.136 265.627  1.00 69.87           C  
ATOM   4652  CD1 LEU D 392     214.126 175.139 264.940  1.00 69.87           C  
ATOM   4653  CD2 LEU D 392     214.674 174.017 267.095  1.00 69.87           C  
ATOM   4654  N   ARG D 393     216.269 169.480 264.615  1.00 68.18           N  
ATOM   4655  CA  ARG D 393     215.967 168.165 264.051  1.00 68.18           C  
ATOM   4656  C   ARG D 393     215.838 167.135 265.172  1.00 68.18           C  
ATOM   4657  O   ARG D 393     216.706 166.292 265.397  1.00 68.18           O  
ATOM   4658  CB  ARG D 393     217.043 167.762 263.054  1.00 68.18           C  
ATOM   4659  CG  ARG D 393     216.934 168.441 261.718  1.00 68.18           C  
ATOM   4660  CD  ARG D 393     218.074 168.026 260.825  1.00 68.18           C  
ATOM   4661  NE  ARG D 393     218.302 169.003 259.772  1.00 68.18           N  
ATOM   4662  CZ  ARG D 393     219.402 169.064 259.038  1.00 68.18           C  
ATOM   4663  NH1 ARG D 393     220.402 168.220 259.221  1.00 68.18           N  
ATOM   4664  NH2 ARG D 393     219.504 170.000 258.100  1.00 68.18           N  
ATOM   4665  N   ASN D 394     214.713 167.212 265.872  1.00 71.16           N  
ATOM   4666  CA  ASN D 394     214.400 166.285 266.948  1.00 71.16           C  
ATOM   4667  C   ASN D 394     212.890 166.220 267.097  1.00 71.16           C  
ATOM   4668  O   ASN D 394     212.149 166.908 266.394  1.00 71.16           O  
ATOM   4669  CB  ASN D 394     215.052 166.715 268.264  1.00 71.16           C  
ATOM   4670  CG  ASN D 394     216.390 166.060 268.493  1.00 71.16           C  
ATOM   4671  OD1 ASN D 394     216.469 164.956 269.028  1.00 71.16           O  
ATOM   4672  ND2 ASN D 394     217.457 166.740 268.094  1.00 71.16           N  
ATOM   4673  N   GLY D 395     212.433 165.378 268.016  1.00 70.84           N  
ATOM   4674  CA  GLY D 395     211.046 165.429 268.413  1.00 70.84           C  
ATOM   4675  C   GLY D 395     210.752 166.689 269.196  1.00 70.84           C  
ATOM   4676  O   GLY D 395     211.647 167.317 269.762  1.00 70.84           O  
ATOM   4677  N   ALA D 396     209.475 167.079 269.209  1.00 71.17           N  
ATOM   4678  CA  ALA D 396     209.097 168.309 269.897  1.00 71.17           C  
ATOM   4679  C   ALA D 396     209.257 168.174 271.405  1.00 71.17           C  
ATOM   4680  O   ALA D 396     209.565 169.158 272.085  1.00 71.17           O  
ATOM   4681  CB  ALA D 396     207.678 168.715 269.524  1.00 71.17           C  
ATOM   4682  N   ASN D 397     209.051 166.976 271.941  1.00 70.98           N  
ATOM   4683  CA  ASN D 397     209.583 166.607 273.241  1.00 70.98           C  
ATOM   4684  C   ASN D 397     210.089 165.177 273.127  1.00 70.98           C  
ATOM   4685  O   ASN D 397     210.060 164.576 272.051  1.00 70.98           O  
ATOM   4686  CB  ASN D 397     208.560 166.768 274.371  1.00 70.98           C  
ATOM   4687  CG  ASN D 397     207.219 166.160 274.052  1.00 70.98           C  
ATOM   4688  OD1 ASN D 397     207.036 165.516 273.023  1.00 70.98           O  
ATOM   4689  ND2 ASN D 397     206.266 166.359 274.947  1.00 70.98           N  
ATOM   4690  N   GLU D 398     210.565 164.628 274.241  1.00 75.81           N  
ATOM   4691  CA  GLU D 398     211.175 163.307 274.210  1.00 75.81           C  
ATOM   4692  C   GLU D 398     210.162 162.178 274.058  1.00 75.81           C  
ATOM   4693  O   GLU D 398     210.565 161.048 273.768  1.00 75.81           O  
ATOM   4694  CB  GLU D 398     211.993 163.101 275.480  1.00 75.81           C  
ATOM   4695  CG  GLU D 398     211.280 163.568 276.734  1.00 75.81           C  
ATOM   4696  CD  GLU D 398     212.103 163.364 277.984  1.00 75.81           C  
ATOM   4697  OE1 GLU D 398     213.342 163.265 277.872  1.00 75.81           O  
ATOM   4698  OE2 GLU D 398     211.513 163.298 279.081  1.00 75.81           O  
ATOM   4699  N   GLY D 399     208.870 162.449 274.245  1.00 70.27           N  
ATOM   4700  CA  GLY D 399     207.871 161.407 274.102  1.00 70.27           C  
ATOM   4701  C   GLY D 399     207.428 161.159 272.678  1.00 70.27           C  
ATOM   4702  O   GLY D 399     207.051 160.030 272.337  1.00 70.27           O  
ATOM   4703  N   PHE D 400     207.473 162.198 271.831  1.00 67.60           N  
ATOM   4704  CA  PHE D 400     206.888 162.130 270.494  1.00 67.60           C  
ATOM   4705  C   PHE D 400     207.610 161.139 269.601  1.00 67.60           C  
ATOM   4706  O   PHE D 400     206.973 160.453 268.789  1.00 67.60           O  
ATOM   4707  CB  PHE D 400     206.922 163.497 269.813  1.00 67.60           C  
ATOM   4708  CG  PHE D 400     205.848 164.438 270.250  1.00 67.60           C  
ATOM   4709  CD1 PHE D 400     204.837 164.033 271.085  1.00 67.60           C  
ATOM   4710  CD2 PHE D 400     205.811 165.715 269.748  1.00 67.60           C  
ATOM   4711  CE1 PHE D 400     203.844 164.913 271.467  1.00 67.60           C  
ATOM   4712  CE2 PHE D 400     204.820 166.592 270.118  1.00 67.60           C  
ATOM   4713  CZ  PHE D 400     203.837 166.189 270.978  1.00 67.60           C  
ATOM   4714  N   HIS D 401     208.937 161.070 269.730  1.00 68.50           N  
ATOM   4715  CA  HIS D 401     209.740 160.259 268.825  1.00 68.50           C  
ATOM   4716  C   HIS D 401     209.423 158.779 268.982  1.00 68.50           C  
ATOM   4717  O   HIS D 401     209.271 158.062 267.990  1.00 68.50           O  
ATOM   4718  CB  HIS D 401     211.222 160.517 269.069  1.00 68.50           C  
ATOM   4719  CG  HIS D 401     212.036 160.528 267.817  1.00 68.50           C  
ATOM   4720  ND1 HIS D 401     212.293 159.392 267.085  1.00 68.50           N  
ATOM   4721  CD2 HIS D 401     212.683 161.536 267.189  1.00 68.50           C  
ATOM   4722  CE1 HIS D 401     213.034 159.705 266.038  1.00 68.50           C  
ATOM   4723  NE2 HIS D 401     213.284 161.000 266.078  1.00 68.50           N  
ATOM   4724  N   GLU D 402     209.289 158.309 270.219  1.00 71.25           N  
ATOM   4725  CA  GLU D 402     208.889 156.925 270.424  1.00 71.25           C  
ATOM   4726  C   GLU D 402     207.392 156.720 270.238  1.00 71.25           C  
ATOM   4727  O   GLU D 402     206.974 155.611 269.882  1.00 71.25           O  
ATOM   4728  CB  GLU D 402     209.336 156.437 271.797  1.00 71.25           C  
ATOM   4729  CG  GLU D 402     210.810 156.644 272.050  1.00 71.25           C  
ATOM   4730  CD  GLU D 402     211.652 155.516 271.488  1.00 71.25           C  
ATOM   4731  OE1 GLU D 402     211.083 154.460 271.142  1.00 71.25           O  
ATOM   4732  OE2 GLU D 402     212.883 155.689 271.386  1.00 71.25           O  
ATOM   4733  N   ALA D 403     206.575 157.757 270.471  1.00 65.58           N  
ATOM   4734  CA  ALA D 403     205.132 157.604 270.315  1.00 65.58           C  
ATOM   4735  C   ALA D 403     204.752 157.372 268.857  1.00 65.58           C  
ATOM   4736  O   ALA D 403     203.870 156.555 268.561  1.00 65.58           O  
ATOM   4737  CB  ALA D 403     204.412 158.830 270.870  1.00 65.58           C  
ATOM   4738  N   VAL D 404     205.418 158.067 267.930  1.00 65.52           N  
ATOM   4739  CA  VAL D 404     205.089 157.903 266.518  1.00 65.52           C  
ATOM   4740  C   VAL D 404     205.572 156.580 265.945  1.00 65.52           C  
ATOM   4741  O   VAL D 404     205.149 156.210 264.848  1.00 65.52           O  
ATOM   4742  CB  VAL D 404     205.651 159.044 265.649  1.00 65.52           C  
ATOM   4743  CG1 VAL D 404     205.067 160.373 266.075  1.00 65.52           C  
ATOM   4744  CG2 VAL D 404     207.154 159.059 265.697  1.00 65.52           C  
ATOM   4745  N   GLY D 405     206.449 155.862 266.642  1.00 66.89           N  
ATOM   4746  CA  GLY D 405     206.819 154.523 266.228  1.00 66.89           C  
ATOM   4747  C   GLY D 405     205.905 153.498 266.861  1.00 66.89           C  
ATOM   4748  O   GLY D 405     205.558 152.471 266.256  1.00 66.89           O  
ATOM   4749  N   GLU D 406     205.481 153.785 268.091  1.00 69.22           N  
ATOM   4750  CA  GLU D 406     204.592 152.859 268.771  1.00 69.22           C  
ATOM   4751  C   GLU D 406     203.187 152.874 268.188  1.00 69.22           C  
ATOM   4752  O   GLU D 406     202.487 151.865 268.289  1.00 69.22           O  
ATOM   4753  CB  GLU D 406     204.551 153.167 270.262  1.00 69.22           C  
ATOM   4754  CG  GLU D 406     205.803 152.747 271.000  1.00 69.22           C  
ATOM   4755  CD  GLU D 406     205.730 151.325 271.506  1.00 69.22           C  
ATOM   4756  OE1 GLU D 406     204.612 150.774 271.571  1.00 69.22           O  
ATOM   4757  OE2 GLU D 406     206.791 150.756 271.836  1.00 69.22           O  
ATOM   4758  N   ILE D 407     202.763 153.973 267.555  1.00 65.91           N  
ATOM   4759  CA  ILE D 407     201.467 153.931 266.874  1.00 65.91           C  
ATOM   4760  C   ILE D 407     201.525 153.040 265.632  1.00 65.91           C  
ATOM   4761  O   ILE D 407     200.536 152.376 265.292  1.00 65.91           O  
ATOM   4762  CB  ILE D 407     200.950 155.343 266.542  1.00 65.91           C  
ATOM   4763  CG1 ILE D 407     201.928 156.127 265.676  1.00 65.91           C  
ATOM   4764  CG2 ILE D 407     200.666 156.105 267.804  1.00 65.91           C  
ATOM   4765  CD1 ILE D 407     201.341 157.394 265.113  1.00 65.91           C  
ATOM   4766  N   MET D 408     202.671 152.993 264.943  1.00 70.06           N  
ATOM   4767  CA  MET D 408     202.830 152.060 263.831  1.00 70.06           C  
ATOM   4768  C   MET D 408     202.858 150.624 264.320  1.00 70.06           C  
ATOM   4769  O   MET D 408     202.300 149.728 263.673  1.00 70.06           O  
ATOM   4770  CB  MET D 408     204.114 152.362 263.070  1.00 70.06           C  
ATOM   4771  CG  MET D 408     204.317 153.809 262.759  1.00 70.06           C  
ATOM   4772  SD  MET D 408     202.798 154.667 262.364  1.00 70.06           S  
ATOM   4773  CE  MET D 408     203.487 156.225 261.847  1.00 70.06           C  
ATOM   4774  N   SER D 409     203.502 150.392 265.466  1.00 71.08           N  
ATOM   4775  CA  SER D 409     203.470 149.065 266.074  1.00 71.08           C  
ATOM   4776  C   SER D 409     202.064 148.685 266.528  1.00 71.08           C  
ATOM   4777  O   SER D 409     201.724 147.498 266.555  1.00 71.08           O  
ATOM   4778  CB  SER D 409     204.446 149.000 267.244  1.00 71.08           C  
ATOM   4779  OG  SER D 409     204.296 147.784 267.953  1.00 71.08           O  
ATOM   4780  N   LEU D 410     201.245 149.673 266.898  1.00 67.83           N  
ATOM   4781  CA  LEU D 410     199.845 149.417 267.222  1.00 67.83           C  
ATOM   4782  C   LEU D 410     199.059 149.014 265.984  1.00 67.83           C  
ATOM   4783  O   LEU D 410     198.301 148.039 266.009  1.00 67.83           O  
ATOM   4784  CB  LEU D 410     199.213 150.656 267.856  1.00 67.83           C  
ATOM   4785  CG  LEU D 410     199.428 150.912 269.341  1.00 67.83           C  
ATOM   4786  CD1 LEU D 410     198.596 152.091 269.789  1.00 67.83           C  
ATOM   4787  CD2 LEU D 410     199.044 149.683 270.113  1.00 67.83           C  
ATOM   4788  N   SER D 411     199.212 149.770 264.895  1.00 72.07           N  
ATOM   4789  CA  SER D 411     198.370 149.539 263.727  1.00 72.07           C  
ATOM   4790  C   SER D 411     198.779 148.281 262.976  1.00 72.07           C  
ATOM   4791  O   SER D 411     197.924 147.610 262.392  1.00 72.07           O  
ATOM   4792  CB  SER D 411     198.413 150.745 262.795  1.00 72.07           C  
ATOM   4793  OG  SER D 411     197.928 151.901 263.449  1.00 72.07           O  
ATOM   4794  N   ALA D 412     200.070 147.942 262.975  1.00 72.42           N  
ATOM   4795  CA  ALA D 412     200.512 146.761 262.246  1.00 72.42           C  
ATOM   4796  C   ALA D 412     200.152 145.465 262.960  1.00 72.42           C  
ATOM   4797  O   ALA D 412     200.107 144.413 262.318  1.00 72.42           O  
ATOM   4798  CB  ALA D 412     202.019 146.819 262.011  1.00 72.42           C  
ATOM   4799  N   ALA D 413     199.888 145.516 264.262  1.00 75.56           N  
ATOM   4800  CA  ALA D 413     199.606 144.327 265.053  1.00 75.56           C  
ATOM   4801  C   ALA D 413     198.140 143.923 265.034  1.00 75.56           C  
ATOM   4802  O   ALA D 413     197.791 142.898 265.627  1.00 75.56           O  
ATOM   4803  CB  ALA D 413     200.045 144.545 266.501  1.00 75.56           C  
ATOM   4804  N   THR D 414     197.282 144.700 264.384  1.00 77.46           N  
ATOM   4805  CA  THR D 414     195.863 144.396 264.353  1.00 77.46           C  
ATOM   4806  C   THR D 414     195.602 143.181 263.465  1.00 77.46           C  
ATOM   4807  O   THR D 414     196.357 142.925 262.526  1.00 77.46           O  
ATOM   4808  CB  THR D 414     195.079 145.596 263.840  1.00 77.46           C  
ATOM   4809  OG1 THR D 414     195.449 145.858 262.484  1.00 77.46           O  
ATOM   4810  CG2 THR D 414     195.384 146.813 264.679  1.00 77.46           C  
ATOM   4811  N   PRO D 415     194.567 142.391 263.774  1.00 81.64           N  
ATOM   4812  CA  PRO D 415     194.219 141.264 262.894  1.00 81.64           C  
ATOM   4813  C   PRO D 415     193.796 141.684 261.502  1.00 81.64           C  
ATOM   4814  O   PRO D 415     194.000 140.919 260.553  1.00 81.64           O  
ATOM   4815  CB  PRO D 415     193.069 140.586 263.646  1.00 81.64           C  
ATOM   4816  CG  PRO D 415     193.310 140.932 265.061  1.00 81.64           C  
ATOM   4817  CD  PRO D 415     193.794 142.348 265.025  1.00 81.64           C  
ATOM   4818  N   LYS D 416     193.213 142.876 261.356  1.00 80.95           N  
ATOM   4819  CA  LYS D 416     192.808 143.362 260.042  1.00 80.95           C  
ATOM   4820  C   LYS D 416     194.014 143.595 259.141  1.00 80.95           C  
ATOM   4821  O   LYS D 416     193.988 143.244 257.955  1.00 80.95           O  
ATOM   4822  CB  LYS D 416     192.001 144.648 260.196  1.00 80.95           C  
ATOM   4823  CG  LYS D 416     191.460 145.210 258.897  1.00 80.95           C  
ATOM   4824  CD  LYS D 416     190.313 146.180 259.138  1.00 80.95           C  
ATOM   4825  CE  LYS D 416     190.672 147.233 260.174  1.00 80.95           C  
ATOM   4826  NZ  LYS D 416     189.532 148.148 260.444  1.00 80.95           N  
ATOM   4827  N   HIS D 417     195.086 144.166 259.694  1.00 77.60           N  
ATOM   4828  CA  HIS D 417     196.286 144.405 258.905  1.00 77.60           C  
ATOM   4829  C   HIS D 417     196.995 143.108 258.548  1.00 77.60           C  
ATOM   4830  O   HIS D 417     197.573 143.000 257.463  1.00 77.60           O  
ATOM   4831  CB  HIS D 417     197.239 145.323 259.662  1.00 77.60           C  
ATOM   4832  CG  HIS D 417     198.376 145.823 258.832  1.00 77.60           C  
ATOM   4833  ND1 HIS D 417     199.634 145.264 258.878  1.00 77.60           N  
ATOM   4834  CD2 HIS D 417     198.444 146.828 257.929  1.00 77.60           C  
ATOM   4835  CE1 HIS D 417     200.428 145.905 258.041  1.00 77.60           C  
ATOM   4836  NE2 HIS D 417     199.730 146.859 257.452  1.00 77.60           N  
ATOM   4837  N   LEU D 418     196.954 142.117 259.438  1.00 82.19           N  
ATOM   4838  CA  LEU D 418     197.581 140.837 259.140  1.00 82.19           C  
ATOM   4839  C   LEU D 418     196.769 140.029 258.136  1.00 82.19           C  
ATOM   4840  O   LEU D 418     197.342 139.250 257.369  1.00 82.19           O  
ATOM   4841  CB  LEU D 418     197.789 140.051 260.430  1.00 82.19           C  
ATOM   4842  CG  LEU D 418     198.681 140.737 261.463  1.00 82.19           C  
ATOM   4843  CD1 LEU D 418     198.800 139.889 262.709  1.00 82.19           C  
ATOM   4844  CD2 LEU D 418     200.047 141.021 260.883  1.00 82.19           C  
ATOM   4845  N   LYS D 419     195.444 140.192 258.122  1.00 87.75           N  
ATOM   4846  CA  LYS D 419     194.651 139.614 257.042  1.00 87.75           C  
ATOM   4847  C   LYS D 419     194.852 140.369 255.740  1.00 87.75           C  
ATOM   4848  O   LYS D 419     194.682 139.794 254.660  1.00 87.75           O  
ATOM   4849  CB  LYS D 419     193.166 139.584 257.403  1.00 87.75           C  
ATOM   4850  CG  LYS D 419     192.818 138.649 258.542  1.00 87.75           C  
ATOM   4851  CD  LYS D 419     191.316 138.478 258.687  1.00 87.75           C  
ATOM   4852  CE  LYS D 419     190.629 139.802 258.971  1.00 87.75           C  
ATOM   4853  NZ  LYS D 419     189.312 139.614 259.640  1.00 87.75           N  
ATOM   4854  N   SER D 420     195.206 141.651 255.822  1.00 87.09           N  
ATOM   4855  CA  SER D 420     195.402 142.450 254.619  1.00 87.09           C  
ATOM   4856  C   SER D 420     196.658 142.039 253.864  1.00 87.09           C  
ATOM   4857  O   SER D 420     196.658 142.000 252.629  1.00 87.09           O  
ATOM   4858  CB  SER D 420     195.467 143.929 254.988  1.00 87.09           C  
ATOM   4859  OG  SER D 420     196.000 144.695 253.925  1.00 87.09           O  
ATOM   4860  N   ILE D 421     197.738 141.728 254.579  1.00 82.71           N  
ATOM   4861  CA  ILE D 421     199.017 141.439 253.947  1.00 82.71           C  
ATOM   4862  C   ILE D 421     199.266 139.942 253.811  1.00 82.71           C  
ATOM   4863  O   ILE D 421     200.356 139.535 253.401  1.00 82.71           O  
ATOM   4864  CB  ILE D 421     200.166 142.117 254.703  1.00 82.71           C  
ATOM   4865  CG1 ILE D 421     200.322 141.494 256.087  1.00 82.71           C  
ATOM   4866  CG2 ILE D 421     199.923 143.610 254.802  1.00 82.71           C  
ATOM   4867  CD1 ILE D 421     201.383 142.144 256.922  1.00 82.71           C  
ATOM   4868  N   GLY D 422     198.280 139.113 254.130  1.00 87.21           N  
ATOM   4869  CA  GLY D 422     198.363 137.696 253.862  1.00 87.21           C  
ATOM   4870  C   GLY D 422     198.990 136.849 254.947  1.00 87.21           C  
ATOM   4871  O   GLY D 422     199.073 135.627 254.776  1.00 87.21           O  
ATOM   4872  N   LEU D 423     199.435 137.446 256.054  1.00 89.04           N  
ATOM   4873  CA  LEU D 423     199.972 136.639 257.144  1.00 89.04           C  
ATOM   4874  C   LEU D 423     198.883 135.909 257.905  1.00 89.04           C  
ATOM   4875  O   LEU D 423     199.109 134.799 258.393  1.00 89.04           O  
ATOM   4876  CB  LEU D 423     200.767 137.505 258.113  1.00 89.04           C  
ATOM   4877  CG  LEU D 423     202.056 138.090 257.568  1.00 89.04           C  
ATOM   4878  CD1 LEU D 423     202.660 139.037 258.571  1.00 89.04           C  
ATOM   4879  CD2 LEU D 423     203.000 136.947 257.288  1.00 89.04           C  
ATOM   4880  N   LEU D 424     197.704 136.493 258.017  1.00 94.90           N  
ATOM   4881  CA  LEU D 424     196.621 135.873 258.755  1.00 94.90           C  
ATOM   4882  C   LEU D 424     195.550 135.451 257.764  1.00 94.90           C  
ATOM   4883  O   LEU D 424     195.278 136.164 256.794  1.00 94.90           O  
ATOM   4884  CB  LEU D 424     196.067 136.833 259.807  1.00 94.90           C  
ATOM   4885  CG  LEU D 424     194.979 136.329 260.741  1.00 94.90           C  
ATOM   4886  CD1 LEU D 424     195.529 135.181 261.557  1.00 94.90           C  
ATOM   4887  CD2 LEU D 424     194.548 137.451 261.654  1.00 94.90           C  
ATOM   4888  N   SER D 425     194.976 134.274 257.995  1.00102.04           N  
ATOM   4889  CA  SER D 425     194.020 133.705 257.065  1.00102.04           C  
ATOM   4890  C   SER D 425     192.731 134.526 257.050  1.00102.04           C  
ATOM   4891  O   SER D 425     192.329 135.079 258.075  1.00102.04           O  
ATOM   4892  CB  SER D 425     193.713 132.261 257.447  1.00102.04           C  
ATOM   4893  OG  SER D 425     193.014 132.206 258.677  1.00102.04           O  
ATOM   4894  N   PRO D 426     192.066 134.625 255.893  1.00105.98           N  
ATOM   4895  CA  PRO D 426     190.770 135.318 255.848  1.00105.98           C  
ATOM   4896  C   PRO D 426     189.655 134.590 256.576  1.00105.98           C  
ATOM   4897  O   PRO D 426     188.608 135.199 256.827  1.00105.98           O  
ATOM   4898  CB  PRO D 426     190.479 135.415 254.347  1.00105.98           C  
ATOM   4899  CG  PRO D 426     191.218 134.273 253.754  1.00105.98           C  
ATOM   4900  CD  PRO D 426     192.476 134.148 254.562  1.00105.98           C  
ATOM   4901  N   ASP D 427     189.840 133.318 256.924  1.00110.82           N  
ATOM   4902  CA  ASP D 427     188.863 132.570 257.696  1.00110.82           C  
ATOM   4903  C   ASP D 427     189.148 132.614 259.190  1.00110.82           C  
ATOM   4904  O   ASP D 427     188.617 131.786 259.938  1.00110.82           O  
ATOM   4905  CB  ASP D 427     188.813 131.121 257.213  1.00110.82           C  
ATOM   4906  CG  ASP D 427     188.236 130.995 255.821  1.00110.82           C  
ATOM   4907  OD1 ASP D 427     187.402 131.844 255.445  1.00110.82           O  
ATOM   4908  OD2 ASP D 427     188.619 130.049 255.101  1.00110.82           O  
ATOM   4909  N   PHE D 428     189.983 133.548 259.639  1.00109.01           N  
ATOM   4910  CA  PHE D 428     190.294 133.666 261.055  1.00109.01           C  
ATOM   4911  C   PHE D 428     189.123 134.319 261.776  1.00109.01           C  
ATOM   4912  O   PHE D 428     188.610 135.352 261.337  1.00109.01           O  
ATOM   4913  CB  PHE D 428     191.570 134.482 261.253  1.00109.01           C  
ATOM   4914  CG  PHE D 428     191.994 134.611 262.686  1.00109.01           C  
ATOM   4915  CD1 PHE D 428     192.597 133.549 263.339  1.00109.01           C  
ATOM   4916  CD2 PHE D 428     191.804 135.797 263.375  1.00109.01           C  
ATOM   4917  CE1 PHE D 428     192.994 133.665 264.659  1.00109.01           C  
ATOM   4918  CE2 PHE D 428     192.198 135.921 264.693  1.00109.01           C  
ATOM   4919  CZ  PHE D 428     192.794 134.853 265.336  1.00109.01           C  
ATOM   4920  N   GLN D 429     188.703 133.715 262.881  1.00110.67           N  
ATOM   4921  CA  GLN D 429     187.587 134.223 263.665  1.00110.67           C  
ATOM   4922  C   GLN D 429     188.104 135.126 264.775  1.00110.67           C  
ATOM   4923  O   GLN D 429     188.846 134.675 265.653  1.00110.67           O  
ATOM   4924  CB  GLN D 429     186.772 133.069 264.245  1.00110.67           C  
ATOM   4925  CG  GLN D 429     186.113 132.207 263.188  1.00110.67           C  
ATOM   4926  CD  GLN D 429     185.051 132.957 262.412  1.00110.67           C  
ATOM   4927  OE1 GLN D 429     184.303 133.757 262.975  1.00110.67           O  
ATOM   4928  NE2 GLN D 429     184.981 132.706 261.110  1.00110.67           N  
ATOM   4929  N   GLU D 430     187.717 136.397 264.733  1.00110.25           N  
ATOM   4930  CA  GLU D 430     188.104 137.367 265.754  1.00110.25           C  
ATOM   4931  C   GLU D 430     186.932 137.503 266.718  1.00110.25           C  
ATOM   4932  O   GLU D 430     186.057 138.351 266.544  1.00110.25           O  
ATOM   4933  CB  GLU D 430     188.478 138.713 265.142  1.00110.25           C  
ATOM   4934  CG  GLU D 430     189.706 138.706 264.244  1.00110.25           C  
ATOM   4935  CD  GLU D 430     189.386 138.334 262.808  1.00110.25           C  
ATOM   4936  OE1 GLU D 430     188.195 138.118 262.499  1.00110.25           O  
ATOM   4937  OE2 GLU D 430     190.324 138.270 261.984  1.00110.25           O  
ATOM   4938  N   ASP D 431     186.913 136.659 267.745  1.00107.44           N  
ATOM   4939  CA  ASP D 431     185.877 136.744 268.758  1.00107.44           C  
ATOM   4940  C   ASP D 431     186.357 137.640 269.896  1.00107.44           C  
ATOM   4941  O   ASP D 431     187.479 138.150 269.881  1.00107.44           O  
ATOM   4942  CB  ASP D 431     185.482 135.349 269.246  1.00107.44           C  
ATOM   4943  CG  ASP D 431     186.679 134.484 269.607  1.00107.44           C  
ATOM   4944  OD1 ASP D 431     187.828 134.957 269.497  1.00107.44           O  
ATOM   4945  OD2 ASP D 431     186.467 133.320 270.004  1.00107.44           O  
ATOM   4946  N   ASN D 432     185.502 137.840 270.900  1.00106.54           N  
ATOM   4947  CA  ASN D 432     185.849 138.770 271.966  1.00106.54           C  
ATOM   4948  C   ASN D 432     186.902 138.218 272.919  1.00106.54           C  
ATOM   4949  O   ASN D 432     187.573 139.008 273.588  1.00106.54           O  
ATOM   4950  CB  ASN D 432     184.601 139.180 272.748  1.00106.54           C  
ATOM   4951  CG  ASN D 432     183.717 138.008 273.100  1.00106.54           C  
ATOM   4952  OD1 ASN D 432     184.080 136.850 272.901  1.00106.54           O  
ATOM   4953  ND2 ASN D 432     182.545 138.308 273.638  1.00106.54           N  
ATOM   4954  N   GLU D 433     187.062 136.895 272.998  1.00100.60           N  
ATOM   4955  CA  GLU D 433     187.998 136.319 273.961  1.00100.60           C  
ATOM   4956  C   GLU D 433     189.444 136.589 273.564  1.00100.60           C  
ATOM   4957  O   GLU D 433     190.278 136.928 274.416  1.00100.60           O  
ATOM   4958  CB  GLU D 433     187.746 134.821 274.113  1.00100.60           C  
ATOM   4959  CG  GLU D 433     186.428 134.497 274.793  1.00100.60           C  
ATOM   4960  CD  GLU D 433     186.183 133.009 274.924  1.00100.60           C  
ATOM   4961  OE1 GLU D 433     186.972 132.223 274.363  1.00100.60           O  
ATOM   4962  OE2 GLU D 433     185.203 132.624 275.593  1.00100.60           O  
ATOM   4963  N   THR D 434     189.762 136.453 272.275  1.00 96.48           N  
ATOM   4964  CA  THR D 434     191.112 136.774 271.832  1.00 96.48           C  
ATOM   4965  C   THR D 434     191.359 138.278 271.871  1.00 96.48           C  
ATOM   4966  O   THR D 434     192.498 138.708 272.063  1.00 96.48           O  
ATOM   4967  CB  THR D 434     191.383 136.184 270.442  1.00 96.48           C  
ATOM   4968  OG1 THR D 434     192.773 136.325 270.126  1.00 96.48           O  
ATOM   4969  CG2 THR D 434     190.546 136.848 269.353  1.00 96.48           C  
ATOM   4970  N   GLU D 435     190.305 139.090 271.754  1.00 92.78           N  
ATOM   4971  CA  GLU D 435     190.463 140.526 271.937  1.00 92.78           C  
ATOM   4972  C   GLU D 435     190.760 140.858 273.391  1.00 92.78           C  
ATOM   4973  O   GLU D 435     191.578 141.738 273.676  1.00 92.78           O  
ATOM   4974  CB  GLU D 435     189.210 141.248 271.466  1.00 92.78           C  
ATOM   4975  CG  GLU D 435     188.984 141.111 269.986  1.00 92.78           C  
ATOM   4976  CD  GLU D 435     187.732 141.808 269.534  1.00 92.78           C  
ATOM   4977  OE1 GLU D 435     186.983 142.309 270.399  1.00 92.78           O  
ATOM   4978  OE2 GLU D 435     187.488 141.845 268.311  1.00 92.78           O  
ATOM   4979  N   ILE D 436     190.129 140.134 274.319  1.00 88.78           N  
ATOM   4980  CA  ILE D 436     190.376 140.337 275.742  1.00 88.78           C  
ATOM   4981  C   ILE D 436     191.800 139.935 276.101  1.00 88.78           C  
ATOM   4982  O   ILE D 436     192.498 140.666 276.813  1.00 88.78           O  
ATOM   4983  CB  ILE D 436     189.329 139.570 276.572  1.00 88.78           C  
ATOM   4984  CG1 ILE D 436     187.997 140.316 276.565  1.00 88.78           C  
ATOM   4985  CG2 ILE D 436     189.789 139.354 278.003  1.00 88.78           C  
ATOM   4986  CD1 ILE D 436     188.084 141.715 277.105  1.00 88.78           C  
ATOM   4987  N   ASN D 437     192.276 138.800 275.583  1.00 90.68           N  
ATOM   4988  CA  ASN D 437     193.631 138.390 275.951  1.00 90.68           C  
ATOM   4989  C   ASN D 437     194.699 139.222 275.237  1.00 90.68           C  
ATOM   4990  O   ASN D 437     195.767 139.469 275.815  1.00 90.68           O  
ATOM   4991  CB  ASN D 437     193.799 136.862 275.795  1.00 90.68           C  
ATOM   4992  CG  ASN D 437     193.725 136.346 274.360  1.00 90.68           C  
ATOM   4993  OD1 ASN D 437     194.228 136.937 273.409  1.00 90.68           O  
ATOM   4994  ND2 ASN D 437     193.076 135.198 274.213  1.00 90.68           N  
ATOM   4995  N   PHE D 438     194.422 139.693 274.014  1.00 83.32           N  
ATOM   4996  CA  PHE D 438     195.320 140.643 273.364  1.00 83.32           C  
ATOM   4997  C   PHE D 438     195.385 141.958 274.126  1.00 83.32           C  
ATOM   4998  O   PHE D 438     196.473 142.520 274.318  1.00 83.32           O  
ATOM   4999  CB  PHE D 438     194.867 140.899 271.930  1.00 83.32           C  
ATOM   5000  CG  PHE D 438     195.538 142.076 271.292  1.00 83.32           C  
ATOM   5001  CD1 PHE D 438     196.901 142.068 271.047  1.00 83.32           C  
ATOM   5002  CD2 PHE D 438     194.806 143.198 270.948  1.00 83.32           C  
ATOM   5003  CE1 PHE D 438     197.519 143.156 270.466  1.00 83.32           C  
ATOM   5004  CE2 PHE D 438     195.418 144.288 270.366  1.00 83.32           C  
ATOM   5005  CZ  PHE D 438     196.776 144.267 270.125  1.00 83.32           C  
ATOM   5006  N   LEU D 439     194.234 142.452 274.589  1.00 77.54           N  
ATOM   5007  CA  LEU D 439     194.220 143.685 275.361  1.00 77.54           C  
ATOM   5008  C   LEU D 439     194.878 143.502 276.716  1.00 77.54           C  
ATOM   5009  O   LEU D 439     195.460 144.447 277.245  1.00 77.54           O  
ATOM   5010  CB  LEU D 439     192.789 144.183 275.535  1.00 77.54           C  
ATOM   5011  CG  LEU D 439     192.214 144.990 274.376  1.00 77.54           C  
ATOM   5012  CD1 LEU D 439     190.813 145.438 274.709  1.00 77.54           C  
ATOM   5013  CD2 LEU D 439     193.096 146.176 274.069  1.00 77.54           C  
ATOM   5014  N   LEU D 440     194.823 142.299 277.284  1.00 80.29           N  
ATOM   5015  CA  LEU D 440     195.512 142.074 278.548  1.00 80.29           C  
ATOM   5016  C   LEU D 440     197.022 141.990 278.360  1.00 80.29           C  
ATOM   5017  O   LEU D 440     197.778 142.449 279.222  1.00 80.29           O  
ATOM   5018  CB  LEU D 440     194.998 140.812 279.226  1.00 80.29           C  
ATOM   5019  CG  LEU D 440     195.393 140.850 280.699  1.00 80.29           C  
ATOM   5020  CD1 LEU D 440     194.575 141.881 281.443  1.00 80.29           C  
ATOM   5021  CD2 LEU D 440     195.263 139.526 281.325  1.00 80.29           C  
ATOM   5022  N   LYS D 441     197.483 141.417 277.242  1.00 82.09           N  
ATOM   5023  CA  LYS D 441     198.909 141.481 276.919  1.00 82.09           C  
ATOM   5024  C   LYS D 441     199.371 142.922 276.742  1.00 82.09           C  
ATOM   5025  O   LYS D 441     200.419 143.323 277.274  1.00 82.09           O  
ATOM   5026  CB  LYS D 441     199.201 140.680 275.653  1.00 82.09           C  
ATOM   5027  CG  LYS D 441     200.681 140.559 275.343  1.00 82.09           C  
ATOM   5028  CD  LYS D 441     200.931 139.663 274.148  1.00 82.09           C  
ATOM   5029  CE  LYS D 441     202.401 139.648 273.777  1.00 82.09           C  
ATOM   5030  NZ  LYS D 441     203.248 139.191 274.912  1.00 82.09           N  
ATOM   5031  N   GLN D 442     198.570 143.727 276.040  1.00 76.27           N  
ATOM   5032  CA  GLN D 442     198.907 145.134 275.868  1.00 76.27           C  
ATOM   5033  C   GLN D 442     198.823 145.896 277.182  1.00 76.27           C  
ATOM   5034  O   GLN D 442     199.589 146.836 277.394  1.00 76.27           O  
ATOM   5035  CB  GLN D 442     197.989 145.773 274.832  1.00 76.27           C  
ATOM   5036  CG  GLN D 442     198.170 145.215 273.448  1.00 76.27           C  
ATOM   5037  CD  GLN D 442     199.347 145.830 272.741  1.00 76.27           C  
ATOM   5038  OE1 GLN D 442     200.437 145.263 272.718  1.00 76.27           O  
ATOM   5039  NE2 GLN D 442     199.138 146.999 272.161  1.00 76.27           N  
ATOM   5040  N   ALA D 443     197.947 145.474 278.093  1.00 72.98           N  
ATOM   5041  CA  ALA D 443     197.852 146.135 279.386  1.00 72.98           C  
ATOM   5042  C   ALA D 443     199.026 145.785 280.278  1.00 72.98           C  
ATOM   5043  O   ALA D 443     199.537 146.655 280.981  1.00 72.98           O  
ATOM   5044  CB  ALA D 443     196.552 145.765 280.079  1.00 72.98           C  
ATOM   5045  N   LEU D 444     199.495 144.540 280.221  1.00 76.90           N  
ATOM   5046  CA  LEU D 444     200.659 144.161 281.009  1.00 76.90           C  
ATOM   5047  C   LEU D 444     201.908 144.848 280.483  1.00 76.90           C  
ATOM   5048  O   LEU D 444     202.829 145.137 281.252  1.00 76.90           O  
ATOM   5049  CB  LEU D 444     200.841 142.645 280.990  1.00 76.90           C  
ATOM   5050  CG  LEU D 444     199.807 141.784 281.719  1.00 76.90           C  
ATOM   5051  CD1 LEU D 444     200.043 140.321 281.410  1.00 76.90           C  
ATOM   5052  CD2 LEU D 444     199.795 142.021 283.210  1.00 76.90           C  
ATOM   5053  N   THR D 445     201.950 145.127 279.180  1.00 77.39           N  
ATOM   5054  CA  THR D 445     203.068 145.893 278.643  1.00 77.39           C  
ATOM   5055  C   THR D 445     202.946 147.388 278.951  1.00 77.39           C  
ATOM   5056  O   THR D 445     203.945 148.039 279.276  1.00 77.39           O  
ATOM   5057  CB  THR D 445     203.171 145.661 277.135  1.00 77.39           C  
ATOM   5058  OG1 THR D 445     203.196 144.254 276.873  1.00 77.39           O  
ATOM   5059  CG2 THR D 445     204.442 146.275 276.576  1.00 77.39           C  
ATOM   5060  N   ILE D 446     201.735 147.944 278.902  1.00 73.89           N  
ATOM   5061  CA  ILE D 446     201.522 149.384 278.808  1.00 73.89           C  
ATOM   5062  C   ILE D 446     201.000 149.978 280.116  1.00 73.89           C  
ATOM   5063  O   ILE D 446     201.557 150.948 280.628  1.00 73.89           O  
ATOM   5064  CB  ILE D 446     200.574 149.703 277.630  1.00 73.89           C  
ATOM   5065  CG1 ILE D 446     201.302 149.521 276.300  1.00 73.89           C  
ATOM   5066  CG2 ILE D 446     200.000 151.087 277.727  1.00 73.89           C  
ATOM   5067  CD1 ILE D 446     200.388 149.213 275.148  1.00 73.89           C  
ATOM   5068  N   VAL D 447     199.910 149.430 280.657  1.00 72.27           N  
ATOM   5069  CA  VAL D 447     199.339 149.976 281.880  1.00 72.27           C  
ATOM   5070  C   VAL D 447     200.200 149.585 283.072  1.00 72.27           C  
ATOM   5071  O   VAL D 447     200.256 150.306 284.075  1.00 72.27           O  
ATOM   5072  CB  VAL D 447     197.882 149.492 282.021  1.00 72.27           C  
ATOM   5073  CG1 VAL D 447     197.169 150.155 283.188  1.00 72.27           C  
ATOM   5074  CG2 VAL D 447     197.130 149.753 280.739  1.00 72.27           C  
ATOM   5075  N   GLY D 448     200.905 148.456 282.971  1.00 74.22           N  
ATOM   5076  CA  GLY D 448     201.757 148.005 284.056  1.00 74.22           C  
ATOM   5077  C   GLY D 448     202.956 148.898 284.296  1.00 74.22           C  
ATOM   5078  O   GLY D 448     203.409 149.036 285.434  1.00 74.22           O  
ATOM   5079  N   THR D 449     203.495 149.503 283.239  1.00 77.18           N  
ATOM   5080  CA  THR D 449     204.688 150.320 283.399  1.00 77.18           C  
ATOM   5081  C   THR D 449     204.388 151.737 283.860  1.00 77.18           C  
ATOM   5082  O   THR D 449     205.318 152.428 284.281  1.00 77.18           O  
ATOM   5083  CB  THR D 449     205.497 150.371 282.096  1.00 77.18           C  
ATOM   5084  OG1 THR D 449     206.758 151.000 282.348  1.00 77.18           O  
ATOM   5085  CG2 THR D 449     204.783 151.160 281.032  1.00 77.18           C  
ATOM   5086  N   LEU D 450     203.129 152.184 283.786  1.00 74.51           N  
ATOM   5087  CA  LEU D 450     202.809 153.567 284.146  1.00 74.51           C  
ATOM   5088  C   LEU D 450     202.996 153.898 285.628  1.00 74.51           C  
ATOM   5089  O   LEU D 450     203.607 154.944 285.917  1.00 74.51           O  
ATOM   5090  CB  LEU D 450     201.402 153.918 283.651  1.00 74.51           C  
ATOM   5091  CG  LEU D 450     201.284 154.013 282.137  1.00 74.51           C  
ATOM   5092  CD1 LEU D 450     199.881 154.394 281.738  1.00 74.51           C  
ATOM   5093  CD2 LEU D 450     202.280 155.020 281.624  1.00 74.51           C  
ATOM   5094  N   PRO D 451     202.503 153.110 286.605  1.00 77.12           N  
ATOM   5095  CA  PRO D 451     202.756 153.502 287.999  1.00 77.12           C  
ATOM   5096  C   PRO D 451     204.201 153.353 288.410  1.00 77.12           C  
ATOM   5097  O   PRO D 451     204.672 154.154 289.222  1.00 77.12           O  
ATOM   5098  CB  PRO D 451     201.848 152.563 288.803  1.00 77.12           C  
ATOM   5099  CG  PRO D 451     200.838 152.129 287.851  1.00 77.12           C  
ATOM   5100  CD  PRO D 451     201.601 151.942 286.603  1.00 77.12           C  
ATOM   5101  N   PHE D 452     204.917 152.374 287.852  1.00 80.27           N  
ATOM   5102  CA  PHE D 452     206.345 152.243 288.119  1.00 80.27           C  
ATOM   5103  C   PHE D 452     207.113 153.450 287.599  1.00 80.27           C  
ATOM   5104  O   PHE D 452     207.988 153.982 288.293  1.00 80.27           O  
ATOM   5105  CB  PHE D 452     206.870 150.960 287.475  1.00 80.27           C  
ATOM   5106  CG  PHE D 452     208.344 150.744 287.655  1.00 80.27           C  
ATOM   5107  CD1 PHE D 452     208.840 150.275 288.859  1.00 80.27           C  
ATOM   5108  CD2 PHE D 452     209.234 151.006 286.625  1.00 80.27           C  
ATOM   5109  CE1 PHE D 452     210.192 150.068 289.033  1.00 80.27           C  
ATOM   5110  CE2 PHE D 452     210.585 150.807 286.795  1.00 80.27           C  
ATOM   5111  CZ  PHE D 452     211.064 150.335 287.999  1.00 80.27           C  
ATOM   5112  N   THR D 453     206.773 153.912 286.394  1.00 76.30           N  
ATOM   5113  CA  THR D 453     207.437 155.068 285.802  1.00 76.30           C  
ATOM   5114  C   THR D 453     207.146 156.345 286.578  1.00 76.30           C  
ATOM   5115  O   THR D 453     208.066 157.117 286.885  1.00 76.30           O  
ATOM   5116  CB  THR D 453     207.000 155.216 284.348  1.00 76.30           C  
ATOM   5117  OG1 THR D 453     207.382 154.047 283.615  1.00 76.30           O  
ATOM   5118  CG2 THR D 453     207.621 156.425 283.714  1.00 76.30           C  
ATOM   5119  N   TYR D 454     205.872 156.572 286.926  1.00 77.40           N  
ATOM   5120  CA  TYR D 454     205.511 157.774 287.671  1.00 77.40           C  
ATOM   5121  C   TYR D 454     206.109 157.760 289.072  1.00 77.40           C  
ATOM   5122  O   TYR D 454     206.586 158.795 289.551  1.00 77.40           O  
ATOM   5123  CB  TYR D 454     203.991 157.928 287.724  1.00 77.40           C  
ATOM   5124  CG  TYR D 454     203.467 158.657 288.942  1.00 77.40           C  
ATOM   5125  CD1 TYR D 454     203.627 160.030 289.080  1.00 77.40           C  
ATOM   5126  CD2 TYR D 454     202.798 157.977 289.942  1.00 77.40           C  
ATOM   5127  CE1 TYR D 454     203.150 160.696 290.184  1.00 77.40           C  
ATOM   5128  CE2 TYR D 454     202.318 158.635 291.052  1.00 77.40           C  
ATOM   5129  CZ  TYR D 454     202.496 159.993 291.166  1.00 77.40           C  
ATOM   5130  OH  TYR D 454     202.016 160.644 292.274  1.00 77.40           O  
ATOM   5131  N   MET D 455     206.126 156.592 289.721  1.00 85.07           N  
ATOM   5132  CA  MET D 455     206.741 156.451 291.036  1.00 85.07           C  
ATOM   5133  C   MET D 455     208.233 156.736 290.988  1.00 85.07           C  
ATOM   5134  O   MET D 455     208.764 157.442 291.854  1.00 85.07           O  
ATOM   5135  CB  MET D 455     206.504 155.038 291.557  1.00 85.07           C  
ATOM   5136  CG  MET D 455     207.075 154.728 292.931  1.00 85.07           C  
ATOM   5137  SD  MET D 455     208.722 154.002 292.812  1.00 85.07           S  
ATOM   5138  CE  MET D 455     208.330 152.301 293.007  1.00 85.07           C  
ATOM   5139  N   LEU D 456     208.934 156.144 290.013  1.00 81.90           N  
ATOM   5140  CA  LEU D 456     210.379 156.312 289.919  1.00 81.90           C  
ATOM   5141  C   LEU D 456     210.744 157.757 289.635  1.00 81.90           C  
ATOM   5142  O   LEU D 456     211.661 158.307 290.259  1.00 81.90           O  
ATOM   5143  CB  LEU D 456     210.943 155.411 288.828  1.00 81.90           C  
ATOM   5144  CG  LEU D 456     212.465 155.459 288.735  1.00 81.90           C  
ATOM   5145  CD1 LEU D 456     213.093 155.027 290.049  1.00 81.90           C  
ATOM   5146  CD2 LEU D 456     212.960 154.625 287.595  1.00 81.90           C  
ATOM   5147  N   GLU D 457     210.013 158.400 288.723  1.00 82.58           N  
ATOM   5148  CA  GLU D 457     210.312 159.790 288.423  1.00 82.58           C  
ATOM   5149  C   GLU D 457     209.956 160.701 289.581  1.00 82.58           C  
ATOM   5150  O   GLU D 457     210.651 161.690 289.807  1.00 82.58           O  
ATOM   5151  CB  GLU D 457     209.598 160.245 287.163  1.00 82.58           C  
ATOM   5152  CG  GLU D 457     210.447 160.092 285.940  1.00 82.58           C  
ATOM   5153  CD  GLU D 457     211.660 161.005 285.933  1.00 82.58           C  
ATOM   5154  OE1 GLU D 457     211.539 162.159 285.479  1.00 82.58           O  
ATOM   5155  OE2 GLU D 457     212.748 160.560 286.352  1.00 82.58           O  
ATOM   5156  N   LYS D 458     208.901 160.393 290.332  1.00 85.11           N  
ATOM   5157  CA  LYS D 458     208.537 161.283 291.422  1.00 85.11           C  
ATOM   5158  C   LYS D 458     209.481 161.107 292.609  1.00 85.11           C  
ATOM   5159  O   LYS D 458     209.791 162.091 293.296  1.00 85.11           O  
ATOM   5160  CB  LYS D 458     207.067 161.059 291.788  1.00 85.11           C  
ATOM   5161  CG  LYS D 458     206.473 162.069 292.754  1.00 85.11           C  
ATOM   5162  CD  LYS D 458     206.357 161.553 294.158  1.00 85.11           C  
ATOM   5163  CE  LYS D 458     205.243 160.540 294.274  1.00 85.11           C  
ATOM   5164  NZ  LYS D 458     205.106 160.030 295.665  1.00 85.11           N  
ATOM   5165  N   TRP D 459     209.995 159.889 292.824  1.00 90.23           N  
ATOM   5166  CA  TRP D 459     211.077 159.690 293.788  1.00 90.23           C  
ATOM   5167  C   TRP D 459     212.338 160.436 293.376  1.00 90.23           C  
ATOM   5168  O   TRP D 459     213.000 161.049 294.220  1.00 90.23           O  
ATOM   5169  CB  TRP D 459     211.402 158.206 293.942  1.00 90.23           C  
ATOM   5170  CG  TRP D 459     212.547 157.934 294.895  1.00 90.23           C  
ATOM   5171  CD1 TRP D 459     212.475 157.828 296.251  1.00 90.23           C  
ATOM   5172  CD2 TRP D 459     213.926 157.739 294.558  1.00 90.23           C  
ATOM   5173  NE1 TRP D 459     213.713 157.574 296.779  1.00 90.23           N  
ATOM   5174  CE2 TRP D 459     214.623 157.517 295.760  1.00 90.23           C  
ATOM   5175  CE3 TRP D 459     214.637 157.732 293.358  1.00 90.23           C  
ATOM   5176  CZ2 TRP D 459     215.995 157.290 295.796  1.00 90.23           C  
ATOM   5177  CZ3 TRP D 459     215.999 157.508 293.395  1.00 90.23           C  
ATOM   5178  CH2 TRP D 459     216.663 157.291 294.606  1.00 90.23           C  
ATOM   5179  N   ARG D 460     212.693 160.384 292.088  1.00 84.00           N  
ATOM   5180  CA  ARG D 460     213.884 161.093 291.629  1.00 84.00           C  
ATOM   5181  C   ARG D 460     213.706 162.604 291.717  1.00 84.00           C  
ATOM   5182  O   ARG D 460     214.643 163.323 292.081  1.00 84.00           O  
ATOM   5183  CB  ARG D 460     214.240 160.661 290.211  1.00 84.00           C  
ATOM   5184  CG  ARG D 460     215.001 159.356 290.182  1.00 84.00           C  
ATOM   5185  CD  ARG D 460     215.969 159.293 289.033  1.00 84.00           C  
ATOM   5186  NE  ARG D 460     215.294 159.348 287.746  1.00 84.00           N  
ATOM   5187  CZ  ARG D 460     215.878 159.060 286.594  1.00 84.00           C  
ATOM   5188  NH1 ARG D 460     217.145 158.699 286.536  1.00 84.00           N  
ATOM   5189  NH2 ARG D 460     215.179 159.157 285.470  1.00 84.00           N  
ATOM   5190  N   TRP D 461     212.499 163.094 291.432  1.00 83.01           N  
ATOM   5191  CA  TRP D 461     212.209 164.516 291.563  1.00 83.01           C  
ATOM   5192  C   TRP D 461     212.289 164.979 293.009  1.00 83.01           C  
ATOM   5193  O   TRP D 461     212.827 166.057 293.283  1.00 83.01           O  
ATOM   5194  CB  TRP D 461     210.840 164.831 290.970  1.00 83.01           C  
ATOM   5195  CG  TRP D 461     210.812 164.758 289.483  1.00 83.01           C  
ATOM   5196  CD1 TRP D 461     211.862 164.932 288.638  1.00 83.01           C  
ATOM   5197  CD2 TRP D 461     209.675 164.489 288.661  1.00 83.01           C  
ATOM   5198  NE1 TRP D 461     211.452 164.793 287.337  1.00 83.01           N  
ATOM   5199  CE2 TRP D 461     210.111 164.520 287.325  1.00 83.01           C  
ATOM   5200  CE3 TRP D 461     208.331 164.222 288.924  1.00 83.01           C  
ATOM   5201  CZ2 TRP D 461     209.252 164.298 286.257  1.00 83.01           C  
ATOM   5202  CZ3 TRP D 461     207.480 164.000 287.862  1.00 83.01           C  
ATOM   5203  CH2 TRP D 461     207.942 164.041 286.546  1.00 83.01           C  
ATOM   5204  N   MET D 462     211.776 164.186 293.955  1.00 92.64           N  
ATOM   5205  CA  MET D 462     211.884 164.639 295.336  1.00 92.64           C  
ATOM   5206  C   MET D 462     213.291 164.474 295.893  1.00 92.64           C  
ATOM   5207  O   MET D 462     213.689 165.250 296.768  1.00 92.64           O  
ATOM   5208  CB  MET D 462     210.910 163.926 296.267  1.00 92.64           C  
ATOM   5209  CG  MET D 462     209.452 164.193 296.015  1.00 92.64           C  
ATOM   5210  SD  MET D 462     208.519 163.406 297.332  1.00 92.64           S  
ATOM   5211  CE  MET D 462     208.736 161.701 296.906  1.00 92.64           C  
ATOM   5212  N   VAL D 463     214.052 163.477 295.434  1.00 90.71           N  
ATOM   5213  CA  VAL D 463     215.402 163.342 295.966  1.00 90.71           C  
ATOM   5214  C   VAL D 463     216.317 164.406 295.360  1.00 90.71           C  
ATOM   5215  O   VAL D 463     217.278 164.844 296.003  1.00 90.71           O  
ATOM   5216  CB  VAL D 463     215.943 161.910 295.771  1.00 90.71           C  
ATOM   5217  CG1 VAL D 463     216.303 161.611 294.341  1.00 90.71           C  
ATOM   5218  CG2 VAL D 463     217.128 161.674 296.643  1.00 90.71           C  
ATOM   5219  N   PHE D 464     216.014 164.887 294.152  1.00 88.33           N  
ATOM   5220  CA  PHE D 464     216.757 166.021 293.628  1.00 88.33           C  
ATOM   5221  C   PHE D 464     216.302 167.317 294.275  1.00 88.33           C  
ATOM   5222  O   PHE D 464     217.112 168.228 294.468  1.00 88.33           O  
ATOM   5223  CB  PHE D 464     216.602 166.104 292.111  1.00 88.33           C  
ATOM   5224  CG  PHE D 464     217.311 165.012 291.372  1.00 88.33           C  
ATOM   5225  CD1 PHE D 464     218.463 164.452 291.885  1.00 88.33           C  
ATOM   5226  CD2 PHE D 464     216.836 164.559 290.156  1.00 88.33           C  
ATOM   5227  CE1 PHE D 464     219.121 163.447 291.211  1.00 88.33           C  
ATOM   5228  CE2 PHE D 464     217.489 163.555 289.480  1.00 88.33           C  
ATOM   5229  CZ  PHE D 464     218.634 163.000 290.006  1.00 88.33           C  
ATOM   5230  N   LYS D 465     215.023 167.406 294.634  1.00 90.67           N  
ATOM   5231  CA  LYS D 465     214.499 168.599 295.281  1.00 90.67           C  
ATOM   5232  C   LYS D 465     214.933 168.709 296.735  1.00 90.67           C  
ATOM   5233  O   LYS D 465     214.908 169.809 297.295  1.00 90.67           O  
ATOM   5234  CB  LYS D 465     212.974 168.582 295.180  1.00 90.67           C  
ATOM   5235  CG  LYS D 465     212.288 169.917 295.331  1.00 90.67           C  
ATOM   5236  CD  LYS D 465     210.795 169.747 295.139  1.00 90.67           C  
ATOM   5237  CE  LYS D 465     210.479 169.368 293.702  1.00 90.67           C  
ATOM   5238  NZ  LYS D 465     209.042 169.035 293.513  1.00 90.67           N  
ATOM   5239  N   GLY D 466     215.341 167.608 297.352  1.00 96.36           N  
ATOM   5240  CA  GLY D 466     215.649 167.622 298.763  1.00 96.36           C  
ATOM   5241  C   GLY D 466     214.453 167.453 299.665  1.00 96.36           C  
ATOM   5242  O   GLY D 466     214.577 167.657 300.877  1.00 96.36           O  
ATOM   5243  N   GLU D 467     213.292 167.105 299.105  1.00100.55           N  
ATOM   5244  CA  GLU D 467     212.118 166.815 299.919  1.00100.55           C  
ATOM   5245  C   GLU D 467     212.329 165.545 300.733  1.00100.55           C  
ATOM   5246  O   GLU D 467     211.920 165.465 301.897  1.00100.55           O  
ATOM   5247  CB  GLU D 467     210.887 166.715 299.017  1.00100.55           C  
ATOM   5248  CG  GLU D 467     209.650 166.118 299.654  1.00100.55           C  
ATOM   5249  CD  GLU D 467     208.373 166.677 299.058  1.00100.55           C  
ATOM   5250  OE1 GLU D 467     208.315 166.842 297.821  1.00100.55           O  
ATOM   5251  OE2 GLU D 467     207.428 166.955 299.825  1.00100.55           O  
ATOM   5252  N   ILE D 468     212.998 164.560 300.147  1.00103.38           N  
ATOM   5253  CA  ILE D 468     213.335 163.319 300.834  1.00103.38           C  
ATOM   5254  C   ILE D 468     214.653 163.545 301.567  1.00103.38           C  
ATOM   5255  O   ILE D 468     215.633 163.964 300.931  1.00103.38           O  
ATOM   5256  CB  ILE D 468     213.448 162.143 299.858  1.00103.38           C  
ATOM   5257  CG1 ILE D 468     212.109 161.879 299.177  1.00103.38           C  
ATOM   5258  CG2 ILE D 468     213.915 160.894 300.576  1.00103.38           C  
ATOM   5259  CD1 ILE D 468     212.213 160.903 298.039  1.00103.38           C  
ATOM   5260  N   PRO D 469     214.719 163.311 302.876  1.00109.80           N  
ATOM   5261  CA  PRO D 469     216.004 163.405 303.576  1.00109.80           C  
ATOM   5262  C   PRO D 469     216.944 162.293 303.146  1.00109.80           C  
ATOM   5263  O   PRO D 469     216.536 161.273 302.590  1.00109.80           O  
ATOM   5264  CB  PRO D 469     215.623 163.270 305.056  1.00109.80           C  
ATOM   5265  CG  PRO D 469     214.134 163.458 305.105  1.00109.80           C  
ATOM   5266  CD  PRO D 469     213.618 162.980 303.791  1.00109.80           C  
ATOM   5267  N   LYS D 470     218.230 162.512 303.425  1.00114.74           N  
ATOM   5268  CA  LYS D 470     219.276 161.650 302.887  1.00114.74           C  
ATOM   5269  C   LYS D 470     219.253 160.261 303.516  1.00114.74           C  
ATOM   5270  O   LYS D 470     219.530 159.266 302.837  1.00114.74           O  
ATOM   5271  CB  LYS D 470     220.632 162.322 303.098  1.00114.74           C  
ATOM   5272  CG  LYS D 470     221.796 161.581 302.504  1.00114.74           C  
ATOM   5273  CD  LYS D 470     221.615 161.518 301.000  1.00114.74           C  
ATOM   5274  CE  LYS D 470     221.697 162.902 300.368  1.00114.74           C  
ATOM   5275  NZ  LYS D 470     223.068 163.474 300.463  1.00114.74           N  
ATOM   5276  N   ASP D 471     218.896 160.172 304.792  1.00118.95           N  
ATOM   5277  CA  ASP D 471     218.857 158.914 305.522  1.00118.95           C  
ATOM   5278  C   ASP D 471     217.484 158.259 305.480  1.00118.95           C  
ATOM   5279  O   ASP D 471     217.238 157.311 306.231  1.00118.95           O  
ATOM   5280  CB  ASP D 471     219.277 159.137 306.974  1.00118.95           C  
ATOM   5281  CG  ASP D 471     218.489 160.243 307.640  1.00118.95           C  
ATOM   5282  OD1 ASP D 471     218.090 161.194 306.935  1.00118.95           O  
ATOM   5283  OD2 ASP D 471     218.266 160.165 308.865  1.00118.95           O  
ATOM   5284  N   GLN D 472     216.572 158.773 304.655  1.00115.70           N  
ATOM   5285  CA  GLN D 472     215.206 158.272 304.574  1.00115.70           C  
ATOM   5286  C   GLN D 472     214.837 157.789 303.177  1.00115.70           C  
ATOM   5287  O   GLN D 472     213.647 157.749 302.852  1.00115.70           O  
ATOM   5288  CB  GLN D 472     214.218 159.347 305.029  1.00115.70           C  
ATOM   5289  CG  GLN D 472     214.355 159.729 306.487  1.00115.70           C  
ATOM   5290  CD  GLN D 472     214.078 158.567 307.415  1.00115.70           C  
ATOM   5291  OE1 GLN D 472     214.987 158.038 308.054  1.00115.70           O  
ATOM   5292  NE2 GLN D 472     212.817 158.159 307.491  1.00115.70           N  
ATOM   5293  N   TRP D 473     215.829 157.487 302.328  1.00111.12           N  
ATOM   5294  CA  TRP D 473     215.554 157.184 300.923  1.00111.12           C  
ATOM   5295  C   TRP D 473     214.723 155.915 300.756  1.00111.12           C  
ATOM   5296  O   TRP D 473     213.594 155.969 300.245  1.00111.12           O  
ATOM   5297  CB  TRP D 473     216.868 157.009 300.163  1.00111.12           C  
ATOM   5298  CG  TRP D 473     217.561 158.257 299.764  1.00111.12           C  
ATOM   5299  CD1 TRP D 473     217.258 159.522 300.146  1.00111.12           C  
ATOM   5300  CD2 TRP D 473     218.695 158.357 298.897  1.00111.12           C  
ATOM   5301  NE1 TRP D 473     218.137 160.410 299.579  1.00111.12           N  
ATOM   5302  CE2 TRP D 473     219.029 159.717 298.804  1.00111.12           C  
ATOM   5303  CE3 TRP D 473     219.460 157.425 298.191  1.00111.12           C  
ATOM   5304  CZ2 TRP D 473     220.090 160.172 298.027  1.00111.12           C  
ATOM   5305  CZ3 TRP D 473     220.514 157.878 297.426  1.00111.12           C  
ATOM   5306  CH2 TRP D 473     220.819 159.239 297.349  1.00111.12           C  
ATOM   5307  N   MET D 474     215.207 154.797 301.317  1.00113.86           N  
ATOM   5308  CA  MET D 474     214.568 153.500 301.098  1.00113.86           C  
ATOM   5309  C   MET D 474     213.193 153.443 301.734  1.00113.86           C  
ATOM   5310  O   MET D 474     212.230 153.018 301.077  1.00113.86           O  
ATOM   5311  CB  MET D 474     215.448 152.373 301.639  1.00113.86           C  
ATOM   5312  CG  MET D 474     216.792 152.063 300.929  1.00113.86           C  
ATOM   5313  SD  MET D 474     216.980 151.945 299.122  1.00113.86           S  
ATOM   5314  CE  MET D 474     217.110 153.644 298.555  1.00113.86           C  
ATOM   5315  N   LYS D 475     213.070 153.995 302.950  1.00113.81           N  
ATOM   5316  CA  LYS D 475     211.781 154.079 303.627  1.00113.81           C  
ATOM   5317  C   LYS D 475     210.796 154.883 302.805  1.00113.81           C  
ATOM   5318  O   LYS D 475     209.611 154.541 302.756  1.00113.81           O  
ATOM   5319  CB  LYS D 475     211.903 154.657 305.038  1.00113.81           C  
ATOM   5320  CG  LYS D 475     212.234 153.634 306.123  1.00113.81           C  
ATOM   5321  CD  LYS D 475     213.660 153.139 306.167  1.00113.81           C  
ATOM   5322  CE  LYS D 475     214.592 154.226 306.642  1.00113.81           C  
ATOM   5323  NZ  LYS D 475     215.963 153.690 306.763  1.00113.81           N  
ATOM   5324  N   LYS D 476     211.246 155.986 302.205  1.00108.44           N  
ATOM   5325  CA  LYS D 476     210.307 156.729 301.382  1.00108.44           C  
ATOM   5326  C   LYS D 476     209.977 155.957 300.110  1.00108.44           C  
ATOM   5327  O   LYS D 476     208.791 155.762 299.802  1.00108.44           O  
ATOM   5328  CB  LYS D 476     210.862 158.108 301.045  1.00108.44           C  
ATOM   5329  CG  LYS D 476     209.806 159.054 300.513  1.00108.44           C  
ATOM   5330  CD  LYS D 476     208.712 159.281 301.539  1.00108.44           C  
ATOM   5331  CE  LYS D 476     207.632 160.197 300.995  1.00108.44           C  
ATOM   5332  NZ  LYS D 476     208.114 161.596 300.850  1.00108.44           N  
ATOM   5333  N   TRP D 477     211.000 155.342 299.487  1.00102.59           N  
ATOM   5334  CA  TRP D 477     210.809 154.692 298.190  1.00102.59           C  
ATOM   5335  C   TRP D 477     209.891 153.495 298.294  1.00102.59           C  
ATOM   5336  O   TRP D 477     208.895 153.406 297.560  1.00102.59           O  
ATOM   5337  CB  TRP D 477     212.158 154.262 297.617  1.00102.59           C  
ATOM   5338  CG  TRP D 477     212.117 153.876 296.168  1.00102.59           C  
ATOM   5339  CD1 TRP D 477     211.879 154.694 295.107  1.00102.59           C  
ATOM   5340  CD2 TRP D 477     212.355 152.576 295.623  1.00102.59           C  
ATOM   5341  NE1 TRP D 477     211.939 153.984 293.934  1.00102.59           N  
ATOM   5342  CE2 TRP D 477     212.226 152.679 294.225  1.00102.59           C  
ATOM   5343  CE3 TRP D 477     212.655 151.334 296.182  1.00102.59           C  
ATOM   5344  CZ2 TRP D 477     212.395 151.591 293.380  1.00102.59           C  
ATOM   5345  CZ3 TRP D 477     212.818 150.254 295.341  1.00102.59           C  
ATOM   5346  CH2 TRP D 477     212.689 150.389 293.956  1.00102.59           C  
ATOM   5347  N   TRP D 478     210.099 152.689 299.329  1.00108.02           N  
ATOM   5348  CA  TRP D 478     209.300 151.496 299.506  1.00108.02           C  
ATOM   5349  C   TRP D 478     207.886 151.868 299.891  1.00108.02           C  
ATOM   5350  O   TRP D 478     206.939 151.239 299.398  1.00108.02           O  
ATOM   5351  CB  TRP D 478     209.937 150.616 300.576  1.00108.02           C  
ATOM   5352  CG  TRP D 478     211.132 149.838 300.100  1.00108.02           C  
ATOM   5353  CD1 TRP D 478     212.367 149.839 300.675  1.00108.02           C  
ATOM   5354  CD2 TRP D 478     211.209 148.919 298.997  1.00108.02           C  
ATOM   5355  NE1 TRP D 478     213.214 149.011 299.989  1.00108.02           N  
ATOM   5356  CE2 TRP D 478     212.526 148.430 298.958  1.00108.02           C  
ATOM   5357  CE3 TRP D 478     210.299 148.464 298.039  1.00108.02           C  
ATOM   5358  CZ2 TRP D 478     212.952 147.519 298.004  1.00108.02           C  
ATOM   5359  CZ3 TRP D 478     210.732 147.561 297.099  1.00108.02           C  
ATOM   5360  CH2 TRP D 478     212.041 147.106 297.081  1.00108.02           C  
ATOM   5361  N   GLU D 479     207.730 152.968 300.647  1.00105.20           N  
ATOM   5362  CA  GLU D 479     206.392 153.419 301.003  1.00105.20           C  
ATOM   5363  C   GLU D 479     205.631 153.848 299.766  1.00105.20           C  
ATOM   5364  O   GLU D 479     204.476 153.440 299.576  1.00105.20           O  
ATOM   5365  CB  GLU D 479     206.463 154.562 302.012  1.00105.20           C  
ATOM   5366  CG  GLU D 479     205.115 155.146 302.388  1.00105.20           C  
ATOM   5367  CD  GLU D 479     205.238 156.346 303.306  1.00105.20           C  
ATOM   5368  OE1 GLU D 479     206.371 156.838 303.494  1.00105.20           O  
ATOM   5369  OE2 GLU D 479     204.204 156.798 303.840  1.00105.20           O  
ATOM   5370  N   MET D 480     206.318 154.528 298.839  1.00 99.18           N  
ATOM   5371  CA  MET D 480     205.651 154.902 297.604  1.00 99.18           C  
ATOM   5372  C   MET D 480     205.364 153.690 296.751  1.00 99.18           C  
ATOM   5373  O   MET D 480     204.318 153.642 296.096  1.00 99.18           O  
ATOM   5374  CB  MET D 480     206.458 155.928 296.828  1.00 99.18           C  
ATOM   5375  CG  MET D 480     206.517 157.256 297.514  1.00 99.18           C  
ATOM   5376  SD  MET D 480     207.407 158.388 296.472  1.00 99.18           S  
ATOM   5377  CE  MET D 480     209.040 157.749 296.737  1.00 99.18           C  
ATOM   5378  N   LYS D 481     206.249 152.689 296.789  1.00 98.61           N  
ATOM   5379  CA  LYS D 481     205.973 151.476 296.039  1.00 98.61           C  
ATOM   5380  C   LYS D 481     204.768 150.765 296.636  1.00 98.61           C  
ATOM   5381  O   LYS D 481     203.975 150.155 295.910  1.00 98.61           O  
ATOM   5382  CB  LYS D 481     207.202 150.577 295.988  1.00 98.61           C  
ATOM   5383  CG  LYS D 481     207.031 149.477 294.964  1.00 98.61           C  
ATOM   5384  CD  LYS D 481     208.164 148.503 294.949  1.00 98.61           C  
ATOM   5385  CE  LYS D 481     209.320 148.990 294.105  1.00 98.61           C  
ATOM   5386  NZ  LYS D 481     209.000 148.964 292.654  1.00 98.61           N  
ATOM   5387  N   ARG D 482     204.615 150.836 297.961  1.00103.91           N  
ATOM   5388  CA  ARG D 482     203.375 150.367 298.562  1.00103.91           C  
ATOM   5389  C   ARG D 482     202.200 151.259 298.178  1.00103.91           C  
ATOM   5390  O   ARG D 482     201.097 150.763 297.929  1.00103.91           O  
ATOM   5391  CB  ARG D 482     203.525 150.274 300.078  1.00103.91           C  
ATOM   5392  CG  ARG D 482     204.520 149.215 300.515  1.00103.91           C  
ATOM   5393  CD  ARG D 482     205.147 149.551 301.852  1.00103.91           C  
ATOM   5394  NE  ARG D 482     205.974 148.459 302.349  1.00103.91           N  
ATOM   5395  CZ  ARG D 482     205.709 147.759 303.443  1.00103.91           C  
ATOM   5396  NH1 ARG D 482     204.633 148.000 304.173  1.00103.91           N  
ATOM   5397  NH2 ARG D 482     206.542 146.790 303.811  1.00103.91           N  
ATOM   5398  N   GLU D 483     202.409 152.574 298.126  1.00 99.13           N  
ATOM   5399  CA  GLU D 483     201.267 153.470 297.997  1.00 99.13           C  
ATOM   5400  C   GLU D 483     200.875 153.721 296.546  1.00 99.13           C  
ATOM   5401  O   GLU D 483     199.684 153.875 296.256  1.00 99.13           O  
ATOM   5402  CB  GLU D 483     201.556 154.785 298.735  1.00 99.13           C  
ATOM   5403  CG  GLU D 483     200.360 155.728 298.950  1.00 99.13           C  
ATOM   5404  CD  GLU D 483     200.068 156.652 297.784  1.00 99.13           C  
ATOM   5405  OE1 GLU D 483     201.015 157.002 297.054  1.00 99.13           O  
ATOM   5406  OE2 GLU D 483     198.891 157.028 297.601  1.00 99.13           O  
ATOM   5407  N   ILE D 484     201.837 153.759 295.626  1.00 90.91           N  
ATOM   5408  CA  ILE D 484     201.543 154.074 294.232  1.00 90.91           C  
ATOM   5409  C   ILE D 484     201.408 152.801 293.414  1.00 90.91           C  
ATOM   5410  O   ILE D 484     200.352 152.530 292.834  1.00 90.91           O  
ATOM   5411  CB  ILE D 484     202.625 154.974 293.615  1.00 90.91           C  
ATOM   5412  CG1 ILE D 484     202.689 156.316 294.331  1.00 90.91           C  
ATOM   5413  CG2 ILE D 484     202.353 155.177 292.146  1.00 90.91           C  
ATOM   5414  CD1 ILE D 484     203.946 157.075 294.043  1.00 90.91           C  
ATOM   5415  N   VAL D 485     202.481 152.014 293.361  1.00 87.90           N  
ATOM   5416  CA  VAL D 485     202.513 150.860 292.475  1.00 87.90           C  
ATOM   5417  C   VAL D 485     201.753 149.694 293.096  1.00 87.90           C  
ATOM   5418  O   VAL D 485     201.181 148.863 292.382  1.00 87.90           O  
ATOM   5419  CB  VAL D 485     203.984 150.517 292.165  1.00 87.90           C  
ATOM   5420  CG1 VAL D 485     204.119 149.347 291.203  1.00 87.90           C  
ATOM   5421  CG2 VAL D 485     204.701 151.733 291.625  1.00 87.90           C  
ATOM   5422  N   GLY D 486     201.656 149.657 294.418  1.00 96.05           N  
ATOM   5423  CA  GLY D 486     201.023 148.529 295.071  1.00 96.05           C  
ATOM   5424  C   GLY D 486     201.886 147.292 295.053  1.00 96.05           C  
ATOM   5425  O   GLY D 486     201.383 146.190 294.805  1.00 96.05           O  
ATOM   5426  N   VAL D 487     203.183 147.456 295.280  1.00 98.76           N  
ATOM   5427  CA  VAL D 487     204.132 146.356 295.330  1.00 98.76           C  
ATOM   5428  C   VAL D 487     204.899 146.475 296.641  1.00 98.76           C  
ATOM   5429  O   VAL D 487     205.386 147.558 296.980  1.00 98.76           O  
ATOM   5430  CB  VAL D 487     205.077 146.386 294.113  1.00 98.76           C  
ATOM   5431  CG1 VAL D 487     206.231 145.470 294.314  1.00 98.76           C  
ATOM   5432  CG2 VAL D 487     204.328 146.000 292.853  1.00 98.76           C  
ATOM   5433  N   VAL D 488     204.967 145.387 297.400  1.00107.58           N  
ATOM   5434  CA  VAL D 488     205.616 145.397 298.704  1.00107.58           C  
ATOM   5435  C   VAL D 488     206.993 144.758 298.572  1.00107.58           C  
ATOM   5436  O   VAL D 488     207.236 143.922 297.693  1.00107.58           O  
ATOM   5437  CB  VAL D 488     204.730 144.688 299.758  1.00107.58           C  
ATOM   5438  CG1 VAL D 488     204.708 143.178 299.557  1.00107.58           C  
ATOM   5439  CG2 VAL D 488     205.132 145.055 301.181  1.00107.58           C  
ATOM   5440  N   GLU D 489     207.928 145.205 299.407  1.00114.48           N  
ATOM   5441  CA  GLU D 489     209.246 144.600 299.429  1.00114.48           C  
ATOM   5442  C   GLU D 489     209.176 143.241 300.122  1.00114.48           C  
ATOM   5443  O   GLU D 489     208.289 143.000 300.945  1.00114.48           O  
ATOM   5444  CB  GLU D 489     210.244 145.499 300.154  1.00114.48           C  
ATOM   5445  CG  GLU D 489     209.881 145.811 301.597  1.00114.48           C  
ATOM   5446  CD  GLU D 489     209.194 147.148 301.760  1.00114.48           C  
ATOM   5447  OE1 GLU D 489     208.187 147.390 301.064  1.00114.48           O  
ATOM   5448  OE2 GLU D 489     209.658 147.955 302.591  1.00114.48           O  
ATOM   5449  N   PRO D 490     210.077 142.324 299.786  1.00119.75           N  
ATOM   5450  CA  PRO D 490     210.182 141.081 300.561  1.00119.75           C  
ATOM   5451  C   PRO D 490     210.683 141.294 301.981  1.00119.75           C  
ATOM   5452  O   PRO D 490     210.030 140.878 302.942  1.00119.75           O  
ATOM   5453  CB  PRO D 490     211.168 140.249 299.739  1.00119.75           C  
ATOM   5454  CG  PRO D 490     211.036 140.783 298.355  1.00119.75           C  
ATOM   5455  CD  PRO D 490     210.855 142.252 298.540  1.00119.75           C  
ATOM   5456  N   VAL D 491     211.837 141.939 302.127  1.00123.64           N  
ATOM   5457  CA  VAL D 491     212.401 142.227 303.444  1.00123.64           C  
ATOM   5458  C   VAL D 491     212.642 143.731 303.511  1.00123.64           C  
ATOM   5459  O   VAL D 491     212.778 144.376 302.461  1.00123.64           O  
ATOM   5460  CB  VAL D 491     213.694 141.434 303.710  1.00123.64           C  
ATOM   5461  CG1 VAL D 491     213.423 139.933 303.732  1.00123.64           C  
ATOM   5462  CG2 VAL D 491     214.776 141.788 302.714  1.00123.64           C  
ATOM   5463  N   PRO D 492     212.648 144.336 304.698  1.00125.26           N  
ATOM   5464  CA  PRO D 492     213.021 145.751 304.799  1.00125.26           C  
ATOM   5465  C   PRO D 492     214.475 145.996 304.427  1.00125.26           C  
ATOM   5466  O   PRO D 492     215.357 145.171 304.675  1.00125.26           O  
ATOM   5467  CB  PRO D 492     212.770 146.074 306.276  1.00125.26           C  
ATOM   5468  CG  PRO D 492     211.724 145.099 306.687  1.00125.26           C  
ATOM   5469  CD  PRO D 492     212.084 143.836 305.965  1.00125.26           C  
ATOM   5470  N   HIS D 493     214.712 147.153 303.814  1.00123.59           N  
ATOM   5471  CA  HIS D 493     216.039 147.568 303.387  1.00123.59           C  
ATOM   5472  C   HIS D 493     216.386 148.896 304.043  1.00123.59           C  
ATOM   5473  O   HIS D 493     215.582 149.833 304.021  1.00123.59           O  
ATOM   5474  CB  HIS D 493     216.122 147.707 301.864  1.00123.59           C  
ATOM   5475  CG  HIS D 493     216.031 146.409 301.126  1.00123.59           C  
ATOM   5476  ND1 HIS D 493     217.072 145.508 301.079  1.00123.59           N  
ATOM   5477  CD2 HIS D 493     215.035 145.872 300.383  1.00123.59           C  
ATOM   5478  CE1 HIS D 493     216.717 144.465 300.350  1.00123.59           C  
ATOM   5479  NE2 HIS D 493     215.486 144.661 299.917  1.00123.59           N  
ATOM   5480  N   ASP D 494     217.579 148.968 304.621  1.00124.27           N  
ATOM   5481  CA  ASP D 494     218.097 150.189 305.215  1.00124.27           C  
ATOM   5482  C   ASP D 494     218.931 150.946 304.180  1.00124.27           C  
ATOM   5483  O   ASP D 494     219.007 150.562 303.010  1.00124.27           O  
ATOM   5484  CB  ASP D 494     218.871 149.871 306.496  1.00124.27           C  
ATOM   5485  CG  ASP D 494     219.990 148.862 306.283  1.00124.27           C  
ATOM   5486  OD1 ASP D 494     220.124 148.313 305.171  1.00124.27           O  
ATOM   5487  OD2 ASP D 494     220.745 148.615 307.246  1.00124.27           O  
ATOM   5488  N   GLU D 495     219.574 152.032 304.603  1.00121.94           N  
ATOM   5489  CA  GLU D 495     220.259 152.942 303.693  1.00121.94           C  
ATOM   5490  C   GLU D 495     221.632 152.445 303.263  1.00121.94           C  
ATOM   5491  O   GLU D 495     222.347 153.175 302.568  1.00121.94           O  
ATOM   5492  CB  GLU D 495     220.377 154.327 304.328  1.00121.94           C  
ATOM   5493  CG  GLU D 495     219.244 155.256 303.946  1.00121.94           C  
ATOM   5494  CD  GLU D 495     217.921 154.829 304.524  1.00121.94           C  
ATOM   5495  OE1 GLU D 495     217.922 154.215 305.609  1.00121.94           O  
ATOM   5496  OE2 GLU D 495     216.879 155.104 303.895  1.00121.94           O  
ATOM   5497  N   THR D 496     222.017 151.227 303.648  1.00124.62           N  
ATOM   5498  CA  THR D 496     223.156 150.578 303.015  1.00124.62           C  
ATOM   5499  C   THR D 496     222.826 150.127 301.600  1.00124.62           C  
ATOM   5500  O   THR D 496     223.740 149.850 300.818  1.00124.62           O  
ATOM   5501  CB  THR D 496     223.619 149.383 303.848  1.00124.62           C  
ATOM   5502  OG1 THR D 496     222.660 148.324 303.740  1.00124.62           O  
ATOM   5503  CG2 THR D 496     223.765 149.780 305.307  1.00124.62           C  
ATOM   5504  N   TYR D 497     221.543 150.048 301.262  1.00124.74           N  
ATOM   5505  CA  TYR D 497     221.082 149.608 299.959  1.00124.74           C  
ATOM   5506  C   TYR D 497     220.722 150.833 299.132  1.00124.74           C  
ATOM   5507  O   TYR D 497     220.369 151.883 299.673  1.00124.74           O  
ATOM   5508  CB  TYR D 497     219.840 148.724 300.090  1.00124.74           C  
ATOM   5509  CG  TYR D 497     220.042 147.419 300.819  1.00124.74           C  
ATOM   5510  CD1 TYR D 497     220.589 146.314 300.184  1.00124.74           C  
ATOM   5511  CD2 TYR D 497     219.674 147.295 302.152  1.00124.74           C  
ATOM   5512  CE1 TYR D 497     220.764 145.119 300.864  1.00124.74           C  
ATOM   5513  CE2 TYR D 497     219.845 146.108 302.835  1.00124.74           C  
ATOM   5514  CZ  TYR D 497     220.391 145.025 302.187  1.00124.74           C  
ATOM   5515  OH  TYR D 497     220.563 143.841 302.866  1.00124.74           O  
ATOM   5516  N   CYS D 498     220.811 150.694 297.815  1.00118.46           N  
ATOM   5517  CA  CYS D 498     220.304 151.707 296.890  1.00118.46           C  
ATOM   5518  C   CYS D 498     219.488 150.918 295.876  1.00118.46           C  
ATOM   5519  O   CYS D 498     219.966 150.567 294.797  1.00118.46           O  
ATOM   5520  CB  CYS D 498     221.421 152.513 296.251  1.00118.46           C  
ATOM   5521  SG  CYS D 498     220.848 154.014 295.429  1.00118.46           S  
ATOM   5522  N   ASP D 499     218.243 150.657 296.233  1.00114.65           N  
ATOM   5523  CA  ASP D 499     217.325 149.847 295.443  1.00114.65           C  
ATOM   5524  C   ASP D 499     216.770 150.498 294.174  1.00114.65           C  
ATOM   5525  O   ASP D 499     216.455 149.754 293.236  1.00114.65           O  
ATOM   5526  CB  ASP D 499     216.179 149.377 296.344  1.00114.65           C  
ATOM   5527  CG  ASP D 499     216.626 148.336 297.349  1.00114.65           C  
ATOM   5528  OD1 ASP D 499     217.628 147.644 297.077  1.00114.65           O  
ATOM   5529  OD2 ASP D 499     216.000 148.224 298.420  1.00114.65           O  
ATOM   5530  N   PRO D 500     216.567 151.829 294.087  1.00107.64           N  
ATOM   5531  CA  PRO D 500     216.314 152.405 292.756  1.00107.64           C  
ATOM   5532  C   PRO D 500     217.426 152.178 291.754  1.00107.64           C  
ATOM   5533  O   PRO D 500     217.133 151.812 290.613  1.00107.64           O  
ATOM   5534  CB  PRO D 500     216.138 153.894 293.059  1.00107.64           C  
ATOM   5535  CG  PRO D 500     215.485 153.897 294.340  1.00107.64           C  
ATOM   5536  CD  PRO D 500     216.119 152.785 295.124  1.00107.64           C  
ATOM   5537  N   ALA D 501     218.691 152.259 292.177  1.00109.56           N  
ATOM   5538  CA  ALA D 501     219.832 152.331 291.264  1.00109.56           C  
ATOM   5539  C   ALA D 501     220.128 151.031 290.530  1.00109.56           C  
ATOM   5540  O   ALA D 501     221.033 151.020 289.691  1.00109.56           O  
ATOM   5541  CB  ALA D 501     221.083 152.772 292.020  1.00109.56           C  
ATOM   5542  N   SER D 502     219.403 149.947 290.805  1.00108.34           N  
ATOM   5543  CA  SER D 502     219.615 148.700 290.085  1.00108.34           C  
ATOM   5544  C   SER D 502     219.046 148.730 288.672  1.00108.34           C  
ATOM   5545  O   SER D 502     219.252 147.770 287.925  1.00108.34           O  
ATOM   5546  CB  SER D 502     219.000 147.539 290.863  1.00108.34           C  
ATOM   5547  OG  SER D 502     217.604 147.719 291.017  1.00108.34           O  
ATOM   5548  N   LEU D 503     218.317 149.778 288.301  1.00101.41           N  
ATOM   5549  CA  LEU D 503     217.737 149.913 286.975  1.00101.41           C  
ATOM   5550  C   LEU D 503     218.698 150.663 286.056  1.00101.41           C  
ATOM   5551  O   LEU D 503     219.527 151.453 286.512  1.00101.41           O  
ATOM   5552  CB  LEU D 503     216.381 150.623 287.064  1.00101.41           C  
ATOM   5553  CG  LEU D 503     215.508 150.847 285.827  1.00101.41           C  
ATOM   5554  CD1 LEU D 503     215.263 149.550 285.103  1.00101.41           C  
ATOM   5555  CD2 LEU D 503     214.193 151.446 286.227  1.00101.41           C  
ATOM   5556  N   PHE D 504     218.597 150.371 284.754  1.00 99.93           N  
ATOM   5557  CA  PHE D 504     219.537 150.887 283.762  1.00 99.93           C  
ATOM   5558  C   PHE D 504     219.465 152.402 283.625  1.00 99.93           C  
ATOM   5559  O   PHE D 504     220.501 153.065 283.499  1.00 99.93           O  
ATOM   5560  CB  PHE D 504     219.255 150.220 282.415  1.00 99.93           C  
ATOM   5561  CG  PHE D 504     219.844 150.940 281.236  1.00 99.93           C  
ATOM   5562  CD1 PHE D 504     221.203 150.896 280.992  1.00 99.93           C  
ATOM   5563  CD2 PHE D 504     219.029 151.635 280.355  1.00 99.93           C  
ATOM   5564  CE1 PHE D 504     221.746 151.553 279.904  1.00 99.93           C  
ATOM   5565  CE2 PHE D 504     219.564 152.294 279.267  1.00 99.93           C  
ATOM   5566  CZ  PHE D 504     220.925 152.251 279.041  1.00 99.93           C  
ATOM   5567  N   HIS D 505     218.257 152.968 283.634  1.00 94.70           N  
ATOM   5568  CA  HIS D 505     218.102 154.384 283.315  1.00 94.70           C  
ATOM   5569  C   HIS D 505     218.567 155.278 284.453  1.00 94.70           C  
ATOM   5570  O   HIS D 505     219.177 156.325 284.213  1.00 94.70           O  
ATOM   5571  CB  HIS D 505     216.652 154.683 282.950  1.00 94.70           C  
ATOM   5572  CG  HIS D 505     216.141 153.862 281.812  1.00 94.70           C  
ATOM   5573  ND1 HIS D 505     215.551 152.631 281.987  1.00 94.70           N  
ATOM   5574  CD2 HIS D 505     216.131 154.099 280.480  1.00 94.70           C  
ATOM   5575  CE1 HIS D 505     215.201 152.142 280.811  1.00 94.70           C  
ATOM   5576  NE2 HIS D 505     215.541 153.014 279.880  1.00 94.70           N  
ATOM   5577  N   VAL D 506     218.268 154.902 285.695  1.00 98.18           N  
ATOM   5578  CA  VAL D 506     218.674 155.732 286.821  1.00 98.18           C  
ATOM   5579  C   VAL D 506     220.178 155.626 287.069  1.00 98.18           C  
ATOM   5580  O   VAL D 506     220.818 156.602 287.483  1.00 98.18           O  
ATOM   5581  CB  VAL D 506     217.812 155.365 288.046  1.00 98.18           C  
ATOM   5582  CG1 VAL D 506     217.986 153.932 288.395  1.00 98.18           C  
ATOM   5583  CG2 VAL D 506     218.134 156.239 289.246  1.00 98.18           C  
ATOM   5584  N   SER D 507     220.779 154.474 286.775  1.00101.29           N  
ATOM   5585  CA  SER D 507     222.203 154.294 287.005  1.00101.29           C  
ATOM   5586  C   SER D 507     223.048 154.981 285.946  1.00101.29           C  
ATOM   5587  O   SER D 507     224.221 155.266 286.198  1.00101.29           O  
ATOM   5588  CB  SER D 507     222.552 152.808 287.044  1.00101.29           C  
ATOM   5589  OG  SER D 507     222.816 152.327 285.739  1.00101.29           O  
ATOM   5590  N   ASN D 508     222.479 155.261 284.777  1.00102.06           N  
ATOM   5591  CA  ASN D 508     223.232 155.827 283.667  1.00102.06           C  
ATOM   5592  C   ASN D 508     222.710 157.191 283.235  1.00102.06           C  
ATOM   5593  O   ASN D 508     222.882 157.574 282.075  1.00102.06           O  
ATOM   5594  CB  ASN D 508     223.239 154.857 282.489  1.00102.06           C  
ATOM   5595  CG  ASN D 508     224.139 153.672 282.733  1.00102.06           C  
ATOM   5596  OD1 ASN D 508     225.259 153.826 283.210  1.00102.06           O  
ATOM   5597  ND2 ASN D 508     223.654 152.482 282.421  1.00102.06           N  
ATOM   5598  N   ASP D 509     222.065 157.911 284.161  1.00100.20           N  
ATOM   5599  CA  ASP D 509     221.664 159.315 284.005  1.00100.20           C  
ATOM   5600  C   ASP D 509     220.712 159.514 282.822  1.00100.20           C  
ATOM   5601  O   ASP D 509     221.012 160.214 281.853  1.00100.20           O  
ATOM   5602  CB  ASP D 509     222.900 160.219 283.889  1.00100.20           C  
ATOM   5603  CG  ASP D 509     222.578 161.681 284.093  1.00100.20           C  
ATOM   5604  OD1 ASP D 509     221.747 161.991 284.967  1.00100.20           O  
ATOM   5605  OD2 ASP D 509     223.160 162.523 283.377  1.00100.20           O  
ATOM   5606  N   TYR D 510     219.557 158.867 282.906  1.00 94.95           N  
ATOM   5607  CA  TYR D 510     218.544 158.962 281.868  1.00 94.95           C  
ATOM   5608  C   TYR D 510     217.236 159.463 282.455  1.00 94.95           C  
ATOM   5609  O   TYR D 510     216.840 159.055 283.551  1.00 94.95           O  
ATOM   5610  CB  TYR D 510     218.318 157.610 281.192  1.00 94.95           C  
ATOM   5611  CG  TYR D 510     219.372 157.260 280.173  1.00 94.95           C  
ATOM   5612  CD1 TYR D 510     219.369 157.848 278.916  1.00 94.95           C  
ATOM   5613  CD2 TYR D 510     220.371 156.342 280.469  1.00 94.95           C  
ATOM   5614  CE1 TYR D 510     220.334 157.533 277.981  1.00 94.95           C  
ATOM   5615  CE2 TYR D 510     221.340 156.020 279.542  1.00 94.95           C  
ATOM   5616  CZ  TYR D 510     221.316 156.618 278.299  1.00 94.95           C  
ATOM   5617  OH  TYR D 510     222.278 156.298 277.370  1.00 94.95           O  
ATOM   5618  N   SER D 511     216.577 160.359 281.724  1.00 84.28           N  
ATOM   5619  CA  SER D 511     215.243 160.796 282.100  1.00 84.28           C  
ATOM   5620  C   SER D 511     214.260 159.650 281.911  1.00 84.28           C  
ATOM   5621  O   SER D 511     214.340 158.899 280.936  1.00 84.28           O  
ATOM   5622  CB  SER D 511     214.820 162.000 281.266  1.00 84.28           C  
ATOM   5623  OG  SER D 511     213.711 162.653 281.851  1.00 84.28           O  
ATOM   5624  N   PHE D 512     213.329 159.514 282.849  1.00 82.23           N  
ATOM   5625  CA  PHE D 512     212.420 158.380 282.854  1.00 82.23           C  
ATOM   5626  C   PHE D 512     210.973 158.745 282.563  1.00 82.23           C  
ATOM   5627  O   PHE D 512     210.182 157.848 282.269  1.00 82.23           O  
ATOM   5628  CB  PHE D 512     212.502 157.654 284.199  1.00 82.23           C  
ATOM   5629  CG  PHE D 512     212.219 156.194 284.121  1.00 82.23           C  
ATOM   5630  CD1 PHE D 512     213.128 155.335 283.536  1.00 82.23           C  
ATOM   5631  CD2 PHE D 512     211.064 155.672 284.667  1.00 82.23           C  
ATOM   5632  CE1 PHE D 512     212.877 153.987 283.474  1.00 82.23           C  
ATOM   5633  CE2 PHE D 512     210.811 154.322 284.610  1.00 82.23           C  
ATOM   5634  CZ  PHE D 512     211.721 153.482 284.020  1.00 82.23           C  
ATOM   5635  N   ILE D 513     210.610 160.030 282.598  1.00 74.01           N  
ATOM   5636  CA  ILE D 513     209.222 160.430 282.367  1.00 74.01           C  
ATOM   5637  C   ILE D 513     208.853 160.391 280.894  1.00 74.01           C  
ATOM   5638  O   ILE D 513     207.664 160.518 280.550  1.00 74.01           O  
ATOM   5639  CB  ILE D 513     208.993 161.825 282.984  1.00 74.01           C  
ATOM   5640  CG1 ILE D 513     207.536 162.005 283.414  1.00 74.01           C  
ATOM   5641  CG2 ILE D 513     209.426 162.923 282.030  1.00 74.01           C  
ATOM   5642  CD1 ILE D 513     207.082 161.009 284.451  1.00 74.01           C  
ATOM   5643  N   ARG D 514     209.843 160.191 280.017  1.00 74.36           N  
ATOM   5644  CA  ARG D 514     209.584 160.077 278.589  1.00 74.36           C  
ATOM   5645  C   ARG D 514     208.728 158.863 278.271  1.00 74.36           C  
ATOM   5646  O   ARG D 514     207.939 158.903 277.330  1.00 74.36           O  
ATOM   5647  CB  ARG D 514     210.897 160.000 277.810  1.00 74.36           C  
ATOM   5648  CG  ARG D 514     211.888 158.998 278.363  1.00 74.36           C  
ATOM   5649  CD  ARG D 514     212.844 158.511 277.290  1.00 74.36           C  
ATOM   5650  NE  ARG D 514     213.447 159.601 276.537  1.00 74.36           N  
ATOM   5651  CZ  ARG D 514     214.537 160.251 276.914  1.00 74.36           C  
ATOM   5652  NH1 ARG D 514     215.180 159.936 278.026  1.00 74.36           N  
ATOM   5653  NH2 ARG D 514     215.000 161.237 276.152  1.00 74.36           N  
ATOM   5654  N   TYR D 515     208.831 157.799 279.069  1.00 74.72           N  
ATOM   5655  CA  TYR D 515     208.022 156.611 278.825  1.00 74.72           C  
ATOM   5656  C   TYR D 515     206.563 156.839 279.203  1.00 74.72           C  
ATOM   5657  O   TYR D 515     205.659 156.394 278.486  1.00 74.72           O  
ATOM   5658  CB  TYR D 515     208.614 155.433 279.588  1.00 74.72           C  
ATOM   5659  CG  TYR D 515     210.055 155.207 279.218  1.00 74.72           C  
ATOM   5660  CD1 TYR D 515     210.424 154.999 277.896  1.00 74.72           C  
ATOM   5661  CD2 TYR D 515     211.052 155.234 280.182  1.00 74.72           C  
ATOM   5662  CE1 TYR D 515     211.742 154.808 277.548  1.00 74.72           C  
ATOM   5663  CE2 TYR D 515     212.374 155.042 279.843  1.00 74.72           C  
ATOM   5664  CZ  TYR D 515     212.712 154.831 278.525  1.00 74.72           C  
ATOM   5665  OH  TYR D 515     214.028 154.638 278.181  1.00 74.72           O  
ATOM   5666  N   TYR D 516     206.318 157.554 280.306  1.00 70.12           N  
ATOM   5667  CA  TYR D 516     204.957 157.917 280.698  1.00 70.12           C  
ATOM   5668  C   TYR D 516     204.308 158.827 279.660  1.00 70.12           C  
ATOM   5669  O   TYR D 516     203.176 158.581 279.208  1.00 70.12           O  
ATOM   5670  CB  TYR D 516     204.998 158.607 282.063  1.00 70.12           C  
ATOM   5671  CG  TYR D 516     203.658 158.848 282.720  1.00 70.12           C  
ATOM   5672  CD1 TYR D 516     202.952 160.022 282.497  1.00 70.12           C  
ATOM   5673  CD2 TYR D 516     203.118 157.919 283.595  1.00 70.12           C  
ATOM   5674  CE1 TYR D 516     201.737 160.246 283.096  1.00 70.12           C  
ATOM   5675  CE2 TYR D 516     201.903 158.138 284.203  1.00 70.12           C  
ATOM   5676  CZ  TYR D 516     201.220 159.303 283.951  1.00 70.12           C  
ATOM   5677  OH  TYR D 516     200.009 159.532 284.552  1.00 70.12           O  
ATOM   5678  N   THR D 517     205.032 159.871 279.250  1.00 69.56           N  
ATOM   5679  CA  THR D 517     204.488 160.794 278.263  1.00 69.56           C  
ATOM   5680  C   THR D 517     204.334 160.132 276.899  1.00 69.56           C  
ATOM   5681  O   THR D 517     203.359 160.402 276.195  1.00 69.56           O  
ATOM   5682  CB  THR D 517     205.362 162.038 278.169  1.00 69.56           C  
ATOM   5683  OG1 THR D 517     206.704 161.659 277.853  1.00 69.56           O  
ATOM   5684  CG2 THR D 517     205.351 162.780 279.488  1.00 69.56           C  
ATOM   5685  N   ARG D 518     205.256 159.233 276.534  1.00 69.57           N  
ATOM   5686  CA  ARG D 518     205.154 158.485 275.286  1.00 69.57           C  
ATOM   5687  C   ARG D 518     203.929 157.590 275.286  1.00 69.57           C  
ATOM   5688  O   ARG D 518     203.221 157.498 274.279  1.00 69.57           O  
ATOM   5689  CB  ARG D 518     206.412 157.641 275.089  1.00 69.57           C  
ATOM   5690  CG  ARG D 518     206.297 156.590 274.001  1.00 69.57           C  
ATOM   5691  CD  ARG D 518     206.993 155.299 274.361  1.00 69.57           C  
ATOM   5692  NE  ARG D 518     206.165 154.476 275.230  1.00 69.57           N  
ATOM   5693  CZ  ARG D 518     206.499 153.265 275.648  1.00 69.57           C  
ATOM   5694  NH1 ARG D 518     207.649 152.709 275.307  1.00 69.57           N  
ATOM   5695  NH2 ARG D 518     205.654 152.591 276.422  1.00 69.57           N  
ATOM   5696  N   THR D 519     203.656 156.946 276.424  1.00 67.59           N  
ATOM   5697  CA  THR D 519     202.492 156.079 276.551  1.00 67.59           C  
ATOM   5698  C   THR D 519     201.198 156.865 276.385  1.00 67.59           C  
ATOM   5699  O   THR D 519     200.263 156.403 275.722  1.00 67.59           O  
ATOM   5700  CB  THR D 519     202.536 155.373 277.904  1.00 67.59           C  
ATOM   5701  OG1 THR D 519     203.718 154.571 277.982  1.00 67.59           O  
ATOM   5702  CG2 THR D 519     201.350 154.478 278.074  1.00 67.59           C  
ATOM   5703  N   LEU D 520     201.138 158.071 276.949  1.00 64.34           N  
ATOM   5704  CA  LEU D 520     199.927 158.876 276.774  1.00 64.34           C  
ATOM   5705  C   LEU D 520     199.794 159.414 275.347  1.00 64.34           C  
ATOM   5706  O   LEU D 520     198.702 159.359 274.754  1.00 64.34           O  
ATOM   5707  CB  LEU D 520     199.897 160.009 277.787  1.00 64.34           C  
ATOM   5708  CG  LEU D 520     199.136 159.684 279.070  1.00 64.34           C  
ATOM   5709  CD1 LEU D 520     199.858 158.696 279.964  1.00 64.34           C  
ATOM   5710  CD2 LEU D 520     198.905 160.957 279.795  1.00 64.34           C  
ATOM   5711  N   TYR D 521     200.894 159.922 274.774  1.00 65.23           N  
ATOM   5712  CA  TYR D 521     200.856 160.495 273.431  1.00 65.23           C  
ATOM   5713  C   TYR D 521     200.582 159.442 272.376  1.00 65.23           C  
ATOM   5714  O   TYR D 521     200.021 159.761 271.326  1.00 65.23           O  
ATOM   5715  CB  TYR D 521     202.190 161.156 273.085  1.00 65.23           C  
ATOM   5716  CG  TYR D 521     202.609 162.329 273.923  1.00 65.23           C  
ATOM   5717  CD1 TYR D 521     201.681 163.111 274.583  1.00 65.23           C  
ATOM   5718  CD2 TYR D 521     203.952 162.629 274.082  1.00 65.23           C  
ATOM   5719  CE1 TYR D 521     202.080 164.178 275.346  1.00 65.23           C  
ATOM   5720  CE2 TYR D 521     204.358 163.686 274.848  1.00 65.23           C  
ATOM   5721  CZ  TYR D 521     203.420 164.456 275.482  1.00 65.23           C  
ATOM   5722  OH  TYR D 521     203.830 165.519 276.246  1.00 65.23           O  
ATOM   5723  N   GLN D 522     200.946 158.191 272.660  1.00 65.72           N  
ATOM   5724  CA  GLN D 522     200.700 157.077 271.756  1.00 65.72           C  
ATOM   5725  C   GLN D 522     199.212 156.892 271.502  1.00 65.72           C  
ATOM   5726  O   GLN D 522     198.757 156.906 270.355  1.00 65.72           O  
ATOM   5727  CB  GLN D 522     201.314 155.825 272.375  1.00 65.72           C  
ATOM   5728  CG  GLN D 522     201.186 154.552 271.610  1.00 65.72           C  
ATOM   5729  CD  GLN D 522     201.472 153.362 272.491  1.00 65.72           C  
ATOM   5730  OE1 GLN D 522     200.593 152.555 272.758  1.00 65.72           O  
ATOM   5731  NE2 GLN D 522     202.685 153.293 273.013  1.00 65.72           N  
ATOM   5732  N   PHE D 523     198.429 156.785 272.567  1.00 65.29           N  
ATOM   5733  CA  PHE D 523     197.000 156.586 272.394  1.00 65.29           C  
ATOM   5734  C   PHE D 523     196.282 157.863 271.992  1.00 65.29           C  
ATOM   5735  O   PHE D 523     195.244 157.783 271.322  1.00 65.29           O  
ATOM   5736  CB  PHE D 523     196.413 155.981 273.659  1.00 65.29           C  
ATOM   5737  CG  PHE D 523     196.951 154.624 273.955  1.00 65.29           C  
ATOM   5738  CD1 PHE D 523     196.667 153.564 273.116  1.00 65.29           C  
ATOM   5739  CD2 PHE D 523     197.782 154.413 275.033  1.00 65.29           C  
ATOM   5740  CE1 PHE D 523     197.173 152.313 273.370  1.00 65.29           C  
ATOM   5741  CE2 PHE D 523     198.288 153.163 275.293  1.00 65.29           C  
ATOM   5742  CZ  PHE D 523     197.981 152.111 274.463  1.00 65.29           C  
ATOM   5743  N   GLN D 524     196.813 159.036 272.359  1.00 66.69           N  
ATOM   5744  CA  GLN D 524     196.241 160.279 271.841  1.00 66.69           C  
ATOM   5745  C   GLN D 524     196.384 160.364 270.324  1.00 66.69           C  
ATOM   5746  O   GLN D 524     195.407 160.640 269.610  1.00 66.69           O  
ATOM   5747  CB  GLN D 524     196.903 161.482 272.505  1.00 66.69           C  
ATOM   5748  CG  GLN D 524     196.352 161.807 273.867  1.00 66.69           C  
ATOM   5749  CD  GLN D 524     196.946 163.063 274.438  1.00 66.69           C  
ATOM   5750  OE1 GLN D 524     197.803 163.016 275.315  1.00 66.69           O  
ATOM   5751  NE2 GLN D 524     196.490 164.203 273.947  1.00 66.69           N  
ATOM   5752  N   PHE D 525     197.589 160.071 269.813  1.00 66.67           N  
ATOM   5753  CA  PHE D 525     197.824 160.039 268.374  1.00 66.67           C  
ATOM   5754  C   PHE D 525     197.000 158.955 267.705  1.00 66.67           C  
ATOM   5755  O   PHE D 525     196.532 159.143 266.579  1.00 66.67           O  
ATOM   5756  CB  PHE D 525     199.304 159.794 268.075  1.00 66.67           C  
ATOM   5757  CG  PHE D 525     200.213 160.930 268.450  1.00 66.67           C  
ATOM   5758  CD1 PHE D 525     199.724 162.204 268.660  1.00 66.67           C  
ATOM   5759  CD2 PHE D 525     201.572 160.709 268.592  1.00 66.67           C  
ATOM   5760  CE1 PHE D 525     200.571 163.235 269.000  1.00 66.67           C  
ATOM   5761  CE2 PHE D 525     202.422 161.736 268.936  1.00 66.67           C  
ATOM   5762  CZ  PHE D 525     201.921 162.999 269.140  1.00 66.67           C  
ATOM   5763  N   GLN D 526     196.803 157.826 268.389  1.00 67.80           N  
ATOM   5764  CA  GLN D 526     196.005 156.747 267.824  1.00 67.80           C  
ATOM   5765  C   GLN D 526     194.545 157.146 267.669  1.00 67.80           C  
ATOM   5766  O   GLN D 526     193.950 156.871 266.625  1.00 67.80           O  
ATOM   5767  CB  GLN D 526     196.147 155.478 268.658  1.00 67.80           C  
ATOM   5768  CG  GLN D 526     195.410 154.280 268.076  1.00 67.80           C  
ATOM   5769  CD  GLN D 526     196.193 153.528 267.011  1.00 67.80           C  
ATOM   5770  OE1 GLN D 526     197.167 154.030 266.454  1.00 67.80           O  
ATOM   5771  NE2 GLN D 526     195.760 152.310 266.723  1.00 67.80           N  
ATOM   5772  N   GLU D 527     193.952 157.809 268.673  1.00 69.79           N  
ATOM   5773  CA  GLU D 527     192.583 158.292 268.486  1.00 69.79           C  
ATOM   5774  C   GLU D 527     192.491 159.351 267.402  1.00 69.79           C  
ATOM   5775  O   GLU D 527     191.526 159.352 266.632  1.00 69.79           O  
ATOM   5776  CB  GLU D 527     191.966 158.860 269.758  1.00 69.79           C  
ATOM   5777  CG  GLU D 527     191.447 157.854 270.732  1.00 69.79           C  
ATOM   5778  CD  GLU D 527     190.590 158.507 271.792  1.00 69.79           C  
ATOM   5779  OE1 GLU D 527     190.538 159.753 271.827  1.00 69.79           O  
ATOM   5780  OE2 GLU D 527     189.940 157.781 272.568  1.00 69.79           O  
ATOM   5781  N   ALA D 528     193.470 160.257 267.323  1.00 68.21           N  
ATOM   5782  CA  ALA D 528     193.401 161.303 266.304  1.00 68.21           C  
ATOM   5783  C   ALA D 528     193.503 160.726 264.895  1.00 68.21           C  
ATOM   5784  O   ALA D 528     192.752 161.128 263.998  1.00 68.21           O  
ATOM   5785  CB  ALA D 528     194.495 162.335 266.533  1.00 68.21           C  
ATOM   5786  N   LEU D 529     194.375 159.737 264.701  1.00 69.06           N  
ATOM   5787  CA  LEU D 529     194.487 159.101 263.396  1.00 69.06           C  
ATOM   5788  C   LEU D 529     193.286 158.218 263.085  1.00 69.06           C  
ATOM   5789  O   LEU D 529     192.886 158.117 261.922  1.00 69.06           O  
ATOM   5790  CB  LEU D 529     195.773 158.289 263.319  1.00 69.06           C  
ATOM   5791  CG  LEU D 529     197.088 159.069 263.351  1.00 69.06           C  
ATOM   5792  CD1 LEU D 529     198.213 158.194 262.857  1.00 69.06           C  
ATOM   5793  CD2 LEU D 529     197.014 160.362 262.566  1.00 69.06           C  
ATOM   5794  N   CYS D 530     192.709 157.556 264.090  1.00 74.83           N  
ATOM   5795  CA  CYS D 530     191.594 156.658 263.823  1.00 74.83           C  
ATOM   5796  C   CYS D 530     190.295 157.413 263.576  1.00 74.83           C  
ATOM   5797  O   CYS D 530     189.447 156.930 262.821  1.00 74.83           O  
ATOM   5798  CB  CYS D 530     191.445 155.655 264.964  1.00 74.83           C  
ATOM   5799  SG  CYS D 530     192.778 154.432 264.961  1.00 74.83           S  
ATOM   5800  N   GLN D 531     190.102 158.581 264.198  1.00 76.21           N  
ATOM   5801  CA  GLN D 531     189.013 159.448 263.762  1.00 76.21           C  
ATOM   5802  C   GLN D 531     189.333 160.150 262.454  1.00 76.21           C  
ATOM   5803  O   GLN D 531     188.407 160.549 261.741  1.00 76.21           O  
ATOM   5804  CB  GLN D 531     188.653 160.504 264.821  1.00 76.21           C  
ATOM   5805  CG  GLN D 531     188.426 160.080 266.300  1.00 76.21           C  
ATOM   5806  CD  GLN D 531     187.478 158.900 266.572  1.00 76.21           C  
ATOM   5807  OE1 GLN D 531     186.735 158.428 265.709  1.00 76.21           O  
ATOM   5808  NE2 GLN D 531     187.517 158.419 267.810  1.00 76.21           N  
ATOM   5809  N   ALA D 532     190.614 160.322 262.128  1.00 73.78           N  
ATOM   5810  CA  ALA D 532     190.967 160.846 260.815  1.00 73.78           C  
ATOM   5811  C   ALA D 532     190.698 159.821 259.721  1.00 73.78           C  
ATOM   5812  O   ALA D 532     190.272 160.180 258.619  1.00 73.78           O  
ATOM   5813  CB  ALA D 532     192.430 161.281 260.796  1.00 73.78           C  
ATOM   5814  N   ALA D 533     190.927 158.545 260.006  1.00 73.69           N  
ATOM   5815  CA  ALA D 533     190.763 157.481 259.027  1.00 73.69           C  
ATOM   5816  C   ALA D 533     189.365 156.886 259.012  1.00 73.69           C  
ATOM   5817  O   ALA D 533     189.137 155.929 258.264  1.00 73.69           O  
ATOM   5818  CB  ALA D 533     191.781 156.368 259.285  1.00 73.69           C  
ATOM   5819  N   LYS D 534     188.446 157.424 259.823  1.00 78.79           N  
ATOM   5820  CA  LYS D 534     187.039 157.010 259.906  1.00 78.79           C  
ATOM   5821  C   LYS D 534     186.912 155.530 260.271  1.00 78.79           C  
ATOM   5822  O   LYS D 534     186.405 154.712 259.505  1.00 78.79           O  
ATOM   5823  CB  LYS D 534     186.279 157.327 258.605  1.00 78.79           C  
ATOM   5824  CG  LYS D 534     186.266 158.787 258.054  1.00 78.79           C  
ATOM   5825  CD  LYS D 534     186.322 160.017 259.004  1.00 78.79           C  
ATOM   5826  CE  LYS D 534     185.261 160.073 260.124  1.00 78.79           C  
ATOM   5827  NZ  LYS D 534     185.508 161.198 261.069  1.00 78.79           N  
ATOM   5828  N   HIS D 535     187.392 155.200 261.464  1.00 81.71           N  
ATOM   5829  CA  HIS D 535     187.247 153.860 262.011  1.00 81.71           C  
ATOM   5830  C   HIS D 535     185.971 153.785 262.839  1.00 81.71           C  
ATOM   5831  O   HIS D 535     185.755 154.611 263.730  1.00 81.71           O  
ATOM   5832  CB  HIS D 535     188.468 153.504 262.857  1.00 81.71           C  
ATOM   5833  CG  HIS D 535     188.326 152.226 263.618  1.00 81.71           C  
ATOM   5834  ND1 HIS D 535     188.489 150.990 263.032  1.00 81.71           N  
ATOM   5835  CD2 HIS D 535     188.051 151.991 264.922  1.00 81.71           C  
ATOM   5836  CE1 HIS D 535     188.307 150.049 263.940  1.00 81.71           C  
ATOM   5837  NE2 HIS D 535     188.045 150.630 265.096  1.00 81.71           N  
ATOM   5838  N   GLU D 536     185.127 152.799 262.538  1.00 89.32           N  
ATOM   5839  CA  GLU D 536     183.787 152.719 263.103  1.00 89.32           C  
ATOM   5840  C   GLU D 536     183.667 151.723 264.248  1.00 89.32           C  
ATOM   5841  O   GLU D 536     182.547 151.431 264.679  1.00 89.32           O  
ATOM   5842  CB  GLU D 536     182.763 152.368 262.018  1.00 89.32           C  
ATOM   5843  CG  GLU D 536     182.535 153.440 260.956  1.00 89.32           C  
ATOM   5844  CD  GLU D 536     183.560 153.414 259.839  1.00 89.32           C  
ATOM   5845  OE1 GLU D 536     184.427 152.517 259.841  1.00 89.32           O  
ATOM   5846  OE2 GLU D 536     183.498 154.297 258.957  1.00 89.32           O  
ATOM   5847  N   GLY D 537     184.773 151.193 264.752  1.00 81.78           N  
ATOM   5848  CA  GLY D 537     184.708 150.237 265.830  1.00 81.78           C  
ATOM   5849  C   GLY D 537     185.459 150.675 267.068  1.00 81.78           C  
ATOM   5850  O   GLY D 537     185.689 151.866 267.297  1.00 81.78           O  
ATOM   5851  N   PRO D 538     185.829 149.712 267.909  1.00 77.93           N  
ATOM   5852  CA  PRO D 538     186.693 150.018 269.050  1.00 77.93           C  
ATOM   5853  C   PRO D 538     188.091 150.397 268.593  1.00 77.93           C  
ATOM   5854  O   PRO D 538     188.510 150.107 267.472  1.00 77.93           O  
ATOM   5855  CB  PRO D 538     186.708 148.710 269.846  1.00 77.93           C  
ATOM   5856  CG  PRO D 538     185.478 147.996 269.414  1.00 77.93           C  
ATOM   5857  CD  PRO D 538     185.323 148.333 267.970  1.00 77.93           C  
ATOM   5858  N   LEU D 539     188.814 151.062 269.495  1.00 72.68           N  
ATOM   5859  CA  LEU D 539     190.083 151.678 269.126  1.00 72.68           C  
ATOM   5860  C   LEU D 539     191.172 150.641 268.887  1.00 72.68           C  
ATOM   5861  O   LEU D 539     192.053 150.857 268.048  1.00 72.68           O  
ATOM   5862  CB  LEU D 539     190.504 152.680 270.198  1.00 72.68           C  
ATOM   5863  CG  LEU D 539     191.755 153.517 269.933  1.00 72.68           C  
ATOM   5864  CD1 LEU D 539     191.500 154.495 268.812  1.00 72.68           C  
ATOM   5865  CD2 LEU D 539     192.168 154.252 271.183  1.00 72.68           C  
ATOM   5866  N   HIS D 540     191.128 149.507 269.586  1.00 76.64           N  
ATOM   5867  CA  HIS D 540     192.202 148.532 269.449  1.00 76.64           C  
ATOM   5868  C   HIS D 540     192.115 147.730 268.159  1.00 76.64           C  
ATOM   5869  O   HIS D 540     193.076 147.032 267.823  1.00 76.64           O  
ATOM   5870  CB  HIS D 540     192.245 147.559 270.634  1.00 76.64           C  
ATOM   5871  CG  HIS D 540     191.039 146.681 270.767  1.00 76.64           C  
ATOM   5872  ND1 HIS D 540     189.752 147.166 270.839  1.00 76.64           N  
ATOM   5873  CD2 HIS D 540     190.933 145.333 270.828  1.00 76.64           C  
ATOM   5874  CE1 HIS D 540     188.907 146.158 270.950  1.00 76.64           C  
ATOM   5875  NE2 HIS D 540     189.599 145.034 270.943  1.00 76.64           N  
ATOM   5876  N   LYS D 541     190.999 147.804 267.439  1.00 78.63           N  
ATOM   5877  CA  LYS D 541     190.863 147.152 266.147  1.00 78.63           C  
ATOM   5878  C   LYS D 541     191.363 148.012 265.000  1.00 78.63           C  
ATOM   5879  O   LYS D 541     191.400 147.537 263.862  1.00 78.63           O  
ATOM   5880  CB  LYS D 541     189.400 146.816 265.866  1.00 78.63           C  
ATOM   5881  CG  LYS D 541     188.796 145.667 266.636  1.00 78.63           C  
ATOM   5882  CD  LYS D 541     187.303 145.674 266.352  1.00 78.63           C  
ATOM   5883  CE  LYS D 541     186.719 144.295 266.157  1.00 78.63           C  
ATOM   5884  NZ  LYS D 541     186.284 143.719 267.447  1.00 78.63           N  
ATOM   5885  N   CYS D 542     191.739 149.256 265.268  1.00 78.65           N  
ATOM   5886  CA  CYS D 542     191.844 150.258 264.221  1.00 78.65           C  
ATOM   5887  C   CYS D 542     193.155 150.162 263.460  1.00 78.65           C  
ATOM   5888  O   CYS D 542     194.215 149.914 264.039  1.00 78.65           O  
ATOM   5889  CB  CYS D 542     191.704 151.653 264.818  1.00 78.65           C  
ATOM   5890  SG  CYS D 542     192.177 152.968 263.699  1.00 78.65           S  
ATOM   5891  N   ASP D 543     193.071 150.377 262.152  1.00 79.66           N  
ATOM   5892  CA  ASP D 543     194.219 150.398 261.261  1.00 79.66           C  
ATOM   5893  C   ASP D 543     194.222 151.723 260.512  1.00 79.66           C  
ATOM   5894  O   ASP D 543     193.179 152.175 260.031  1.00 79.66           O  
ATOM   5895  CB  ASP D 543     194.151 149.237 260.271  1.00 79.66           C  
ATOM   5896  CG  ASP D 543     195.462 148.985 259.561  1.00 79.66           C  
ATOM   5897  OD1 ASP D 543     196.409 149.783 259.701  1.00 79.66           O  
ATOM   5898  OD2 ASP D 543     195.532 147.986 258.822  1.00 79.66           O  
ATOM   5899  N   ILE D 544     195.400 152.335 260.393  1.00 74.99           N  
ATOM   5900  CA  ILE D 544     195.545 153.577 259.647  1.00 74.99           C  
ATOM   5901  C   ILE D 544     196.000 153.331 258.214  1.00 74.99           C  
ATOM   5902  O   ILE D 544     196.366 154.279 257.519  1.00 74.99           O  
ATOM   5903  CB  ILE D 544     196.490 154.558 260.355  1.00 74.99           C  
ATOM   5904  CG1 ILE D 544     197.895 153.980 260.463  1.00 74.99           C  
ATOM   5905  CG2 ILE D 544     195.962 154.891 261.729  1.00 74.99           C  
ATOM   5906  CD1 ILE D 544     198.913 154.984 260.937  1.00 74.99           C  
ATOM   5907  N   SER D 545     196.000 152.080 257.762  1.00 76.80           N  
ATOM   5908  CA  SER D 545     196.423 151.768 256.405  1.00 76.80           C  
ATOM   5909  C   SER D 545     195.402 152.277 255.397  1.00 76.80           C  
ATOM   5910  O   SER D 545     194.216 152.420 255.707  1.00 76.80           O  
ATOM   5911  CB  SER D 545     196.598 150.263 256.237  1.00 76.80           C  
ATOM   5912  OG  SER D 545     197.559 149.757 257.137  1.00 76.80           O  
ATOM   5913  N   ASN D 546     195.892 152.572 254.184  1.00 83.57           N  
ATOM   5914  CA  ASN D 546     195.104 153.030 253.033  1.00 83.57           C  
ATOM   5915  C   ASN D 546     194.362 154.333 253.310  1.00 83.57           C  
ATOM   5916  O   ASN D 546     193.356 154.625 252.659  1.00 83.57           O  
ATOM   5917  CB  ASN D 546     194.113 151.962 252.547  1.00 83.57           C  
ATOM   5918  CG  ASN D 546     194.745 150.604 252.391  1.00 83.57           C  
ATOM   5919  OD1 ASN D 546     194.982 149.910 253.374  1.00 83.57           O  
ATOM   5920  ND2 ASN D 546     194.982 150.195 251.146  1.00 83.57           N  
ATOM   5921  N   SER D 547     194.832 155.127 254.266  1.00 77.66           N  
ATOM   5922  CA  SER D 547     194.195 156.386 254.632  1.00 77.66           C  
ATOM   5923  C   SER D 547     195.201 157.509 254.454  1.00 77.66           C  
ATOM   5924  O   SER D 547     196.134 157.644 255.250  1.00 77.66           O  
ATOM   5925  CB  SER D 547     193.690 156.337 256.068  1.00 77.66           C  
ATOM   5926  OG  SER D 547     193.114 157.573 256.438  1.00 77.66           O  
ATOM   5927  N   THR D 548     195.009 158.312 253.410  1.00 78.74           N  
ATOM   5928  CA  THR D 548     195.937 159.395 253.119  1.00 78.74           C  
ATOM   5929  C   THR D 548     195.732 160.574 254.060  1.00 78.74           C  
ATOM   5930  O   THR D 548     196.697 161.268 254.396  1.00 78.74           O  
ATOM   5931  CB  THR D 548     195.779 159.832 251.663  1.00 78.74           C  
ATOM   5932  OG1 THR D 548     195.707 158.670 250.830  1.00 78.74           O  
ATOM   5933  CG2 THR D 548     196.970 160.660 251.212  1.00 78.74           C  
ATOM   5934  N   GLU D 549     194.491 160.809 254.494  1.00 80.35           N  
ATOM   5935  CA  GLU D 549     194.198 161.966 255.334  1.00 80.35           C  
ATOM   5936  C   GLU D 549     194.794 161.809 256.727  1.00 80.35           C  
ATOM   5937  O   GLU D 549     195.261 162.790 257.318  1.00 80.35           O  
ATOM   5938  CB  GLU D 549     192.687 162.208 255.414  1.00 80.35           C  
ATOM   5939  CG  GLU D 549     191.816 161.008 255.795  1.00 80.35           C  
ATOM   5940  CD  GLU D 549     191.425 160.130 254.616  1.00 80.35           C  
ATOM   5941  OE1 GLU D 549     192.326 159.595 253.937  1.00 80.35           O  
ATOM   5942  OE2 GLU D 549     190.212 159.970 254.372  1.00 80.35           O  
ATOM   5943  N   ALA D 550     194.794 160.585 257.266  1.00 75.49           N  
ATOM   5944  CA  ALA D 550     195.448 160.332 258.545  1.00 75.49           C  
ATOM   5945  C   ALA D 550     196.956 160.513 258.439  1.00 75.49           C  
ATOM   5946  O   ALA D 550     197.587 161.064 259.350  1.00 75.49           O  
ATOM   5947  CB  ALA D 550     195.113 158.927 259.035  1.00 75.49           C  
ATOM   5948  N   GLY D 551     197.540 160.083 257.320  1.00 73.47           N  
ATOM   5949  CA  GLY D 551     198.957 160.309 257.095  1.00 73.47           C  
ATOM   5950  C   GLY D 551     199.307 161.776 256.953  1.00 73.47           C  
ATOM   5951  O   GLY D 551     200.358 162.213 257.419  1.00 73.47           O  
ATOM   5952  N   GLN D 552     198.432 162.554 256.315  1.00 76.74           N  
ATOM   5953  CA  GLN D 552     198.649 163.994 256.203  1.00 76.74           C  
ATOM   5954  C   GLN D 552     198.522 164.683 257.557  1.00 76.74           C  
ATOM   5955  O   GLN D 552     199.311 165.582 257.880  1.00 76.74           O  
ATOM   5956  CB  GLN D 552     197.668 164.591 255.198  1.00 76.74           C  
ATOM   5957  CG  GLN D 552     197.928 166.045 254.874  1.00 76.74           C  
ATOM   5958  CD  GLN D 552     199.300 166.259 254.271  1.00 76.74           C  
ATOM   5959  OE1 GLN D 552     200.194 166.807 254.914  1.00 76.74           O  
ATOM   5960  NE2 GLN D 552     199.478 165.814 253.035  1.00 76.74           N  
ATOM   5961  N   LYS D 553     197.538 164.262 258.359  1.00 72.90           N  
ATOM   5962  CA  LYS D 553     197.354 164.811 259.699  1.00 72.90           C  
ATOM   5963  C   LYS D 553     198.549 164.511 260.588  1.00 72.90           C  
ATOM   5964  O   LYS D 553     198.947 165.342 261.410  1.00 72.90           O  
ATOM   5965  CB  LYS D 553     196.089 164.227 260.323  1.00 72.90           C  
ATOM   5966  CG  LYS D 553     195.543 165.003 261.496  1.00 72.90           C  
ATOM   5967  CD  LYS D 553     194.660 166.142 261.049  1.00 72.90           C  
ATOM   5968  CE  LYS D 553     193.950 166.755 262.238  1.00 72.90           C  
ATOM   5969  NZ  LYS D 553     193.370 165.704 263.116  1.00 72.90           N  
ATOM   5970  N   LEU D 554     199.133 163.327 260.432  1.00 70.00           N  
ATOM   5971  CA  LEU D 554     200.316 162.987 261.209  1.00 70.00           C  
ATOM   5972  C   LEU D 554     201.550 163.727 260.695  1.00 70.00           C  
ATOM   5973  O   LEU D 554     202.309 164.304 261.483  1.00 70.00           O  
ATOM   5974  CB  LEU D 554     200.502 161.475 261.173  1.00 70.00           C  
ATOM   5975  CG  LEU D 554     201.373 160.826 262.234  1.00 70.00           C  
ATOM   5976  CD1 LEU D 554     200.732 160.917 263.603  1.00 70.00           C  
ATOM   5977  CD2 LEU D 554     201.634 159.401 261.854  1.00 70.00           C  
ATOM   5978  N   PHE D 555     201.728 163.775 259.369  1.00 72.38           N  
ATOM   5979  CA  PHE D 555     202.859 164.444 258.735  1.00 72.38           C  
ATOM   5980  C   PHE D 555     202.879 165.945 258.976  1.00 72.38           C  
ATOM   5981  O   PHE D 555     203.947 166.557 258.880  1.00 72.38           O  
ATOM   5982  CB  PHE D 555     202.828 164.166 257.230  1.00 72.38           C  
ATOM   5983  CG  PHE D 555     204.037 164.657 256.488  1.00 72.38           C  
ATOM   5984  CD1 PHE D 555     205.225 163.952 256.523  1.00 72.38           C  
ATOM   5985  CD2 PHE D 555     203.980 165.831 255.753  1.00 72.38           C  
ATOM   5986  CE1 PHE D 555     206.330 164.406 255.837  1.00 72.38           C  
ATOM   5987  CE2 PHE D 555     205.083 166.292 255.073  1.00 72.38           C  
ATOM   5988  CZ  PHE D 555     206.259 165.579 255.115  1.00 72.38           C  
ATOM   5989  N   ASN D 556     201.732 166.549 259.295  1.00 73.95           N  
ATOM   5990  CA  ASN D 556     201.738 167.936 259.749  1.00 73.95           C  
ATOM   5991  C   ASN D 556     202.524 168.104 261.045  1.00 73.95           C  
ATOM   5992  O   ASN D 556     203.143 169.149 261.259  1.00 73.95           O  
ATOM   5993  CB  ASN D 556     200.306 168.430 259.924  1.00 73.95           C  
ATOM   5994  CG  ASN D 556     199.711 168.936 258.632  1.00 73.95           C  
ATOM   5995  OD1 ASN D 556     200.373 168.948 257.595  1.00 73.95           O  
ATOM   5996  ND2 ASN D 556     198.452 169.350 258.682  1.00 73.95           N  
ATOM   5997  N   MET D 557     202.506 167.096 261.919  1.00 71.52           N  
ATOM   5998  CA  MET D 557     203.314 167.139 263.132  1.00 71.52           C  
ATOM   5999  C   MET D 557     204.740 166.673 262.880  1.00 71.52           C  
ATOM   6000  O   MET D 557     205.684 167.236 263.444  1.00 71.52           O  
ATOM   6001  CB  MET D 557     202.678 166.280 264.213  1.00 71.52           C  
ATOM   6002  CG  MET D 557     203.389 166.297 265.551  1.00 71.52           C  
ATOM   6003  SD  MET D 557     204.335 164.804 265.872  1.00 71.52           S  
ATOM   6004  CE  MET D 557     203.086 163.563 265.581  1.00 71.52           C  
ATOM   6005  N   LEU D 558     204.910 165.644 262.042  1.00 69.12           N  
ATOM   6006  CA  LEU D 558     206.251 165.156 261.719  1.00 69.12           C  
ATOM   6007  C   LEU D 558     207.111 166.179 260.992  1.00 69.12           C  
ATOM   6008  O   LEU D 558     208.334 166.169 261.152  1.00 69.12           O  
ATOM   6009  CB  LEU D 558     206.169 163.885 260.876  1.00 69.12           C  
ATOM   6010  CG  LEU D 558     205.987 162.465 261.387  1.00 69.12           C  
ATOM   6011  CD1 LEU D 558     204.684 162.208 261.952  1.00 69.12           C  
ATOM   6012  CD2 LEU D 558     206.223 161.505 260.236  1.00 69.12           C  
ATOM   6013  N   ARG D 559     206.512 167.076 260.216  1.00 72.16           N  
ATOM   6014  CA  ARG D 559     207.323 168.030 259.473  1.00 72.16           C  
ATOM   6015  C   ARG D 559     207.842 169.158 260.351  1.00 72.16           C  
ATOM   6016  O   ARG D 559     208.798 169.837 259.963  1.00 72.16           O  
ATOM   6017  CB  ARG D 559     206.530 168.608 258.299  1.00 72.16           C  
ATOM   6018  CG  ARG D 559     205.394 169.525 258.694  1.00 72.16           C  
ATOM   6019  CD  ARG D 559     205.034 170.449 257.555  1.00 72.16           C  
ATOM   6020  NE  ARG D 559     206.225 171.033 256.955  1.00 72.16           N  
ATOM   6021  CZ  ARG D 559     206.807 172.148 257.376  1.00 72.16           C  
ATOM   6022  NH1 ARG D 559     206.330 172.830 258.404  1.00 72.16           N  
ATOM   6023  NH2 ARG D 559     207.897 172.585 256.754  1.00 72.16           N  
ATOM   6024  N   LEU D 560     207.247 169.357 261.528  1.00 70.65           N  
ATOM   6025  CA  LEU D 560     207.632 170.475 262.380  1.00 70.65           C  
ATOM   6026  C   LEU D 560     208.967 170.226 263.063  1.00 70.65           C  
ATOM   6027  O   LEU D 560     209.800 171.134 263.150  1.00 70.65           O  
ATOM   6028  CB  LEU D 560     206.546 170.733 263.418  1.00 70.65           C  
ATOM   6029  CG  LEU D 560     205.223 171.228 262.846  1.00 70.65           C  
ATOM   6030  CD1 LEU D 560     204.206 171.408 263.951  1.00 70.65           C  
ATOM   6031  CD2 LEU D 560     205.422 172.510 262.068  1.00 70.65           C  
ATOM   6032  N   GLY D 561     209.189 169.015 263.551  1.00 71.24           N  
ATOM   6033  CA  GLY D 561     210.389 168.762 264.328  1.00 71.24           C  
ATOM   6034  C   GLY D 561     210.294 169.431 265.682  1.00 71.24           C  
ATOM   6035  O   GLY D 561     209.286 169.320 266.386  1.00 71.24           O  
ATOM   6036  N   LYS D 562     211.355 170.135 266.058  1.00 71.88           N  
ATOM   6037  CA  LYS D 562     211.412 170.865 267.315  1.00 71.88           C  
ATOM   6038  C   LYS D 562     211.167 172.355 267.128  1.00 71.88           C  
ATOM   6039  O   LYS D 562     211.361 173.127 268.070  1.00 71.88           O  
ATOM   6040  CB  LYS D 562     212.769 170.639 267.979  1.00 71.88           C  
ATOM   6041  CG  LYS D 562     212.737 170.478 269.478  1.00 71.88           C  
ATOM   6042  CD  LYS D 562     214.149 170.394 270.020  1.00 71.88           C  
ATOM   6043  CE  LYS D 562     214.157 170.069 271.500  1.00 71.88           C  
ATOM   6044  NZ  LYS D 562     215.528 169.730 271.973  1.00 71.88           N  
ATOM   6045  N   SER D 563     210.750 172.772 265.931  1.00 76.23           N  
ATOM   6046  CA  SER D 563     210.577 174.191 265.637  1.00 76.23           C  
ATOM   6047  C   SER D 563     209.377 174.783 266.355  1.00 76.23           C  
ATOM   6048  O   SER D 563     209.384 175.969 266.698  1.00 76.23           O  
ATOM   6049  CB  SER D 563     210.433 174.400 264.136  1.00 76.23           C  
ATOM   6050  OG  SER D 563     209.199 173.884 263.676  1.00 76.23           O  
ATOM   6051  N   GLU D 564     208.359 174.006 266.568  1.00 79.10           N  
ATOM   6052  CA  GLU D 564     207.160 174.459 267.240  1.00 79.10           C  
ATOM   6053  C   GLU D 564     207.130 173.914 268.657  1.00 79.10           C  
ATOM   6054  O   GLU D 564     207.849 172.963 268.975  1.00 79.10           O  
ATOM   6055  CB  GLU D 564     205.917 174.000 266.470  1.00 79.10           C  
ATOM   6056  CG  GLU D 564     205.734 174.662 265.115  1.00 79.10           C  
ATOM   6057  CD  GLU D 564     205.938 176.163 265.147  1.00 79.10           C  
ATOM   6058  OE1 GLU D 564     205.251 176.851 265.929  1.00 79.10           O  
ATOM   6059  OE2 GLU D 564     206.784 176.660 264.377  1.00 79.10           O  
ATOM   6060  N   PRO D 565     206.359 174.530 269.555  1.00 74.61           N  
ATOM   6061  CA  PRO D 565     206.136 173.920 270.869  1.00 74.61           C  
ATOM   6062  C   PRO D 565     205.429 172.582 270.741  1.00 74.61           C  
ATOM   6063  O   PRO D 565     204.655 172.355 269.809  1.00 74.61           O  
ATOM   6064  CB  PRO D 565     205.253 174.946 271.580  1.00 74.61           C  
ATOM   6065  CG  PRO D 565     205.654 176.222 270.978  1.00 74.61           C  
ATOM   6066  CD  PRO D 565     205.861 175.916 269.529  1.00 74.61           C  
ATOM   6067  N   TRP D 566     205.722 171.680 271.684  1.00 70.55           N  
ATOM   6068  CA  TRP D 566     205.093 170.363 271.660  1.00 70.55           C  
ATOM   6069  C   TRP D 566     203.602 170.455 271.940  1.00 70.55           C  
ATOM   6070  O   TRP D 566     202.840 169.579 271.518  1.00 70.55           O  
ATOM   6071  CB  TRP D 566     205.770 169.424 272.658  1.00 70.55           C  
ATOM   6072  CG  TRP D 566     205.622 169.812 274.083  1.00 70.55           C  
ATOM   6073  CD1 TRP D 566     206.474 170.575 274.815  1.00 70.55           C  
ATOM   6074  CD2 TRP D 566     204.571 169.420 274.970  1.00 70.55           C  
ATOM   6075  NE1 TRP D 566     206.009 170.704 276.097  1.00 70.55           N  
ATOM   6076  CE2 TRP D 566     204.841 170.000 276.217  1.00 70.55           C  
ATOM   6077  CE3 TRP D 566     203.420 168.643 274.824  1.00 70.55           C  
ATOM   6078  CZ2 TRP D 566     204.006 169.829 277.312  1.00 70.55           C  
ATOM   6079  CZ3 TRP D 566     202.593 168.476 275.909  1.00 70.55           C  
ATOM   6080  CH2 TRP D 566     202.890 169.064 277.138  1.00 70.55           C  
ATOM   6081  N   THR D 567     203.177 171.499 272.652  1.00 73.21           N  
ATOM   6082  CA  THR D 567     201.757 171.775 272.809  1.00 73.21           C  
ATOM   6083  C   THR D 567     201.113 172.105 271.467  1.00 73.21           C  
ATOM   6084  O   THR D 567     200.000 171.656 271.177  1.00 73.21           O  
ATOM   6085  CB  THR D 567     201.573 172.919 273.797  1.00 73.21           C  
ATOM   6086  OG1 THR D 567     202.325 174.043 273.342  1.00 73.21           O  
ATOM   6087  CG2 THR D 567     202.093 172.525 275.156  1.00 73.21           C  
ATOM   6088  N   LEU D 568     201.808 172.876 270.629  1.00 75.90           N  
ATOM   6089  CA  LEU D 568     201.280 173.212 269.309  1.00 75.90           C  
ATOM   6090  C   LEU D 568     201.273 172.003 268.382  1.00 75.90           C  
ATOM   6091  O   LEU D 568     200.351 171.842 267.578  1.00 75.90           O  
ATOM   6092  CB  LEU D 568     202.081 174.357 268.695  1.00 75.90           C  
ATOM   6093  CG  LEU D 568     201.558 174.971 267.394  1.00 75.90           C  
ATOM   6094  CD1 LEU D 568     200.058 175.179 267.426  1.00 75.90           C  
ATOM   6095  CD2 LEU D 568     202.248 176.288 267.146  1.00 75.90           C  
ATOM   6096  N   ALA D 569     202.290 171.144 268.476  1.00 72.46           N  
ATOM   6097  CA  ALA D 569     202.301 169.917 267.684  1.00 72.46           C  
ATOM   6098  C   ALA D 569     201.185 168.975 268.118  1.00 72.46           C  
ATOM   6099  O   ALA D 569     200.536 168.332 267.279  1.00 72.46           O  
ATOM   6100  CB  ALA D 569     203.662 169.238 267.805  1.00 72.46           C  
ATOM   6101  N   LEU D 570     200.935 168.905 269.427  1.00 72.75           N  
ATOM   6102  CA  LEU D 570     199.834 168.103 269.941  1.00 72.75           C  
ATOM   6103  C   LEU D 570     198.492 168.663 269.485  1.00 72.75           C  
ATOM   6104  O   LEU D 570     197.599 167.901 269.105  1.00 72.75           O  
ATOM   6105  CB  LEU D 570     199.910 168.047 271.464  1.00 72.75           C  
ATOM   6106  CG  LEU D 570     199.293 166.849 272.175  1.00 72.75           C  
ATOM   6107  CD1 LEU D 570     199.926 165.572 271.688  1.00 72.75           C  
ATOM   6108  CD2 LEU D 570     199.470 166.990 273.668  1.00 72.75           C  
ATOM   6109  N   GLU D 571     198.352 169.992 269.464  1.00 77.57           N  
ATOM   6110  CA  GLU D 571     197.144 170.617 268.932  1.00 77.57           C  
ATOM   6111  C   GLU D 571     196.998 170.376 267.436  1.00 77.57           C  
ATOM   6112  O   GLU D 571     195.874 170.298 266.928  1.00 77.57           O  
ATOM   6113  CB  GLU D 571     197.167 172.118 269.217  1.00 77.57           C  
ATOM   6114  CG  GLU D 571     195.863 172.842 268.944  1.00 77.57           C  
ATOM   6115  CD  GLU D 571     195.607 173.959 269.925  1.00 77.57           C  
ATOM   6116  OE1 GLU D 571     195.874 173.764 271.126  1.00 77.57           O  
ATOM   6117  OE2 GLU D 571     195.140 175.033 269.495  1.00 77.57           O  
ATOM   6118  N   ASN D 572     198.117 170.250 266.723  1.00 75.96           N  
ATOM   6119  CA  ASN D 572     198.061 169.878 265.317  1.00 75.96           C  
ATOM   6120  C   ASN D 572     197.547 168.460 265.135  1.00 75.96           C  
ATOM   6121  O   ASN D 572     196.848 168.182 264.156  1.00 75.96           O  
ATOM   6122  CB  ASN D 572     199.435 170.025 264.668  1.00 75.96           C  
ATOM   6123  CG  ASN D 572     199.734 171.446 264.263  1.00 75.96           C  
ATOM   6124  OD1 ASN D 572     198.994 172.369 264.602  1.00 75.96           O  
ATOM   6125  ND2 ASN D 572     200.818 171.633 263.525  1.00 75.96           N  
ATOM   6126  N   VAL D 573     197.869 167.549 266.054  1.00 74.02           N  
ATOM   6127  CA  VAL D 573     197.369 166.189 265.878  1.00 74.02           C  
ATOM   6128  C   VAL D 573     195.997 166.002 266.514  1.00 74.02           C  
ATOM   6129  O   VAL D 573     195.015 165.731 265.817  1.00 74.02           O  
ATOM   6130  CB  VAL D 573     198.329 165.135 266.445  1.00 74.02           C  
ATOM   6131  CG1 VAL D 573     197.886 163.759 266.000  1.00 74.02           C  
ATOM   6132  CG2 VAL D 573     199.702 165.391 265.995  1.00 74.02           C  
ATOM   6133  N   VAL D 574     195.913 166.146 267.839  1.00 73.60           N  
ATOM   6134  CA  VAL D 574     194.712 165.743 268.560  1.00 73.60           C  
ATOM   6135  C   VAL D 574     193.778 166.900 268.860  1.00 73.60           C  
ATOM   6136  O   VAL D 574     192.716 166.678 269.456  1.00 73.60           O  
ATOM   6137  CB  VAL D 574     195.072 165.042 269.885  1.00 73.60           C  
ATOM   6138  CG1 VAL D 574     195.919 163.833 269.624  1.00 73.60           C  
ATOM   6139  CG2 VAL D 574     195.711 165.988 270.876  1.00 73.60           C  
ATOM   6140  N   GLY D 575     194.117 168.121 268.451  1.00 77.03           N  
ATOM   6141  CA  GLY D 575     193.271 169.256 268.768  1.00 77.03           C  
ATOM   6142  C   GLY D 575     193.240 169.635 270.232  1.00 77.03           C  
ATOM   6143  O   GLY D 575     192.357 170.390 270.647  1.00 77.03           O  
ATOM   6144  N   ALA D 576     194.176 169.125 271.027  1.00 78.08           N  
ATOM   6145  CA  ALA D 576     194.361 169.498 272.418  1.00 78.08           C  
ATOM   6146  C   ALA D 576     195.825 169.846 272.635  1.00 78.08           C  
ATOM   6147  O   ALA D 576     196.710 169.305 271.971  1.00 78.08           O  
ATOM   6148  CB  ALA D 576     193.939 168.376 273.369  1.00 78.08           C  
ATOM   6149  N   LYS D 577     196.076 170.745 273.578  1.00 79.79           N  
ATOM   6150  CA  LYS D 577     197.419 171.246 273.827  1.00 79.79           C  
ATOM   6151  C   LYS D 577     198.052 170.653 275.076  1.00 79.79           C  
ATOM   6152  O   LYS D 577     199.151 171.063 275.451  1.00 79.79           O  
ATOM   6153  CB  LYS D 577     197.398 172.772 273.936  1.00 79.79           C  
ATOM   6154  CG  LYS D 577     196.688 173.298 275.166  1.00 79.79           C  
ATOM   6155  CD  LYS D 577     196.607 174.810 275.137  1.00 79.79           C  
ATOM   6156  CE  LYS D 577     195.652 175.276 274.055  1.00 79.79           C  
ATOM   6157  NZ  LYS D 577     196.041 176.591 273.479  1.00 79.79           N  
ATOM   6158  N   ASN D 578     197.393 169.700 275.723  1.00 77.97           N  
ATOM   6159  CA  ASN D 578     197.877 169.144 276.974  1.00 77.97           C  
ATOM   6160  C   ASN D 578     197.641 167.644 276.967  1.00 77.97           C  
ATOM   6161  O   ASN D 578     196.855 167.130 276.169  1.00 77.97           O  
ATOM   6162  CB  ASN D 578     197.191 169.789 278.183  1.00 77.97           C  
ATOM   6163  CG  ASN D 578     198.076 169.809 279.409  1.00 77.97           C  
ATOM   6164  OD1 ASN D 578     199.186 169.280 279.394  1.00 77.97           O  
ATOM   6165  ND2 ASN D 578     197.590 170.424 280.479  1.00 77.97           N  
ATOM   6166  N   MET D 579     198.401 166.949 277.816  1.00 74.90           N  
ATOM   6167  CA  MET D 579     198.282 165.504 277.965  1.00 74.90           C  
ATOM   6168  C   MET D 579     196.876 165.109 278.379  1.00 74.90           C  
ATOM   6169  O   MET D 579     196.299 165.693 279.299  1.00 74.90           O  
ATOM   6170  CB  MET D 579     199.260 165.000 279.024  1.00 74.90           C  
ATOM   6171  CG  MET D 579     200.563 164.460 278.509  1.00 74.90           C  
ATOM   6172  SD  MET D 579     201.515 163.615 279.784  1.00 74.90           S  
ATOM   6173  CE  MET D 579     201.217 164.673 281.194  1.00 74.90           C  
ATOM   6174  N   ASN D 580     196.328 164.109 277.706  1.00 71.97           N  
ATOM   6175  CA  ASN D 580     195.003 163.618 278.030  1.00 71.97           C  
ATOM   6176  C   ASN D 580     195.146 162.125 278.248  1.00 71.97           C  
ATOM   6177  O   ASN D 580     195.845 161.445 277.495  1.00 71.97           O  
ATOM   6178  CB  ASN D 580     193.996 163.931 276.926  1.00 71.97           C  
ATOM   6179  CG  ASN D 580     192.567 163.817 277.399  1.00 71.97           C  
ATOM   6180  OD1 ASN D 580     192.311 163.604 278.583  1.00 71.97           O  
ATOM   6181  ND2 ASN D 580     191.624 163.975 276.480  1.00 71.97           N  
ATOM   6182  N   VAL D 581     194.492 161.616 279.287  1.00 70.41           N  
ATOM   6183  CA  VAL D 581     194.472 160.182 279.526  1.00 70.41           C  
ATOM   6184  C   VAL D 581     193.228 159.486 278.982  1.00 70.41           C  
ATOM   6185  O   VAL D 581     193.196 158.244 278.963  1.00 70.41           O  
ATOM   6186  CB  VAL D 581     194.645 159.919 281.037  1.00 70.41           C  
ATOM   6187  CG1 VAL D 581     193.322 160.013 281.760  1.00 70.41           C  
ATOM   6188  CG2 VAL D 581     195.380 158.632 281.294  1.00 70.41           C  
ATOM   6189  N   ARG D 582     192.198 160.234 278.577  1.00 73.75           N  
ATOM   6190  CA  ARG D 582     191.000 159.636 277.983  1.00 73.75           C  
ATOM   6191  C   ARG D 582     191.238 158.711 276.784  1.00 73.75           C  
ATOM   6192  O   ARG D 582     190.511 157.708 276.687  1.00 73.75           O  
ATOM   6193  CB  ARG D 582     189.998 160.743 277.611  1.00 73.75           C  
ATOM   6194  CG  ARG D 582     189.564 161.680 278.729  1.00 73.75           C  
ATOM   6195  CD  ARG D 582     189.025 161.037 280.015  1.00 73.75           C  
ATOM   6196  NE  ARG D 582     187.969 160.053 279.790  1.00 73.75           N  
ATOM   6197  CZ  ARG D 582     188.112 158.736 279.858  1.00 73.75           C  
ATOM   6198  NH1 ARG D 582     189.199 158.183 280.365  1.00 73.75           N  
ATOM   6199  NH2 ARG D 582     187.111 157.954 279.464  1.00 73.75           N  
ATOM   6200  N   PRO D 583     192.166 158.973 275.841  1.00 68.99           N  
ATOM   6201  CA  PRO D 583     192.427 157.962 274.802  1.00 68.99           C  
ATOM   6202  C   PRO D 583     192.942 156.628 275.312  1.00 68.99           C  
ATOM   6203  O   PRO D 583     192.597 155.590 274.737  1.00 68.99           O  
ATOM   6204  CB  PRO D 583     193.462 158.652 273.917  1.00 68.99           C  
ATOM   6205  CG  PRO D 583     193.091 160.032 273.973  1.00 68.99           C  
ATOM   6206  CD  PRO D 583     192.738 160.267 275.404  1.00 68.99           C  
ATOM   6207  N   LEU D 584     193.754 156.620 276.372  1.00 65.73           N  
ATOM   6208  CA  LEU D 584     194.315 155.365 276.859  1.00 65.73           C  
ATOM   6209  C   LEU D 584     193.249 154.514 277.530  1.00 65.73           C  
ATOM   6210  O   LEU D 584     193.201 153.298 277.327  1.00 65.73           O  
ATOM   6211  CB  LEU D 584     195.473 155.652 277.819  1.00 65.73           C  
ATOM   6212  CG  LEU D 584     196.404 154.555 278.351  1.00 65.73           C  
ATOM   6213  CD1 LEU D 584     197.727 155.192 278.665  1.00 65.73           C  
ATOM   6214  CD2 LEU D 584     195.908 153.836 279.592  1.00 65.73           C  
ATOM   6215  N   LEU D 585     192.383 155.135 278.327  1.00 69.03           N  
ATOM   6216  CA  LEU D 585     191.300 154.390 278.952  1.00 69.03           C  
ATOM   6217  C   LEU D 585     190.225 154.027 277.943  1.00 69.03           C  
ATOM   6218  O   LEU D 585     189.520 153.029 278.126  1.00 69.03           O  
ATOM   6219  CB  LEU D 585     190.704 155.179 280.117  1.00 69.03           C  
ATOM   6220  CG  LEU D 585     191.410 155.233 281.478  1.00 69.03           C  
ATOM   6221  CD1 LEU D 585     192.665 156.073 281.492  1.00 69.03           C  
ATOM   6222  CD2 LEU D 585     190.444 155.744 282.526  1.00 69.03           C  
ATOM   6223  N   ASN D 586     190.075 154.824 276.885  1.00 71.28           N  
ATOM   6224  CA  ASN D 586     189.163 154.452 275.813  1.00 71.28           C  
ATOM   6225  C   ASN D 586     189.705 153.269 275.017  1.00 71.28           C  
ATOM   6226  O   ASN D 586     188.926 152.460 274.503  1.00 71.28           O  
ATOM   6227  CB  ASN D 586     188.908 155.667 274.922  1.00 71.28           C  
ATOM   6228  CG  ASN D 586     188.131 155.328 273.676  1.00 71.28           C  
ATOM   6229  OD1 ASN D 586     187.025 154.797 273.749  1.00 71.28           O  
ATOM   6230  ND2 ASN D 586     188.698 155.646 272.520  1.00 71.28           N  
ATOM   6231  N   TYR D 587     191.033 153.151 274.917  1.00 68.67           N  
ATOM   6232  CA  TYR D 587     191.650 151.992 274.278  1.00 68.67           C  
ATOM   6233  C   TYR D 587     191.378 150.718 275.066  1.00 68.67           C  
ATOM   6234  O   TYR D 587     191.086 149.670 274.482  1.00 68.67           O  
ATOM   6235  CB  TYR D 587     193.155 152.217 274.136  1.00 68.67           C  
ATOM   6236  CG  TYR D 587     193.909 151.160 273.356  1.00 68.67           C  
ATOM   6237  CD1 TYR D 587     194.073 151.271 271.986  1.00 68.67           C  
ATOM   6238  CD2 TYR D 587     194.492 150.074 273.996  1.00 68.67           C  
ATOM   6239  CE1 TYR D 587     194.772 150.324 271.273  1.00 68.67           C  
ATOM   6240  CE2 TYR D 587     195.187 149.120 273.290  1.00 68.67           C  
ATOM   6241  CZ  TYR D 587     195.323 149.250 271.931  1.00 68.67           C  
ATOM   6242  OH  TYR D 587     196.021 148.303 271.223  1.00 68.67           O  
ATOM   6243  N   PHE D 588     191.473 150.786 276.392  1.00 67.43           N  
ATOM   6244  CA  PHE D 588     191.353 149.615 277.245  1.00 67.43           C  
ATOM   6245  C   PHE D 588     189.956 149.466 277.829  1.00 67.43           C  
ATOM   6246  O   PHE D 588     189.797 148.827 278.872  1.00 67.43           O  
ATOM   6247  CB  PHE D 588     192.386 149.679 278.368  1.00 67.43           C  
ATOM   6248  CG  PHE D 588     193.788 149.431 277.910  1.00 67.43           C  
ATOM   6249  CD1 PHE D 588     194.225 148.147 277.646  1.00 67.43           C  
ATOM   6250  CD2 PHE D 588     194.670 150.481 277.742  1.00 67.43           C  
ATOM   6251  CE1 PHE D 588     195.514 147.919 277.219  1.00 67.43           C  
ATOM   6252  CE2 PHE D 588     195.960 150.258 277.315  1.00 67.43           C  
ATOM   6253  CZ  PHE D 588     196.381 148.977 277.056  1.00 67.43           C  
ATOM   6254  N   GLU D 589     188.953 150.063 277.186  1.00 77.64           N  
ATOM   6255  CA  GLU D 589     187.585 150.047 277.707  1.00 77.64           C  
ATOM   6256  C   GLU D 589     186.952 148.652 277.797  1.00 77.64           C  
ATOM   6257  O   GLU D 589     186.347 148.360 278.846  1.00 77.64           O  
ATOM   6258  CB  GLU D 589     186.743 151.052 276.900  1.00 77.64           C  
ATOM   6259  CG  GLU D 589     185.210 151.142 277.149  1.00 77.64           C  
ATOM   6260  CD  GLU D 589     184.353 150.052 276.513  1.00 77.64           C  
ATOM   6261  OE1 GLU D 589     184.807 149.417 275.542  1.00 77.64           O  
ATOM   6262  OE2 GLU D 589     183.221 149.833 276.992  1.00 77.64           O  
ATOM   6263  N   PRO D 590     187.018 147.757 276.784  1.00 77.42           N  
ATOM   6264  CA  PRO D 590     186.409 146.433 277.001  1.00 77.42           C  
ATOM   6265  C   PRO D 590     187.178 145.587 277.987  1.00 77.42           C  
ATOM   6266  O   PRO D 590     186.567 144.799 278.720  1.00 77.42           O  
ATOM   6267  CB  PRO D 590     186.400 145.793 275.605  1.00 77.42           C  
ATOM   6268  CG  PRO D 590     186.849 146.816 274.674  1.00 77.42           C  
ATOM   6269  CD  PRO D 590     187.625 147.802 275.436  1.00 77.42           C  
ATOM   6270  N   LEU D 591     188.496 145.763 278.057  1.00 76.97           N  
ATOM   6271  CA  LEU D 591     189.264 145.114 279.107  1.00 76.97           C  
ATOM   6272  C   LEU D 591     188.909 145.673 280.477  1.00 76.97           C  
ATOM   6273  O   LEU D 591     188.872 144.921 281.452  1.00 76.97           O  
ATOM   6274  CB  LEU D 591     190.754 145.267 278.837  1.00 76.97           C  
ATOM   6275  CG  LEU D 591     191.634 144.509 279.820  1.00 76.97           C  
ATOM   6276  CD1 LEU D 591     191.565 143.025 279.541  1.00 76.97           C  
ATOM   6277  CD2 LEU D 591     193.023 145.004 279.717  1.00 76.97           C  
ATOM   6278  N   PHE D 592     188.606 146.970 280.562  1.00 78.38           N  
ATOM   6279  CA  PHE D 592     188.181 147.557 281.829  1.00 78.38           C  
ATOM   6280  C   PHE D 592     186.843 146.989 282.283  1.00 78.38           C  
ATOM   6281  O   PHE D 592     186.670 146.680 283.468  1.00 78.38           O  
ATOM   6282  CB  PHE D 592     188.110 149.077 281.703  1.00 78.38           C  
ATOM   6283  CG  PHE D 592     187.995 149.796 283.016  1.00 78.38           C  
ATOM   6284  CD1 PHE D 592     188.557 149.271 284.165  1.00 78.38           C  
ATOM   6285  CD2 PHE D 592     187.341 151.012 283.093  1.00 78.38           C  
ATOM   6286  CE1 PHE D 592     188.457 149.936 285.365  1.00 78.38           C  
ATOM   6287  CE2 PHE D 592     187.240 151.683 284.294  1.00 78.38           C  
ATOM   6288  CZ  PHE D 592     187.802 151.143 285.429  1.00 78.38           C  
ATOM   6289  N   THR D 593     185.893 146.829 281.356  1.00 81.65           N  
ATOM   6290  CA  THR D 593     184.614 146.219 281.720  1.00 81.65           C  
ATOM   6291  C   THR D 593     184.777 144.751 282.102  1.00 81.65           C  
ATOM   6292  O   THR D 593     184.135 144.278 283.046  1.00 81.65           O  
ATOM   6293  CB  THR D 593     183.615 146.359 280.576  1.00 81.65           C  
ATOM   6294  OG1 THR D 593     184.121 145.691 279.416  1.00 81.65           O  
ATOM   6295  CG2 THR D 593     183.375 147.821 280.255  1.00 81.65           C  
ATOM   6296  N   TRP D 594     185.648 144.024 281.397  1.00 85.28           N  
ATOM   6297  CA  TRP D 594     185.919 142.626 281.730  1.00 85.28           C  
ATOM   6298  C   TRP D 594     186.578 142.483 283.101  1.00 85.28           C  
ATOM   6299  O   TRP D 594     186.232 141.580 283.879  1.00 85.28           O  
ATOM   6300  CB  TRP D 594     186.788 142.023 280.632  1.00 85.28           C  
ATOM   6301  CG  TRP D 594     187.003 140.563 280.719  1.00 85.28           C  
ATOM   6302  CD1 TRP D 594     186.192 139.583 280.238  1.00 85.28           C  
ATOM   6303  CD2 TRP D 594     188.144 139.908 281.269  1.00 85.28           C  
ATOM   6304  NE1 TRP D 594     186.743 138.351 280.485  1.00 85.28           N  
ATOM   6305  CE2 TRP D 594     187.946 138.527 281.116  1.00 85.28           C  
ATOM   6306  CE3 TRP D 594     189.309 140.357 281.892  1.00 85.28           C  
ATOM   6307  CZ2 TRP D 594     188.873 137.592 281.553  1.00 85.28           C  
ATOM   6308  CZ3 TRP D 594     190.222 139.430 282.333  1.00 85.28           C  
ATOM   6309  CH2 TRP D 594     189.998 138.064 282.168  1.00 85.28           C  
ATOM   6310  N   LEU D 595     187.518 143.376 283.418  1.00 83.02           N  
ATOM   6311  CA  LEU D 595     188.178 143.354 284.717  1.00 83.02           C  
ATOM   6312  C   LEU D 595     187.226 143.756 285.829  1.00 83.02           C  
ATOM   6313  O   LEU D 595     187.345 143.255 286.950  1.00 83.02           O  
ATOM   6314  CB  LEU D 595     189.395 144.275 284.704  1.00 83.02           C  
ATOM   6315  CG  LEU D 595     190.621 143.753 283.956  1.00 83.02           C  
ATOM   6316  CD1 LEU D 595     191.755 144.755 284.001  1.00 83.02           C  
ATOM   6317  CD2 LEU D 595     191.048 142.414 284.491  1.00 83.02           C  
ATOM   6318  N   LYS D 596     186.287 144.663 285.544  1.00 85.37           N  
ATOM   6319  CA  LYS D 596     185.231 144.954 286.505  1.00 85.37           C  
ATOM   6320  C   LYS D 596     184.321 143.753 286.707  1.00 85.37           C  
ATOM   6321  O   LYS D 596     183.803 143.551 287.810  1.00 85.37           O  
ATOM   6322  CB  LYS D 596     184.398 146.145 286.039  1.00 85.37           C  
ATOM   6323  CG  LYS D 596     185.000 147.508 286.284  1.00 85.37           C  
ATOM   6324  CD  LYS D 596     183.975 148.573 285.943  1.00 85.37           C  
ATOM   6325  CE  LYS D 596     184.502 149.966 286.188  1.00 85.37           C  
ATOM   6326  NZ  LYS D 596     184.764 150.212 287.632  1.00 85.37           N  
ATOM   6327  N   ASP D 597     184.104 142.962 285.653  1.00 91.92           N  
ATOM   6328  CA  ASP D 597     183.257 141.781 285.776  1.00 91.92           C  
ATOM   6329  C   ASP D 597     183.904 140.705 286.637  1.00 91.92           C  
ATOM   6330  O   ASP D 597     183.234 140.110 287.488  1.00 91.92           O  
ATOM   6331  CB  ASP D 597     182.916 141.220 284.397  1.00 91.92           C  
ATOM   6332  CG  ASP D 597     181.978 142.118 283.622  1.00 91.92           C  
ATOM   6333  OD1 ASP D 597     181.545 143.147 284.183  1.00 91.92           O  
ATOM   6334  OD2 ASP D 597     181.673 141.798 282.454  1.00 91.92           O  
ATOM   6335  N   GLN D 598     185.191 140.424 286.440  1.00 93.50           N  
ATOM   6336  CA  GLN D 598     185.776 139.297 287.157  1.00 93.50           C  
ATOM   6337  C   GLN D 598     186.487 139.680 288.446  1.00 93.50           C  
ATOM   6338  O   GLN D 598     187.151 138.829 289.042  1.00 93.50           O  
ATOM   6339  CB  GLN D 598     186.728 138.500 286.274  1.00 93.50           C  
ATOM   6340  CG  GLN D 598     186.036 137.784 285.150  1.00 93.50           C  
ATOM   6341  CD  GLN D 598     187.001 136.982 284.335  1.00 93.50           C  
ATOM   6342  OE1 GLN D 598     188.203 137.007 284.590  1.00 93.50           O  
ATOM   6343  NE2 GLN D 598     186.489 136.246 283.357  1.00 93.50           N  
ATOM   6344  N   ASN D 599     186.374 140.926 288.896  1.00 93.21           N  
ATOM   6345  CA  ASN D 599     186.904 141.291 290.201  1.00 93.21           C  
ATOM   6346  C   ASN D 599     185.804 141.421 291.242  1.00 93.21           C  
ATOM   6347  O   ASN D 599     185.992 142.110 292.249  1.00 93.21           O  
ATOM   6348  CB  ASN D 599     187.708 142.585 290.115  1.00 93.21           C  
ATOM   6349  CG  ASN D 599     189.060 142.382 289.481  1.00 93.21           C  
ATOM   6350  OD1 ASN D 599     189.657 141.316 289.602  1.00 93.21           O  
ATOM   6351  ND2 ASN D 599     189.553 143.404 288.799  1.00 93.21           N  
ATOM   6352  N   LYS D 600     184.658 140.778 291.011  1.00100.68           N  
ATOM   6353  CA  LYS D 600     183.552 140.871 291.956  1.00100.68           C  
ATOM   6354  C   LYS D 600     183.854 140.107 293.238  1.00100.68           C  
ATOM   6355  O   LYS D 600     183.596 140.605 294.340  1.00100.68           O  
ATOM   6356  CB  LYS D 600     182.268 140.344 291.303  1.00100.68           C  
ATOM   6357  CG  LYS D 600     180.933 140.445 292.098  1.00100.68           C  
ATOM   6358  CD  LYS D 600     180.658 141.682 292.999  1.00100.68           C  
ATOM   6359  CE  LYS D 600     180.756 143.051 292.293  1.00100.68           C  
ATOM   6360  NZ  LYS D 600     180.779 144.178 293.265  1.00100.68           N  
ATOM   6361  N   ASN D 601     184.400 138.898 293.116  1.00105.98           N  
ATOM   6362  CA  ASN D 601     184.741 138.117 294.299  1.00105.98           C  
ATOM   6363  C   ASN D 601     186.009 138.630 294.970  1.00105.98           C  
ATOM   6364  O   ASN D 601     186.102 138.641 296.202  1.00105.98           O  
ATOM   6365  CB  ASN D 601     184.894 136.644 293.924  1.00105.98           C  
ATOM   6366  CG  ASN D 601     183.575 135.902 293.941  1.00105.98           C  
ATOM   6367  OD1 ASN D 601     182.507 136.514 293.931  1.00105.98           O  
ATOM   6368  ND2 ASN D 601     183.641 134.576 293.965  1.00105.98           N  
ATOM   6369  N   SER D 602     186.988 139.057 294.178  1.00103.89           N  
ATOM   6370  CA  SER D 602     188.253 139.543 294.699  1.00103.89           C  
ATOM   6371  C   SER D 602     188.113 140.971 295.219  1.00103.89           C  
ATOM   6372  O   SER D 602     187.107 141.650 295.000  1.00103.89           O  
ATOM   6373  CB  SER D 602     189.339 139.470 293.628  1.00103.89           C  
ATOM   6374  OG  SER D 602     189.066 140.368 292.570  1.00103.89           O  
ATOM   6375  N   PHE D 603     189.146 141.423 295.922  1.00102.81           N  
ATOM   6376  CA  PHE D 603     189.184 142.760 296.496  1.00102.81           C  
ATOM   6377  C   PHE D 603     190.036 143.660 295.613  1.00102.81           C  
ATOM   6378  O   PHE D 603     191.237 143.421 295.452  1.00102.81           O  
ATOM   6379  CB  PHE D 603     189.752 142.721 297.914  1.00102.81           C  
ATOM   6380  CG  PHE D 603     189.796 144.060 298.589  1.00102.81           C  
ATOM   6381  CD1 PHE D 603     188.641 144.639 299.091  1.00102.81           C  
ATOM   6382  CD2 PHE D 603     190.996 144.744 298.720  1.00102.81           C  
ATOM   6383  CE1 PHE D 603     188.682 145.875 299.714  1.00102.81           C  
ATOM   6384  CE2 PHE D 603     191.045 145.978 299.341  1.00102.81           C  
ATOM   6385  CZ  PHE D 603     189.887 146.544 299.838  1.00102.81           C  
ATOM   6386  N   VAL D 604     189.417 144.687 295.051  1.00 99.16           N  
ATOM   6387  CA  VAL D 604     190.139 145.677 294.263  1.00 99.16           C  
ATOM   6388  C   VAL D 604     190.848 146.632 295.217  1.00 99.16           C  
ATOM   6389  O   VAL D 604     190.326 146.974 296.285  1.00 99.16           O  
ATOM   6390  CB  VAL D 604     189.178 146.392 293.287  1.00 99.16           C  
ATOM   6391  CG1 VAL D 604     188.032 147.090 294.016  1.00 99.16           C  
ATOM   6392  CG2 VAL D 604     189.921 147.349 292.361  1.00 99.16           C  
ATOM   6393  N   GLY D 605     192.071 147.022 294.870  1.00 98.38           N  
ATOM   6394  CA  GLY D 605     192.877 147.848 295.740  1.00 98.38           C  
ATOM   6395  C   GLY D 605     193.763 147.028 296.657  1.00 98.38           C  
ATOM   6396  O   GLY D 605     193.634 145.810 296.790  1.00 98.38           O  
ATOM   6397  N   TRP D 606     194.691 147.725 297.303  1.00 97.70           N  
ATOM   6398  CA  TRP D 606     195.672 147.098 298.172  1.00 97.70           C  
ATOM   6399  C   TRP D 606     195.794 147.864 299.480  1.00 97.70           C  
ATOM   6400  O   TRP D 606     195.342 149.004 299.608  1.00 97.70           O  
ATOM   6401  CB  TRP D 606     197.042 147.013 297.490  1.00 97.70           C  
ATOM   6402  CG  TRP D 606     197.540 148.337 297.005  1.00 97.70           C  
ATOM   6403  CD1 TRP D 606     198.235 149.265 297.718  1.00 97.70           C  
ATOM   6404  CD2 TRP D 606     197.399 148.868 295.686  1.00 97.70           C  
ATOM   6405  NE1 TRP D 606     198.520 150.351 296.930  1.00 97.70           N  
ATOM   6406  CE2 TRP D 606     198.014 150.132 295.677  1.00 97.70           C  
ATOM   6407  CE3 TRP D 606     196.804 148.402 294.514  1.00 97.70           C  
ATOM   6408  CZ2 TRP D 606     198.061 150.928 294.540  1.00 97.70           C  
ATOM   6409  CZ3 TRP D 606     196.849 149.194 293.389  1.00 97.70           C  
ATOM   6410  CH2 TRP D 606     197.471 150.443 293.409  1.00 97.70           C  
ATOM   6411  N   SER D 607     196.420 147.211 300.452  1.00111.18           N  
ATOM   6412  CA  SER D 607     196.779 147.811 301.725  1.00111.18           C  
ATOM   6413  C   SER D 607     198.294 147.919 301.819  1.00111.18           C  
ATOM   6414  O   SER D 607     199.026 147.070 301.304  1.00111.18           O  
ATOM   6415  CB  SER D 607     196.240 146.990 302.898  1.00111.18           C  
ATOM   6416  OG  SER D 607     196.599 147.578 304.135  1.00111.18           O  
ATOM   6417  N   THR D 608     198.763 148.960 302.502  1.00117.11           N  
ATOM   6418  CA  THR D 608     200.194 149.204 302.621  1.00117.11           C  
ATOM   6419  C   THR D 608     200.865 148.358 303.696  1.00117.11           C  
ATOM   6420  O   THR D 608     202.078 148.489 303.891  1.00117.11           O  
ATOM   6421  CB  THR D 608     200.451 150.683 302.908  1.00117.11           C  
ATOM   6422  OG1 THR D 608     201.859 150.903 303.053  1.00117.11           O  
ATOM   6423  CG2 THR D 608     199.745 151.103 304.184  1.00117.11           C  
ATOM   6424  N   ASP D 609     200.118 147.509 304.394  1.00127.58           N  
ATOM   6425  CA  ASP D 609     200.690 146.650 305.417  1.00127.58           C  
ATOM   6426  C   ASP D 609     201.496 145.530 304.753  1.00127.58           C  
ATOM   6427  O   ASP D 609     201.341 145.240 303.564  1.00127.58           O  
ATOM   6428  CB  ASP D 609     199.569 146.091 306.302  1.00127.58           C  
ATOM   6429  CG  ASP D 609     200.080 145.432 307.572  1.00127.58           C  
ATOM   6430  OD1 ASP D 609     200.508 146.162 308.490  1.00127.58           O  
ATOM   6431  OD2 ASP D 609     200.053 144.186 307.650  1.00127.58           O  
ATOM   6432  N   TRP D 610     202.358 144.883 305.541  1.00131.24           N  
ATOM   6433  CA  TRP D 610     203.243 143.828 305.057  1.00131.24           C  
ATOM   6434  C   TRP D 610     202.605 142.446 305.146  1.00131.24           C  
ATOM   6435  O   TRP D 610     203.319 141.449 305.323  1.00131.24           O  
ATOM   6436  CB  TRP D 610     204.577 143.861 305.809  1.00131.24           C  
ATOM   6437  CG  TRP D 610     204.502 143.503 307.269  1.00131.24           C  
ATOM   6438  CD1 TRP D 610     203.898 144.215 308.265  1.00131.24           C  
ATOM   6439  CD2 TRP D 610     205.061 142.339 307.890  1.00131.24           C  
ATOM   6440  NE1 TRP D 610     204.044 143.564 309.467  1.00131.24           N  
ATOM   6441  CE2 TRP D 610     204.755 142.410 309.264  1.00131.24           C  
ATOM   6442  CE3 TRP D 610     205.791 141.243 307.417  1.00131.24           C  
ATOM   6443  CZ2 TRP D 610     205.152 141.427 310.168  1.00131.24           C  
ATOM   6444  CZ3 TRP D 610     206.184 140.268 308.316  1.00131.24           C  
ATOM   6445  CH2 TRP D 610     205.864 140.367 309.676  1.00131.24           C  
ATOM   6446  N   SER D 611     201.273 142.381 305.050  1.00127.80           N  
ATOM   6447  CA  SER D 611     200.539 141.121 305.178  1.00127.80           C  
ATOM   6448  C   SER D 611     200.942 140.009 304.202  1.00127.80           C  
ATOM   6449  O   SER D 611     200.914 138.842 304.630  1.00127.80           O  
ATOM   6450  CB  SER D 611     199.031 141.404 305.086  1.00127.80           C  
ATOM   6451  OG  SER D 611     198.280 140.211 305.224  1.00127.80           O  
ATOM   6452  N   PRO D 612     201.254 140.250 302.911  1.00126.14           N  
ATOM   6453  CA  PRO D 612     201.840 139.143 302.126  1.00126.14           C  
ATOM   6454  C   PRO D 612     203.187 138.682 302.659  1.00126.14           C  
ATOM   6455  O   PRO D 612     203.351 137.492 302.959  1.00126.14           O  
ATOM   6456  CB  PRO D 612     201.947 139.728 300.710  1.00126.14           C  
ATOM   6457  CG  PRO D 612     201.841 141.183 300.876  1.00126.14           C  
ATOM   6458  CD  PRO D 612     200.923 141.380 302.020  1.00126.14           C  
ATOM   6459  N   TYR D 613     204.146 139.592 302.811  1.00128.32           N  
ATOM   6460  CA  TYR D 613     205.435 139.249 303.396  1.00128.32           C  
ATOM   6461  C   TYR D 613     206.008 140.571 303.909  1.00128.32           C  
ATOM   6462  O   TYR D 613     205.594 141.645 303.475  1.00128.32           O  
ATOM   6463  CB  TYR D 613     206.359 138.578 302.365  1.00128.32           C  
ATOM   6464  CG  TYR D 613     207.762 138.201 302.831  1.00128.32           C  
ATOM   6465  CD1 TYR D 613     208.064 138.021 304.184  1.00128.32           C  
ATOM   6466  CD2 TYR D 613     208.779 137.994 301.906  1.00128.32           C  
ATOM   6467  CE1 TYR D 613     209.337 137.672 304.597  1.00128.32           C  
ATOM   6468  CE2 TYR D 613     210.057 137.642 302.311  1.00128.32           C  
ATOM   6469  CZ  TYR D 613     210.328 137.483 303.656  1.00128.32           C  
ATOM   6470  OH  TYR D 613     211.594 137.132 304.065  1.00128.32           O  
TER    6471      TYR D 613                                                      
HETATM 6472  C1  NAG A1301     229.635 162.117 226.626  1.00104.20           C  
HETATM 6473  C2  NAG A1301     229.239 162.484 225.183  1.00104.20           C  
HETATM 6474  C3  NAG A1301     227.984 161.718 224.745  1.00104.20           C  
HETATM 6475  C4  NAG A1301     228.146 160.222 224.989  1.00104.20           C  
HETATM 6476  C5  NAG A1301     228.541 159.965 226.442  1.00104.20           C  
HETATM 6477  C6  NAG A1301     228.814 158.507 226.731  1.00104.20           C  
HETATM 6478  C7  NAG A1301     228.203 164.745 225.564  1.00104.20           C  
HETATM 6479  C8  NAG A1301     228.276 166.180 225.140  1.00104.20           C  
HETATM 6480  N2  NAG A1301     229.090 163.923 224.972  1.00104.20           N  
HETATM 6481  O3  NAG A1301     227.735 161.965 223.366  1.00104.20           O  
HETATM 6482  O4  NAG A1301     226.926 159.546 224.707  1.00104.20           O  
HETATM 6483  O5  NAG A1301     229.747 160.682 226.749  1.00104.20           O  
HETATM 6484  O6  NAG A1301     227.954 157.660 225.981  1.00104.20           O  
HETATM 6485  O7  NAG A1301     227.386 164.364 226.403  1.00104.20           O  
HETATM 6486  C1  NAG D 701     234.513 144.675 259.396  1.00120.00           C  
HETATM 6487  C2  NAG D 701     234.560 144.861 257.878  1.00120.00           C  
HETATM 6488  C3  NAG D 701     235.631 143.958 257.266  1.00120.00           C  
HETATM 6489  C4  NAG D 701     236.978 144.187 257.940  1.00120.00           C  
HETATM 6490  C5  NAG D 701     236.846 144.021 259.453  1.00120.00           C  
HETATM 6491  C6  NAG D 701     238.117 144.356 260.198  1.00120.00           C  
HETATM 6492  C7  NAG D 701     232.690 145.411 256.389  1.00120.00           C  
HETATM 6493  C8  NAG D 701     231.349 144.984 255.874  1.00120.00           C  
HETATM 6494  N2  NAG D 701     233.262 144.596 257.280  1.00120.00           N  
HETATM 6495  O3  NAG D 701     235.733 144.226 255.872  1.00120.00           O  
HETATM 6496  O4  NAG D 701     237.934 143.255 257.447  1.00120.00           O  
HETATM 6497  O5  NAG D 701     235.828 144.901 259.954  1.00120.00           O  
HETATM 6498  O6  NAG D 701     239.267 144.131 259.394  1.00120.00           O  
HETATM 6499  O7  NAG D 701     233.231 146.446 256.014  1.00120.00           O  
HETATM 6500  C1  NAG D 702     212.669 183.490 261.707  1.00101.80           C  
HETATM 6501  C2  NAG D 702     211.528 184.081 260.859  1.00101.80           C  
HETATM 6502  C3  NAG D 702     211.220 183.168 259.671  1.00101.80           C  
HETATM 6503  C4  NAG D 702     212.483 182.869 258.872  1.00101.80           C  
HETATM 6504  C5  NAG D 702     213.560 182.300 259.792  1.00101.80           C  
HETATM 6505  C6  NAG D 702     214.880 182.076 259.092  1.00101.80           C  
HETATM 6506  C7  NAG D 702     209.930 185.497 262.075  1.00101.80           C  
HETATM 6507  C8  NAG D 702     208.674 185.525 262.891  1.00101.80           C  
HETATM 6508  N2  NAG D 702     210.332 184.291 261.659  1.00101.80           N  
HETATM 6509  O3  NAG D 702     210.251 183.787 258.834  1.00101.80           O  
HETATM 6510  O4  NAG D 702     212.196 181.929 257.843  1.00101.80           O  
HETATM 6511  O5  NAG D 702     213.812 183.221 260.864  1.00101.80           O  
HETATM 6512  O6  NAG D 702     215.960 182.054 260.015  1.00101.80           O  
HETATM 6513  O7  NAG D 702     210.555 186.518 261.807  1.00101.80           O  
HETATM 6514  C1  NAG D 703     227.212 178.944 280.792  1.00103.22           C  
HETATM 6515  C2  NAG D 703     226.242 180.091 281.062  1.00103.22           C  
HETATM 6516  C3  NAG D 703     226.965 181.431 280.943  1.00103.22           C  
HETATM 6517  C4  NAG D 703     228.199 181.460 281.838  1.00103.22           C  
HETATM 6518  C5  NAG D 703     229.094 180.258 281.545  1.00103.22           C  
HETATM 6519  C6  NAG D 703     230.269 180.151 282.488  1.00103.22           C  
HETATM 6520  C7  NAG D 703     223.872 179.721 280.556  1.00103.22           C  
HETATM 6521  C8  NAG D 703     222.818 179.719 279.492  1.00103.22           C  
HETATM 6522  N2  NAG D 703     225.107 180.040 280.157  1.00103.22           N  
HETATM 6523  O3  NAG D 703     226.076 182.482 281.302  1.00103.22           O  
HETATM 6524  O4  NAG D 703     228.934 182.658 281.613  1.00103.22           O  
HETATM 6525  O5  NAG D 703     228.340 179.044 281.686  1.00103.22           O  
HETATM 6526  O6  NAG D 703     229.864 180.303 283.842  1.00103.22           O  
HETATM 6527  O7  NAG D 703     223.619 179.446 281.724  1.00103.22           O  
HETATM 6528  C1  NAG D 704     209.417 155.654 245.832  1.00109.91           C  
HETATM 6529  C2  NAG D 704     210.261 154.755 244.928  1.00109.91           C  
HETATM 6530  C3  NAG D 704     210.557 155.466 243.608  1.00109.91           C  
HETATM 6531  C4  NAG D 704     209.265 155.930 242.946  1.00109.91           C  
HETATM 6532  C5  NAG D 704     208.449 156.783 243.917  1.00109.91           C  
HETATM 6533  C6  NAG D 704     207.092 157.164 243.375  1.00109.91           C  
HETATM 6534  C7  NAG D 704     211.655 153.193 246.212  1.00109.91           C  
HETATM 6535  C8  NAG D 704     212.998 152.957 246.835  1.00109.91           C  
HETATM 6536  N2  NAG D 704     211.498 154.365 245.586  1.00109.91           N  
HETATM 6537  O3  NAG D 704     211.259 154.583 242.740  1.00109.91           O  
HETATM 6538  O4  NAG D 704     209.560 156.695 241.783  1.00109.91           O  
HETATM 6539  O5  NAG D 704     208.218 156.056 245.135  1.00109.91           O  
HETATM 6540  O6  NAG D 704     206.072 156.953 244.342  1.00109.91           O  
HETATM 6541  O7  NAG D 704     210.754 152.363 246.274  1.00109.91           O  
HETATM 6542  C1  NAG D 705     181.614 137.288 274.034  1.00118.40           C  
HETATM 6543  C2  NAG D 705     181.526 137.223 275.561  1.00118.40           C  
HETATM 6544  C3  NAG D 705     180.504 136.171 275.992  1.00118.40           C  
HETATM 6545  C4  NAG D 705     179.159 136.416 275.318  1.00118.40           C  
HETATM 6546  C5  NAG D 705     179.336 136.495 273.804  1.00118.40           C  
HETATM 6547  C6  NAG D 705     178.061 136.855 273.078  1.00118.40           C  
HETATM 6548  C7  NAG D 705     183.602 137.893 276.686  1.00118.40           C  
HETATM 6549  C8  NAG D 705     184.912 137.431 277.245  1.00118.40           C  
HETATM 6550  N2  NAG D 705     182.827 136.945 276.148  1.00118.40           N  
HETATM 6551  O3  NAG D 705     180.353 136.212 277.407  1.00118.40           O  
HETATM 6552  O4  NAG D 705     178.259 135.359 275.630  1.00118.40           O  
HETATM 6553  O5  NAG D 705     180.297 137.513 273.480  1.00118.40           O  
HETATM 6554  O6  NAG D 705     177.450 138.007 273.642  1.00118.40           O  
HETATM 6555  O7  NAG D 705     183.260 139.069 276.719  1.00118.40           O  
HETATM 6556  C1  NAG D 706     195.570 148.936 250.726  1.00100.53           C  
HETATM 6557  C2  NAG D 706     194.739 147.674 251.044  1.00100.53           C  
HETATM 6558  C3  NAG D 706     195.379 146.438 250.413  1.00100.53           C  
HETATM 6559  C4  NAG D 706     195.610 146.647 248.922  1.00100.53           C  
HETATM 6560  C5  NAG D 706     196.442 147.906 248.697  1.00100.53           C  
HETATM 6561  C6  NAG D 706     196.628 148.237 247.235  1.00100.53           C  
HETATM 6562  C7  NAG D 706     193.439 147.175 253.067  1.00100.53           C  
HETATM 6563  C8  NAG D 706     193.476 147.036 254.558  1.00100.53           C  
HETATM 6564  N2  NAG D 706     194.597 147.491 252.480  1.00100.53           N  
HETATM 6565  O3  NAG D 706     194.538 145.310 250.623  1.00100.53           O  
HETATM 6566  O4  NAG D 706     196.289 145.524 248.370  1.00100.53           O  
HETATM 6567  O5  NAG D 706     195.782 149.032 249.295  1.00100.53           O  
HETATM 6568  O6  NAG D 706     195.521 148.967 246.724  1.00100.53           O  
HETATM 6569  O7  NAG D 706     192.407 147.009 252.424  1.00100.53           O  
CONECT   52  263                                                                
CONECT  113 6472                                                                
CONECT  263   52                                                                
CONECT  411  823                                                                
CONECT  501 1577                                                                
CONECT  823  411                                                                
CONECT 1221 1274                                                                
CONECT 1274 1221                                                                
CONECT 1577  501                                                                
CONECT 1906 6486                                                                
CONECT 2205 6500                                                                
CONECT 2309 6514                                                                
CONECT 2532 2594                                                                
CONECT 2594 2532                                                                
CONECT 4097 6528                                                                
CONECT 4953 6542                                                                
CONECT 5799 5890                                                                
CONECT 5890 5799                                                                
CONECT 5920 6556                                                                
CONECT 6472  113 6473 6483                                                      
CONECT 6473 6472 6474 6480                                                      
CONECT 6474 6473 6475 6481                                                      
CONECT 6475 6474 6476 6482                                                      
CONECT 6476 6475 6477 6483                                                      
CONECT 6477 6476 6484                                                           
CONECT 6478 6479 6480 6485                                                      
CONECT 6479 6478                                                                
CONECT 6480 6473 6478                                                           
CONECT 6481 6474                                                                
CONECT 6482 6475                                                                
CONECT 6483 6472 6476                                                           
CONECT 6484 6477                                                                
CONECT 6485 6478                                                                
CONECT 6486 1906 6487 6497                                                      
CONECT 6487 6486 6488 6494                                                      
CONECT 6488 6487 6489 6495                                                      
CONECT 6489 6488 6490 6496                                                      
CONECT 6490 6489 6491 6497                                                      
CONECT 6491 6490 6498                                                           
CONECT 6492 6493 6494 6499                                                      
CONECT 6493 6492                                                                
CONECT 6494 6487 6492                                                           
CONECT 6495 6488                                                                
CONECT 6496 6489                                                                
CONECT 6497 6486 6490                                                           
CONECT 6498 6491                                                                
CONECT 6499 6492                                                                
CONECT 6500 2205 6501 6511                                                      
CONECT 6501 6500 6502 6508                                                      
CONECT 6502 6501 6503 6509                                                      
CONECT 6503 6502 6504 6510                                                      
CONECT 6504 6503 6505 6511                                                      
CONECT 6505 6504 6512                                                           
CONECT 6506 6507 6508 6513                                                      
CONECT 6507 6506                                                                
CONECT 6508 6501 6506                                                           
CONECT 6509 6502                                                                
CONECT 6510 6503                                                                
CONECT 6511 6500 6504                                                           
CONECT 6512 6505                                                                
CONECT 6513 6506                                                                
CONECT 6514 2309 6515 6525                                                      
CONECT 6515 6514 6516 6522                                                      
CONECT 6516 6515 6517 6523                                                      
CONECT 6517 6516 6518 6524                                                      
CONECT 6518 6517 6519 6525                                                      
CONECT 6519 6518 6526                                                           
CONECT 6520 6521 6522 6527                                                      
CONECT 6521 6520                                                                
CONECT 6522 6515 6520                                                           
CONECT 6523 6516                                                                
CONECT 6524 6517                                                                
CONECT 6525 6514 6518                                                           
CONECT 6526 6519                                                                
CONECT 6527 6520                                                                
CONECT 6528 4097 6529 6539                                                      
CONECT 6529 6528 6530 6536                                                      
CONECT 6530 6529 6531 6537                                                      
CONECT 6531 6530 6532 6538                                                      
CONECT 6532 6531 6533 6539                                                      
CONECT 6533 6532 6540                                                           
CONECT 6534 6535 6536 6541                                                      
CONECT 6535 6534                                                                
CONECT 6536 6529 6534                                                           
CONECT 6537 6530                                                                
CONECT 6538 6531                                                                
CONECT 6539 6528 6532                                                           
CONECT 6540 6533                                                                
CONECT 6541 6534                                                                
CONECT 6542 4953 6543 6553                                                      
CONECT 6543 6542 6544 6550                                                      
CONECT 6544 6543 6545 6551                                                      
CONECT 6545 6544 6546 6552                                                      
CONECT 6546 6545 6547 6553                                                      
CONECT 6547 6546 6554                                                           
CONECT 6548 6549 6550 6555                                                      
CONECT 6549 6548                                                                
CONECT 6550 6543 6548                                                           
CONECT 6551 6544                                                                
CONECT 6552 6545                                                                
CONECT 6553 6542 6546                                                           
CONECT 6554 6547                                                                
CONECT 6555 6548                                                                
CONECT 6556 5920 6557 6567                                                      
CONECT 6557 6556 6558 6564                                                      
CONECT 6558 6557 6559 6565                                                      
CONECT 6559 6558 6560 6566                                                      
CONECT 6560 6559 6561 6567                                                      
CONECT 6561 6560 6568                                                           
CONECT 6562 6563 6564 6569                                                      
CONECT 6563 6562                                                                
CONECT 6564 6557 6562                                                           
CONECT 6565 6558                                                                
CONECT 6566 6559                                                                
CONECT 6567 6556 6560                                                           
CONECT 6568 6561                                                                
CONECT 6569 6562                                                                
MASTER     1224    0    7   37   13    0    0    6 6567    2  117  146          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.