HEADER    MEMBRANE PROTEIN                        03-APR-22   7UL4              
TITLE     CRYOEM STRUCTURE OF INACTIVE MOR BOUND TO ALVIMOPAN AND MB6           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MU-TYPE OPIOID RECEPTOR;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: M-OR-1,MOR-1;                                               
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: MEGABODY 6;                                                
COMPND   8 CHAIN: D;                                                            
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MUS MUSCULUS;                                   
SOURCE   3 ORGANISM_COMMON: HOUSE MOUSE;                                        
SOURCE   4 ORGANISM_TAXID: 10090;                                               
SOURCE   5 GENE: OPRM1, MOR, OPRM;                                              
SOURCE   6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT;                            
SOURCE  12 ORGANISM_TAXID: 32630;                                               
SOURCE  13 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE  14 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ANTAGONIST, COMPLEX, MEMBRANE PROTEIN                                 
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    M.J.ROBERTSON,G.SKINIOTIS                                             
REVDAT   5   28-DEC-22 7UL4    1       JRNL                                     
REVDAT   4   30-NOV-22 7UL4    1       JRNL                                     
REVDAT   3   23-NOV-22 7UL4    1       JRNL                                     
REVDAT   2   02-NOV-22 7UL4    1       HETSYN                                   
REVDAT   1   29-JUN-22 7UL4    0                                                
JRNL        AUTH   M.J.ROBERTSON,M.M.PAPASERGI-SCOTT,F.HE,A.B.SEVEN,            
JRNL        AUTH 2 J.G.MEYEROWITZ,O.PANOVA,M.C.PEROTO,T.CHE,G.SKINIOTIS         
JRNL        TITL   STRUCTURE DETERMINATION OF INACTIVE-STATE GPCRS WITH A       
JRNL        TITL 2 UNIVERSAL NANOBODY.                                          
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  29  1188 2022              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   36396979                                                     
JRNL        DOI    10.1038/S41594-022-00859-8                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 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)  : 2.800                          
REMARK   3   NUMBER OF PARTICLES               : 301332                         
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 7UL4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-22.                  
REMARK 100 THE DEPOSITION ID IS D_1000264352.                                   
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                 : COMPLEX OF MOR AND NB6; MOR;      
REMARK 245                                    MB6                               
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : NULL                              
REMARK 245   SAMPLE VITRIFICATION DETAILS   : NULL                              
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.50                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : NULL                           
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : GATAN K3 (6K X 4K)             
REMARK 245   MINIMUM DEFOCUS (NM)              : 700.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 1500.00                        
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)  : 6138.00                        
REMARK 245   ILLUMINATION MODE                 : OTHER                          
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   -19                                                      
REMARK 465     LYS A   -18                                                      
REMARK 465     THR A   -17                                                      
REMARK 465     ILE A   -16                                                      
REMARK 465     ILE A   -15                                                      
REMARK 465     ALA A   -14                                                      
REMARK 465     LEU A   -13                                                      
REMARK 465     SER A   -12                                                      
REMARK 465     TYR A   -11                                                      
REMARK 465     ILE A   -10                                                      
REMARK 465     PHE A    -9                                                      
REMARK 465     CYS A    -8                                                      
REMARK 465     LEU A    -7                                                      
REMARK 465     VAL A    -6                                                      
REMARK 465     PHE A    -5                                                      
REMARK 465     ALA A    -4                                                      
REMARK 465     ASP A    -3                                                      
REMARK 465     TYR A    -2                                                      
REMARK 465     LYS A    -1                                                      
REMARK 465     ASP A     0                                                      
REMARK 465     ASP A     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ALA A     4                                                      
REMARK 465     MET A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     PRO A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     ASN A     9                                                      
REMARK 465     ILE A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     ASP A    12                                                      
REMARK 465     CYS A    13                                                      
REMARK 465     SER A    14                                                      
REMARK 465     ASP A    15                                                      
REMARK 465     PRO A    16                                                      
REMARK 465     LEU A    17                                                      
REMARK 465     ALA A    18                                                      
REMARK 465     PRO A    19                                                      
REMARK 465     ALA A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     CYS A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     PRO A    24                                                      
REMARK 465     ALA A    25                                                      
REMARK 465     PRO A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     SER A    28                                                      
REMARK 465     TRP A    29                                                      
REMARK 465     LEU A    30                                                      
REMARK 465     ASN A    31                                                      
REMARK 465     LEU A    32                                                      
REMARK 465     SER A    33                                                      
REMARK 465     HIS A    34                                                      
REMARK 465     VAL A    35                                                      
REMARK 465     ASP A    36                                                      
REMARK 465     GLY A    37                                                      
REMARK 465     ASN A    38                                                      
REMARK 465     GLN A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     ASP A    41                                                      
REMARK 465     PRO A    42                                                      
REMARK 465     CYS A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     PRO A    45                                                      
REMARK 465     ASN A    46                                                      
REMARK 465     ARG A    47                                                      
REMARK 465     THR A    48                                                      
REMARK 465     GLY A    49                                                      
REMARK 465     LEU A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     GLY A    52                                                      
REMARK 465     SER A    53                                                      
REMARK 465     HIS A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     LEU A    56                                                      
REMARK 465     CYS A    57                                                      
REMARK 465     PRO A    58                                                      
REMARK 465     GLN A    59                                                      
REMARK 465     THR A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     PRO A    63                                                      
REMARK 465     SER A    64                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     PRO A   353                                                      
REMARK 465     THR A   354                                                      
REMARK 465     SER A   355                                                      
REMARK 465     SER A   356                                                      
REMARK 465     THR A   357                                                      
REMARK 465     ILE A   358                                                      
REMARK 465     GLU A   359                                                      
REMARK 465     GLN A   360                                                      
REMARK 465     GLN A   361                                                      
REMARK 465     ASN A   362                                                      
REMARK 465     SER A   363                                                      
REMARK 465     ALA A   364                                                      
REMARK 465     ARG A   365                                                      
REMARK 465     ILE A   366                                                      
REMARK 465     ARG A   367                                                      
REMARK 465     GLN A   368                                                      
REMARK 465     ASN A   369                                                      
REMARK 465     THR A   370                                                      
REMARK 465     ARG A   371                                                      
REMARK 465     GLU A   372                                                      
REMARK 465     HIS A   373                                                      
REMARK 465     PRO A   374                                                      
REMARK 465     SER A   375                                                      
REMARK 465     THR A   376                                                      
REMARK 465     ALA A   377                                                      
REMARK 465     ASN A   378                                                      
REMARK 465     THR A   379                                                      
REMARK 465     VAL A   380                                                      
REMARK 465     ASP A   381                                                      
REMARK 465     ARG A   382                                                      
REMARK 465     THR A   383                                                      
REMARK 465     ASN A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     GLN A   386                                                      
REMARK 465     LEU A   387                                                      
REMARK 465     GLU A   388                                                      
REMARK 465     ASN A   389                                                      
REMARK 465     LEU A   390                                                      
REMARK 465     GLU A   391                                                      
REMARK 465     ALA A   392                                                      
REMARK 465     GLU A   393                                                      
REMARK 465     THR A   394                                                      
REMARK 465     ALA A   395                                                      
REMARK 465     PRO A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     PRO A   398                                                      
REMARK 465     ASP A   399                                                      
REMARK 465     ILE A   400                                                      
REMARK 465     HIS A   401                                                      
REMARK 465     HIS A   402                                                      
REMARK 465     HIS A   403                                                      
REMARK 465     HIS A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     GLN D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLN D     3                                                      
REMARK 465     LEU D     4                                                      
REMARK 465     GLN D     5                                                      
REMARK 465     GLU D     6                                                      
REMARK 465     SER D     7                                                      
REMARK 465     GLY D     8                                                      
REMARK 465     GLY D     9                                                      
REMARK 465     GLY D    10                                                      
REMARK 465     LEU D    11                                                      
REMARK 465     VAL D    12                                                      
REMARK 465     ARG D    13                                                      
REMARK 465     LYS D    14                                                      
REMARK 465     THR D    15                                                      
REMARK 465     THR D    16                                                      
REMARK 465     THR D    17                                                      
REMARK 465     SER D    18                                                      
REMARK 465     VAL D    19                                                      
REMARK 465     ILE D    20                                                      
REMARK 465     ASP D    21                                                      
REMARK 465     THR D    22                                                      
REMARK 465     THR D    23                                                      
REMARK 465     ASN D    24                                                      
REMARK 465     ASP D    25                                                      
REMARK 465     ALA D    26                                                      
REMARK 465     GLN D    27                                                      
REMARK 465     ASN D    28                                                      
REMARK 465     LEU D    29                                                      
REMARK 465     LEU D    30                                                      
REMARK 465     THR D    31                                                      
REMARK 465     GLN D    32                                                      
REMARK 465     ALA D    33                                                      
REMARK 465     GLN D    34                                                      
REMARK 465     THR D    35                                                      
REMARK 465     ILE D    36                                                      
REMARK 465     VAL D    37                                                      
REMARK 465     ASN D    38                                                      
REMARK 465     THR D    39                                                      
REMARK 465     LEU D    40                                                      
REMARK 465     LYS D    41                                                      
REMARK 465     ASP D    42                                                      
REMARK 465     TYR D    43                                                      
REMARK 465     CYS D    44                                                      
REMARK 465     PRO D    45                                                      
REMARK 465     ILE D    46                                                      
REMARK 465     LEU D    47                                                      
REMARK 465     ILE D    48                                                      
REMARK 465     ALA D    49                                                      
REMARK 465     LYS D    50                                                      
REMARK 465     SER D    51                                                      
REMARK 465     SER D    52                                                      
REMARK 465     SER D    53                                                      
REMARK 465     SER D    54                                                      
REMARK 465     ASN D    55                                                      
REMARK 465     GLY D    56                                                      
REMARK 465     GLY D    57                                                      
REMARK 465     THR D    58                                                      
REMARK 465     ASN D    59                                                      
REMARK 465     ASN D    60                                                      
REMARK 465     ALA D    61                                                      
REMARK 465     ASN D    62                                                      
REMARK 465     THR D    63                                                      
REMARK 465     PRO D    64                                                      
REMARK 465     SER D    65                                                      
REMARK 465     TRP D    66                                                      
REMARK 465     GLN D    67                                                      
REMARK 465     THR D    68                                                      
REMARK 465     ALA D    69                                                      
REMARK 465     GLY D    70                                                      
REMARK 465     GLY D    71                                                      
REMARK 465     GLY D    72                                                      
REMARK 465     LYS D    73                                                      
REMARK 465     ASN D    74                                                      
REMARK 465     SER D    75                                                      
REMARK 465     CYS D    76                                                      
REMARK 465     ALA D    77                                                      
REMARK 465     THR D    78                                                      
REMARK 465     PHE D    79                                                      
REMARK 465     GLY D    80                                                      
REMARK 465     ALA D    81                                                      
REMARK 465     GLU D    82                                                      
REMARK 465     PHE D    83                                                      
REMARK 465     SER D    84                                                      
REMARK 465     ALA D    85                                                      
REMARK 465     ALA D    86                                                      
REMARK 465     SER D    87                                                      
REMARK 465     ASP D    88                                                      
REMARK 465     MET D    89                                                      
REMARK 465     ILE D    90                                                      
REMARK 465     ASN D    91                                                      
REMARK 465     ASN D    92                                                      
REMARK 465     ALA D    93                                                      
REMARK 465     GLN D    94                                                      
REMARK 465     LYS D    95                                                      
REMARK 465     ILE D    96                                                      
REMARK 465     VAL D    97                                                      
REMARK 465     GLN D    98                                                      
REMARK 465     GLU D    99                                                      
REMARK 465     THR D   100                                                      
REMARK 465     GLN D   101                                                      
REMARK 465     GLN D   102                                                      
REMARK 465     LEU D   103                                                      
REMARK 465     SER D   104                                                      
REMARK 465     ALA D   105                                                      
REMARK 465     ASN D   106                                                      
REMARK 465     GLN D   107                                                      
REMARK 465     PRO D   108                                                      
REMARK 465     LYS D   109                                                      
REMARK 465     ASN D   110                                                      
REMARK 465     ILE D   111                                                      
REMARK 465     THR D   112                                                      
REMARK 465     GLN D   113                                                      
REMARK 465     PRO D   114                                                      
REMARK 465     HIS D   115                                                      
REMARK 465     ASN D   116                                                      
REMARK 465     LEU D   117                                                      
REMARK 465     ASN D   118                                                      
REMARK 465     LEU D   119                                                      
REMARK 465     ASN D   120                                                      
REMARK 465     SER D   121                                                      
REMARK 465     PRO D   122                                                      
REMARK 465     SER D   123                                                      
REMARK 465     SER D   124                                                      
REMARK 465     LEU D   125                                                      
REMARK 465     THR D   126                                                      
REMARK 465     ALA D   127                                                      
REMARK 465     LEU D   128                                                      
REMARK 465     ALA D   129                                                      
REMARK 465     GLN D   130                                                      
REMARK 465     LYS D   131                                                      
REMARK 465     MET D   132                                                      
REMARK 465     LEU D   133                                                      
REMARK 465     LYS D   134                                                      
REMARK 465     ASN D   135                                                      
REMARK 465     ALA D   136                                                      
REMARK 465     GLN D   137                                                      
REMARK 465     SER D   138                                                      
REMARK 465     GLN D   139                                                      
REMARK 465     ALA D   140                                                      
REMARK 465     GLU D   141                                                      
REMARK 465     ILE D   142                                                      
REMARK 465     LEU D   143                                                      
REMARK 465     LYS D   144                                                      
REMARK 465     LEU D   145                                                      
REMARK 465     ALA D   146                                                      
REMARK 465     ASN D   147                                                      
REMARK 465     GLN D   148                                                      
REMARK 465     VAL D   149                                                      
REMARK 465     GLU D   150                                                      
REMARK 465     SER D   151                                                      
REMARK 465     ASP D   152                                                      
REMARK 465     PHE D   153                                                      
REMARK 465     ASN D   154                                                      
REMARK 465     LYS D   155                                                      
REMARK 465     LEU D   156                                                      
REMARK 465     SER D   157                                                      
REMARK 465     SER D   158                                                      
REMARK 465     GLY D   159                                                      
REMARK 465     HIS D   160                                                      
REMARK 465     LEU D   161                                                      
REMARK 465     LYS D   162                                                      
REMARK 465     ASP D   163                                                      
REMARK 465     TYR D   164                                                      
REMARK 465     ILE D   165                                                      
REMARK 465     GLY D   166                                                      
REMARK 465     LYS D   167                                                      
REMARK 465     CYS D   168                                                      
REMARK 465     ASP D   169                                                      
REMARK 465     ALA D   170                                                      
REMARK 465     SER D   171                                                      
REMARK 465     ALA D   172                                                      
REMARK 465     ILE D   173                                                      
REMARK 465     SER D   174                                                      
REMARK 465     SER D   175                                                      
REMARK 465     ALA D   176                                                      
REMARK 465     ASN D   177                                                      
REMARK 465     MET D   178                                                      
REMARK 465     THR D   179                                                      
REMARK 465     MET D   180                                                      
REMARK 465     GLN D   181                                                      
REMARK 465     ASN D   182                                                      
REMARK 465     GLN D   183                                                      
REMARK 465     LYS D   184                                                      
REMARK 465     ASN D   185                                                      
REMARK 465     ASN D   186                                                      
REMARK 465     TRP D   187                                                      
REMARK 465     GLY D   188                                                      
REMARK 465     ASN D   189                                                      
REMARK 465     GLY D   190                                                      
REMARK 465     CYS D   191                                                      
REMARK 465     ALA D   192                                                      
REMARK 465     GLY D   193                                                      
REMARK 465     VAL D   194                                                      
REMARK 465     GLU D   195                                                      
REMARK 465     GLU D   196                                                      
REMARK 465     THR D   197                                                      
REMARK 465     GLN D   198                                                      
REMARK 465     SER D   199                                                      
REMARK 465     LEU D   200                                                      
REMARK 465     LEU D   201                                                      
REMARK 465     LYS D   202                                                      
REMARK 465     THR D   203                                                      
REMARK 465     SER D   204                                                      
REMARK 465     ALA D   205                                                      
REMARK 465     ALA D   206                                                      
REMARK 465     ASP D   207                                                      
REMARK 465     PHE D   208                                                      
REMARK 465     ASN D   209                                                      
REMARK 465     ASN D   210                                                      
REMARK 465     GLN D   211                                                      
REMARK 465     THR D   212                                                      
REMARK 465     PRO D   213                                                      
REMARK 465     GLN D   214                                                      
REMARK 465     ILE D   215                                                      
REMARK 465     ASN D   216                                                      
REMARK 465     GLN D   217                                                      
REMARK 465     ALA D   218                                                      
REMARK 465     GLN D   219                                                      
REMARK 465     ASN D   220                                                      
REMARK 465     LEU D   221                                                      
REMARK 465     ALA D   222                                                      
REMARK 465     ASN D   223                                                      
REMARK 465     THR D   224                                                      
REMARK 465     LEU D   225                                                      
REMARK 465     ILE D   226                                                      
REMARK 465     GLN D   227                                                      
REMARK 465     GLU D   228                                                      
REMARK 465     LEU D   229                                                      
REMARK 465     GLY D   230                                                      
REMARK 465     ASN D   231                                                      
REMARK 465     ASN D   232                                                      
REMARK 465     THR D   233                                                      
REMARK 465     TYR D   234                                                      
REMARK 465     GLU D   235                                                      
REMARK 465     GLN D   236                                                      
REMARK 465     LEU D   237                                                      
REMARK 465     SER D   238                                                      
REMARK 465     ARG D   239                                                      
REMARK 465     LEU D   240                                                      
REMARK 465     LEU D   241                                                      
REMARK 465     THR D   242                                                      
REMARK 465     ASN D   243                                                      
REMARK 465     ASP D   244                                                      
REMARK 465     ASN D   245                                                      
REMARK 465     GLY D   246                                                      
REMARK 465     THR D   247                                                      
REMARK 465     ASN D   248                                                      
REMARK 465     SER D   249                                                      
REMARK 465     LYS D   250                                                      
REMARK 465     THR D   251                                                      
REMARK 465     SER D   252                                                      
REMARK 465     ALA D   253                                                      
REMARK 465     GLN D   254                                                      
REMARK 465     ALA D   255                                                      
REMARK 465     ILE D   256                                                      
REMARK 465     ASN D   257                                                      
REMARK 465     GLN D   258                                                      
REMARK 465     ALA D   259                                                      
REMARK 465     VAL D   260                                                      
REMARK 465     ASN D   261                                                      
REMARK 465     ASN D   262                                                      
REMARK 465     LEU D   263                                                      
REMARK 465     ASN D   264                                                      
REMARK 465     GLU D   265                                                      
REMARK 465     ARG D   266                                                      
REMARK 465     ALA D   267                                                      
REMARK 465     LYS D   268                                                      
REMARK 465     THR D   269                                                      
REMARK 465     LEU D   270                                                      
REMARK 465     ALA D   271                                                      
REMARK 465     GLY D   272                                                      
REMARK 465     GLY D   273                                                      
REMARK 465     THR D   274                                                      
REMARK 465     THR D   275                                                      
REMARK 465     ASN D   276                                                      
REMARK 465     SER D   277                                                      
REMARK 465     PRO D   278                                                      
REMARK 465     ALA D   279                                                      
REMARK 465     TYR D   280                                                      
REMARK 465     GLN D   281                                                      
REMARK 465     ALA D   282                                                      
REMARK 465     THR D   283                                                      
REMARK 465     LEU D   284                                                      
REMARK 465     LEU D   285                                                      
REMARK 465     ALA D   286                                                      
REMARK 465     LEU D   287                                                      
REMARK 465     ARG D   288                                                      
REMARK 465     SER D   289                                                      
REMARK 465     VAL D   290                                                      
REMARK 465     LEU D   291                                                      
REMARK 465     GLY D   292                                                      
REMARK 465     LEU D   293                                                      
REMARK 465     TRP D   294                                                      
REMARK 465     ASN D   295                                                      
REMARK 465     SER D   296                                                      
REMARK 465     MET D   297                                                      
REMARK 465     GLY D   298                                                      
REMARK 465     TYR D   299                                                      
REMARK 465     ALA D   300                                                      
REMARK 465     VAL D   301                                                      
REMARK 465     ILE D   302                                                      
REMARK 465     CYS D   303                                                      
REMARK 465     GLY D   304                                                      
REMARK 465     GLY D   305                                                      
REMARK 465     TYR D   306                                                      
REMARK 465     THR D   307                                                      
REMARK 465     LYS D   308                                                      
REMARK 465     SER D   309                                                      
REMARK 465     PRO D   310                                                      
REMARK 465     GLY D   311                                                      
REMARK 465     GLU D   312                                                      
REMARK 465     ASN D   313                                                      
REMARK 465     ASN D   314                                                      
REMARK 465     GLN D   315                                                      
REMARK 465     LYS D   316                                                      
REMARK 465     ASP D   317                                                      
REMARK 465     PHE D   318                                                      
REMARK 465     HIS D   319                                                      
REMARK 465     TYR D   320                                                      
REMARK 465     THR D   321                                                      
REMARK 465     ASP D   322                                                      
REMARK 465     GLU D   323                                                      
REMARK 465     ASN D   324                                                      
REMARK 465     GLY D   325                                                      
REMARK 465     ASN D   326                                                      
REMARK 465     GLY D   327                                                      
REMARK 465     THR D   328                                                      
REMARK 465     THR D   329                                                      
REMARK 465     ILE D   330                                                      
REMARK 465     ASN D   331                                                      
REMARK 465     CYS D   332                                                      
REMARK 465     GLY D   333                                                      
REMARK 465     GLY D   334                                                      
REMARK 465     SER D   335                                                      
REMARK 465     THR D   336                                                      
REMARK 465     ASN D   337                                                      
REMARK 465     SER D   338                                                      
REMARK 465     ASN D   339                                                      
REMARK 465     GLY D   340                                                      
REMARK 465     THR D   341                                                      
REMARK 465     HIS D   342                                                      
REMARK 465     SER D   343                                                      
REMARK 465     TYR D   344                                                      
REMARK 465     ASN D   345                                                      
REMARK 465     GLY D   346                                                      
REMARK 465     THR D   347                                                      
REMARK 465     ASN D   348                                                      
REMARK 465     THR D   349                                                      
REMARK 465     LEU D   350                                                      
REMARK 465     LYS D   351                                                      
REMARK 465     ALA D   352                                                      
REMARK 465     ASP D   353                                                      
REMARK 465     LYS D   354                                                      
REMARK 465     ASN D   355                                                      
REMARK 465     VAL D   356                                                      
REMARK 465     SER D   357                                                      
REMARK 465     LEU D   358                                                      
REMARK 465     SER D   359                                                      
REMARK 465     ILE D   360                                                      
REMARK 465     GLU D   361                                                      
REMARK 465     GLN D   362                                                      
REMARK 465     TYR D   363                                                      
REMARK 465     GLU D   364                                                      
REMARK 465     LYS D   365                                                      
REMARK 465     ILE D   366                                                      
REMARK 465     HIS D   367                                                      
REMARK 465     GLU D   368                                                      
REMARK 465     ALA D   369                                                      
REMARK 465     TYR D   370                                                      
REMARK 465     GLN D   371                                                      
REMARK 465     ILE D   372                                                      
REMARK 465     LEU D   373                                                      
REMARK 465     SER D   374                                                      
REMARK 465     LYS D   375                                                      
REMARK 465     ALA D   376                                                      
REMARK 465     LEU D   377                                                      
REMARK 465     LYS D   378                                                      
REMARK 465     GLN D   379                                                      
REMARK 465     ALA D   380                                                      
REMARK 465     GLY D   381                                                      
REMARK 465     LEU D   382                                                      
REMARK 465     ALA D   383                                                      
REMARK 465     PRO D   384                                                      
REMARK 465     LEU D   385                                                      
REMARK 465     ASN D   386                                                      
REMARK 465     SER D   387                                                      
REMARK 465     LYS D   388                                                      
REMARK 465     GLY D   389                                                      
REMARK 465     GLU D   390                                                      
REMARK 465     LYS D   391                                                      
REMARK 465     LEU D   392                                                      
REMARK 465     GLU D   393                                                      
REMARK 465     ALA D   394                                                      
REMARK 465     HIS D   395                                                      
REMARK 465     VAL D   396                                                      
REMARK 465     THR D   397                                                      
REMARK 465     THR D   398                                                      
REMARK 465     SER D   399                                                      
REMARK 465     LYS D   400                                                      
REMARK 465     PRO D   401                                                      
REMARK 465     SER D   402                                                      
REMARK 465     LEU D   403                                                      
REMARK 465     ARG D   404                                                      
REMARK 465     ARG D   424                                                      
REMARK 465     VAL D   425                                                      
REMARK 465     SER D   426                                                      
REMARK 465     GLY D   427                                                      
REMARK 465     ASN D   428                                                      
REMARK 465     GLN D   429                                                      
REMARK 465     ARG D   430                                                      
REMARK 465     GLU D   431                                                      
REMARK 465     TYR D   444                                                      
REMARK 465     GLY D   445                                                      
REMARK 465     ASP D   446                                                      
REMARK 465     SER D   447                                                      
REMARK 465     VAL D   448                                                      
REMARK 465     LYS D   449                                                      
REMARK 465     GLY D   450                                                      
REMARK 465     ARG D   451                                                      
REMARK 465     PHE D   452                                                      
REMARK 465     ALA D   459                                                      
REMARK 465     LYS D   460                                                      
REMARK 465     GLN D   466                                                      
REMARK 465     MET D   467                                                      
REMARK 465     SER D   468                                                      
REMARK 465     SER D   469                                                      
REMARK 465     LEU D   470                                                      
REMARK 465     LYS D   471                                                      
REMARK 465     PRO D   472                                                      
REMARK 465     GLU D   473                                                      
REMARK 465     ASP D   474                                                      
REMARK 465     THR D   475                                                      
REMARK 465     GLY D   499                                                      
REMARK 465     THR D   500                                                      
REMARK 465     GLN D   501                                                      
REMARK 465     VAL D   502                                                      
REMARK 465     THR D   503                                                      
REMARK 465     VAL D   504                                                      
REMARK 465     SER D   505                                                      
REMARK 465     SER D   506                                                      
REMARK 465     HIS D   507                                                      
REMARK 465     HIS D   508                                                      
REMARK 465     HIS D   509                                                      
REMARK 465     HIS D   510                                                      
REMARK 465     HIS D   511                                                      
REMARK 465     HIS D   512                                                      
REMARK 465     GLU D   513                                                      
REMARK 465     PRO D   514                                                      
REMARK 465     GLU D   515                                                      
REMARK 465     ALA D   516                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     MET A  65    CG   SD   CE                                        
REMARK 470     VAL A  66    CG1  CG2                                            
REMARK 470     THR A  67    OG1  CG2                                            
REMARK 470     ILE A  77    CG1  CG2  CD1                                       
REMARK 470     PHE A  84    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     PHE A  87    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     MET A  90    CG   SD   CE                                        
REMARK 470     VAL A  94    CG1  CG2                                            
REMARK 470     ARG A  95    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A  96    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     THR A  97    OG1  CG2                                            
REMARK 470     LYS A  98    CG   CD   CE   NZ                                   
REMARK 470     LYS A 100    CG   CD   CE   NZ                                   
REMARK 470     VAL A 126    CG1  CG2                                            
REMARK 470     LEU A 129    CG   CD1  CD2                                       
REMARK 470     VAL A 173    CG1  CG2                                            
REMARK 470     LYS A 174    CG   CD   CE   NZ                                   
REMARK 470     LEU A 176    CG   CD1  CD2                                       
REMARK 470     ASP A 177    CG   OD1  OD2                                       
REMARK 470     PHE A 178    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ARG A 182    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ILE A 198    CG1  CG2  CD1                                       
REMARK 470     LYS A 209    CG   CD   CE   NZ                                   
REMARK 470     TYR A 210    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG A 211    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLN A 212    CG   CD   OE1  NE2                                  
REMARK 470     SER A 214    OG                                                  
REMARK 470     ASP A 216    CG   OD1  OD2                                       
REMARK 470     THR A 220    OG1  CG2                                            
REMARK 470     SER A 222    OG                                                  
REMARK 470     THR A 225    OG1  CG2                                            
REMARK 470     TRP A 226    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 226    CZ3  CH2                                            
REMARK 470     GLU A 229    CG   CD   OE1  OE2                                  
REMARK 470     MET A 243    CG   SD   CE                                        
REMARK 470     ARG A 258    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 260    CG   CD   CE   NZ                                   
REMARK 470     SER A 261    OG                                                  
REMARK 470     SER A 266    OG                                                  
REMARK 470     SER A 268    OG                                                  
REMARK 470     GLU A 270    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 271    CG   CD   CE   NZ                                   
REMARK 470     ARG A 273    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 277    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR A 299    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ILE A 306    CG1  CG2  CD1                                       
REMARK 470     THR A 307    OG1  CG2                                            
REMARK 470     GLU A 310    CG   CD   OE1  OE2                                  
REMARK 470     THR A 311    OG1  CG2                                            
REMARK 470     THR A 312    OG1  CG2                                            
REMARK 470     THR A 315    OG1  CG2                                            
REMARK 470     LEU A 335    CG   CD1  CD2                                       
REMARK 470     PHE A 338    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU A 341    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 344    CG   CD   CE   NZ                                   
REMARK 470     ARG A 345    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ARG A 348    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     GLU A 349    CG   CD   OE1  OE2                                  
REMARK 470     PHE A 350    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     CYS A 351    SG                                                  
REMARK 470     ILE A 352    CG1  CG2  CD1                                       
REMARK 470     LEU D 405    CG   CD1  CD2                                       
REMARK 470     SER D 406    OG                                                  
REMARK 470     CYS D 407    SG                                                  
REMARK 470     SER D 410    OG                                                  
REMARK 470     THR D 412    OG1  CG2                                            
REMARK 470     ILE D 413    CG1  CG2  CD1                                       
REMARK 470     ARG D 415    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TYR D 417    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     ARG D 423    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LEU D 432    CG   CD1  CD2                                       
REMARK 470     VAL D 433    CG1  CG2                                            
REMARK 470     SER D 435    OG                                                  
REMARK 470     ILE D 436    CG1  CG2  CD1                                       
REMARK 470     SER D 438    OG                                                  
REMARK 470     SER D 441    OG                                                  
REMARK 470     THR D 442    OG1  CG2                                            
REMARK 470     LYS D 443    CG   CD   CE   NZ                                   
REMARK 470     THR D 453    OG1  CG2                                            
REMARK 470     ILE D 454    CG1  CG2  CD1                                       
REMARK 470     SER D 455    OG                                                  
REMARK 470     ARG D 456    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP D 457    CG   OD1  OD2                                       
REMARK 470     ASN D 458    CG   OD1  ND2                                       
REMARK 470     ASN D 461    CG   OD1  ND2                                       
REMARK 470     THR D 462    OG1  CG2                                            
REMARK 470     VAL D 463    CG1  CG2                                            
REMARK 470     TYR D 464    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LEU D 465    CG   CD1  CD2                                       
REMARK 470     VAL D 477    CG1  CG2                                            
REMARK 470     CYS D 480    SG                                                  
REMARK 470     THR D 486    OG1  CG2                                            
REMARK 470     ILE D 488    CG1  CG2  CD1                                       
REMARK 470     GLU D 490    CG   CD   OE1  OE2                                  
REMARK 470     ASP D 494    CG   OD1  OD2                                       
REMARK 470     GLN D 498    CG   CD   OE1  NE2                                  
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    PHE A 241      -63.47   -138.09                                   
REMARK 500    TYR D 417      -78.60   -106.69                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-26591   RELATED DB: EMDB                             
REMARK 900 CRYOEM STRUCTURE OF INACTIVE MOR BOUND TO ALVIMOPAN AND MB6          
DBREF  7UL4 A    6   398  UNP    P42866   OPRM_MOUSE       6    398             
DBREF  7UL4 D    1   516  PDB    7UL4     7UL4             1    516             
SEQADV 7UL4 MET A  -19  UNP  P42866              INITIATING METHIONINE          
SEQADV 7UL4 LYS A  -18  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 THR A  -17  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ILE A  -16  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ILE A  -15  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ALA A  -14  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 LEU A  -13  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 SER A  -12  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 TYR A  -11  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ILE A  -10  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 PHE A   -9  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 CYS A   -8  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 LEU A   -7  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 VAL A   -6  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 PHE A   -5  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ALA A   -4  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ASP A   -3  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 TYR A   -2  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 LYS A   -1  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ASP A    0  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ASP A    1  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ASP A    2  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ASP A    3  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ALA A    4  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 MET A    5  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 LEU A  264  UNP  P42866    MET   264 ENGINEERED MUTATION            
SEQADV 7UL4 ARG A  269  UNP  P42866    LYS   269 ENGINEERED MUTATION            
SEQADV 7UL4 ASP A  399  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 ILE A  400  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  401  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  402  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  403  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  404  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  405  UNP  P42866              EXPRESSION TAG                 
SEQADV 7UL4 HIS A  406  UNP  P42866              EXPRESSION TAG                 
SEQRES   1 A  426  MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU          
SEQRES   2 A  426  VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY          
SEQRES   3 A  426  PRO GLY ASN ILE SER ASP CYS SER ASP PRO LEU ALA PRO          
SEQRES   4 A  426  ALA SER CYS SER PRO ALA PRO GLY SER TRP LEU ASN LEU          
SEQRES   5 A  426  SER HIS VAL ASP GLY ASN GLN SER ASP PRO CYS GLY PRO          
SEQRES   6 A  426  ASN ARG THR GLY LEU GLY GLY SER HIS SER LEU CYS PRO          
SEQRES   7 A  426  GLN THR GLY SER PRO SER MET VAL THR ALA ILE THR ILE          
SEQRES   8 A  426  MET ALA LEU TYR SER ILE VAL CYS VAL VAL GLY LEU PHE          
SEQRES   9 A  426  GLY ASN PHE LEU VAL MET TYR VAL ILE VAL ARG TYR THR          
SEQRES  10 A  426  LYS MET LYS THR ALA THR ASN ILE TYR ILE PHE ASN LEU          
SEQRES  11 A  426  ALA LEU ALA ASP ALA LEU ALA THR SER THR LEU PRO PHE          
SEQRES  12 A  426  GLN SER VAL ASN TYR LEU MET GLY THR TRP PRO PHE GLY          
SEQRES  13 A  426  ASN ILE LEU CYS LYS ILE VAL ILE SER ILE ASP TYR TYR          
SEQRES  14 A  426  ASN MET PHE THR SER ILE PHE THR LEU CYS THR MET SER          
SEQRES  15 A  426  VAL ASP ARG TYR ILE ALA VAL CYS HIS PRO VAL LYS ALA          
SEQRES  16 A  426  LEU ASP PHE ARG THR PRO ARG ASN ALA LYS ILE VAL ASN          
SEQRES  17 A  426  VAL CYS ASN TRP ILE LEU SER SER ALA ILE GLY LEU PRO          
SEQRES  18 A  426  VAL MET PHE MET ALA THR THR LYS TYR ARG GLN GLY SER          
SEQRES  19 A  426  ILE ASP CYS THR LEU THR PHE SER HIS PRO THR TRP TYR          
SEQRES  20 A  426  TRP GLU ASN LEU LEU LYS ILE CYS VAL PHE ILE PHE ALA          
SEQRES  21 A  426  PHE ILE MET PRO VAL LEU ILE ILE THR VAL CYS TYR GLY          
SEQRES  22 A  426  LEU MET ILE LEU ARG LEU LYS SER VAL ARG LEU LEU SER          
SEQRES  23 A  426  GLY SER ARG GLU LYS ASP ARG ASN LEU ARG ARG ILE THR          
SEQRES  24 A  426  ARG MET VAL LEU VAL VAL VAL ALA VAL PHE ILE VAL CYS          
SEQRES  25 A  426  TRP THR PRO ILE HIS ILE TYR VAL ILE ILE LYS ALA LEU          
SEQRES  26 A  426  ILE THR ILE PRO GLU THR THR PHE GLN THR VAL SER TRP          
SEQRES  27 A  426  HIS PHE CYS ILE ALA LEU GLY TYR THR ASN SER CYS LEU          
SEQRES  28 A  426  ASN PRO VAL LEU TYR ALA PHE LEU ASP GLU ASN PHE LYS          
SEQRES  29 A  426  ARG CYS PHE ARG GLU PHE CYS ILE PRO THR SER SER THR          
SEQRES  30 A  426  ILE GLU GLN GLN ASN SER ALA ARG ILE ARG GLN ASN THR          
SEQRES  31 A  426  ARG GLU HIS PRO SER THR ALA ASN THR VAL ASP ARG THR          
SEQRES  32 A  426  ASN HIS GLN LEU GLU ASN LEU GLU ALA GLU THR ALA PRO          
SEQRES  33 A  426  LEU PRO ASP ILE HIS HIS HIS HIS HIS HIS                      
SEQRES   1 D  516  GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL ARG          
SEQRES   2 D  516  LYS THR THR THR SER VAL ILE ASP THR THR ASN ASP ALA          
SEQRES   3 D  516  GLN ASN LEU LEU THR GLN ALA GLN THR ILE VAL ASN THR          
SEQRES   4 D  516  LEU LYS ASP TYR CYS PRO ILE LEU ILE ALA LYS SER SER          
SEQRES   5 D  516  SER SER ASN GLY GLY THR ASN ASN ALA ASN THR PRO SER          
SEQRES   6 D  516  TRP GLN THR ALA GLY GLY GLY LYS ASN SER CYS ALA THR          
SEQRES   7 D  516  PHE GLY ALA GLU PHE SER ALA ALA SER ASP MET ILE ASN          
SEQRES   8 D  516  ASN ALA GLN LYS ILE VAL GLN GLU THR GLN GLN LEU SER          
SEQRES   9 D  516  ALA ASN GLN PRO LYS ASN ILE THR GLN PRO HIS ASN LEU          
SEQRES  10 D  516  ASN LEU ASN SER PRO SER SER LEU THR ALA LEU ALA GLN          
SEQRES  11 D  516  LYS MET LEU LYS ASN ALA GLN SER GLN ALA GLU ILE LEU          
SEQRES  12 D  516  LYS LEU ALA ASN GLN VAL GLU SER ASP PHE ASN LYS LEU          
SEQRES  13 D  516  SER SER GLY HIS LEU LYS ASP TYR ILE GLY LYS CYS ASP          
SEQRES  14 D  516  ALA SER ALA ILE SER SER ALA ASN MET THR MET GLN ASN          
SEQRES  15 D  516  GLN LYS ASN ASN TRP GLY ASN GLY CYS ALA GLY VAL GLU          
SEQRES  16 D  516  GLU THR GLN SER LEU LEU LYS THR SER ALA ALA ASP PHE          
SEQRES  17 D  516  ASN ASN GLN THR PRO GLN ILE ASN GLN ALA GLN ASN LEU          
SEQRES  18 D  516  ALA ASN THR LEU ILE GLN GLU LEU GLY ASN ASN THR TYR          
SEQRES  19 D  516  GLU GLN LEU SER ARG LEU LEU THR ASN ASP ASN GLY THR          
SEQRES  20 D  516  ASN SER LYS THR SER ALA GLN ALA ILE ASN GLN ALA VAL          
SEQRES  21 D  516  ASN ASN LEU ASN GLU ARG ALA LYS THR LEU ALA GLY GLY          
SEQRES  22 D  516  THR THR ASN SER PRO ALA TYR GLN ALA THR LEU LEU ALA          
SEQRES  23 D  516  LEU ARG SER VAL LEU GLY LEU TRP ASN SER MET GLY TYR          
SEQRES  24 D  516  ALA VAL ILE CYS GLY GLY TYR THR LYS SER PRO GLY GLU          
SEQRES  25 D  516  ASN ASN GLN LYS ASP PHE HIS TYR THR ASP GLU ASN GLY          
SEQRES  26 D  516  ASN GLY THR THR ILE ASN CYS GLY GLY SER THR ASN SER          
SEQRES  27 D  516  ASN GLY THR HIS SER TYR ASN GLY THR ASN THR LEU LYS          
SEQRES  28 D  516  ALA ASP LYS ASN VAL SER LEU SER ILE GLU GLN TYR GLU          
SEQRES  29 D  516  LYS ILE HIS GLU ALA TYR GLN ILE LEU SER LYS ALA LEU          
SEQRES  30 D  516  LYS GLN ALA GLY LEU ALA PRO LEU ASN SER LYS GLY GLU          
SEQRES  31 D  516  LYS LEU GLU ALA HIS VAL THR THR SER LYS PRO SER LEU          
SEQRES  32 D  516  ARG LEU SER CYS ALA ALA SER GLY THR ILE PHE ARG LEU          
SEQRES  33 D  516  TYR ASP MET GLY TRP TYR ARG ARG VAL SER GLY ASN GLN          
SEQRES  34 D  516  ARG GLU LEU VAL ALA SER ILE THR SER GLY GLY SER THR          
SEQRES  35 D  516  LYS TYR GLY ASP SER VAL LYS GLY ARG PHE THR ILE SER          
SEQRES  36 D  516  ARG ASP ASN ALA LYS ASN THR VAL TYR LEU GLN MET SER          
SEQRES  37 D  516  SER LEU LYS PRO GLU ASP THR ALA VAL TYR TYR CYS ASN          
SEQRES  38 D  516  ALA GLU TYR ARG THR GLY ILE TRP GLU GLU LEU LEU ASP          
SEQRES  39 D  516  GLY TRP GLY GLN GLY THR GLN VAL THR VAL SER SER HIS          
SEQRES  40 D  516  HIS HIS HIS HIS HIS GLU PRO GLU ALA                          
HET    NG0  A 900      31                                                       
HETNAM     NG0 N-[(2S)-2-{[(3R,4R)-4-(3-HYDROXYPHENYL)-3,4-                     
HETNAM   2 NG0  DIMETHYLPIPERIDIN-1-YL]METHYL}-3-                               
HETNAM   3 NG0  PHENYLPROPANOYL]GLYCINE                                         
HETSYN     NG0 ALVIMOPAN                                                        
FORMUL   3  NG0    C25 H32 N2 O4                                                
FORMUL   4  HOH   *4(H2 O)                                                      
HELIX    1 AA1 MET A   65  TYR A   96  1                                  32    
HELIX    2 AA2 THR A  101  THR A  120  1                                  20    
HELIX    3 AA3 THR A  120  GLY A  131  1                                  12    
HELIX    4 AA4 GLY A  136  HIS A  171  1                                  36    
HELIX    5 AA5 HIS A  171  ARG A  179  1                                   9    
HELIX    6 AA6 THR A  180  ALA A  206  1                                  27    
HELIX    7 AA7 TRP A  226  ALA A  240  1                                  15    
HELIX    8 AA8 PHE A  241  SER A  261  1                                  21    
HELIX    9 AA9 SER A  268  LEU A  305  1                                  38    
HELIX   10 AB1 THR A  311  ASP A  340  1                                  30    
HELIX   11 AB2 ASP A  340  ILE A  352  1                                  13    
SHEET    1 AA1 2 THR A 207  TYR A 210  0                                        
SHEET    2 AA1 2 ILE A 215  THR A 218 -1  O  THR A 218   N  THR A 207           
SHEET    1 AA2 3 SER D 406  ALA D 408  0                                        
SHEET    2 AA2 3 THR D 462  TYR D 464 -1  O  VAL D 463   N  CYS D 407           
SHEET    3 AA2 3 SER D 455  ASP D 457 -1  N  SER D 455   O  TYR D 464           
SHEET    1 AA3 5 THR D 442  LYS D 443  0                                        
SHEET    2 AA3 5 ALA D 434  THR D 437 -1  N  SER D 435   O  LYS D 443           
SHEET    3 AA3 5 ARG D 415  TYR D 422 -1  N  MET D 419   O  ILE D 436           
SHEET    4 AA3 5 TYR D 479  ARG D 485 -1  O  TYR D 479   N  TYR D 422           
SHEET    5 AA3 5 LEU D 493  TRP D 496 -1  O  LEU D 493   N  TYR D 484           
SSBOND   1 CYS A  140    CYS A  217                          1555   1555  2.01  
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   MET A  65     156.467 152.712 181.880  1.00 15.89           N  
ATOM      2  CA  MET A  65     156.277 154.143 182.064  1.00 15.89           C  
ATOM      3  C   MET A  65     155.739 154.760 180.778  1.00 15.89           C  
ATOM      4  O   MET A  65     154.553 154.639 180.481  1.00 15.89           O  
ATOM      5  CB  MET A  65     157.590 154.806 182.478  1.00 15.89           C  
ATOM      6  N   VAL A  66     156.616 155.415 180.017  1.00 13.96           N  
ATOM      7  CA  VAL A  66     156.185 156.132 178.822  1.00 13.96           C  
ATOM      8  C   VAL A  66     155.445 155.200 177.872  1.00 13.96           C  
ATOM      9  O   VAL A  66     154.409 155.562 177.299  1.00 13.96           O  
ATOM     10  CB  VAL A  66     157.397 156.782 178.134  1.00 13.96           C  
ATOM     11  N   THR A  67     155.950 153.977 177.709  1.00 13.88           N  
ATOM     12  CA  THR A  67     155.302 153.021 176.818  1.00 13.88           C  
ATOM     13  C   THR A  67     153.906 152.662 177.314  1.00 13.88           C  
ATOM     14  O   THR A  67     152.965 152.562 176.519  1.00 13.88           O  
ATOM     15  CB  THR A  67     156.175 151.774 176.668  1.00 13.88           C  
ATOM     16  N   ALA A  68     153.746 152.471 178.624  1.00 14.17           N  
ATOM     17  CA  ALA A  68     152.436 152.103 179.155  1.00 14.17           C  
ATOM     18  C   ALA A  68     151.418 153.221 178.931  1.00 14.17           C  
ATOM     19  O   ALA A  68     150.262 152.956 178.577  1.00 14.17           O  
ATOM     20  CB  ALA A  68     152.544 151.755 180.639  1.00 14.17           C  
ATOM     21  N   ILE A  69     151.829 154.478 179.132  1.00 13.29           N  
ATOM     22  CA  ILE A  69     150.918 155.600 178.912  1.00 13.29           C  
ATOM     23  C   ILE A  69     150.563 155.722 177.431  1.00 13.29           C  
ATOM     24  O   ILE A  69     149.402 155.972 177.072  1.00 13.29           O  
ATOM     25  CB  ILE A  69     151.539 156.894 179.484  1.00 13.29           C  
ATOM     26  CG1 ILE A  69     151.636 156.787 181.010  1.00 13.29           C  
ATOM     27  CG2 ILE A  69     150.745 158.124 179.085  1.00 13.29           C  
ATOM     28  CD1 ILE A  69     152.450 157.863 181.667  1.00 13.29           C  
ATOM     29  N   THR A  70     151.540 155.528 176.548  1.00 13.16           N  
ATOM     30  CA  THR A  70     151.232 155.583 175.124  1.00 13.16           C  
ATOM     31  C   THR A  70     150.233 154.496 174.749  1.00 13.16           C  
ATOM     32  O   THR A  70     149.290 154.732 173.977  1.00 13.16           O  
ATOM     33  CB  THR A  70     152.509 155.440 174.303  1.00 13.16           C  
ATOM     34  OG1 THR A  70     153.459 156.420 174.727  1.00 13.16           O  
ATOM     35  CG2 THR A  70     152.228 155.612 172.842  1.00 13.16           C  
ATOM     36  N   ILE A  71     150.424 153.297 175.292  1.00 12.43           N  
ATOM     37  CA  ILE A  71     149.530 152.201 174.960  1.00 12.43           C  
ATOM     38  C   ILE A  71     148.132 152.520 175.439  1.00 12.43           C  
ATOM     39  O   ILE A  71     147.154 152.280 174.727  1.00 12.43           O  
ATOM     40  CB  ILE A  71     150.052 150.881 175.559  1.00 12.43           C  
ATOM     41  CG1 ILE A  71     151.140 150.290 174.661  1.00 12.43           C  
ATOM     42  CG2 ILE A  71     148.913 149.875 175.766  1.00 12.43           C  
ATOM     43  CD1 ILE A  71     151.858 149.118 175.275  1.00 12.43           C  
ATOM     44  N   MET A  72     148.009 153.060 176.653  1.00 13.84           N  
ATOM     45  CA  MET A  72     146.675 153.344 177.174  1.00 13.84           C  
ATOM     46  C   MET A  72     145.969 154.371 176.302  1.00 13.84           C  
ATOM     47  O   MET A  72     144.781 154.222 175.985  1.00 13.84           O  
ATOM     48  CB  MET A  72     146.761 153.817 178.626  1.00 13.84           C  
ATOM     49  CG  MET A  72     145.398 154.097 179.249  1.00 13.84           C  
ATOM     50  SD  MET A  72     145.455 154.594 180.977  1.00 13.84           S  
ATOM     51  CE  MET A  72     143.725 154.922 181.290  1.00 13.84           C  
ATOM     52  N   ALA A  73     146.704 155.395 175.865  1.00 11.89           N  
ATOM     53  CA  ALA A  73     146.102 156.453 175.066  1.00 11.89           C  
ATOM     54  C   ALA A  73     145.593 155.916 173.732  1.00 11.89           C  
ATOM     55  O   ALA A  73     144.418 156.106 173.365  1.00 11.89           O  
ATOM     56  CB  ALA A  73     147.125 157.567 174.845  1.00 11.89           C  
ATOM     57  N   LEU A  74     146.448 155.179 173.021  1.00 11.71           N  
ATOM     58  CA  LEU A  74     146.030 154.621 171.738  1.00 11.71           C  
ATOM     59  C   LEU A  74     144.906 153.609 171.910  1.00 11.71           C  
ATOM     60  O   LEU A  74     143.976 153.568 171.098  1.00 11.71           O  
ATOM     61  CB  LEU A  74     147.225 153.981 171.032  1.00 11.71           C  
ATOM     62  CG  LEU A  74     147.007 153.428 169.622  1.00 11.71           C  
ATOM     63  CD1 LEU A  74     148.322 153.446 168.863  1.00 11.71           C  
ATOM     64  CD2 LEU A  74     146.427 152.015 169.605  1.00 11.71           C  
ATOM     65  N   TYR A  75     144.976 152.773 172.946  1.00 11.03           N  
ATOM     66  CA  TYR A  75     143.986 151.720 173.108  1.00 11.03           C  
ATOM     67  C   TYR A  75     142.610 152.314 173.354  1.00 11.03           C  
ATOM     68  O   TYR A  75     141.614 151.848 172.790  1.00 11.03           O  
ATOM     69  CB  TYR A  75     144.379 150.819 174.274  1.00 11.03           C  
ATOM     70  CG  TYR A  75     145.285 149.658 173.931  1.00 11.03           C  
ATOM     71  CD1 TYR A  75     146.241 149.774 172.945  1.00 11.03           C  
ATOM     72  CD2 TYR A  75     145.220 148.471 174.636  1.00 11.03           C  
ATOM     73  CE1 TYR A  75     147.074 148.735 172.641  1.00 11.03           C  
ATOM     74  CE2 TYR A  75     146.059 147.425 174.345  1.00 11.03           C  
ATOM     75  CZ  TYR A  75     146.988 147.565 173.348  1.00 11.03           C  
ATOM     76  OH  TYR A  75     147.844 146.537 173.047  1.00 11.03           O  
ATOM     77  N   SER A  76     142.535 153.393 174.148  1.00 11.04           N  
ATOM     78  CA  SER A  76     141.274 154.125 174.445  1.00 11.04           C  
ATOM     79  C   SER A  76     140.717 154.773 173.175  1.00 11.04           C  
ATOM     80  O   SER A  76     139.519 154.754 173.021  1.00 11.04           O  
ATOM     81  CB  SER A  76     141.511 155.136 175.516  1.00 11.04           C  
ATOM     82  OG  SER A  76     141.950 154.507 176.711  1.00 11.04           O  
ATOM     83  N   ILE A  77     141.559 155.342 172.316  1.00 10.99           N  
ATOM     84  CA  ILE A  77     141.136 155.923 171.007  1.00 10.99           C  
ATOM     85  C   ILE A  77     140.615 154.812 170.080  1.00 10.99           C  
ATOM     86  O   ILE A  77     139.605 155.052 169.412  1.00 10.99           O  
ATOM     87  CB  ILE A  77     142.289 156.723 170.376  1.00 10.99           C  
ATOM     88  N   VAL A  78     141.271 153.653 170.016  1.00 11.12           N  
ATOM     89  CA  VAL A  78     140.841 152.482 169.189  1.00 11.12           C  
ATOM     90  C   VAL A  78     139.598 151.851 169.828  1.00 11.12           C  
ATOM     91  O   VAL A  78     138.860 151.189 169.098  1.00 11.12           O  
ATOM     92  CB  VAL A  78     142.005 151.481 168.982  1.00 11.12           C  
ATOM     93  CG1 VAL A  78     141.548 150.124 168.459  1.00 11.12           C  
ATOM     94  CG2 VAL A  78     143.080 152.051 168.070  1.00 11.12           C  
ATOM     95  N   CYS A  79     139.385 152.006 171.136  1.00 11.50           N  
ATOM     96  CA  CYS A  79     138.263 151.369 171.881  1.00 11.50           C  
ATOM     97  C   CYS A  79     136.954 152.130 171.659  1.00 11.50           C  
ATOM     98  O   CYS A  79     135.941 151.469 171.491  1.00 11.50           O  
ATOM     99  CB  CYS A  79     138.550 151.297 173.376  1.00 11.50           C  
ATOM    100  SG  CYS A  79     137.114 150.821 174.372  1.00 11.50           S  
ATOM    101  N   VAL A  80     136.962 153.460 171.709  1.00 11.45           N  
ATOM    102  CA  VAL A  80     135.744 154.229 171.544  1.00 11.45           C  
ATOM    103  C   VAL A  80     135.351 154.229 170.071  1.00 11.45           C  
ATOM    104  O   VAL A  80     134.193 153.954 169.725  1.00 11.45           O  
ATOM    105  CB  VAL A  80     135.922 155.651 172.115  1.00 11.45           C  
ATOM    106  CG1 VAL A  80     136.185 155.579 173.600  1.00 11.45           C  
ATOM    107  CG2 VAL A  80     137.050 156.393 171.423  1.00 11.45           C  
ATOM    108  N   VAL A  81     136.321 154.451 169.171  1.00 11.20           N  
ATOM    109  CA  VAL A  81     135.970 154.457 167.754  1.00 11.20           C  
ATOM    110  C   VAL A  81     135.472 153.080 167.318  1.00 11.20           C  
ATOM    111  O   VAL A  81     134.448 152.972 166.626  1.00 11.20           O  
ATOM    112  CB  VAL A  81     137.163 154.932 166.903  1.00 11.20           C  
ATOM    113  CG1 VAL A  81     136.965 154.586 165.431  1.00 11.20           C  
ATOM    114  CG2 VAL A  81     137.357 156.422 167.056  1.00 11.20           C  
ATOM    115  N   GLY A  82     136.153 152.003 167.727  1.00 10.87           N  
ATOM    116  CA  GLY A  82     135.744 150.688 167.273  1.00 10.87           C  
ATOM    117  C   GLY A  82     134.380 150.288 167.797  1.00 10.87           C  
ATOM    118  O   GLY A  82     133.538 149.774 167.052  1.00 10.87           O  
ATOM    119  N   LEU A  83     134.136 150.519 169.086  1.00 11.35           N  
ATOM    120  CA  LEU A  83     132.857 150.122 169.650  1.00 11.35           C  
ATOM    121  C   LEU A  83     131.716 150.889 168.991  1.00 11.35           C  
ATOM    122  O   LEU A  83     130.692 150.295 168.622  1.00 11.35           O  
ATOM    123  CB  LEU A  83     132.888 150.317 171.164  1.00 11.35           C  
ATOM    124  CG  LEU A  83     131.784 149.677 172.000  1.00 11.35           C  
ATOM    125  CD1 LEU A  83     131.694 148.172 171.755  1.00 11.35           C  
ATOM    126  CD2 LEU A  83     132.060 149.933 173.458  1.00 11.35           C  
ATOM    127  N   PHE A  84     131.886 152.201 168.791  1.00 11.37           N  
ATOM    128  CA  PHE A  84     130.825 152.980 168.160  1.00 11.37           C  
ATOM    129  C   PHE A  84     130.560 152.510 166.728  1.00 11.37           C  
ATOM    130  O   PHE A  84     129.407 152.274 166.341  1.00 11.37           O  
ATOM    131  CB  PHE A  84     131.201 154.461 168.183  1.00 11.37           C  
ATOM    132  N   GLY A  85     131.620 152.359 165.929  1.00 11.41           N  
ATOM    133  CA  GLY A  85     131.440 151.985 164.535  1.00 11.41           C  
ATOM    134  C   GLY A  85     130.792 150.625 164.361  1.00 11.41           C  
ATOM    135  O   GLY A  85     129.885 150.453 163.532  1.00 11.41           O  
ATOM    136  N   ASN A  86     131.203 149.648 165.173  1.00 11.50           N  
ATOM    137  CA  ASN A  86     130.638 148.325 164.985  1.00 11.50           C  
ATOM    138  C   ASN A  86     129.290 148.178 165.647  1.00 11.50           C  
ATOM    139  O   ASN A  86     128.558 147.252 165.294  1.00 11.50           O  
ATOM    140  CB  ASN A  86     131.572 147.241 165.528  1.00 11.50           C  
ATOM    141  CG  ASN A  86     132.915 147.245 164.868  1.00 11.50           C  
ATOM    142  OD1 ASN A  86     133.012 147.243 163.650  1.00 11.50           O  
ATOM    143  ND2 ASN A  86     133.963 147.252 165.663  1.00 11.50           N  
ATOM    144  N   PHE A  87     128.913 149.074 166.558  1.00 12.54           N  
ATOM    145  CA  PHE A  87     127.526 149.039 166.991  1.00 12.54           C  
ATOM    146  C   PHE A  87     126.647 149.588 165.880  1.00 12.54           C  
ATOM    147  O   PHE A  87     125.559 149.061 165.609  1.00 12.54           O  
ATOM    148  CB  PHE A  87     127.351 149.831 168.285  1.00 12.54           C  
ATOM    149  N   LEU A  88     127.133 150.633 165.210  1.00 13.21           N  
ATOM    150  CA  LEU A  88     126.341 151.297 164.186  1.00 13.21           C  
ATOM    151  C   LEU A  88     126.054 150.356 163.018  1.00 13.21           C  
ATOM    152  O   LEU A  88     124.926 150.300 162.510  1.00 13.21           O  
ATOM    153  CB  LEU A  88     127.083 152.552 163.727  1.00 13.21           C  
ATOM    154  CG  LEU A  88     126.389 153.504 162.758  1.00 13.21           C  
ATOM    155  CD1 LEU A  88     125.112 154.020 163.385  1.00 13.21           C  
ATOM    156  CD2 LEU A  88     127.298 154.656 162.343  1.00 13.21           C  
ATOM    157  N   VAL A  89     127.067 149.599 162.582  1.00 13.40           N  
ATOM    158  CA  VAL A  89     126.882 148.693 161.442  1.00 13.40           C  
ATOM    159  C   VAL A  89     125.810 147.647 161.735  1.00 13.40           C  
ATOM    160  O   VAL A  89     124.905 147.407 160.924  1.00 13.40           O  
ATOM    161  CB  VAL A  89     128.222 148.027 161.079  1.00 13.40           C  
ATOM    162  CG1 VAL A  89     128.029 146.893 160.094  1.00 13.40           C  
ATOM    163  CG2 VAL A  89     129.161 149.041 160.497  1.00 13.40           C  
ATOM    164  N   MET A  90     125.880 147.031 162.913  1.00 12.99           N  
ATOM    165  CA  MET A  90     124.885 146.035 163.290  1.00 12.99           C  
ATOM    166  C   MET A  90     123.494 146.643 163.394  1.00 12.99           C  
ATOM    167  O   MET A  90     122.503 146.038 162.952  1.00 12.99           O  
ATOM    168  CB  MET A  90     125.284 145.385 164.610  1.00 12.99           C  
ATOM    169  N   TYR A  91     123.393 147.838 163.975  1.00 13.53           N  
ATOM    170  CA  TYR A  91     122.084 148.453 164.105  1.00 13.53           C  
ATOM    171  C   TYR A  91     121.470 148.686 162.731  1.00 13.53           C  
ATOM    172  O   TYR A  91     120.285 148.422 162.520  1.00 13.53           O  
ATOM    173  CB  TYR A  91     122.205 149.762 164.883  1.00 13.53           C  
ATOM    174  CG  TYR A  91     120.974 150.630 164.856  1.00 13.53           C  
ATOM    175  CD1 TYR A  91     119.889 150.330 165.649  1.00 13.53           C  
ATOM    176  CD2 TYR A  91     120.900 151.746 164.043  1.00 13.53           C  
ATOM    177  CE1 TYR A  91     118.766 151.114 165.638  1.00 13.53           C  
ATOM    178  CE2 TYR A  91     119.782 152.535 164.024  1.00 13.53           C  
ATOM    179  CZ  TYR A  91     118.716 152.214 164.822  1.00 13.53           C  
ATOM    180  OH  TYR A  91     117.591 153.003 164.806  1.00 13.53           O  
ATOM    181  N   VAL A  92     122.264 149.179 161.782  1.00 14.62           N  
ATOM    182  CA  VAL A  92     121.740 149.462 160.446  1.00 14.62           C  
ATOM    183  C   VAL A  92     121.291 148.185 159.744  1.00 14.62           C  
ATOM    184  O   VAL A  92     120.263 148.167 159.058  1.00 14.62           O  
ATOM    185  CB  VAL A  92     122.782 150.229 159.620  1.00 14.62           C  
ATOM    186  CG1 VAL A  92     122.379 150.280 158.164  1.00 14.62           C  
ATOM    187  CG2 VAL A  92     122.926 151.638 160.171  1.00 14.62           C  
ATOM    188  N   ILE A  93     122.060 147.106 159.873  1.00 13.69           N  
ATOM    189  CA  ILE A  93     121.649 145.861 159.229  1.00 13.69           C  
ATOM    190  C   ILE A  93     120.330 145.367 159.819  1.00 13.69           C  
ATOM    191  O   ILE A  93     119.450 144.896 159.092  1.00 13.69           O  
ATOM    192  CB  ILE A  93     122.766 144.804 159.333  1.00 13.69           C  
ATOM    193  CG1 ILE A  93     123.983 145.251 158.524  1.00 13.69           C  
ATOM    194  CG2 ILE A  93     122.294 143.464 158.790  1.00 13.69           C  
ATOM    195  CD1 ILE A  93     125.224 144.433 158.759  1.00 13.69           C  
ATOM    196  N   VAL A  94     120.170 145.459 161.137  1.00 13.43           N  
ATOM    197  CA  VAL A  94     118.924 145.019 161.762  1.00 13.43           C  
ATOM    198  C   VAL A  94     117.745 145.932 161.403  1.00 13.43           C  
ATOM    199  O   VAL A  94     116.629 145.462 161.161  1.00 13.43           O  
ATOM    200  CB  VAL A  94     119.113 144.928 163.285  1.00 13.43           C  
ATOM    201  N   ARG A  95     117.963 147.247 161.411  1.00 17.21           N  
ATOM    202  CA  ARG A  95     116.879 148.226 161.285  1.00 17.21           C  
ATOM    203  C   ARG A  95     116.223 148.252 159.903  1.00 17.21           C  
ATOM    204  O   ARG A  95     114.991 148.250 159.803  1.00 17.21           O  
ATOM    205  CB  ARG A  95     117.413 149.615 161.630  1.00 17.21           C  
ATOM    206  N   TYR A  96     117.008 148.250 158.828  1.00 16.40           N  
ATOM    207  CA  TYR A  96     116.475 148.428 157.481  1.00 16.40           C  
ATOM    208  C   TYR A  96     116.321 147.107 156.736  1.00 16.40           C  
ATOM    209  O   TYR A  96     117.266 146.320 156.647  1.00 16.40           O  
ATOM    210  CB  TYR A  96     117.379 149.360 156.681  1.00 16.40           C  
ATOM    211  N   THR A  97     115.124 146.886 156.187  1.00 17.18           N  
ATOM    212  CA  THR A  97     114.809 145.636 155.499  1.00 17.18           C  
ATOM    213  C   THR A  97     115.633 145.453 154.225  1.00 17.18           C  
ATOM    214  O   THR A  97     116.051 144.335 153.906  1.00 17.18           O  
ATOM    215  CB  THR A  97     113.318 145.594 155.166  1.00 17.18           C  
ATOM    216  N   LYS A  98     115.876 146.525 153.482  1.00 16.38           N  
ATOM    217  CA  LYS A  98     116.621 146.393 152.236  1.00 16.38           C  
ATOM    218  C   LYS A  98     118.010 145.819 152.465  1.00 16.38           C  
ATOM    219  O   LYS A  98     118.525 145.078 151.621  1.00 16.38           O  
ATOM    220  CB  LYS A  98     116.730 147.750 151.544  1.00 16.38           C  
ATOM    221  N   MET A  99     118.629 146.150 153.596  1.00 16.55           N  
ATOM    222  CA  MET A  99     120.019 145.778 153.841  1.00 16.55           C  
ATOM    223  C   MET A  99     120.242 144.270 153.847  1.00 16.55           C  
ATOM    224  O   MET A  99     121.298 143.800 153.416  1.00 16.55           O  
ATOM    225  CB  MET A  99     120.482 146.389 155.158  1.00 16.55           C  
ATOM    226  CG  MET A  99     120.649 147.890 155.097  1.00 16.55           C  
ATOM    227  SD  MET A  99     121.696 148.412 153.727  1.00 16.55           S  
ATOM    228  CE  MET A  99     123.300 148.412 154.499  1.00 16.55           C  
ATOM    229  N   LYS A 100     119.282 143.492 154.332  1.00 15.55           N  
ATOM    230  CA  LYS A 100     119.504 142.056 154.452  1.00 15.55           C  
ATOM    231  C   LYS A 100     119.858 141.410 153.112  1.00 15.55           C  
ATOM    232  O   LYS A 100     119.125 141.529 152.127  1.00 15.55           O  
ATOM    233  CB  LYS A 100     118.255 141.396 155.037  1.00 15.55           C  
ATOM    234  N   THR A 101     121.014 140.742 153.052  1.00 13.51           N  
ATOM    235  CA  THR A 101     121.536 140.016 151.860  1.00 13.51           C  
ATOM    236  C   THR A 101     122.431 138.921 152.445  1.00 13.51           C  
ATOM    237  O   THR A 101     122.668 138.992 153.648  1.00 13.51           O  
ATOM    238  CB  THR A 101     122.361 140.908 150.919  1.00 13.51           C  
ATOM    239  OG1 THR A 101     123.528 141.345 151.610  1.00 13.51           O  
ATOM    240  CG2 THR A 101     121.617 142.112 150.384  1.00 13.51           C  
ATOM    241  N   ALA A 102     122.924 137.963 151.666  1.00 13.16           N  
ATOM    242  CA  ALA A 102     123.880 136.927 152.139  1.00 13.16           C  
ATOM    243  C   ALA A 102     125.198 137.582 152.570  1.00 13.16           C  
ATOM    244  O   ALA A 102     125.727 137.188 153.614  1.00 13.16           O  
ATOM    245  CB  ALA A 102     124.096 135.909 151.048  1.00 13.16           C  
ATOM    246  N   THR A 103     125.694 138.557 151.813  1.00 13.08           N  
ATOM    247  CA  THR A 103     126.939 139.294 152.125  1.00 13.08           C  
ATOM    248  C   THR A 103     126.771 140.072 153.430  1.00 13.08           C  
ATOM    249  O   THR A 103     127.748 140.153 154.178  1.00 13.08           O  
ATOM    250  CB  THR A 103     127.299 140.253 150.982  1.00 13.08           C  
ATOM    251  OG1 THR A 103     126.982 139.590 149.758  1.00 13.08           O  
ATOM    252  CG2 THR A 103     128.750 140.679 150.992  1.00 13.08           C  
ATOM    253  N   ASN A 104     125.606 140.671 153.657  1.00 12.76           N  
ATOM    254  CA  ASN A 104     125.336 141.503 154.852  1.00 12.76           C  
ATOM    255  C   ASN A 104     125.337 140.614 156.090  1.00 12.76           C  
ATOM    256  O   ASN A 104     125.799 141.121 157.120  1.00 12.76           O  
ATOM    257  CB  ASN A 104     124.098 142.383 154.662  1.00 12.76           C  
ATOM    258  CG  ASN A 104     124.410 143.685 153.950  1.00 12.76           C  
ATOM    259  OD1 ASN A 104     125.276 143.740 153.079  1.00 12.76           O  
ATOM    260  ND2 ASN A 104     123.725 144.750 154.324  1.00 12.76           N  
ATOM    261  N   ILE A 105     124.834 139.371 156.014  1.00 12.01           N  
ATOM    262  CA  ILE A 105     124.875 138.407 157.153  1.00 12.01           C  
ATOM    263  C   ILE A 105     126.350 138.165 157.491  1.00 12.01           C  
ATOM    264  O   ILE A 105     126.669 138.202 158.678  1.00 12.01           O  
ATOM    265  CB  ILE A 105     124.128 137.085 156.853  1.00 12.01           C  
ATOM    266  CG1 ILE A 105     122.656 137.255 156.451  1.00 12.01           C  
ATOM    267  CG2 ILE A 105     124.265 136.106 158.012  1.00 12.01           C  
ATOM    268  CD1 ILE A 105     121.889 138.326 157.191  1.00 12.01           C  
ATOM    269  N   TYR A 106     127.224 137.984 156.502  1.00 11.55           N  
ATOM    270  CA  TYR A 106     128.678 137.757 156.708  1.00 11.55           C  
ATOM    271  C   TYR A 106     129.358 138.998 157.291  1.00 11.55           C  
ATOM    272  O   TYR A 106     130.213 138.818 158.152  1.00 11.55           O  
ATOM    273  CB  TYR A 106     129.359 137.267 155.421  1.00 11.55           C  
ATOM    274  CG  TYR A 106     128.883 135.937 154.889  1.00 11.55           C  
ATOM    275  CD1 TYR A 106     128.785 134.828 155.712  1.00 11.55           C  
ATOM    276  CD2 TYR A 106     128.550 135.774 153.554  1.00 11.55           C  
ATOM    277  CE1 TYR A 106     128.347 133.606 155.235  1.00 11.55           C  
ATOM    278  CE2 TYR A 106     128.114 134.558 153.058  1.00 11.55           C  
ATOM    279  CZ  TYR A 106     128.009 133.467 153.903  1.00 11.55           C  
ATOM    280  OH  TYR A 106     127.586 132.250 153.450  1.00 11.55           O  
ATOM    281  N   ILE A 107     129.035 140.197 156.822  1.00 12.16           N  
ATOM    282  CA  ILE A 107     129.598 141.493 157.315  1.00 12.16           C  
ATOM    283  C   ILE A 107     129.181 141.704 158.773  1.00 12.16           C  
ATOM    284  O   ILE A 107     129.990 142.258 159.521  1.00 12.16           O  
ATOM    285  CB  ILE A 107     129.170 142.655 156.393  1.00 12.16           C  
ATOM    286  CG1 ILE A 107     129.947 142.640 155.073  1.00 12.16           C  
ATOM    287  CG2 ILE A 107     129.292 144.002 157.097  1.00 12.16           C  
ATOM    288  CD1 ILE A 107     129.276 143.383 153.940  1.00 12.16           C  
ATOM    289  N   PHE A 108     127.964 141.326 159.153  1.00 11.27           N  
ATOM    290  CA  PHE A 108     127.445 141.429 160.539  1.00 11.27           C  
ATOM    291  C   PHE A 108     128.241 140.520 161.481  1.00 11.27           C  
ATOM    292  O   PHE A 108     128.371 140.914 162.632  1.00 11.27           O  
ATOM    293  CB  PHE A 108     125.961 141.054 160.580  1.00 11.27           C  
ATOM    294  CG  PHE A 108     125.286 141.189 161.921  1.00 11.27           C  
ATOM    295  CD1 PHE A 108     124.600 142.344 162.255  1.00 11.27           C  
ATOM    296  CD2 PHE A 108     125.313 140.150 162.839  1.00 11.27           C  
ATOM    297  CE1 PHE A 108     123.974 142.464 163.484  1.00 11.27           C  
ATOM    298  CE2 PHE A 108     124.690 140.274 164.069  1.00 11.27           C  
ATOM    299  CZ  PHE A 108     124.019 141.430 164.388  1.00 11.27           C  
ATOM    300  N   ASN A 109     128.678 139.332 161.052  1.00 10.97           N  
ATOM    301  CA  ASN A 109     129.483 138.428 161.874  1.00 10.97           C  
ATOM    302  C   ASN A 109     130.877 138.997 162.133  1.00 10.97           C  
ATOM    303  O   ASN A 109     131.386 138.955 163.269  1.00 10.97           O  
ATOM    304  CB  ASN A 109     129.571 137.061 161.193  1.00 10.97           C  
ATOM    305  CG  ASN A 109     130.166 135.999 162.087  1.00 10.97           C  
ATOM    306  OD1 ASN A 109     130.538 136.271 163.221  1.00 10.97           O  
ATOM    307  ND2 ASN A 109     130.278 134.789 161.575  1.00 10.97           N  
ATOM    308  N   LEU A 110     131.484 139.566 161.095  1.00 11.46           N  
ATOM    309  CA  LEU A 110     132.759 140.262 161.246  1.00 11.46           C  
ATOM    310  C   LEU A 110     132.681 141.388 162.284  1.00 11.46           C  
ATOM    311  O   LEU A 110     133.582 141.540 163.126  1.00 11.46           O  
ATOM    312  CB  LEU A 110     133.193 140.779 159.877  1.00 11.46           C  
ATOM    313  CG  LEU A 110     134.560 141.435 159.736  1.00 11.46           C  
ATOM    314  CD1 LEU A 110     135.661 140.393 159.793  1.00 11.46           C  
ATOM    315  CD2 LEU A 110     134.657 142.174 158.442  1.00 11.46           C  
ATOM    316  N   ALA A 111     131.573 142.124 162.318  1.00 10.90           N  
ATOM    317  CA  ALA A 111     131.543 143.295 163.188  1.00 10.90           C  
ATOM    318  C   ALA A 111     131.167 142.920 164.610  1.00 10.90           C  
ATOM    319  O   ALA A 111     131.593 143.588 165.560  1.00 10.90           O  
ATOM    320  CB  ALA A 111     130.555 144.335 162.650  1.00 10.90           C  
ATOM    321  N   LEU A 112     130.455 141.811 164.778  1.00 10.90           N  
ATOM    322  CA  LEU A 112     130.290 141.235 166.104  1.00 10.90           C  
ATOM    323  C   LEU A 112     131.651 140.884 166.696  1.00 10.90           C  
ATOM    324  O   LEU A 112     131.983 141.277 167.828  1.00 10.90           O  
ATOM    325  CB  LEU A 112     129.386 140.007 166.020  1.00 10.90           C  
ATOM    326  CG  LEU A 112     128.909 139.387 167.331  1.00 10.90           C  
ATOM    327  CD1 LEU A 112     127.596 138.688 167.089  1.00 10.90           C  
ATOM    328  CD2 LEU A 112     129.912 138.406 167.914  1.00 10.90           C  
ATOM    329  N   ALA A 113     132.436 140.089 165.959  1.00 11.39           N  
ATOM    330  CA  ALA A 113     133.769 139.744 166.452  1.00 11.39           C  
ATOM    331  C   ALA A 113     134.626 140.974 166.750  1.00 11.39           C  
ATOM    332  O   ALA A 113     135.381 140.966 167.729  1.00 11.39           O  
ATOM    333  CB  ALA A 113     134.486 138.849 165.444  1.00 11.39           C  
ATOM    334  N   ASP A 114     134.469 142.072 166.008  1.00 11.94           N  
ATOM    335  CA  ASP A 114     135.316 143.227 166.324  1.00 11.94           C  
ATOM    336  C   ASP A 114     134.796 144.046 167.505  1.00 11.94           C  
ATOM    337  O   ASP A 114     135.599 144.673 168.215  1.00 11.94           O  
ATOM    338  CB  ASP A 114     135.474 144.148 165.120  1.00 11.94           C  
ATOM    339  CG  ASP A 114     136.308 143.541 164.030  1.00 11.94           C  
ATOM    340  OD1 ASP A 114     137.194 142.724 164.345  1.00 11.94           O  
ATOM    341  OD2 ASP A 114     136.106 143.907 162.855  1.00 11.94           O  
ATOM    342  N   ALA A 115     133.511 143.945 167.829  1.00 11.25           N  
ATOM    343  CA  ALA A 115     133.044 144.631 169.025  1.00 11.25           C  
ATOM    344  C   ALA A 115     133.555 143.893 170.250  1.00 11.25           C  
ATOM    345  O   ALA A 115     134.025 144.513 171.221  1.00 11.25           O  
ATOM    346  CB  ALA A 115     131.518 144.718 169.039  1.00 11.25           C  
ATOM    347  N   LEU A 116     133.476 142.560 170.215  1.00 11.85           N  
ATOM    348  CA  LEU A 116     134.014 141.793 171.329  1.00 11.85           C  
ATOM    349  C   LEU A 116     135.516 142.003 171.447  1.00 11.85           C  
ATOM    350  O   LEU A 116     136.047 142.053 172.561  1.00 11.85           O  
ATOM    351  CB  LEU A 116     133.705 140.308 171.175  1.00 11.85           C  
ATOM    352  CG  LEU A 116     132.254 139.882 171.318  1.00 11.85           C  
ATOM    353  CD1 LEU A 116     132.098 138.406 170.989  1.00 11.85           C  
ATOM    354  CD2 LEU A 116     131.775 140.167 172.725  1.00 11.85           C  
ATOM    355  N   ALA A 117     136.212 142.181 170.318  1.00 11.49           N  
ATOM    356  CA  ALA A 117     137.648 142.416 170.398  1.00 11.49           C  
ATOM    357  C   ALA A 117     137.974 143.772 171.010  1.00 11.49           C  
ATOM    358  O   ALA A 117     139.010 143.912 171.665  1.00 11.49           O  
ATOM    359  CB  ALA A 117     138.279 142.303 169.014  1.00 11.49           C  
ATOM    360  N   THR A 118     137.124 144.780 170.829  1.00 11.24           N  
ATOM    361  CA  THR A 118     137.509 146.109 171.303  1.00 11.24           C  
ATOM    362  C   THR A 118     137.094 146.346 172.750  1.00 11.24           C  
ATOM    363  O   THR A 118     137.741 147.128 173.451  1.00 11.24           O  
ATOM    364  CB  THR A 118     136.933 147.220 170.410  1.00 11.24           C  
ATOM    365  OG1 THR A 118     135.521 147.049 170.242  1.00 11.24           O  
ATOM    366  CG2 THR A 118     137.629 147.248 169.070  1.00 11.24           C  
ATOM    367  N   SER A 119     136.049 145.670 173.218  1.00 11.61           N  
ATOM    368  CA  SER A 119     135.642 145.795 174.618  1.00 11.61           C  
ATOM    369  C   SER A 119     136.693 145.320 175.633  1.00 11.61           C  
ATOM    370  O   SER A 119     136.611 145.705 176.803  1.00 11.61           O  
ATOM    371  CB  SER A 119     134.347 145.022 174.850  1.00 11.61           C  
ATOM    372  OG  SER A 119     134.569 143.631 174.775  1.00 11.61           O  
ATOM    373  N   THR A 120     137.664 144.493 175.235  1.00 11.34           N  
ATOM    374  CA  THR A 120     138.737 144.066 176.138  1.00 11.34           C  
ATOM    375  C   THR A 120     139.857 145.087 176.371  1.00 11.34           C  
ATOM    376  O   THR A 120     140.533 145.006 177.399  1.00 11.34           O  
ATOM    377  CB  THR A 120     139.377 142.775 175.617  1.00 11.34           C  
ATOM    378  OG1 THR A 120     139.765 142.946 174.250  1.00 11.34           O  
ATOM    379  CG2 THR A 120     138.423 141.611 175.733  1.00 11.34           C  
ATOM    380  N   LEU A 121     140.103 146.018 175.462  1.00 11.59           N  
ATOM    381  CA  LEU A 121     141.355 146.779 175.488  1.00 11.59           C  
ATOM    382  C   LEU A 121     141.593 147.693 176.697  1.00 11.59           C  
ATOM    383  O   LEU A 121     142.760 147.966 177.035  1.00 11.59           O  
ATOM    384  CB  LEU A 121     141.438 147.649 174.233  1.00 11.59           C  
ATOM    385  CG  LEU A 121     141.865 147.042 172.898  1.00 11.59           C  
ATOM    386  CD1 LEU A 121     141.915 148.153 171.856  1.00 11.59           C  
ATOM    387  CD2 LEU A 121     143.201 146.323 172.966  1.00 11.59           C  
ATOM    388  N   PRO A 122     140.554 148.139 177.416  1.00 11.20           N  
ATOM    389  CA  PRO A 122     140.829 148.918 178.634  1.00 11.20           C  
ATOM    390  C   PRO A 122     141.470 148.112 179.750  1.00 11.20           C  
ATOM    391  O   PRO A 122     142.362 148.630 180.434  1.00 11.20           O  
ATOM    392  CB  PRO A 122     139.437 149.433 179.027  1.00 11.20           C  
ATOM    393  CG  PRO A 122     138.682 149.451 177.773  1.00 11.20           C  
ATOM    394  CD  PRO A 122     139.141 148.253 177.019  1.00 11.20           C  
ATOM    395  N   PHE A 123     141.046 146.866 179.974  1.00 11.54           N  
ATOM    396  CA  PHE A 123     141.670 146.085 181.034  1.00 11.54           C  
ATOM    397  C   PHE A 123     143.149 145.868 180.748  1.00 11.54           C  
ATOM    398  O   PHE A 123     143.983 145.946 181.656  1.00 11.54           O  
ATOM    399  CB  PHE A 123     140.972 144.738 181.190  1.00 11.54           C  
ATOM    400  CG  PHE A 123     139.517 144.838 181.492  1.00 11.54           C  
ATOM    401  CD1 PHE A 123     138.586 144.906 180.477  1.00 11.54           C  
ATOM    402  CD2 PHE A 123     139.074 144.834 182.797  1.00 11.54           C  
ATOM    403  CE1 PHE A 123     137.243 144.988 180.764  1.00 11.54           C  
ATOM    404  CE2 PHE A 123     137.738 144.915 183.085  1.00 11.54           C  
ATOM    405  CZ  PHE A 123     136.821 144.991 182.070  1.00 11.54           C  
ATOM    406  N   GLN A 124     143.495 145.601 179.487  1.00 11.69           N  
ATOM    407  CA  GLN A 124     144.897 145.389 179.146  1.00 11.69           C  
ATOM    408  C   GLN A 124     145.692 146.665 179.344  1.00 11.69           C  
ATOM    409  O   GLN A 124     146.834 146.628 179.815  1.00 11.69           O  
ATOM    410  CB  GLN A 124     145.047 144.862 177.719  1.00 11.69           C  
ATOM    411  CG  GLN A 124     144.226 143.622 177.443  1.00 11.69           C  
ATOM    412  CD  GLN A 124     144.266 143.223 176.002  1.00 11.69           C  
ATOM    413  OE1 GLN A 124     145.058 143.748 175.231  1.00 11.69           O  
ATOM    414  NE2 GLN A 124     143.405 142.303 175.620  1.00 11.69           N  
ATOM    415  N   SER A 125     145.113 147.805 178.960  1.00 12.26           N  
ATOM    416  CA  SER A 125     145.819 149.064 179.143  1.00 12.26           C  
ATOM    417  C   SER A 125     146.081 149.333 180.623  1.00 12.26           C  
ATOM    418  O   SER A 125     147.181 149.755 181.000  1.00 12.26           O  
ATOM    419  CB  SER A 125     144.997 150.191 178.539  1.00 12.26           C  
ATOM    420  OG  SER A 125     143.703 150.188 179.109  1.00 12.26           O  
ATOM    421  N   VAL A 126     145.089 149.074 181.480  1.00 12.63           N  
ATOM    422  CA  VAL A 126     145.296 149.223 182.920  1.00 12.63           C  
ATOM    423  C   VAL A 126     146.346 148.239 183.426  1.00 12.63           C  
ATOM    424  O   VAL A 126     147.111 148.549 184.346  1.00 12.63           O  
ATOM    425  CB  VAL A 126     143.963 149.058 183.672  1.00 12.63           C  
ATOM    426  N   ASN A 127     146.379 147.026 182.867  1.00 13.04           N  
ATOM    427  CA  ASN A 127     147.375 146.048 183.298  1.00 13.04           C  
ATOM    428  C   ASN A 127     148.779 146.536 182.992  1.00 13.04           C  
ATOM    429  O   ASN A 127     149.682 146.428 183.827  1.00 13.04           O  
ATOM    430  CB  ASN A 127     147.124 144.711 182.610  1.00 13.04           C  
ATOM    431  CG  ASN A 127     148.082 143.650 183.050  1.00 13.04           C  
ATOM    432  OD1 ASN A 127     148.549 143.658 184.183  1.00 13.04           O  
ATOM    433  ND2 ASN A 127     148.390 142.728 182.157  1.00 13.04           N  
ATOM    434  N   TYR A 128     148.977 147.083 181.794  1.00 13.10           N  
ATOM    435  CA  TYR A 128     150.281 147.617 181.429  1.00 13.10           C  
ATOM    436  C   TYR A 128     150.625 148.830 182.278  1.00 13.10           C  
ATOM    437  O   TYR A 128     151.782 149.010 182.669  1.00 13.10           O  
ATOM    438  CB  TYR A 128     150.329 147.973 179.945  1.00 13.10           C  
ATOM    439  CG  TYR A 128     150.503 146.805 178.996  1.00 13.10           C  
ATOM    440  CD1 TYR A 128     151.504 145.870 179.193  1.00 13.10           C  
ATOM    441  CD2 TYR A 128     149.678 146.651 177.892  1.00 13.10           C  
ATOM    442  CE1 TYR A 128     151.672 144.818 178.333  1.00 13.10           C  
ATOM    443  CE2 TYR A 128     149.838 145.594 177.026  1.00 13.10           C  
ATOM    444  CZ  TYR A 128     150.836 144.681 177.250  1.00 13.10           C  
ATOM    445  OH  TYR A 128     151.012 143.627 176.386  1.00 13.10           O  
ATOM    446  N   LEU A 129     149.642 149.692 182.550  1.00 13.54           N  
ATOM    447  CA  LEU A 129     149.918 150.889 183.338  1.00 13.54           C  
ATOM    448  C   LEU A 129     150.316 150.553 184.768  1.00 13.54           C  
ATOM    449  O   LEU A 129     151.280 151.121 185.292  1.00 13.54           O  
ATOM    450  CB  LEU A 129     148.693 151.801 183.338  1.00 13.54           C  
ATOM    451  N   MET A 130     149.598 149.636 185.413  1.00 14.63           N  
ATOM    452  CA  MET A 130     149.806 149.350 186.828  1.00 14.63           C  
ATOM    453  C   MET A 130     150.848 148.275 187.094  1.00 14.63           C  
ATOM    454  O   MET A 130     151.250 148.107 188.247  1.00 14.63           O  
ATOM    455  CB  MET A 130     148.494 148.940 187.492  1.00 14.63           C  
ATOM    456  CG  MET A 130     147.474 150.044 187.555  1.00 14.63           C  
ATOM    457  SD  MET A 130     146.588 150.068 189.120  1.00 14.63           S  
ATOM    458  CE  MET A 130     145.819 148.459 189.123  1.00 14.63           C  
ATOM    459  N   GLY A 131     151.279 147.532 186.073  1.00 15.78           N  
ATOM    460  CA  GLY A 131     152.247 146.462 186.237  1.00 15.78           C  
ATOM    461  C   GLY A 131     151.680 145.185 186.820  1.00 15.78           C  
ATOM    462  O   GLY A 131     152.420 144.214 186.984  1.00 15.78           O  
ATOM    463  N   THR A 132     150.402 145.170 187.161  1.00 15.49           N  
ATOM    464  CA  THR A 132     149.764 144.058 187.839  1.00 15.49           C  
ATOM    465  C   THR A 132     148.397 143.838 187.209  1.00 15.49           C  
ATOM    466  O   THR A 132     147.803 144.773 186.671  1.00 15.49           O  
ATOM    467  CB  THR A 132     149.634 144.329 189.338  1.00 15.49           C  
ATOM    468  OG1 THR A 132     150.852 144.906 189.821  1.00 15.49           O  
ATOM    469  CG2 THR A 132     149.340 143.050 190.084  1.00 15.49           C  
ATOM    470  N   TRP A 133     147.923 142.592 187.231  1.00 12.70           N  
ATOM    471  CA  TRP A 133     146.554 142.309 186.825  1.00 12.70           C  
ATOM    472  C   TRP A 133     145.670 142.275 188.062  1.00 12.70           C  
ATOM    473  O   TRP A 133     145.776 141.335 188.859  1.00 12.70           O  
ATOM    474  CB  TRP A 133     146.478 140.979 186.073  1.00 12.70           C  
ATOM    475  CG  TRP A 133     145.117 140.623 185.551  1.00 12.70           C  
ATOM    476  CD1 TRP A 133     144.217 139.793 186.135  1.00 12.70           C  
ATOM    477  CD2 TRP A 133     144.515 141.070 184.331  1.00 12.70           C  
ATOM    478  NE1 TRP A 133     143.090 139.698 185.369  1.00 12.70           N  
ATOM    479  CE2 TRP A 133     143.248 140.473 184.252  1.00 12.70           C  
ATOM    480  CE3 TRP A 133     144.924 141.920 183.300  1.00 12.70           C  
ATOM    481  CZ2 TRP A 133     142.385 140.692 183.184  1.00 12.70           C  
ATOM    482  CZ3 TRP A 133     144.067 142.136 182.241  1.00 12.70           C  
ATOM    483  CH2 TRP A 133     142.813 141.524 182.191  1.00 12.70           C  
ATOM    484  N   PRO A 134     144.778 143.245 188.258  1.00 13.32           N  
ATOM    485  CA  PRO A 134     143.891 143.243 189.434  1.00 13.32           C  
ATOM    486  C   PRO A 134     142.460 142.789 189.173  1.00 13.32           C  
ATOM    487  O   PRO A 134     141.636 142.914 190.081  1.00 13.32           O  
ATOM    488  CB  PRO A 134     143.909 144.721 189.826  1.00 13.32           C  
ATOM    489  CG  PRO A 134     143.918 145.409 188.510  1.00 13.32           C  
ATOM    490  CD  PRO A 134     144.664 144.521 187.532  1.00 13.32           C  
ATOM    491  N   PHE A 135     142.143 142.287 187.985  1.00 12.06           N  
ATOM    492  CA  PHE A 135     140.767 141.981 187.622  1.00 12.06           C  
ATOM    493  C   PHE A 135     140.320 140.548 187.902  1.00 12.06           C  
ATOM    494  O   PHE A 135     139.189 140.203 187.555  1.00 12.06           O  
ATOM    495  CB  PHE A 135     140.553 142.304 186.142  1.00 12.06           C  
ATOM    496  CG  PHE A 135     140.878 143.727 185.778  1.00 12.06           C  
ATOM    497  CD1 PHE A 135     140.036 144.763 186.156  1.00 12.06           C  
ATOM    498  CD2 PHE A 135     142.009 144.038 185.058  1.00 12.06           C  
ATOM    499  CE1 PHE A 135     140.329 146.076 185.822  1.00 12.06           C  
ATOM    500  CE2 PHE A 135     142.295 145.341 184.730  1.00 12.06           C  
ATOM    501  CZ  PHE A 135     141.450 146.358 185.112  1.00 12.06           C  
ATOM    502  N   GLY A 136     141.141 139.695 188.502  1.00 14.84           N  
ATOM    503  CA  GLY A 136     140.669 138.378 188.868  1.00 14.84           C  
ATOM    504  C   GLY A 136     140.919 137.309 187.815  1.00 14.84           C  
ATOM    505  O   GLY A 136     141.379 137.564 186.699  1.00 14.84           O  
ATOM    506  N   ASN A 137     140.637 136.069 188.221  1.00 16.59           N  
ATOM    507  CA  ASN A 137     140.874 134.908 187.366  1.00 16.59           C  
ATOM    508  C   ASN A 137     139.872 134.820 186.217  1.00 16.59           C  
ATOM    509  O   ASN A 137     140.256 134.622 185.054  1.00 16.59           O  
ATOM    510  CB  ASN A 137     140.835 133.638 188.209  1.00 16.59           C  
ATOM    511  CG  ASN A 137     141.729 132.561 187.662  1.00 16.59           C  
ATOM    512  OD1 ASN A 137     142.151 132.618 186.506  1.00 16.59           O  
ATOM    513  ND2 ASN A 137     142.047 131.576 188.492  1.00 16.59           N  
ATOM    514  N   ILE A 138     138.580 134.947 186.518  1.00 14.32           N  
ATOM    515  CA  ILE A 138     137.565 134.657 185.509  1.00 14.32           C  
ATOM    516  C   ILE A 138     137.683 135.636 184.351  1.00 14.32           C  
ATOM    517  O   ILE A 138     137.582 135.253 183.175  1.00 14.32           O  
ATOM    518  CB  ILE A 138     136.169 134.654 186.156  1.00 14.32           C  
ATOM    519  CG1 ILE A 138     136.083 133.485 187.131  1.00 14.32           C  
ATOM    520  CG2 ILE A 138     135.084 134.525 185.127  1.00 14.32           C  
ATOM    521  CD1 ILE A 138     134.872 133.513 188.024  1.00 14.32           C  
ATOM    522  N   LEU A 139     137.852 136.906 184.674  1.00 13.76           N  
ATOM    523  CA  LEU A 139     138.031 137.938 183.639  1.00 13.76           C  
ATOM    524  C   LEU A 139     139.320 137.636 182.886  1.00 13.76           C  
ATOM    525  O   LEU A 139     139.345 137.978 181.753  1.00 13.76           O  
ATOM    526  CB  LEU A 139     138.040 139.330 184.284  1.00 13.76           C  
ATOM    527  CG  LEU A 139     136.711 139.813 184.875  1.00 13.76           C  
ATOM    528  CD1 LEU A 139     136.800 141.276 185.284  1.00 13.76           C  
ATOM    529  CD2 LEU A 139     135.547 139.615 183.911  1.00 13.76           C  
ATOM    530  N   CYS A 140     140.348 137.030 183.486  1.00 13.87           N  
ATOM    531  CA  CYS A 140     141.590 136.605 182.768  1.00 13.87           C  
ATOM    532  C   CYS A 140     141.257 135.508 181.736  1.00 13.87           C  
ATOM    533  O   CYS A 140     141.738 135.600 180.611  1.00 13.87           O  
ATOM    534  CB  CYS A 140     142.672 136.170 183.757  1.00 13.87           C  
ATOM    535  SG  CYS A 140     144.199 135.533 183.020  1.00 13.87           S  
ATOM    536  N   LYS A 141     140.413 134.544 182.090  1.00 14.47           N  
ATOM    537  CA  LYS A 141     140.033 133.412 181.210  1.00 14.47           C  
ATOM    538  C   LYS A 141     139.158 133.907 180.052  1.00 14.47           C  
ATOM    539  O   LYS A 141     139.265 133.315 178.973  1.00 14.47           O  
ATOM    540  CB  LYS A 141     139.318 132.324 182.018  1.00 14.47           C  
ATOM    541  CG  LYS A 141     140.212 131.413 182.843  1.00 14.47           C  
ATOM    542  CD  LYS A 141     139.463 130.223 183.415  1.00 14.47           C  
ATOM    543  CE  LYS A 141     140.359 129.116 183.930  1.00 14.47           C  
ATOM    544  NZ  LYS A 141     141.187 129.557 185.077  1.00 14.47           N  
ATOM    545  N   ILE A 142     138.307 134.910 180.263  1.00 13.07           N  
ATOM    546  CA  ILE A 142     137.472 135.484 179.211  1.00 13.07           C  
ATOM    547  C   ILE A 142     138.300 136.305 178.223  1.00 13.07           C  
ATOM    548  O   ILE A 142     138.156 136.165 177.002  1.00 13.07           O  
ATOM    549  CB  ILE A 142     136.333 136.305 179.836  1.00 13.07           C  
ATOM    550  CG1 ILE A 142     135.412 135.362 180.610  1.00 13.07           C  
ATOM    551  CG2 ILE A 142     135.550 137.035 178.764  1.00 13.07           C  
ATOM    552  CD1 ILE A 142     134.347 136.041 181.408  1.00 13.07           C  
ATOM    553  N   VAL A 143     139.190 137.155 178.728  1.00 12.70           N  
ATOM    554  CA  VAL A 143     139.950 138.030 177.841  1.00 12.70           C  
ATOM    555  C   VAL A 143     140.844 137.212 176.916  1.00 12.70           C  
ATOM    556  O   VAL A 143     140.935 137.490 175.710  1.00 12.70           O  
ATOM    557  CB  VAL A 143     140.755 139.055 178.672  1.00 12.70           C  
ATOM    558  CG1 VAL A 143     141.686 139.890 177.791  1.00 12.70           C  
ATOM    559  CG2 VAL A 143     139.827 139.977 179.449  1.00 12.70           C  
ATOM    560  N   ILE A 144     141.477 136.156 177.440  1.00 12.85           N  
ATOM    561  CA  ILE A 144     142.405 135.401 176.599  1.00 12.85           C  
ATOM    562  C   ILE A 144     141.636 134.583 175.564  1.00 12.85           C  
ATOM    563  O   ILE A 144     142.028 134.500 174.380  1.00 12.85           O  
ATOM    564  CB  ILE A 144     143.351 134.550 177.470  1.00 12.85           C  
ATOM    565  CG1 ILE A 144     144.329 135.480 178.213  1.00 12.85           C  
ATOM    566  CG2 ILE A 144     144.145 133.561 176.624  1.00 12.85           C  
ATOM    567  CD1 ILE A 144     145.248 134.803 179.187  1.00 12.85           C  
ATOM    568  N   SER A 145     140.511 133.995 175.972  1.00 13.00           N  
ATOM    569  CA  SER A 145     139.736 133.234 175.010  1.00 13.00           C  
ATOM    570  C   SER A 145     139.272 134.149 173.887  1.00 13.00           C  
ATOM    571  O   SER A 145     139.315 133.770 172.711  1.00 13.00           O  
ATOM    572  CB  SER A 145     138.556 132.557 175.694  1.00 13.00           C  
ATOM    573  OG  SER A 145     137.899 131.691 174.787  1.00 13.00           O  
ATOM    574  N   ILE A 146     138.825 135.359 174.232  1.00 12.24           N  
ATOM    575  CA  ILE A 146     138.386 136.315 173.219  1.00 12.24           C  
ATOM    576  C   ILE A 146     139.534 136.641 172.273  1.00 12.24           C  
ATOM    577  O   ILE A 146     139.335 136.840 171.070  1.00 12.24           O  
ATOM    578  CB  ILE A 146     137.815 137.573 173.898  1.00 12.24           C  
ATOM    579  CG1 ILE A 146     136.424 137.269 174.451  1.00 12.24           C  
ATOM    580  CG2 ILE A 146     137.792 138.764 172.940  1.00 12.24           C  
ATOM    581  CD1 ILE A 146     135.940 138.255 175.490  1.00 12.24           C  
ATOM    582  N   ASP A 147     140.750 136.711 172.804  1.00 12.22           N  
ATOM    583  CA  ASP A 147     141.899 137.037 171.965  1.00 12.22           C  
ATOM    584  C   ASP A 147     142.070 135.999 170.857  1.00 12.22           C  
ATOM    585  O   ASP A 147     142.335 136.347 169.703  1.00 12.22           O  
ATOM    586  CB  ASP A 147     143.145 137.097 172.853  1.00 12.22           C  
ATOM    587  CG  ASP A 147     144.247 137.969 172.300  1.00 12.22           C  
ATOM    588  OD1 ASP A 147     143.966 138.984 171.640  1.00 12.22           O  
ATOM    589  OD2 ASP A 147     145.420 137.654 172.564  1.00 12.22           O  
ATOM    590  N   TYR A 148     141.950 134.711 171.199  1.00 12.03           N  
ATOM    591  CA  TYR A 148     142.000 133.652 170.175  1.00 12.03           C  
ATOM    592  C   TYR A 148     140.765 133.626 169.257  1.00 12.03           C  
ATOM    593  O   TYR A 148     140.876 133.371 168.039  1.00 12.03           O  
ATOM    594  CB  TYR A 148     142.228 132.311 170.869  1.00 12.03           C  
ATOM    595  CG  TYR A 148     143.681 132.173 171.218  1.00 12.03           C  
ATOM    596  CD1 TYR A 148     144.169 132.653 172.421  1.00 12.03           C  
ATOM    597  CD2 TYR A 148     144.574 131.613 170.329  1.00 12.03           C  
ATOM    598  CE1 TYR A 148     145.496 132.560 172.729  1.00 12.03           C  
ATOM    599  CE2 TYR A 148     145.907 131.517 170.632  1.00 12.03           C  
ATOM    600  CZ  TYR A 148     146.363 131.986 171.835  1.00 12.03           C  
ATOM    601  OH  TYR A 148     147.694 131.891 172.145  1.00 12.03           O  
ATOM    602  N   TYR A 149     139.582 133.864 169.822  1.00 10.89           N  
ATOM    603  CA  TYR A 149     138.361 133.863 169.021  1.00 10.89           C  
ATOM    604  C   TYR A 149     138.415 134.922 167.934  1.00 10.89           C  
ATOM    605  O   TYR A 149     137.953 134.694 166.810  1.00 10.89           O  
ATOM    606  CB  TYR A 149     137.144 134.076 169.909  1.00 10.89           C  
ATOM    607  CG  TYR A 149     136.544 132.798 170.420  1.00 10.89           C  
ATOM    608  CD1 TYR A 149     135.917 131.920 169.558  1.00 10.89           C  
ATOM    609  CD2 TYR A 149     136.603 132.467 171.760  1.00 10.89           C  
ATOM    610  CE1 TYR A 149     135.361 130.757 170.014  1.00 10.89           C  
ATOM    611  CE2 TYR A 149     136.046 131.297 172.226  1.00 10.89           C  
ATOM    612  CZ  TYR A 149     135.429 130.446 171.348  1.00 10.89           C  
ATOM    613  OH  TYR A 149     134.871 129.280 171.805  1.00 10.89           O  
ATOM    614  N   ASN A 150     138.967 136.088 168.247  1.00 10.37           N  
ATOM    615  CA  ASN A 150     139.046 137.137 167.247  1.00 10.37           C  
ATOM    616  C   ASN A 150     139.716 136.590 165.992  1.00 10.37           C  
ATOM    617  O   ASN A 150     139.148 136.641 164.894  1.00 10.37           O  
ATOM    618  CB  ASN A 150     139.810 138.329 167.843  1.00 10.37           C  
ATOM    619  CG  ASN A 150     139.830 139.551 166.946  1.00 10.37           C  
ATOM    620  OD1 ASN A 150     140.853 140.215 166.815  1.00 10.37           O  
ATOM    621  ND2 ASN A 150     138.690 139.874 166.354  1.00 10.37           N  
ATOM    622  N   MET A 151     140.884 135.970 166.161  1.00 11.05           N  
ATOM    623  CA  MET A 151     141.677 135.512 165.023  1.00 11.05           C  
ATOM    624  C   MET A 151     140.955 134.431 164.217  1.00 11.05           C  
ATOM    625  O   MET A 151     140.801 134.551 162.987  1.00 11.05           O  
ATOM    626  CB  MET A 151     143.028 134.997 165.524  1.00 11.05           C  
ATOM    627  CG  MET A 151     144.052 136.087 165.769  1.00 11.05           C  
ATOM    628  SD  MET A 151     145.758 135.510 165.930  1.00 11.05           S  
ATOM    629  CE  MET A 151     145.713 134.671 167.511  1.00 11.05           C  
ATOM    630  N   PHE A 152     140.394 133.427 164.899  1.00 11.68           N  
ATOM    631  CA  PHE A 152     139.808 132.316 164.142  1.00 11.68           C  
ATOM    632  C   PHE A 152     138.494 132.710 163.470  1.00 11.68           C  
ATOM    633  O   PHE A 152     138.288 132.429 162.277  1.00 11.68           O  
ATOM    634  CB  PHE A 152     139.624 131.093 165.044  1.00 11.68           C  
ATOM    635  CG  PHE A 152     140.885 130.293 165.231  1.00 11.68           C  
ATOM    636  CD1 PHE A 152     141.848 130.684 166.145  1.00 11.68           C  
ATOM    637  CD2 PHE A 152     141.106 129.149 164.489  1.00 11.68           C  
ATOM    638  CE1 PHE A 152     143.004 129.957 166.305  1.00 11.68           C  
ATOM    639  CE2 PHE A 152     142.266 128.411 164.654  1.00 11.68           C  
ATOM    640  CZ  PHE A 152     143.213 128.818 165.557  1.00 11.68           C  
ATOM    641  N   THR A 153     137.602 133.384 164.194  1.00 10.61           N  
ATOM    642  CA  THR A 153     136.330 133.733 163.580  1.00 10.61           C  
ATOM    643  C   THR A 153     136.541 134.720 162.443  1.00 10.61           C  
ATOM    644  O   THR A 153     135.887 134.613 161.401  1.00 10.61           O  
ATOM    645  CB  THR A 153     135.364 134.303 164.613  1.00 10.61           C  
ATOM    646  OG1 THR A 153     135.897 135.513 165.155  1.00 10.61           O  
ATOM    647  CG2 THR A 153     135.119 133.309 165.724  1.00 10.61           C  
ATOM    648  N   SER A 154     137.454 135.682 162.604  1.00 10.14           N  
ATOM    649  CA  SER A 154     137.617 136.676 161.555  1.00 10.14           C  
ATOM    650  C   SER A 154     138.168 136.054 160.277  1.00 10.14           C  
ATOM    651  O   SER A 154     137.666 136.340 159.176  1.00 10.14           O  
ATOM    652  CB  SER A 154     138.529 137.794 162.049  1.00 10.14           C  
ATOM    653  OG  SER A 154     137.972 138.428 163.178  1.00 10.14           O  
ATOM    654  N   ILE A 155     139.132 135.129 160.398  1.00 11.42           N  
ATOM    655  CA  ILE A 155     139.709 134.566 159.182  1.00 11.42           C  
ATOM    656  C   ILE A 155     138.699 133.646 158.489  1.00 11.42           C  
ATOM    657  O   ILE A 155     138.572 133.654 157.255  1.00 11.42           O  
ATOM    658  CB  ILE A 155     141.045 133.857 159.507  1.00 11.42           C  
ATOM    659  CG1 ILE A 155     141.824 133.537 158.240  1.00 11.42           C  
ATOM    660  CG2 ILE A 155     140.836 132.579 160.264  1.00 11.42           C  
ATOM    661  CD1 ILE A 155     142.319 134.744 157.505  1.00 11.42           C  
ATOM    662  N   PHE A 156     137.911 132.898 159.259  1.00  9.33           N  
ATOM    663  CA  PHE A 156     136.938 132.013 158.625  1.00  9.33           C  
ATOM    664  C   PHE A 156     135.778 132.788 157.998  1.00  9.33           C  
ATOM    665  O   PHE A 156     135.262 132.388 156.948  1.00  9.33           O  
ATOM    666  CB  PHE A 156     136.439 130.965 159.616  1.00  9.33           C  
ATOM    667  CG  PHE A 156     137.513 130.040 160.111  1.00  9.33           C  
ATOM    668  CD1 PHE A 156     138.718 129.937 159.449  1.00  9.33           C  
ATOM    669  CD2 PHE A 156     137.304 129.242 161.207  1.00  9.33           C  
ATOM    670  CE1 PHE A 156     139.695 129.088 159.886  1.00  9.33           C  
ATOM    671  CE2 PHE A 156     138.286 128.389 161.647  1.00  9.33           C  
ATOM    672  CZ  PHE A 156     139.480 128.312 160.981  1.00  9.33           C  
ATOM    673  N   THR A 157     135.317 133.864 158.643  1.00 11.06           N  
ATOM    674  CA  THR A 157     134.263 134.678 158.045  1.00 11.06           C  
ATOM    675  C   THR A 157     134.715 135.297 156.726  1.00 11.06           C  
ATOM    676  O   THR A 157     133.952 135.317 155.752  1.00 11.06           O  
ATOM    677  CB  THR A 157     133.818 135.758 159.032  1.00 11.06           C  
ATOM    678  OG1 THR A 157     133.285 135.138 160.204  1.00 11.06           O  
ATOM    679  CG2 THR A 157     132.736 136.635 158.440  1.00 11.06           C  
ATOM    680  N   LEU A 158     135.959 135.779 156.652  1.00 11.05           N  
ATOM    681  CA  LEU A 158     136.443 136.266 155.361  1.00 11.05           C  
ATOM    682  C   LEU A 158     136.514 135.146 154.320  1.00 11.05           C  
ATOM    683  O   LEU A 158     136.199 135.361 153.139  1.00 11.05           O  
ATOM    684  CB  LEU A 158     137.800 136.952 155.517  1.00 11.05           C  
ATOM    685  CG  LEU A 158     137.785 138.277 156.279  1.00 11.05           C  
ATOM    686  CD1 LEU A 158     139.174 138.658 156.763  1.00 11.05           C  
ATOM    687  CD2 LEU A 158     137.216 139.379 155.410  1.00 11.05           C  
ATOM    688  N   CYS A 159     136.918 133.942 154.734  1.00 11.57           N  
ATOM    689  CA  CYS A 159     136.994 132.834 153.782  1.00 11.57           C  
ATOM    690  C   CYS A 159     135.615 132.466 153.222  1.00 11.57           C  
ATOM    691  O   CYS A 159     135.454 132.264 152.007  1.00 11.57           O  
ATOM    692  CB  CYS A 159     137.656 131.633 154.472  1.00 11.57           C  
ATOM    693  SG  CYS A 159     137.978 130.195 153.436  1.00 11.57           S  
ATOM    694  N   THR A 160     134.604 132.395 154.086  1.00 11.92           N  
ATOM    695  CA  THR A 160     133.263 132.083 153.602  1.00 11.92           C  
ATOM    696  C   THR A 160     132.720 133.199 152.721  1.00 11.92           C  
ATOM    697  O   THR A 160     132.005 132.933 151.749  1.00 11.92           O  
ATOM    698  CB  THR A 160     132.321 131.802 154.767  1.00 11.92           C  
ATOM    699  OG1 THR A 160     132.386 132.870 155.718  1.00 11.92           O  
ATOM    700  CG2 THR A 160     132.678 130.485 155.430  1.00 11.92           C  
ATOM    701  N   MET A 161     133.020 134.453 153.058  1.00 12.35           N  
ATOM    702  CA  MET A 161     132.627 135.564 152.199  1.00 12.35           C  
ATOM    703  C   MET A 161     133.173 135.375 150.787  1.00 12.35           C  
ATOM    704  O   MET A 161     132.456 135.553 149.794  1.00 12.35           O  
ATOM    705  CB  MET A 161     133.119 136.873 152.811  1.00 12.35           C  
ATOM    706  CG  MET A 161     132.546 138.131 152.188  1.00 12.35           C  
ATOM    707  SD  MET A 161     133.046 139.616 153.080  1.00 12.35           S  
ATOM    708  CE  MET A 161     131.993 139.521 154.513  1.00 12.35           C  
ATOM    709  N   SER A 162     134.453 135.014 150.680  1.00 11.82           N  
ATOM    710  CA  SER A 162     135.079 134.882 149.365  1.00 11.82           C  
ATOM    711  C   SER A 162     134.481 133.721 148.572  1.00 11.82           C  
ATOM    712  O   SER A 162     134.267 133.829 147.357  1.00 11.82           O  
ATOM    713  CB  SER A 162     136.584 134.698 149.523  1.00 11.82           C  
ATOM    714  OG  SER A 162     137.135 135.749 150.290  1.00 11.82           O  
ATOM    715  N   VAL A 163     134.197 132.602 149.233  1.00 12.64           N  
ATOM    716  CA  VAL A 163     133.545 131.504 148.520  1.00 12.64           C  
ATOM    717  C   VAL A 163     132.133 131.897 148.080  1.00 12.64           C  
ATOM    718  O   VAL A 163     131.674 131.488 147.005  1.00 12.64           O  
ATOM    719  CB  VAL A 163     133.555 130.221 149.371  1.00 12.64           C  
ATOM    720  CG1 VAL A 163     132.681 129.154 148.747  1.00 12.64           C  
ATOM    721  CG2 VAL A 163     134.955 129.701 149.489  1.00 12.64           C  
ATOM    722  N   ASP A 164     131.403 132.653 148.906  1.00 12.85           N  
ATOM    723  CA  ASP A 164     130.075 133.108 148.496  1.00 12.85           C  
ATOM    724  C   ASP A 164     130.155 133.992 147.257  1.00 12.85           C  
ATOM    725  O   ASP A 164     129.348 133.848 146.324  1.00 12.85           O  
ATOM    726  CB  ASP A 164     129.409 133.854 149.652  1.00 12.85           C  
ATOM    727  CG  ASP A 164     128.086 134.510 149.265  1.00 12.85           C  
ATOM    728  OD1 ASP A 164     127.038 133.825 149.305  1.00 12.85           O  
ATOM    729  OD2 ASP A 164     128.089 135.723 148.962  1.00 12.85           O  
ATOM    730  N   ARG A 165     131.166 134.862 147.187  1.00 12.79           N  
ATOM    731  CA  ARG A 165     131.256 135.710 146.009  1.00 12.79           C  
ATOM    732  C   ARG A 165     131.713 134.905 144.807  1.00 12.79           C  
ATOM    733  O   ARG A 165     131.360 135.245 143.673  1.00 12.79           O  
ATOM    734  CB  ARG A 165     132.220 136.880 146.221  1.00 12.79           C  
ATOM    735  CG  ARG A 165     131.899 137.812 147.392  1.00 12.79           C  
ATOM    736  CD  ARG A 165     130.496 138.380 147.344  1.00 12.79           C  
ATOM    737  NE  ARG A 165     130.253 139.175 146.152  1.00 12.79           N  
ATOM    738  CZ  ARG A 165     129.054 139.386 145.633  1.00 12.79           C  
ATOM    739  NH1 ARG A 165     127.971 138.842 146.154  1.00 12.79           N  
ATOM    740  NH2 ARG A 165     128.943 140.151 144.554  1.00 12.79           N  
ATOM    741  N   TYR A 166     132.375 133.769 145.044  1.00 12.07           N  
ATOM    742  CA  TYR A 166     132.779 132.917 143.933  1.00 12.07           C  
ATOM    743  C   TYR A 166     131.576 132.193 143.357  1.00 12.07           C  
ATOM    744  O   TYR A 166     131.418 132.103 142.136  1.00 12.07           O  
ATOM    745  CB  TYR A 166     133.833 131.913 144.400  1.00 12.07           C  
ATOM    746  CG  TYR A 166     134.244 130.926 143.335  1.00 12.07           C  
ATOM    747  CD1 TYR A 166     135.194 131.253 142.384  1.00 12.07           C  
ATOM    748  CD2 TYR A 166     133.680 129.661 143.290  1.00 12.07           C  
ATOM    749  CE1 TYR A 166     135.558 130.350 141.418  1.00 12.07           C  
ATOM    750  CE2 TYR A 166     134.040 128.760 142.337  1.00 12.07           C  
ATOM    751  CZ  TYR A 166     134.975 129.103 141.400  1.00 12.07           C  
ATOM    752  OH  TYR A 166     135.331 128.185 140.442  1.00 12.07           O  
ATOM    753  N   ILE A 167     130.715 131.675 144.222  1.00 12.77           N  
ATOM    754  CA  ILE A 167     129.537 130.987 143.719  1.00 12.77           C  
ATOM    755  C   ILE A 167     128.690 131.969 142.933  1.00 12.77           C  
ATOM    756  O   ILE A 167     128.166 131.644 141.864  1.00 12.77           O  
ATOM    757  CB  ILE A 167     128.755 130.336 144.871  1.00 12.77           C  
ATOM    758  CG1 ILE A 167     129.633 129.275 145.542  1.00 12.77           C  
ATOM    759  CG2 ILE A 167     127.435 129.767 144.364  1.00 12.77           C  
ATOM    760  CD1 ILE A 167     128.957 128.521 146.677  1.00 12.77           C  
ATOM    761  N   ALA A 168     128.554 133.196 143.446  1.00 13.32           N  
ATOM    762  CA  ALA A 168     127.733 134.194 142.766  1.00 13.32           C  
ATOM    763  C   ALA A 168     128.300 134.555 141.390  1.00 13.32           C  
ATOM    764  O   ALA A 168     127.550 134.693 140.420  1.00 13.32           O  
ATOM    765  CB  ALA A 168     127.609 135.448 143.629  1.00 13.32           C  
ATOM    766  N   VAL A 169     129.615 134.760 141.296  1.00 13.44           N  
ATOM    767  CA  VAL A 169     130.215 135.170 140.029  1.00 13.44           C  
ATOM    768  C   VAL A 169     130.271 134.038 138.995  1.00 13.44           C  
ATOM    769  O   VAL A 169     130.026 134.274 137.808  1.00 13.44           O  
ATOM    770  CB  VAL A 169     131.608 135.767 140.283  1.00 13.44           C  
ATOM    771  CG1 VAL A 169     132.314 136.065 138.974  1.00 13.44           C  
ATOM    772  CG2 VAL A 169     131.483 137.034 141.103  1.00 13.44           C  
ATOM    773  N   CYS A 170     130.621 132.813 139.396  1.00 13.42           N  
ATOM    774  CA  CYS A 170     130.931 131.779 138.405  1.00 13.42           C  
ATOM    775  C   CYS A 170     129.845 130.740 138.154  1.00 13.42           C  
ATOM    776  O   CYS A 170     129.906 130.071 137.120  1.00 13.42           O  
ATOM    777  CB  CYS A 170     132.212 131.031 138.800  1.00 13.42           C  
ATOM    778  SG  CYS A 170     133.720 132.009 138.736  1.00 13.42           S  
ATOM    779  N   HIS A 171     128.881 130.555 139.054  1.00 14.81           N  
ATOM    780  CA  HIS A 171     127.835 129.537 138.904  1.00 14.81           C  
ATOM    781  C   HIS A 171     126.470 130.152 139.186  1.00 14.81           C  
ATOM    782  O   HIS A 171     125.773 129.745 140.121  1.00 14.81           O  
ATOM    783  CB  HIS A 171     128.088 128.362 139.847  1.00 14.81           C  
ATOM    784  CG  HIS A 171     129.478 127.811 139.783  1.00 14.81           C  
ATOM    785  ND1 HIS A 171     129.866 126.867 138.858  1.00 14.81           N  
ATOM    786  CD2 HIS A 171     130.572 128.071 140.537  1.00 14.81           C  
ATOM    787  CE1 HIS A 171     131.139 126.573 139.042  1.00 14.81           C  
ATOM    788  NE2 HIS A 171     131.591 127.291 140.053  1.00 14.81           N  
ATOM    789  N   PRO A 172     126.024 131.098 138.357  1.00 16.31           N  
ATOM    790  CA  PRO A 172     124.783 131.816 138.686  1.00 16.31           C  
ATOM    791  C   PRO A 172     123.545 130.938 138.734  1.00 16.31           C  
ATOM    792  O   PRO A 172     122.715 131.091 139.650  1.00 16.31           O  
ATOM    793  CB  PRO A 172     124.684 132.842 137.556  1.00 16.31           C  
ATOM    794  CG  PRO A 172     125.445 132.241 136.456  1.00 16.31           C  
ATOM    795  CD  PRO A 172     126.591 131.558 137.085  1.00 16.31           C  
ATOM    796  N   VAL A 173     123.439 129.964 137.827  1.00 17.16           N  
ATOM    797  CA  VAL A 173     122.221 129.165 137.765  1.00 17.16           C  
ATOM    798  C   VAL A 173     122.048 128.420 139.071  1.00 17.16           C  
ATOM    799  O   VAL A 173     120.938 128.317 139.603  1.00 17.16           O  
ATOM    800  CB  VAL A 173     122.264 128.208 136.561  1.00 17.16           C  
ATOM    801  N   LYS A 174     123.141 127.888 139.608  1.00 17.02           N  
ATOM    802  CA  LYS A 174     123.082 127.199 140.882  1.00 17.02           C  
ATOM    803  C   LYS A 174     123.437 128.135 142.029  1.00 17.02           C  
ATOM    804  O   LYS A 174     123.237 127.770 143.191  1.00 17.02           O  
ATOM    805  CB  LYS A 174     124.028 125.991 140.871  1.00 17.02           C  
ATOM    806  N   ALA A 175     123.961 129.330 141.722  1.00 15.35           N  
ATOM    807  CA  ALA A 175     124.203 130.330 142.758  1.00 15.35           C  
ATOM    808  C   ALA A 175     122.894 130.755 143.387  1.00 15.35           C  
ATOM    809  O   ALA A 175     122.825 131.013 144.592  1.00 15.35           O  
ATOM    810  CB  ALA A 175     124.926 131.550 142.190  1.00 15.35           C  
ATOM    811  N   LEU A 176     121.840 130.829 142.574  1.00 16.88           N  
ATOM    812  CA  LEU A 176     120.569 131.350 143.061  1.00 16.88           C  
ATOM    813  C   LEU A 176     120.013 130.512 144.209  1.00 16.88           C  
ATOM    814  O   LEU A 176     119.504 131.058 145.195  1.00 16.88           O  
ATOM    815  CB  LEU A 176     119.566 131.409 141.912  1.00 16.88           C  
ATOM    816  N   ASP A 177     120.106 129.188 144.105  1.00 17.92           N  
ATOM    817  CA  ASP A 177     119.580 128.309 145.148  1.00 17.92           C  
ATOM    818  C   ASP A 177     120.360 128.398 146.460  1.00 17.92           C  
ATOM    819  O   ASP A 177     119.761 128.361 147.540  1.00 17.92           O  
ATOM    820  CB  ASP A 177     119.566 126.866 144.644  1.00 17.92           C  
ATOM    821  N   PHE A 178     121.687 128.508 146.400  1.00 15.24           N  
ATOM    822  CA  PHE A 178     122.517 128.423 147.598  1.00 15.24           C  
ATOM    823  C   PHE A 178     122.817 129.754 148.272  1.00 15.24           C  
ATOM    824  O   PHE A 178     123.438 129.749 149.339  1.00 15.24           O  
ATOM    825  CB  PHE A 178     123.847 127.744 147.260  1.00 15.24           C  
ATOM    826  N   ARG A 179     122.402 130.885 147.706  1.00 14.08           N  
ATOM    827  CA  ARG A 179     122.701 132.194 148.277  1.00 14.08           C  
ATOM    828  C   ARG A 179     121.550 132.771 149.092  1.00 14.08           C  
ATOM    829  O   ARG A 179     121.526 133.979 149.339  1.00 14.08           O  
ATOM    830  CB  ARG A 179     123.120 133.180 147.194  1.00 14.08           C  
ATOM    831  CG  ARG A 179     124.459 132.866 146.609  1.00 14.08           C  
ATOM    832  CD  ARG A 179     124.927 133.962 145.686  1.00 14.08           C  
ATOM    833  NE  ARG A 179     125.698 134.984 146.377  1.00 14.08           N  
ATOM    834  CZ  ARG A 179     125.201 136.087 146.916  1.00 14.08           C  
ATOM    835  NH1 ARG A 179     123.909 136.360 146.877  1.00 14.08           N  
ATOM    836  NH2 ARG A 179     126.027 136.943 147.508  1.00 14.08           N  
ATOM    837  N   THR A 180     120.584 131.955 149.485  1.00 14.62           N  
ATOM    838  CA  THR A 180     119.546 132.445 150.372  1.00 14.62           C  
ATOM    839  C   THR A 180     120.145 132.812 151.733  1.00 14.62           C  
ATOM    840  O   THR A 180     121.115 132.195 152.175  1.00 14.62           O  
ATOM    841  CB  THR A 180     118.464 131.385 150.538  1.00 14.62           C  
ATOM    842  OG1 THR A 180     117.432 131.874 151.398  1.00 14.62           O  
ATOM    843  CG2 THR A 180     119.047 130.111 151.118  1.00 14.62           C  
ATOM    844  N   PRO A 181     119.600 133.833 152.409  1.00 13.20           N  
ATOM    845  CA  PRO A 181     120.245 134.314 153.645  1.00 13.20           C  
ATOM    846  C   PRO A 181     120.293 133.291 154.765  1.00 13.20           C  
ATOM    847  O   PRO A 181     121.255 133.287 155.550  1.00 13.20           O  
ATOM    848  CB  PRO A 181     119.413 135.550 154.014  1.00 13.20           C  
ATOM    849  CG  PRO A 181     118.120 135.370 153.340  1.00 13.20           C  
ATOM    850  CD  PRO A 181     118.389 134.609 152.088  1.00 13.20           C  
ATOM    851  N   ARG A 182     119.277 132.437 154.891  1.00 12.84           N  
ATOM    852  CA  ARG A 182     119.284 131.472 155.983  1.00 12.84           C  
ATOM    853  C   ARG A 182     120.530 130.607 155.904  1.00 12.84           C  
ATOM    854  O   ARG A 182     121.095 130.212 156.931  1.00 12.84           O  
ATOM    855  CB  ARG A 182     118.024 130.613 155.939  1.00 12.84           C  
ATOM    856  N   ASN A 183     120.964 130.288 154.686  1.00 13.79           N  
ATOM    857  CA  ASN A 183     122.182 129.508 154.519  1.00 13.79           C  
ATOM    858  C   ASN A 183     123.378 130.238 155.111  1.00 13.79           C  
ATOM    859  O   ASN A 183     124.251 129.620 155.725  1.00 13.79           O  
ATOM    860  CB  ASN A 183     122.419 129.212 153.041  1.00 13.79           C  
ATOM    861  CG  ASN A 183     121.394 128.275 152.468  1.00 13.79           C  
ATOM    862  OD1 ASN A 183     120.372 128.001 153.092  1.00 13.79           O  
ATOM    863  ND2 ASN A 183     121.663 127.764 151.277  1.00 13.79           N  
ATOM    864  N   ALA A 184     123.432 131.559 154.933  1.00 11.85           N  
ATOM    865  CA  ALA A 184     124.513 132.346 155.517  1.00 11.85           C  
ATOM    866  C   ALA A 184     124.462 132.313 157.038  1.00 11.85           C  
ATOM    867  O   ALA A 184     125.500 132.236 157.705  1.00 11.85           O  
ATOM    868  CB  ALA A 184     124.445 133.781 155.004  1.00 11.85           C  
ATOM    869  N   LYS A 185     123.260 132.358 157.606  1.00 12.69           N  
ATOM    870  CA  LYS A 185     123.140 132.287 159.059  1.00 12.69           C  
ATOM    871  C   LYS A 185     123.622 130.941 159.598  1.00 12.69           C  
ATOM    872  O   LYS A 185     124.349 130.880 160.604  1.00 12.69           O  
ATOM    873  CB  LYS A 185     121.688 132.545 159.453  1.00 12.69           C  
ATOM    874  CG  LYS A 185     121.151 133.864 158.937  1.00 12.69           C  
ATOM    875  CD  LYS A 185     119.680 134.042 159.235  1.00 12.69           C  
ATOM    876  CE  LYS A 185     119.388 134.018 160.714  1.00 12.69           C  
ATOM    877  NZ  LYS A 185     117.958 134.321 160.969  1.00 12.69           N  
ATOM    878  N   ILE A 186     123.249 129.850 158.930  1.00 11.47           N  
ATOM    879  CA  ILE A 186     123.738 128.538 159.349  1.00 11.47           C  
ATOM    880  C   ILE A 186     125.250 128.461 159.182  1.00 11.47           C  
ATOM    881  O   ILE A 186     125.951 127.879 160.018  1.00 11.47           O  
ATOM    882  CB  ILE A 186     123.007 127.412 158.592  1.00 11.47           C  
ATOM    883  CG1 ILE A 186     121.491 127.596 158.719  1.00 11.47           C  
ATOM    884  CG2 ILE A 186     123.437 126.037 159.122  1.00 11.47           C  
ATOM    885  CD1 ILE A 186     120.665 126.566 157.977  1.00 11.47           C  
ATOM    886  N   VAL A 187     125.778 129.047 158.108  1.00 10.82           N  
ATOM    887  CA  VAL A 187     127.223 129.049 157.898  1.00 10.82           C  
ATOM    888  C   VAL A 187     127.926 129.734 159.063  1.00 10.82           C  
ATOM    889  O   VAL A 187     128.944 129.248 159.563  1.00 10.82           O  
ATOM    890  CB  VAL A 187     127.556 129.722 156.550  1.00 10.82           C  
ATOM    891  CG1 VAL A 187     128.983 130.220 156.508  1.00 10.82           C  
ATOM    892  CG2 VAL A 187     127.322 128.762 155.416  1.00 10.82           C  
ATOM    893  N   ASN A 188     127.402 130.879 159.503  1.00 10.42           N  
ATOM    894  CA  ASN A 188     128.026 131.622 160.598  1.00 10.42           C  
ATOM    895  C   ASN A 188     127.974 130.849 161.912  1.00 10.42           C  
ATOM    896  O   ASN A 188     128.956 130.836 162.676  1.00 10.42           O  
ATOM    897  CB  ASN A 188     127.353 132.980 160.745  1.00 10.42           C  
ATOM    898  CG  ASN A 188     127.825 133.981 159.715  1.00 10.42           C  
ATOM    899  OD1 ASN A 188     128.771 133.731 158.973  1.00 10.42           O  
ATOM    900  ND2 ASN A 188     127.159 135.123 159.663  1.00 10.42           N  
ATOM    901  N   VAL A 189     126.847 130.192 162.201  1.00 10.64           N  
ATOM    902  CA  VAL A 189     126.803 129.363 163.407  1.00 10.64           C  
ATOM    903  C   VAL A 189     127.834 128.242 163.326  1.00 10.64           C  
ATOM    904  O   VAL A 189     128.514 127.930 164.313  1.00 10.64           O  
ATOM    905  CB  VAL A 189     125.384 128.815 163.637  1.00 10.64           C  
ATOM    906  CG1 VAL A 189     125.381 127.793 164.752  1.00 10.64           C  
ATOM    907  CG2 VAL A 189     124.442 129.942 163.994  1.00 10.64           C  
ATOM    908  N   CYS A 190     127.975 127.622 162.155  1.00 11.28           N  
ATOM    909  CA  CYS A 190     128.967 126.564 162.010  1.00 11.28           C  
ATOM    910  C   CYS A 190     130.376 127.108 162.203  1.00 11.28           C  
ATOM    911  O   CYS A 190     131.244 126.425 162.754  1.00 11.28           O  
ATOM    912  CB  CYS A 190     128.819 125.878 160.651  1.00 11.28           C  
ATOM    913  SG  CYS A 190     127.234 125.025 160.451  1.00 11.28           S  
ATOM    914  N   ASN A 191     130.621 128.334 161.742  1.00 10.78           N  
ATOM    915  CA  ASN A 191     131.916 128.972 161.956  1.00 10.78           C  
ATOM    916  C   ASN A 191     132.247 129.126 163.437  1.00 10.78           C  
ATOM    917  O   ASN A 191     133.373 128.836 163.862  1.00 10.78           O  
ATOM    918  CB  ASN A 191     131.913 130.337 161.269  1.00 10.78           C  
ATOM    919  CG  ASN A 191     133.220 131.064 161.408  1.00 10.78           C  
ATOM    920  OD1 ASN A 191     134.043 130.731 162.255  1.00 10.78           O  
ATOM    921  ND2 ASN A 191     133.420 132.076 160.578  1.00 10.78           N  
ATOM    922  N   TRP A 192     131.276 129.545 164.246  1.00 10.74           N  
ATOM    923  CA  TRP A 192     131.561 129.658 165.675  1.00 10.74           C  
ATOM    924  C   TRP A 192     131.758 128.293 166.326  1.00 10.74           C  
ATOM    925  O   TRP A 192     132.658 128.116 167.165  1.00 10.74           O  
ATOM    926  CB  TRP A 192     130.469 130.463 166.377  1.00 10.74           C  
ATOM    927  CG  TRP A 192     130.593 131.931 166.108  1.00 10.74           C  
ATOM    928  CD1 TRP A 192     130.044 132.626 165.080  1.00 10.74           C  
ATOM    929  CD2 TRP A 192     131.338 132.881 166.881  1.00 10.74           C  
ATOM    930  NE1 TRP A 192     130.394 133.947 165.159  1.00 10.74           N  
ATOM    931  CE2 TRP A 192     131.189 134.132 166.257  1.00 10.74           C  
ATOM    932  CE3 TRP A 192     132.117 132.793 168.040  1.00 10.74           C  
ATOM    933  CZ2 TRP A 192     131.784 135.285 166.751  1.00 10.74           C  
ATOM    934  CZ3 TRP A 192     132.707 133.938 168.527  1.00 10.74           C  
ATOM    935  CH2 TRP A 192     132.537 135.168 167.884  1.00 10.74           C  
ATOM    936  N   ILE A 193     130.965 127.298 165.922  1.00 11.60           N  
ATOM    937  CA  ILE A 193     131.117 125.975 166.520  1.00 11.60           C  
ATOM    938  C   ILE A 193     132.480 125.399 166.181  1.00 11.60           C  
ATOM    939  O   ILE A 193     133.126 124.774 167.028  1.00 11.60           O  
ATOM    940  CB  ILE A 193     129.976 125.043 166.073  1.00 11.60           C  
ATOM    941  CG1 ILE A 193     128.622 125.632 166.466  1.00 11.60           C  
ATOM    942  CG2 ILE A 193     130.132 123.657 166.672  1.00 11.60           C  
ATOM    943  CD1 ILE A 193     127.433 124.904 165.876  1.00 11.60           C  
ATOM    944  N   LEU A 194     132.948 125.600 164.949  1.00 11.78           N  
ATOM    945  CA  LEU A 194     134.278 125.121 164.588  1.00 11.78           C  
ATOM    946  C   LEU A 194     135.362 125.849 165.377  1.00 11.78           C  
ATOM    947  O   LEU A 194     136.300 125.219 165.876  1.00 11.78           O  
ATOM    948  CB  LEU A 194     134.480 125.259 163.077  1.00 11.78           C  
ATOM    949  CG  LEU A 194     135.708 124.624 162.409  1.00 11.78           C  
ATOM    950  CD1 LEU A 194     135.386 124.304 160.969  1.00 11.78           C  
ATOM    951  CD2 LEU A 194     136.909 125.526 162.450  1.00 11.78           C  
ATOM    952  N   SER A 195     135.258 127.175 165.509  1.00 11.59           N  
ATOM    953  CA  SER A 195     136.301 127.918 166.218  1.00 11.59           C  
ATOM    954  C   SER A 195     136.368 127.578 167.706  1.00 11.59           C  
ATOM    955  O   SER A 195     137.415 127.778 168.334  1.00 11.59           O  
ATOM    956  CB  SER A 195     136.097 129.416 166.026  1.00 11.59           C  
ATOM    957  OG  SER A 195     136.220 129.764 164.661  1.00 11.59           O  
ATOM    958  N   SER A 196     135.291 127.033 168.273  1.00 12.06           N  
ATOM    959  CA  SER A 196     135.336 126.642 169.679  1.00 12.06           C  
ATOM    960  C   SER A 196     136.374 125.556 169.949  1.00 12.06           C  
ATOM    961  O   SER A 196     136.931 125.505 171.047  1.00 12.06           O  
ATOM    962  CB  SER A 196     133.963 126.163 170.145  1.00 12.06           C  
ATOM    963  OG  SER A 196     132.967 127.127 169.889  1.00 12.06           O  
ATOM    964  N   ALA A 197     136.659 124.692 168.974  1.00 12.06           N  
ATOM    965  CA  ALA A 197     137.610 123.604 169.201  1.00 12.06           C  
ATOM    966  C   ALA A 197     138.973 124.130 169.628  1.00 12.06           C  
ATOM    967  O   ALA A 197     139.640 123.530 170.477  1.00 12.06           O  
ATOM    968  CB  ALA A 197     137.745 122.755 167.941  1.00 12.06           C  
ATOM    969  N   ILE A 198     139.409 125.241 169.045  1.00 12.55           N  
ATOM    970  CA  ILE A 198     140.634 125.893 169.490  1.00 12.55           C  
ATOM    971  C   ILE A 198     140.359 126.788 170.693  1.00 12.55           C  
ATOM    972  O   ILE A 198     141.183 126.891 171.606  1.00 12.55           O  
ATOM    973  CB  ILE A 198     141.265 126.684 168.333  1.00 12.55           C  
ATOM    974  N   GLY A 199     139.202 127.452 170.711  1.00 13.23           N  
ATOM    975  CA  GLY A 199     138.955 128.471 171.720  1.00 13.23           C  
ATOM    976  C   GLY A 199     138.796 127.946 173.133  1.00 13.23           C  
ATOM    977  O   GLY A 199     139.353 128.511 174.074  1.00 13.23           O  
ATOM    978  N   LEU A 200     138.014 126.891 173.313  1.00 13.17           N  
ATOM    979  CA  LEU A 200     137.691 126.410 174.658  1.00 13.17           C  
ATOM    980  C   LEU A 200     138.883 125.857 175.430  1.00 13.17           C  
ATOM    981  O   LEU A 200     139.010 126.139 176.626  1.00 13.17           O  
ATOM    982  CB  LEU A 200     136.603 125.341 174.591  1.00 13.17           C  
ATOM    983  CG  LEU A 200     135.289 125.817 173.999  1.00 13.17           C  
ATOM    984  CD1 LEU A 200     134.289 124.688 174.031  1.00 13.17           C  
ATOM    985  CD2 LEU A 200     134.770 127.030 174.726  1.00 13.17           C  
ATOM    986  N   PRO A 201     139.768 125.073 174.815  1.00 13.50           N  
ATOM    987  CA  PRO A 201     140.978 124.669 175.546  1.00 13.50           C  
ATOM    988  C   PRO A 201     141.791 125.849 176.049  1.00 13.50           C  
ATOM    989  O   PRO A 201     142.303 125.814 177.176  1.00 13.50           O  
ATOM    990  CB  PRO A 201     141.729 123.838 174.497  1.00 13.50           C  
ATOM    991  CG  PRO A 201     140.636 123.213 173.749  1.00 13.50           C  
ATOM    992  CD  PRO A 201     139.655 124.322 173.552  1.00 13.50           C  
ATOM    993  N   VAL A 202     141.908 126.908 175.252  1.00 13.92           N  
ATOM    994  CA  VAL A 202     142.647 128.079 175.704  1.00 13.92           C  
ATOM    995  C   VAL A 202     141.972 128.681 176.929  1.00 13.92           C  
ATOM    996  O   VAL A 202     142.641 129.114 177.870  1.00 13.92           O  
ATOM    997  CB  VAL A 202     142.781 129.101 174.562  1.00 13.92           C  
ATOM    998  CG1 VAL A 202     143.152 130.463 175.117  1.00 13.92           C  
ATOM    999  CG2 VAL A 202     143.804 128.638 173.551  1.00 13.92           C  
ATOM   1000  N   MET A 203     140.638 128.723 176.939  1.00 15.55           N  
ATOM   1001  CA  MET A 203     139.940 129.264 178.100  1.00 15.55           C  
ATOM   1002  C   MET A 203     140.192 128.409 179.326  1.00 15.55           C  
ATOM   1003  O   MET A 203     140.425 128.931 180.420  1.00 15.55           O  
ATOM   1004  CB  MET A 203     138.434 129.357 177.845  1.00 15.55           C  
ATOM   1005  CG  MET A 203     137.693 130.056 178.980  1.00 15.55           C  
ATOM   1006  SD  MET A 203     135.905 130.159 178.817  1.00 15.55           S  
ATOM   1007  CE  MET A 203     135.740 131.380 177.524  1.00 15.55           C  
ATOM   1008  N   PHE A 204     140.132 127.088 179.161  1.00 16.38           N  
ATOM   1009  CA  PHE A 204     140.324 126.188 180.287  1.00 16.38           C  
ATOM   1010  C   PHE A 204     141.732 126.308 180.864  1.00 16.38           C  
ATOM   1011  O   PHE A 204     141.918 126.168 182.076  1.00 16.38           O  
ATOM   1012  CB  PHE A 204     140.003 124.765 179.844  1.00 16.38           C  
ATOM   1013  CG  PHE A 204     140.223 123.733 180.901  1.00 16.38           C  
ATOM   1014  CD1 PHE A 204     139.283 123.538 181.889  1.00 16.38           C  
ATOM   1015  CD2 PHE A 204     141.361 122.948 180.904  1.00 16.38           C  
ATOM   1016  CE1 PHE A 204     139.476 122.588 182.870  1.00 16.38           C  
ATOM   1017  CE2 PHE A 204     141.560 121.995 181.880  1.00 16.38           C  
ATOM   1018  CZ  PHE A 204     140.615 121.810 182.860  1.00 16.38           C  
ATOM   1019  N   MET A 205     142.734 126.557 180.019  1.00 17.15           N  
ATOM   1020  CA  MET A 205     144.120 126.592 180.481  1.00 17.15           C  
ATOM   1021  C   MET A 205     144.468 127.890 181.218  1.00 17.15           C  
ATOM   1022  O   MET A 205     145.139 127.851 182.254  1.00 17.15           O  
ATOM   1023  CB  MET A 205     145.044 126.403 179.276  1.00 17.15           C  
ATOM   1024  CG  MET A 205     144.958 125.020 178.636  1.00 17.15           C  
ATOM   1025  SD  MET A 205     145.904 124.855 177.103  1.00 17.15           S  
ATOM   1026  CE  MET A 205     147.613 124.894 177.630  1.00 17.15           C  
ATOM   1027  N   ALA A 206     144.044 129.042 180.691  1.00 16.41           N  
ATOM   1028  CA  ALA A 206     144.472 130.345 181.202  1.00 16.41           C  
ATOM   1029  C   ALA A 206     144.331 130.443 182.719  1.00 16.41           C  
ATOM   1030  O   ALA A 206     143.408 129.882 183.314  1.00 16.41           O  
ATOM   1031  CB  ALA A 206     143.674 131.465 180.531  1.00 16.41           C  
ATOM   1032  N   THR A 207     145.265 131.166 183.345  1.00 17.01           N  
ATOM   1033  CA  THR A 207     145.337 131.256 184.798  1.00 17.01           C  
ATOM   1034  C   THR A 207     145.972 132.576 185.229  1.00 17.01           C  
ATOM   1035  O   THR A 207     146.642 133.262 184.452  1.00 17.01           O  
ATOM   1036  CB  THR A 207     146.137 130.092 185.392  1.00 17.01           C  
ATOM   1037  OG1 THR A 207     146.287 130.279 186.803  1.00 17.01           O  
ATOM   1038  CG2 THR A 207     147.514 130.011 184.764  1.00 17.01           C  
ATOM   1039  N   THR A 208     145.705 132.943 186.485  1.00 17.38           N  
ATOM   1040  CA  THR A 208     146.369 134.057 187.157  1.00 17.38           C  
ATOM   1041  C   THR A 208     147.510 133.493 187.993  1.00 17.38           C  
ATOM   1042  O   THR A 208     147.272 132.826 189.002  1.00 17.38           O  
ATOM   1043  CB  THR A 208     145.407 134.847 188.043  1.00 17.38           C  
ATOM   1044  OG1 THR A 208     144.833 133.984 189.027  1.00 17.38           O  
ATOM   1045  CG2 THR A 208     144.318 135.473 187.224  1.00 17.38           C  
ATOM   1046  N   LYS A 209     148.742 133.770 187.581  1.00 19.09           N  
ATOM   1047  CA  LYS A 209     149.921 133.289 188.291  1.00 19.09           C  
ATOM   1048  C   LYS A 209     150.411 134.353 189.262  1.00 19.09           C  
ATOM   1049  O   LYS A 209     150.689 135.487 188.865  1.00 19.09           O  
ATOM   1050  CB  LYS A 209     151.031 132.925 187.308  1.00 19.09           C  
ATOM   1051  N   TYR A 210     150.533 133.975 190.532  1.00 21.63           N  
ATOM   1052  CA  TYR A 210     150.871 134.925 191.588  1.00 21.63           C  
ATOM   1053  C   TYR A 210     152.390 135.047 191.721  1.00 21.63           C  
ATOM   1054  O   TYR A 210     153.013 134.552 192.660  1.00 21.63           O  
ATOM   1055  CB  TYR A 210     150.224 134.500 192.902  1.00 21.63           C  
ATOM   1056  N   ARG A 211     152.987 135.737 190.755  1.00 23.22           N  
ATOM   1057  CA  ARG A 211     154.406 136.039 190.853  1.00 23.22           C  
ATOM   1058  C   ARG A 211     154.646 136.970 192.035  1.00 23.22           C  
ATOM   1059  O   ARG A 211     153.817 137.823 192.356  1.00 23.22           O  
ATOM   1060  CB  ARG A 211     154.915 136.684 189.565  1.00 23.22           C  
ATOM   1061  N   GLN A 212     155.791 136.794 192.696  1.00 25.34           N  
ATOM   1062  CA  GLN A 212     156.056 137.584 193.892  1.00 25.34           C  
ATOM   1063  C   GLN A 212     156.018 139.073 193.582  1.00 25.34           C  
ATOM   1064  O   GLN A 212     155.471 139.864 194.360  1.00 25.34           O  
ATOM   1065  CB  GLN A 212     157.408 137.196 194.486  1.00 25.34           C  
ATOM   1066  N   GLY A 213     156.586 139.475 192.443  1.00 26.00           N  
ATOM   1067  CA  GLY A 213     156.574 140.884 192.090  1.00 26.00           C  
ATOM   1068  C   GLY A 213     155.173 141.408 191.839  1.00 26.00           C  
ATOM   1069  O   GLY A 213     154.785 142.458 192.357  1.00 26.00           O  
ATOM   1070  N   SER A 214     154.393 140.680 191.042  1.00 21.27           N  
ATOM   1071  CA  SER A 214     153.053 141.121 190.682  1.00 21.27           C  
ATOM   1072  C   SER A 214     152.276 139.956 190.092  1.00 21.27           C  
ATOM   1073  O   SER A 214     152.855 139.017 189.544  1.00 21.27           O  
ATOM   1074  CB  SER A 214     153.100 142.285 189.686  1.00 21.27           C  
ATOM   1075  N   ILE A 215     150.952 140.034 190.220  1.00 16.61           N  
ATOM   1076  CA  ILE A 215     150.061 139.082 189.570  1.00 16.61           C  
ATOM   1077  C   ILE A 215     150.243 139.128 188.059  1.00 16.61           C  
ATOM   1078  O   ILE A 215     150.412 140.201 187.468  1.00 16.61           O  
ATOM   1079  CB  ILE A 215     148.610 139.404 189.954  1.00 16.61           C  
ATOM   1080  CG1 ILE A 215     148.402 139.172 191.443  1.00 16.61           C  
ATOM   1081  CG2 ILE A 215     147.653 138.539 189.153  1.00 16.61           C  
ATOM   1082  CD1 ILE A 215     147.099 139.712 191.956  1.00 16.61           C  
ATOM   1083  N   ASP A 216     150.271 137.960 187.409  1.00 16.61           N  
ATOM   1084  CA  ASP A 216     150.355 137.851 185.928  1.00 16.61           C  
ATOM   1085  C   ASP A 216     149.089 137.134 185.470  1.00 16.61           C  
ATOM   1086  O   ASP A 216     148.420 136.581 186.337  1.00 16.61           O  
ATOM   1087  CB  ASP A 216     151.617 137.110 185.486  1.00 16.61           C  
ATOM   1088  N   CYS A 217     148.704 137.265 184.206  1.00 15.93           N  
ATOM   1089  CA  CYS A 217     147.546 136.560 183.597  1.00 15.93           C  
ATOM   1090  C   CYS A 217     148.153 135.886 182.363  1.00 15.93           C  
ATOM   1091  O   CYS A 217     148.591 136.640 181.475  1.00 15.93           O  
ATOM   1092  CB  CYS A 217     146.419 137.567 183.351  1.00 15.93           C  
ATOM   1093  SG  CYS A 217     145.145 137.086 182.159  1.00 15.93           S  
ATOM   1094  N   THR A 218     148.198 134.551 182.285  1.00 16.98           N  
ATOM   1095  CA  THR A 218     148.917 133.840 181.190  1.00 16.98           C  
ATOM   1096  C   THR A 218     148.257 132.510 180.833  1.00 16.98           C  
ATOM   1097  O   THR A 218     147.129 132.349 181.223  1.00 16.98           O  
ATOM   1098  CB  THR A 218     150.379 133.609 181.609  1.00 16.98           C  
ATOM   1099  OG1 THR A 218     150.329 132.888 182.841  1.00 16.98           O  
ATOM   1100  CG2 THR A 218     151.185 134.878 181.783  1.00 16.98           C  
ATOM   1101  N   LEU A 219     148.885 131.666 180.014  1.00 16.58           N  
ATOM   1102  CA  LEU A 219     148.437 130.335 179.611  1.00 16.58           C  
ATOM   1103  C   LEU A 219     149.358 129.274 180.201  1.00 16.58           C  
ATOM   1104  O   LEU A 219     150.575 129.332 180.006  1.00 16.58           O  
ATOM   1105  CB  LEU A 219     148.436 130.178 178.092  1.00 16.58           C  
ATOM   1106  CG  LEU A 219     147.471 130.998 177.263  1.00 16.58           C  
ATOM   1107  CD1 LEU A 219     147.822 130.890 175.815  1.00 16.58           C  
ATOM   1108  CD2 LEU A 219     146.080 130.462 177.505  1.00 16.58           C  
ATOM   1109  N   THR A 220     148.779 128.317 180.928  1.00 18.68           N  
ATOM   1110  CA  THR A 220     149.532 127.251 181.585  1.00 18.68           C  
ATOM   1111  C   THR A 220     149.513 125.979 180.738  1.00 18.68           C  
ATOM   1112  O   THR A 220     148.443 125.421 180.481  1.00 18.68           O  
ATOM   1113  CB  THR A 220     148.961 126.964 182.972  1.00 18.68           C  
ATOM   1114  N   PHE A 221     150.695 125.511 180.334  1.00 20.14           N  
ATOM   1115  CA  PHE A 221     150.853 124.343 179.475  1.00 20.14           C  
ATOM   1116  C   PHE A 221     151.349 123.144 180.275  1.00 20.14           C  
ATOM   1117  O   PHE A 221     152.065 123.292 181.268  1.00 20.14           O  
ATOM   1118  CB  PHE A 221     151.848 124.606 178.338  1.00 20.14           C  
ATOM   1119  CG  PHE A 221     151.444 125.709 177.421  1.00 20.14           C  
ATOM   1120  CD1 PHE A 221     151.748 127.020 177.721  1.00 20.14           C  
ATOM   1121  CD2 PHE A 221     150.756 125.438 176.253  1.00 20.14           C  
ATOM   1122  CE1 PHE A 221     151.371 128.038 176.871  1.00 20.14           C  
ATOM   1123  CE2 PHE A 221     150.377 126.453 175.406  1.00 20.14           C  
ATOM   1124  CZ  PHE A 221     150.690 127.750 175.713  1.00 20.14           C  
ATOM   1125  N   SER A 222     150.961 121.952 179.827  1.00 26.91           N  
ATOM   1126  CA  SER A 222     151.389 120.722 180.475  1.00 26.91           C  
ATOM   1127  C   SER A 222     152.861 120.458 180.157  1.00 26.91           C  
ATOM   1128  O   SER A 222     153.420 121.001 179.203  1.00 26.91           O  
ATOM   1129  CB  SER A 222     150.521 119.546 180.023  1.00 26.91           C  
ATOM   1130  N   THR A 225     156.778 121.304 178.286  1.00 27.84           N  
ATOM   1131  CA  THR A 225     156.244 122.570 177.797  1.00 27.84           C  
ATOM   1132  C   THR A 225     156.482 122.744 176.304  1.00 27.84           C  
ATOM   1133  O   THR A 225     155.650 123.325 175.600  1.00 27.84           O  
ATOM   1134  CB  THR A 225     156.869 123.732 178.570  1.00 27.84           C  
ATOM   1135  N   TRP A 226     157.621 122.273 175.806  1.00 24.84           N  
ATOM   1136  CA  TRP A 226     157.953 122.475 174.401  1.00 24.84           C  
ATOM   1137  C   TRP A 226     156.923 121.829 173.487  1.00 24.84           C  
ATOM   1138  O   TRP A 226     156.364 122.484 172.597  1.00 24.84           O  
ATOM   1139  CB  TRP A 226     159.346 121.914 174.117  1.00 24.84           C  
ATOM   1140  N   TYR A 227     156.561 120.581 173.782  1.00 26.96           N  
ATOM   1141  CA  TYR A 227     155.581 119.874 172.966  1.00 26.96           C  
ATOM   1142  C   TYR A 227     154.227 120.571 172.981  1.00 26.96           C  
ATOM   1143  O   TYR A 227     153.578 120.683 171.937  1.00 26.96           O  
ATOM   1144  CB  TYR A 227     155.417 118.430 173.440  1.00 26.96           C  
ATOM   1145  CG  TYR A 227     154.452 117.652 172.575  1.00 26.96           C  
ATOM   1146  CD1 TYR A 227     154.838 117.187 171.324  1.00 26.96           C  
ATOM   1147  CD2 TYR A 227     153.144 117.430 172.978  1.00 26.96           C  
ATOM   1148  CE1 TYR A 227     153.962 116.495 170.519  1.00 26.96           C  
ATOM   1149  CE2 TYR A 227     152.257 116.739 172.171  1.00 26.96           C  
ATOM   1150  CZ  TYR A 227     152.675 116.276 170.945  1.00 26.96           C  
ATOM   1151  OH  TYR A 227     151.800 115.582 170.143  1.00 26.96           O  
ATOM   1152  N   TRP A 228     153.773 121.042 174.139  1.00 25.28           N  
ATOM   1153  CA  TRP A 228     152.418 121.566 174.205  1.00 25.28           C  
ATOM   1154  C   TRP A 228     152.318 123.024 173.790  1.00 25.28           C  
ATOM   1155  O   TRP A 228     151.210 123.488 173.498  1.00 25.28           O  
ATOM   1156  CB  TRP A 228     151.830 121.395 175.604  1.00 25.28           C  
ATOM   1157  CG  TRP A 228     151.545 119.978 175.903  1.00 25.28           C  
ATOM   1158  CD1 TRP A 228     152.141 119.199 176.848  1.00 25.28           C  
ATOM   1159  CD2 TRP A 228     150.629 119.136 175.208  1.00 25.28           C  
ATOM   1160  NE1 TRP A 228     151.630 117.929 176.804  1.00 25.28           N  
ATOM   1161  CE2 TRP A 228     150.701 117.862 175.801  1.00 25.28           C  
ATOM   1162  CE3 TRP A 228     149.739 119.338 174.150  1.00 25.28           C  
ATOM   1163  CZ2 TRP A 228     149.914 116.797 175.377  1.00 25.28           C  
ATOM   1164  CZ3 TRP A 228     148.954 118.276 173.732  1.00 25.28           C  
ATOM   1165  CH2 TRP A 228     149.050 117.023 174.343  1.00 25.28           C  
ATOM   1166  N   GLU A 229     153.423 123.761 173.763  1.00 19.63           N  
ATOM   1167  CA  GLU A 229     153.376 125.186 173.480  1.00 19.63           C  
ATOM   1168  C   GLU A 229     153.729 125.465 172.030  1.00 19.63           C  
ATOM   1169  O   GLU A 229     153.039 126.252 171.351  1.00 19.63           O  
ATOM   1170  CB  GLU A 229     154.335 125.946 174.399  1.00 19.63           C  
ATOM   1171  N   ASN A 230     154.777 124.802 171.529  1.00 18.88           N  
ATOM   1172  CA  ASN A 230     155.109 124.949 170.126  1.00 18.88           C  
ATOM   1173  C   ASN A 230     153.996 124.372 169.270  1.00 18.88           C  
ATOM   1174  O   ASN A 230     153.766 124.845 168.154  1.00 18.88           O  
ATOM   1175  CB  ASN A 230     156.434 124.252 169.847  1.00 18.88           C  
ATOM   1176  CG  ASN A 230     157.620 125.040 170.346  1.00 18.88           C  
ATOM   1177  OD1 ASN A 230     157.657 126.261 170.244  1.00 18.88           O  
ATOM   1178  ND2 ASN A 230     158.579 124.343 170.936  1.00 18.88           N  
ATOM   1179  N   LEU A 231     153.272 123.379 169.805  1.00 19.24           N  
ATOM   1180  CA  LEU A 231     152.134 122.797 169.100  1.00 19.24           C  
ATOM   1181  C   LEU A 231     151.013 123.815 168.930  1.00 19.24           C  
ATOM   1182  O   LEU A 231     150.425 123.927 167.846  1.00 19.24           O  
ATOM   1183  CB  LEU A 231     151.637 121.562 169.851  1.00 19.24           C  
ATOM   1184  CG  LEU A 231     150.596 120.641 169.201  1.00 19.24           C  
ATOM   1185  CD1 LEU A 231     150.746 119.237 169.762  1.00 19.24           C  
ATOM   1186  CD2 LEU A 231     149.172 121.119 169.400  1.00 19.24           C  
ATOM   1187  N   LEU A 232     150.698 124.569 169.979  1.00 15.71           N  
ATOM   1188  CA  LEU A 232     149.642 125.564 169.848  1.00 15.71           C  
ATOM   1189  C   LEU A 232     150.043 126.650 168.858  1.00 15.71           C  
ATOM   1190  O   LEU A 232     149.249 127.031 167.982  1.00 15.71           O  
ATOM   1191  CB  LEU A 232     149.314 126.172 171.213  1.00 15.71           C  
ATOM   1192  CG  LEU A 232     148.264 127.285 171.232  1.00 15.71           C  
ATOM   1193  CD1 LEU A 232     146.895 126.752 170.882  1.00 15.71           C  
ATOM   1194  CD2 LEU A 232     148.239 127.976 172.570  1.00 15.71           C  
ATOM   1195  N   LYS A 233     151.293 127.121 168.936  1.00 15.05           N  
ATOM   1196  CA  LYS A 233     151.720 128.144 167.985  1.00 15.05           C  
ATOM   1197  C   LYS A 233     151.711 127.635 166.545  1.00 15.05           C  
ATOM   1198  O   LYS A 233     151.307 128.367 165.631  1.00 15.05           O  
ATOM   1199  CB  LYS A 233     153.110 128.668 168.334  1.00 15.05           C  
ATOM   1200  CG  LYS A 233     153.271 129.230 169.721  1.00 15.05           C  
ATOM   1201  CD  LYS A 233     154.682 129.671 169.893  1.00 15.05           C  
ATOM   1202  CE  LYS A 233     154.914 130.401 171.182  1.00 15.05           C  
ATOM   1203  NZ  LYS A 233     156.257 131.023 171.149  1.00 15.05           N  
ATOM   1204  N   ILE A 234     152.127 126.382 166.315  1.00 15.28           N  
ATOM   1205  CA  ILE A 234     152.109 125.844 164.952  1.00 15.28           C  
ATOM   1206  C   ILE A 234     150.686 125.728 164.434  1.00 15.28           C  
ATOM   1207  O   ILE A 234     150.411 126.048 163.273  1.00 15.28           O  
ATOM   1208  CB  ILE A 234     152.855 124.498 164.857  1.00 15.28           C  
ATOM   1209  CG1 ILE A 234     152.886 124.038 163.400  1.00 15.28           C  
ATOM   1210  CG2 ILE A 234     152.229 123.455 165.731  1.00 15.28           C  
ATOM   1211  CD1 ILE A 234     153.823 122.915 163.135  1.00 15.28           C  
ATOM   1212  N   CYS A 235     149.769 125.219 165.258  1.00 15.03           N  
ATOM   1213  CA  CYS A 235     148.405 125.046 164.783  1.00 15.03           C  
ATOM   1214  C   CYS A 235     147.805 126.391 164.422  1.00 15.03           C  
ATOM   1215  O   CYS A 235     147.068 126.505 163.436  1.00 15.03           O  
ATOM   1216  CB  CYS A 235     147.554 124.338 165.835  1.00 15.03           C  
ATOM   1217  SG  CYS A 235     148.034 122.629 166.154  1.00 15.03           S  
ATOM   1218  N   VAL A 236     148.092 127.424 165.217  1.00 12.88           N  
ATOM   1219  CA  VAL A 236     147.559 128.740 164.889  1.00 12.88           C  
ATOM   1220  C   VAL A 236     148.160 129.239 163.585  1.00 12.88           C  
ATOM   1221  O   VAL A 236     147.464 129.829 162.755  1.00 12.88           O  
ATOM   1222  CB  VAL A 236     147.793 129.730 166.046  1.00 12.88           C  
ATOM   1223  CG1 VAL A 236     147.209 131.092 165.718  1.00 12.88           C  
ATOM   1224  CG2 VAL A 236     147.133 129.228 167.301  1.00 12.88           C  
ATOM   1225  N   PHE A 237     149.447 128.995 163.366  1.00 12.76           N  
ATOM   1226  CA  PHE A 237     150.055 129.439 162.117  1.00 12.76           C  
ATOM   1227  C   PHE A 237     149.476 128.718 160.901  1.00 12.76           C  
ATOM   1228  O   PHE A 237     149.359 129.311 159.823  1.00 12.76           O  
ATOM   1229  CB  PHE A 237     151.565 129.253 162.160  1.00 12.76           C  
ATOM   1230  CG  PHE A 237     152.284 130.012 161.093  1.00 12.76           C  
ATOM   1231  CD1 PHE A 237     152.149 131.382 160.989  1.00 12.76           C  
ATOM   1232  CD2 PHE A 237     153.088 129.355 160.188  1.00 12.76           C  
ATOM   1233  CE1 PHE A 237     152.807 132.081 160.006  1.00 12.76           C  
ATOM   1234  CE2 PHE A 237     153.749 130.052 159.203  1.00 12.76           C  
ATOM   1235  CZ  PHE A 237     153.605 131.414 159.110  1.00 12.76           C  
ATOM   1236  N   ILE A 238     149.149 127.438 161.032  1.00 13.51           N  
ATOM   1237  CA  ILE A 238     148.706 126.664 159.875  1.00 13.51           C  
ATOM   1238  C   ILE A 238     147.211 126.807 159.610  1.00 13.51           C  
ATOM   1239  O   ILE A 238     146.799 127.276 158.545  1.00 13.51           O  
ATOM   1240  CB  ILE A 238     149.064 125.171 160.050  1.00 13.51           C  
ATOM   1241  CG1 ILE A 238     150.581 124.967 160.054  1.00 13.51           C  
ATOM   1242  CG2 ILE A 238     148.401 124.301 158.963  1.00 13.51           C  
ATOM   1243  CD1 ILE A 238     151.291 125.417 158.795  1.00 13.51           C  
ATOM   1244  N   PHE A 239     146.390 126.395 160.568  1.00 13.35           N  
ATOM   1245  CA  PHE A 239     144.954 126.358 160.332  1.00 13.35           C  
ATOM   1246  C   PHE A 239     144.330 127.745 160.255  1.00 13.35           C  
ATOM   1247  O   PHE A 239     143.409 127.963 159.463  1.00 13.35           O  
ATOM   1248  CB  PHE A 239     144.308 125.487 161.396  1.00 13.35           C  
ATOM   1249  CG  PHE A 239     144.838 124.091 161.390  1.00 13.35           C  
ATOM   1250  CD1 PHE A 239     144.450 123.203 160.403  1.00 13.35           C  
ATOM   1251  CD2 PHE A 239     145.761 123.677 162.329  1.00 13.35           C  
ATOM   1252  CE1 PHE A 239     144.945 121.922 160.373  1.00 13.35           C  
ATOM   1253  CE2 PHE A 239     146.263 122.395 162.302  1.00 13.35           C  
ATOM   1254  CZ  PHE A 239     145.857 121.517 161.320  1.00 13.35           C  
ATOM   1255  N   ALA A 240     144.795 128.695 161.053  1.00 12.11           N  
ATOM   1256  CA  ALA A 240     144.154 130.000 161.087  1.00 12.11           C  
ATOM   1257  C   ALA A 240     144.881 131.045 160.262  1.00 12.11           C  
ATOM   1258  O   ALA A 240     144.592 132.232 160.417  1.00 12.11           O  
ATOM   1259  CB  ALA A 240     144.032 130.502 162.521  1.00 12.11           C  
ATOM   1260  N   PHE A 241     145.848 130.657 159.435  1.00 11.74           N  
ATOM   1261  CA  PHE A 241     146.462 131.654 158.573  1.00 11.74           C  
ATOM   1262  C   PHE A 241     146.708 131.163 157.142  1.00 11.74           C  
ATOM   1263  O   PHE A 241     146.155 131.723 156.192  1.00 11.74           O  
ATOM   1264  CB  PHE A 241     147.751 132.151 159.230  1.00 11.74           C  
ATOM   1265  CG  PHE A 241     148.204 133.484 158.733  1.00 11.74           C  
ATOM   1266  CD1 PHE A 241     147.435 134.611 158.953  1.00 11.74           C  
ATOM   1267  CD2 PHE A 241     149.397 133.622 158.069  1.00 11.74           C  
ATOM   1268  CE1 PHE A 241     147.853 135.839 158.506  1.00 11.74           C  
ATOM   1269  CE2 PHE A 241     149.809 134.845 157.629  1.00 11.74           C  
ATOM   1270  CZ  PHE A 241     149.040 135.950 157.844  1.00 11.74           C  
ATOM   1271  N   ILE A 242     147.561 130.148 156.971  1.00 12.60           N  
ATOM   1272  CA  ILE A 242     148.018 129.747 155.635  1.00 12.60           C  
ATOM   1273  C   ILE A 242     146.887 129.165 154.787  1.00 12.60           C  
ATOM   1274  O   ILE A 242     146.665 129.587 153.647  1.00 12.60           O  
ATOM   1275  CB  ILE A 242     149.186 128.750 155.762  1.00 12.60           C  
ATOM   1276  CG1 ILE A 242     150.351 129.369 156.544  1.00 12.60           C  
ATOM   1277  CG2 ILE A 242     149.659 128.268 154.398  1.00 12.60           C  
ATOM   1278  CD1 ILE A 242     150.914 130.650 155.952  1.00 12.60           C  
ATOM   1279  N   MET A 243     146.154 128.193 155.326  1.00 12.69           N  
ATOM   1280  CA  MET A 243     145.168 127.482 154.513  1.00 12.69           C  
ATOM   1281  C   MET A 243     144.027 128.374 154.053  1.00 12.69           C  
ATOM   1282  O   MET A 243     143.674 128.330 152.858  1.00 12.69           O  
ATOM   1283  CB  MET A 243     144.644 126.273 155.293  1.00 12.69           C  
ATOM   1284  N   PRO A 244     143.405 129.185 154.911  1.00 12.16           N  
ATOM   1285  CA  PRO A 244     142.379 130.104 154.403  1.00 12.16           C  
ATOM   1286  C   PRO A 244     142.930 131.102 153.401  1.00 12.16           C  
ATOM   1287  O   PRO A 244     142.222 131.470 152.458  1.00 12.16           O  
ATOM   1288  CB  PRO A 244     141.841 130.766 155.681  1.00 12.16           C  
ATOM   1289  CG  PRO A 244     142.899 130.565 156.705  1.00 12.16           C  
ATOM   1290  CD  PRO A 244     143.522 129.255 156.379  1.00 12.16           C  
ATOM   1291  N   VAL A 245     144.167 131.564 153.574  1.00 12.53           N  
ATOM   1292  CA  VAL A 245     144.751 132.461 152.579  1.00 12.53           C  
ATOM   1293  C   VAL A 245     144.872 131.777 151.220  1.00 12.53           C  
ATOM   1294  O   VAL A 245     144.609 132.396 150.182  1.00 12.53           O  
ATOM   1295  CB  VAL A 245     146.104 133.005 153.068  1.00 12.53           C  
ATOM   1296  CG1 VAL A 245     146.841 133.698 151.948  1.00 12.53           C  
ATOM   1297  CG2 VAL A 245     145.890 133.991 154.190  1.00 12.53           C  
ATOM   1298  N   LEU A 246     145.263 130.498 151.188  1.00 12.31           N  
ATOM   1299  CA  LEU A 246     145.290 129.802 149.899  1.00 12.31           C  
ATOM   1300  C   LEU A 246     143.893 129.645 149.302  1.00 12.31           C  
ATOM   1301  O   LEU A 246     143.704 129.842 148.093  1.00 12.31           O  
ATOM   1302  CB  LEU A 246     145.967 128.437 150.022  1.00 12.31           C  
ATOM   1303  CG  LEU A 246     147.502 128.370 150.008  1.00 12.31           C  
ATOM   1304  CD1 LEU A 246     148.047 128.848 148.665  1.00 12.31           C  
ATOM   1305  CD2 LEU A 246     148.154 129.136 151.133  1.00 12.31           C  
ATOM   1306  N   ILE A 247     142.899 129.305 150.124  1.00 11.90           N  
ATOM   1307  CA  ILE A 247     141.545 129.173 149.588  1.00 11.90           C  
ATOM   1308  C   ILE A 247     141.100 130.492 148.965  1.00 11.90           C  
ATOM   1309  O   ILE A 247     140.549 130.527 147.852  1.00 11.90           O  
ATOM   1310  CB  ILE A 247     140.572 128.694 150.679  1.00 11.90           C  
ATOM   1311  CG1 ILE A 247     141.018 127.333 151.217  1.00 11.90           C  
ATOM   1312  CG2 ILE A 247     139.165 128.583 150.119  1.00 11.90           C  
ATOM   1313  CD1 ILE A 247     140.213 126.815 152.409  1.00 11.90           C  
ATOM   1314  N   ILE A 248     141.377 131.598 149.655  1.00 11.48           N  
ATOM   1315  CA  ILE A 248     140.970 132.916 149.185  1.00 11.48           C  
ATOM   1316  C   ILE A 248     141.700 133.263 147.893  1.00 11.48           C  
ATOM   1317  O   ILE A 248     141.110 133.820 146.957  1.00 11.48           O  
ATOM   1318  CB  ILE A 248     141.204 133.950 150.307  1.00 11.48           C  
ATOM   1319  CG1 ILE A 248     140.188 133.715 151.430  1.00 11.48           C  
ATOM   1320  CG2 ILE A 248     141.101 135.375 149.798  1.00 11.48           C  
ATOM   1321  CD1 ILE A 248     140.401 134.540 152.671  1.00 11.48           C  
ATOM   1322  N   THR A 249     142.989 132.943 147.812  1.00 11.83           N  
ATOM   1323  CA  THR A 249     143.748 133.331 146.632  1.00 11.83           C  
ATOM   1324  C   THR A 249     143.254 132.578 145.405  1.00 11.83           C  
ATOM   1325  O   THR A 249     143.149 133.152 144.316  1.00 11.83           O  
ATOM   1326  CB  THR A 249     145.241 133.063 146.853  1.00 11.83           C  
ATOM   1327  OG1 THR A 249     145.716 133.829 147.962  1.00 11.83           O  
ATOM   1328  CG2 THR A 249     146.039 133.445 145.632  1.00 11.83           C  
ATOM   1329  N   VAL A 250     142.949 131.291 145.560  1.00 12.17           N  
ATOM   1330  CA  VAL A 250     142.439 130.527 144.427  1.00 12.17           C  
ATOM   1331  C   VAL A 250     141.060 131.033 143.999  1.00 12.17           C  
ATOM   1332  O   VAL A 250     140.779 131.153 142.798  1.00 12.17           O  
ATOM   1333  CB  VAL A 250     142.436 129.022 144.750  1.00 12.17           C  
ATOM   1334  CG1 VAL A 250     141.726 128.232 143.651  1.00 12.17           C  
ATOM   1335  CG2 VAL A 250     143.867 128.522 144.908  1.00 12.17           C  
ATOM   1336  N   CYS A 251     140.168 131.325 144.958  1.00 12.58           N  
ATOM   1337  CA  CYS A 251     138.849 131.827 144.568  1.00 12.58           C  
ATOM   1338  C   CYS A 251     138.940 133.154 143.824  1.00 12.58           C  
ATOM   1339  O   CYS A 251     138.264 133.343 142.808  1.00 12.58           O  
ATOM   1340  CB  CYS A 251     137.952 131.995 145.793  1.00 12.58           C  
ATOM   1341  SG  CYS A 251     137.400 130.488 146.573  1.00 12.58           S  
ATOM   1342  N   TYR A 252     139.768 134.086 144.296  1.00 12.07           N  
ATOM   1343  CA  TYR A 252     139.942 135.331 143.550  1.00 12.07           C  
ATOM   1344  C   TYR A 252     140.652 135.148 142.214  1.00 12.07           C  
ATOM   1345  O   TYR A 252     140.354 135.884 141.273  1.00 12.07           O  
ATOM   1346  CB  TYR A 252     140.575 136.416 144.415  1.00 12.07           C  
ATOM   1347  CG  TYR A 252     139.481 137.147 145.159  1.00 12.07           C  
ATOM   1348  CD1 TYR A 252     138.815 138.194 144.534  1.00 12.07           C  
ATOM   1349  CD2 TYR A 252     139.041 136.751 146.406  1.00 12.07           C  
ATOM   1350  CE1 TYR A 252     137.801 138.856 145.142  1.00 12.07           C  
ATOM   1351  CE2 TYR A 252     138.006 137.415 147.030  1.00 12.07           C  
ATOM   1352  CZ  TYR A 252     137.391 138.465 146.385  1.00 12.07           C  
ATOM   1353  OH  TYR A 252     136.362 139.141 146.980  1.00 12.07           O  
ATOM   1354  N   GLY A 253     141.593 134.218 142.087  1.00 12.09           N  
ATOM   1355  CA  GLY A 253     142.177 134.000 140.775  1.00 12.09           C  
ATOM   1356  C   GLY A 253     141.149 133.516 139.767  1.00 12.09           C  
ATOM   1357  O   GLY A 253     141.060 134.034 138.648  1.00 12.09           O  
ATOM   1358  N   LEU A 254     140.305 132.575 140.177  1.00 12.84           N  
ATOM   1359  CA  LEU A 254     139.249 132.104 139.284  1.00 12.84           C  
ATOM   1360  C   LEU A 254     138.217 133.197 138.980  1.00 12.84           C  
ATOM   1361  O   LEU A 254     137.790 133.350 137.826  1.00 12.84           O  
ATOM   1362  CB  LEU A 254     138.590 130.868 139.896  1.00 12.84           C  
ATOM   1363  CG  LEU A 254     139.428 129.585 139.855  1.00 12.84           C  
ATOM   1364  CD1 LEU A 254     138.765 128.486 140.628  1.00 12.84           C  
ATOM   1365  CD2 LEU A 254     139.651 129.129 138.434  1.00 12.84           C  
ATOM   1366  N   MET A 255     137.814 133.981 139.985  1.00 12.47           N  
ATOM   1367  CA  MET A 255     136.888 135.080 139.712  1.00 12.47           C  
ATOM   1368  C   MET A 255     137.488 136.126 138.775  1.00 12.47           C  
ATOM   1369  O   MET A 255     136.784 136.662 137.913  1.00 12.47           O  
ATOM   1370  CB  MET A 255     136.436 135.750 141.008  1.00 12.47           C  
ATOM   1371  CG  MET A 255     135.155 135.171 141.578  1.00 12.47           C  
ATOM   1372  SD  MET A 255     134.610 135.949 143.106  1.00 12.47           S  
ATOM   1373  CE  MET A 255     135.926 135.517 144.227  1.00 12.47           C  
ATOM   1374  N   ILE A 256     138.766 136.465 138.946  1.00 13.41           N  
ATOM   1375  CA  ILE A 256     139.387 137.429 138.047  1.00 13.41           C  
ATOM   1376  C   ILE A 256     139.398 136.879 136.631  1.00 13.41           C  
ATOM   1377  O   ILE A 256     139.178 137.615 135.654  1.00 13.41           O  
ATOM   1378  CB  ILE A 256     140.803 137.774 138.552  1.00 13.41           C  
ATOM   1379  CG1 ILE A 256     140.740 138.684 139.788  1.00 13.41           C  
ATOM   1380  CG2 ILE A 256     141.644 138.425 137.466  1.00 13.41           C  
ATOM   1381  CD1 ILE A 256     140.041 140.014 139.592  1.00 13.41           C  
ATOM   1382  N   LEU A 257     139.594 135.564 136.495  1.00 13.87           N  
ATOM   1383  CA  LEU A 257     139.528 134.970 135.166  1.00 13.87           C  
ATOM   1384  C   LEU A 257     138.147 135.162 134.559  1.00 13.87           C  
ATOM   1385  O   LEU A 257     138.022 135.533 133.389  1.00 13.87           O  
ATOM   1386  CB  LEU A 257     139.897 133.485 135.200  1.00 13.87           C  
ATOM   1387  CG  LEU A 257     141.337 133.134 135.571  1.00 13.87           C  
ATOM   1388  CD1 LEU A 257     141.497 131.640 135.690  1.00 13.87           C  
ATOM   1389  CD2 LEU A 257     142.316 133.700 134.554  1.00 13.87           C  
ATOM   1390  N   ARG A 258     137.091 134.904 135.332  1.00 13.93           N  
ATOM   1391  CA  ARG A 258     135.752 135.061 134.768  1.00 13.93           C  
ATOM   1392  C   ARG A 258     135.493 136.516 134.392  1.00 13.93           C  
ATOM   1393  O   ARG A 258     135.022 136.809 133.290  1.00 13.93           O  
ATOM   1394  CB  ARG A 258     134.693 134.560 135.748  1.00 13.93           C  
ATOM   1395  N   LEU A 259     135.815 137.450 135.286  1.00 14.72           N  
ATOM   1396  CA  LEU A 259     135.474 138.850 135.037  1.00 14.72           C  
ATOM   1397  C   LEU A 259     136.222 139.426 133.843  1.00 14.72           C  
ATOM   1398  O   LEU A 259     135.701 140.322 133.174  1.00 14.72           O  
ATOM   1399  CB  LEU A 259     135.691 139.734 136.264  1.00 14.72           C  
ATOM   1400  CG  LEU A 259     134.587 139.746 137.326  1.00 14.72           C  
ATOM   1401  CD1 LEU A 259     134.375 138.442 138.034  1.00 14.72           C  
ATOM   1402  CD2 LEU A 259     134.900 140.838 138.321  1.00 14.72           C  
ATOM   1403  N   LYS A 260     137.445 138.985 133.569  1.00 15.91           N  
ATOM   1404  CA  LYS A 260     138.176 139.668 132.510  1.00 15.91           C  
ATOM   1405  C   LYS A 260     137.619 139.387 131.117  1.00 15.91           C  
ATOM   1406  O   LYS A 260     137.857 140.190 130.210  1.00 15.91           O  
ATOM   1407  CB  LYS A 260     139.652 139.275 132.546  1.00 15.91           C  
ATOM   1408  N   SER A 261     136.906 138.277 130.904  1.00 16.99           N  
ATOM   1409  CA  SER A 261     136.496 137.882 129.558  1.00 16.99           C  
ATOM   1410  C   SER A 261     134.981 137.770 129.353  1.00 16.99           C  
ATOM   1411  O   SER A 261     134.552 137.135 128.386  1.00 16.99           O  
ATOM   1412  CB  SER A 261     137.164 136.555 129.194  1.00 16.99           C  
ATOM   1413  N   VAL A 262     134.151 138.366 130.204  1.00 17.72           N  
ATOM   1414  CA  VAL A 262     132.699 138.346 130.027  1.00 17.72           C  
ATOM   1415  C   VAL A 262     132.198 139.749 129.718  1.00 17.72           C  
ATOM   1416  O   VAL A 262     132.645 140.730 130.322  1.00 17.72           O  
ATOM   1417  CB  VAL A 262     131.985 137.768 131.263  1.00 17.72           C  
ATOM   1418  CG1 VAL A 262     130.501 137.662 131.022  1.00 17.72           C  
ATOM   1419  CG2 VAL A 262     132.517 136.400 131.571  1.00 17.72           C  
ATOM   1420  N   ARG A 263     131.310 139.843 128.726  1.00 20.52           N  
ATOM   1421  CA  ARG A 263     130.643 141.104 128.411  1.00 20.52           C  
ATOM   1422  C   ARG A 263     129.603 141.493 129.467  1.00 20.52           C  
ATOM   1423  O   ARG A 263     129.541 142.654 129.885  1.00 20.52           O  
ATOM   1424  CB  ARG A 263     129.998 141.003 127.032  1.00 20.52           C  
ATOM   1425  CG  ARG A 263     129.359 142.279 126.545  1.00 20.52           C  
ATOM   1426  CD  ARG A 263     128.076 141.982 125.820  1.00 20.52           C  
ATOM   1427  NE  ARG A 263     127.331 143.202 125.563  1.00 20.52           N  
ATOM   1428  CZ  ARG A 263     126.080 143.236 125.141  1.00 20.52           C  
ATOM   1429  NH1 ARG A 263     125.391 142.128 124.943  1.00 20.52           N  
ATOM   1430  NH2 ARG A 263     125.502 144.412 124.927  1.00 20.52           N  
ATOM   1431  N   LEU A 264     128.770 140.550 129.901  1.00 18.76           N  
ATOM   1432  CA  LEU A 264     127.815 140.808 130.970  1.00 18.76           C  
ATOM   1433  C   LEU A 264     127.757 139.614 131.901  1.00 18.76           C  
ATOM   1434  O   LEU A 264     127.828 138.467 131.455  1.00 18.76           O  
ATOM   1435  CB  LEU A 264     126.404 141.075 130.431  1.00 18.76           C  
ATOM   1436  CG  LEU A 264     126.013 142.500 130.053  1.00 18.76           C  
ATOM   1437  CD1 LEU A 264     124.758 142.469 129.232  1.00 18.76           C  
ATOM   1438  CD2 LEU A 264     125.817 143.363 131.274  1.00 18.76           C  
ATOM   1439  N   LEU A 265     127.581 139.885 133.188  1.00 16.75           N  
ATOM   1440  CA  LEU A 265     127.636 138.832 134.190  1.00 16.75           C  
ATOM   1441  C   LEU A 265     126.267 138.342 134.629  1.00 16.75           C  
ATOM   1442  O   LEU A 265     126.143 137.187 135.042  1.00 16.75           O  
ATOM   1443  CB  LEU A 265     128.419 139.312 135.415  1.00 16.75           C  
ATOM   1444  CG  LEU A 265     129.937 139.095 135.350  1.00 16.75           C  
ATOM   1445  CD1 LEU A 265     130.617 139.871 136.458  1.00 16.75           C  
ATOM   1446  CD2 LEU A 265     130.327 137.630 135.383  1.00 16.75           C  
ATOM   1447  N   SER A 266     125.235 139.185 134.570  1.00 19.80           N  
ATOM   1448  CA  SER A 266     123.917 138.796 135.052  1.00 19.80           C  
ATOM   1449  C   SER A 266     122.813 139.179 134.074  1.00 19.80           C  
ATOM   1450  O   SER A 266     121.640 139.221 134.458  1.00 19.80           O  
ATOM   1451  CB  SER A 266     123.642 139.418 136.423  1.00 19.80           C  
ATOM   1452  N   GLY A 267     123.159 139.454 132.821  1.00 21.28           N  
ATOM   1453  CA  GLY A 267     122.183 139.899 131.846  1.00 21.28           C  
ATOM   1454  C   GLY A 267     121.846 141.373 131.911  1.00 21.28           C  
ATOM   1455  O   GLY A 267     122.003 142.090 130.920  1.00 21.28           O  
ATOM   1456  N   SER A 268     121.363 141.834 133.061  1.00 20.32           N  
ATOM   1457  CA  SER A 268     121.065 143.247 133.256  1.00 20.32           C  
ATOM   1458  C   SER A 268     122.330 144.046 133.542  1.00 20.32           C  
ATOM   1459  O   SER A 268     123.211 143.598 134.278  1.00 20.32           O  
ATOM   1460  CB  SER A 268     120.067 143.419 134.399  1.00 20.32           C  
ATOM   1461  N   ARG A 269     122.416 145.237 132.944  1.00 20.12           N  
ATOM   1462  CA  ARG A 269     123.591 146.087 133.127  1.00 20.12           C  
ATOM   1463  C   ARG A 269     123.748 146.534 134.583  1.00 20.12           C  
ATOM   1464  O   ARG A 269     124.866 146.556 135.126  1.00 20.12           O  
ATOM   1465  CB  ARG A 269     123.473 147.305 132.216  1.00 20.12           C  
ATOM   1466  CG  ARG A 269     123.826 147.051 130.771  1.00 20.12           C  
ATOM   1467  CD  ARG A 269     124.223 148.342 130.079  1.00 20.12           C  
ATOM   1468  NE  ARG A 269     124.497 148.159 128.660  1.00 20.12           N  
ATOM   1469  CZ  ARG A 269     124.949 149.110 127.855  1.00 20.12           C  
ATOM   1470  NH1 ARG A 269     125.191 150.331 128.296  1.00 20.12           N  
ATOM   1471  NH2 ARG A 269     125.171 148.826 126.577  1.00 20.12           N  
ATOM   1472  N   GLU A 270     122.635 146.876 135.236  1.00 17.99           N  
ATOM   1473  CA  GLU A 270     122.693 147.278 136.636  1.00 17.99           C  
ATOM   1474  C   GLU A 270     123.153 146.129 137.517  1.00 17.99           C  
ATOM   1475  O   GLU A 270     123.934 146.327 138.458  1.00 17.99           O  
ATOM   1476  CB  GLU A 270     121.325 147.784 137.090  1.00 17.99           C  
ATOM   1477  N   LYS A 271     122.658 144.921 137.245  1.00 17.07           N  
ATOM   1478  CA  LYS A 271     123.051 143.779 138.056  1.00 17.07           C  
ATOM   1479  C   LYS A 271     124.542 143.518 137.907  1.00 17.07           C  
ATOM   1480  O   LYS A 271     125.227 143.175 138.879  1.00 17.07           O  
ATOM   1481  CB  LYS A 271     122.231 142.555 137.655  1.00 17.07           C  
ATOM   1482  N   ASP A 272     125.062 143.715 136.695  1.00 16.50           N  
ATOM   1483  CA  ASP A 272     126.487 143.555 136.443  1.00 16.50           C  
ATOM   1484  C   ASP A 272     127.291 144.529 137.292  1.00 16.50           C  
ATOM   1485  O   ASP A 272     128.263 144.141 137.965  1.00 16.50           O  
ATOM   1486  CB  ASP A 272     126.749 143.769 134.946  1.00 16.50           C  
ATOM   1487  CG  ASP A 272     128.185 143.515 134.547  1.00 16.50           C  
ATOM   1488  OD1 ASP A 272     128.535 142.353 134.301  1.00 16.50           O  
ATOM   1489  OD2 ASP A 272     128.960 144.479 134.452  1.00 16.50           O  
ATOM   1490  N   ARG A 273     126.872 145.799 137.310  1.00 15.72           N  
ATOM   1491  CA  ARG A 273     127.645 146.795 138.048  1.00 15.72           C  
ATOM   1492  C   ARG A 273     127.592 146.516 139.546  1.00 15.72           C  
ATOM   1493  O   ARG A 273     128.607 146.640 140.246  1.00 15.72           O  
ATOM   1494  CB  ARG A 273     127.128 148.199 137.737  1.00 15.72           C  
ATOM   1495  N   ASN A 274     126.421 146.126 140.054  1.00 16.03           N  
ATOM   1496  CA  ASN A 274     126.309 145.834 141.479  1.00 16.03           C  
ATOM   1497  C   ASN A 274     127.203 144.660 141.861  1.00 16.03           C  
ATOM   1498  O   ASN A 274     127.872 144.681 142.907  1.00 16.03           O  
ATOM   1499  CB  ASN A 274     124.857 145.539 141.848  1.00 16.03           C  
ATOM   1500  CG  ASN A 274     123.944 146.716 141.597  1.00 16.03           C  
ATOM   1501  OD1 ASN A 274     124.312 147.865 141.828  1.00 16.03           O  
ATOM   1502  ND2 ASN A 274     122.736 146.434 141.129  1.00 16.03           N  
ATOM   1503  N   LEU A 275     127.232 143.628 141.014  1.00 14.92           N  
ATOM   1504  CA  LEU A 275     128.025 142.444 141.311  1.00 14.92           C  
ATOM   1505  C   LEU A 275     129.501 142.801 141.409  1.00 14.92           C  
ATOM   1506  O   LEU A 275     130.193 142.402 142.362  1.00 14.92           O  
ATOM   1507  CB  LEU A 275     127.785 141.409 140.209  1.00 14.92           C  
ATOM   1508  CG  LEU A 275     127.967 139.911 140.434  1.00 14.92           C  
ATOM   1509  CD1 LEU A 275     127.095 139.413 141.571  1.00 14.92           C  
ATOM   1510  CD2 LEU A 275     127.638 139.174 139.152  1.00 14.92           C  
ATOM   1511  N   ARG A 276     129.980 143.619 140.469  1.00 14.81           N  
ATOM   1512  CA  ARG A 276     131.395 143.967 140.468  1.00 14.81           C  
ATOM   1513  C   ARG A 276     131.754 144.882 141.637  1.00 14.81           C  
ATOM   1514  O   ARG A 276     132.839 144.745 142.226  1.00 14.81           O  
ATOM   1515  CB  ARG A 276     131.756 144.604 139.128  1.00 14.81           C  
ATOM   1516  CG  ARG A 276     131.672 143.618 137.972  1.00 14.81           C  
ATOM   1517  CD  ARG A 276     131.827 144.268 136.605  1.00 14.81           C  
ATOM   1518  NE  ARG A 276     131.665 143.297 135.525  1.00 14.81           N  
ATOM   1519  CZ  ARG A 276     132.642 142.835 134.757  1.00 14.81           C  
ATOM   1520  NH1 ARG A 276     133.887 143.254 134.885  1.00 14.81           N  
ATOM   1521  NH2 ARG A 276     132.359 141.935 133.825  1.00 14.81           N  
ATOM   1522  N   ARG A 277     130.820 145.734 142.063  1.00 13.43           N  
ATOM   1523  CA  ARG A 277     131.097 146.614 143.193  1.00 13.43           C  
ATOM   1524  C   ARG A 277     131.220 145.819 144.487  1.00 13.43           C  
ATOM   1525  O   ARG A 277     132.148 146.040 145.280  1.00 13.43           O  
ATOM   1526  CB  ARG A 277     129.997 147.671 143.306  1.00 13.43           C  
ATOM   1527  N   ILE A 278     130.289 144.895 144.734  1.00 13.56           N  
ATOM   1528  CA  ILE A 278     130.368 144.132 145.976  1.00 13.56           C  
ATOM   1529  C   ILE A 278     131.643 143.294 145.992  1.00 13.56           C  
ATOM   1530  O   ILE A 278     132.317 143.170 147.031  1.00 13.56           O  
ATOM   1531  CB  ILE A 278     129.108 143.269 146.174  1.00 13.56           C  
ATOM   1532  CG1 ILE A 278     127.876 144.154 146.313  1.00 13.56           C  
ATOM   1533  CG2 ILE A 278     129.218 142.413 147.424  1.00 13.56           C  
ATOM   1534  CD1 ILE A 278     126.650 143.585 145.677  1.00 13.56           C  
ATOM   1535  N   THR A 279     132.012 142.725 144.835  1.00 12.83           N  
ATOM   1536  CA  THR A 279     133.214 141.900 144.786  1.00 12.83           C  
ATOM   1537  C   THR A 279     134.455 142.718 145.137  1.00 12.83           C  
ATOM   1538  O   THR A 279     135.301 142.276 145.935  1.00 12.83           O  
ATOM   1539  CB  THR A 279     133.338 141.265 143.394  1.00 12.83           C  
ATOM   1540  OG1 THR A 279     132.169 140.487 143.120  1.00 12.83           O  
ATOM   1541  CG2 THR A 279     134.563 140.361 143.280  1.00 12.83           C  
ATOM   1542  N   ARG A 280     134.553 143.943 144.611  1.00 13.37           N  
ATOM   1543  CA  ARG A 280     135.703 144.774 144.954  1.00 13.37           C  
ATOM   1544  C   ARG A 280     135.725 145.138 146.438  1.00 13.37           C  
ATOM   1545  O   ARG A 280     136.799 145.165 147.064  1.00 13.37           O  
ATOM   1546  CB  ARG A 280     135.713 146.050 144.123  1.00 13.37           C  
ATOM   1547  CG  ARG A 280     136.963 146.879 144.366  1.00 13.37           C  
ATOM   1548  CD  ARG A 280     136.960 148.148 143.580  1.00 13.37           C  
ATOM   1549  NE  ARG A 280     135.862 148.996 144.017  1.00 13.37           N  
ATOM   1550  CZ  ARG A 280     135.518 150.131 143.432  1.00 13.37           C  
ATOM   1551  NH1 ARG A 280     136.173 150.591 142.379  1.00 13.37           N  
ATOM   1552  NH2 ARG A 280     134.482 150.814 143.906  1.00 13.37           N  
ATOM   1553  N   MET A 281     134.562 145.434 147.027  1.00 13.73           N  
ATOM   1554  CA  MET A 281     134.571 145.812 148.438  1.00 13.73           C  
ATOM   1555  C   MET A 281     135.111 144.671 149.294  1.00 13.73           C  
ATOM   1556  O   MET A 281     135.941 144.888 150.198  1.00 13.73           O  
ATOM   1557  CB  MET A 281     133.163 146.216 148.888  1.00 13.73           C  
ATOM   1558  CG  MET A 281     133.097 146.722 150.325  1.00 13.73           C  
ATOM   1559  SD  MET A 281     131.469 147.222 150.916  1.00 13.73           S  
ATOM   1560  CE  MET A 281     130.621 145.657 151.048  1.00 13.73           C  
ATOM   1561  N   VAL A 282     134.677 143.441 148.998  1.00 11.98           N  
ATOM   1562  CA  VAL A 282     135.132 142.296 149.786  1.00 11.98           C  
ATOM   1563  C   VAL A 282     136.636 142.105 149.628  1.00 11.98           C  
ATOM   1564  O   VAL A 282     137.350 141.789 150.596  1.00 11.98           O  
ATOM   1565  CB  VAL A 282     134.352 141.030 149.391  1.00 11.98           C  
ATOM   1566  CG1 VAL A 282     134.886 139.809 150.129  1.00 11.98           C  
ATOM   1567  CG2 VAL A 282     132.884 141.212 149.693  1.00 11.98           C  
ATOM   1568  N   LEU A 283     137.151 142.322 148.416  1.00 11.62           N  
ATOM   1569  CA  LEU A 283     138.589 142.166 148.229  1.00 11.62           C  
ATOM   1570  C   LEU A 283     139.374 143.171 149.065  1.00 11.62           C  
ATOM   1571  O   LEU A 283     140.429 142.837 149.629  1.00 11.62           O  
ATOM   1572  CB  LEU A 283     138.949 142.319 146.755  1.00 11.62           C  
ATOM   1573  CG  LEU A 283     140.399 141.997 146.400  1.00 11.62           C  
ATOM   1574  CD1 LEU A 283     140.787 140.578 146.800  1.00 11.62           C  
ATOM   1575  CD2 LEU A 283     140.633 142.236 144.926  1.00 11.62           C  
ATOM   1576  N   VAL A 284     138.891 144.411 149.150  1.00 11.61           N  
ATOM   1577  CA  VAL A 284     139.629 145.408 149.924  1.00 11.61           C  
ATOM   1578  C   VAL A 284     139.645 145.039 151.403  1.00 11.61           C  
ATOM   1579  O   VAL A 284     140.680 145.151 152.077  1.00 11.61           O  
ATOM   1580  CB  VAL A 284     139.043 146.812 149.683  1.00 11.61           C  
ATOM   1581  CG1 VAL A 284     139.722 147.850 150.561  1.00 11.61           C  
ATOM   1582  CG2 VAL A 284     139.203 147.193 148.235  1.00 11.61           C  
ATOM   1583  N   VAL A 285     138.521 144.553 151.923  1.00 11.28           N  
ATOM   1584  CA  VAL A 285     138.503 144.143 153.327  1.00 11.28           C  
ATOM   1585  C   VAL A 285     139.513 143.023 153.583  1.00 11.28           C  
ATOM   1586  O   VAL A 285     140.273 143.058 154.567  1.00 11.28           O  
ATOM   1587  CB  VAL A 285     137.076 143.738 153.736  1.00 11.28           C  
ATOM   1588  CG1 VAL A 285     137.034 143.241 155.176  1.00 11.28           C  
ATOM   1589  CG2 VAL A 285     136.137 144.906 153.560  1.00 11.28           C  
ATOM   1590  N   VAL A 286     139.565 142.030 152.688  1.00 10.92           N  
ATOM   1591  CA  VAL A 286     140.502 140.921 152.874  1.00 10.92           C  
ATOM   1592  C   VAL A 286     141.942 141.427 152.891  1.00 10.92           C  
ATOM   1593  O   VAL A 286     142.752 141.036 153.750  1.00 10.92           O  
ATOM   1594  CB  VAL A 286     140.288 139.859 151.778  1.00 10.92           C  
ATOM   1595  CG1 VAL A 286     141.416 138.832 151.765  1.00 10.92           C  
ATOM   1596  CG2 VAL A 286     138.966 139.162 151.971  1.00 10.92           C  
ATOM   1597  N   ALA A 287     142.282 142.314 151.955  1.00 11.03           N  
ATOM   1598  CA  ALA A 287     143.661 142.774 151.871  1.00 11.03           C  
ATOM   1599  C   ALA A 287     144.061 143.541 153.124  1.00 11.03           C  
ATOM   1600  O   ALA A 287     145.181 143.382 153.635  1.00 11.03           O  
ATOM   1601  CB  ALA A 287     143.847 143.636 150.626  1.00 11.03           C  
ATOM   1602  N   VAL A 288     143.156 144.378 153.637  1.00 10.77           N  
ATOM   1603  CA  VAL A 288     143.470 145.162 154.830  1.00 10.77           C  
ATOM   1604  C   VAL A 288     143.720 144.248 156.024  1.00 10.77           C  
ATOM   1605  O   VAL A 288     144.657 144.465 156.807  1.00 10.77           O  
ATOM   1606  CB  VAL A 288     142.341 146.175 155.107  1.00 10.77           C  
ATOM   1607  CG1 VAL A 288     142.473 146.799 156.491  1.00 10.77           C  
ATOM   1608  CG2 VAL A 288     142.351 147.260 154.056  1.00 10.77           C  
ATOM   1609  N   PHE A 289     142.901 143.203 156.177  1.00 10.89           N  
ATOM   1610  CA  PHE A 289     143.107 142.284 157.295  1.00 10.89           C  
ATOM   1611  C   PHE A 289     144.450 141.570 157.198  1.00 10.89           C  
ATOM   1612  O   PHE A 289     145.161 141.432 158.203  1.00 10.89           O  
ATOM   1613  CB  PHE A 289     141.963 141.277 157.341  1.00 10.89           C  
ATOM   1614  CG  PHE A 289     142.096 140.224 158.410  1.00 10.89           C  
ATOM   1615  CD1 PHE A 289     142.952 139.148 158.250  1.00 10.89           C  
ATOM   1616  CD2 PHE A 289     141.319 140.281 159.551  1.00 10.89           C  
ATOM   1617  CE1 PHE A 289     143.054 138.182 159.216  1.00 10.89           C  
ATOM   1618  CE2 PHE A 289     141.416 139.310 160.518  1.00 10.89           C  
ATOM   1619  CZ  PHE A 289     142.279 138.260 160.349  1.00 10.89           C  
ATOM   1620  N   ILE A 290     144.833 141.131 155.996  1.00 10.43           N  
ATOM   1621  CA  ILE A 290     146.108 140.427 155.861  1.00 10.43           C  
ATOM   1622  C   ILE A 290     147.273 141.349 156.202  1.00 10.43           C  
ATOM   1623  O   ILE A 290     148.224 140.947 156.889  1.00 10.43           O  
ATOM   1624  CB  ILE A 290     146.255 139.817 154.452  1.00 10.43           C  
ATOM   1625  CG1 ILE A 290     145.221 138.717 154.244  1.00 10.43           C  
ATOM   1626  CG2 ILE A 290     147.655 139.261 154.235  1.00 10.43           C  
ATOM   1627  CD1 ILE A 290     145.101 138.262 152.818  1.00 10.43           C  
ATOM   1628  N   VAL A 291     147.220 142.596 155.734  1.00 10.66           N  
ATOM   1629  CA  VAL A 291     148.306 143.531 156.014  1.00 10.66           C  
ATOM   1630  C   VAL A 291     148.400 143.822 157.508  1.00 10.66           C  
ATOM   1631  O   VAL A 291     149.498 143.986 158.049  1.00 10.66           O  
ATOM   1632  CB  VAL A 291     148.136 144.822 155.188  1.00 10.66           C  
ATOM   1633  CG1 VAL A 291     149.120 145.896 155.637  1.00 10.66           C  
ATOM   1634  CG2 VAL A 291     148.327 144.536 153.721  1.00 10.66           C  
ATOM   1635  N   CYS A 292     147.264 143.969 158.186  1.00 10.94           N  
ATOM   1636  CA  CYS A 292     147.316 144.226 159.624  1.00 10.94           C  
ATOM   1637  C   CYS A 292     147.833 143.032 160.422  1.00 10.94           C  
ATOM   1638  O   CYS A 292     148.476 143.222 161.458  1.00 10.94           O  
ATOM   1639  CB  CYS A 292     145.955 144.676 160.144  1.00 10.94           C  
ATOM   1640  SG  CYS A 292     145.559 146.374 159.670  1.00 10.94           S  
ATOM   1641  N   TRP A 293     147.522 141.797 160.016  1.00  9.16           N  
ATOM   1642  CA  TRP A 293     147.863 140.662 160.874  1.00  9.16           C  
ATOM   1643  C   TRP A 293     149.144 139.908 160.532  1.00  9.16           C  
ATOM   1644  O   TRP A 293     149.616 139.146 161.377  1.00  9.16           O  
ATOM   1645  CB  TRP A 293     146.714 139.659 160.902  1.00  9.16           C  
ATOM   1646  CG  TRP A 293     145.647 140.050 161.837  1.00  9.16           C  
ATOM   1647  CD1 TRP A 293     144.456 140.610 161.524  1.00  9.16           C  
ATOM   1648  CD2 TRP A 293     145.666 139.907 163.253  1.00  9.16           C  
ATOM   1649  NE1 TRP A 293     143.725 140.835 162.656  1.00  9.16           N  
ATOM   1650  CE2 TRP A 293     144.447 140.411 163.737  1.00  9.16           C  
ATOM   1651  CE3 TRP A 293     146.597 139.407 164.166  1.00  9.16           C  
ATOM   1652  CZ2 TRP A 293     144.129 140.421 165.090  1.00  9.16           C  
ATOM   1653  CZ3 TRP A 293     146.275 139.419 165.507  1.00  9.16           C  
ATOM   1654  CH2 TRP A 293     145.052 139.924 165.955  1.00  9.16           C  
ATOM   1655  N   THR A 294     149.730 140.073 159.350  1.00 11.64           N  
ATOM   1656  CA  THR A 294     150.897 139.252 159.014  1.00 11.64           C  
ATOM   1657  C   THR A 294     152.105 139.464 159.931  1.00 11.64           C  
ATOM   1658  O   THR A 294     152.716 138.463 160.359  1.00 11.64           O  
ATOM   1659  CB  THR A 294     151.268 139.509 157.548  1.00 11.64           C  
ATOM   1660  OG1 THR A 294     150.348 138.823 156.695  1.00 11.64           O  
ATOM   1661  CG2 THR A 294     152.679 139.044 157.232  1.00 11.64           C  
ATOM   1662  N   PRO A 295     152.505 140.699 160.271  1.00 11.11           N  
ATOM   1663  CA  PRO A 295     153.751 140.879 161.049  1.00 11.11           C  
ATOM   1664  C   PRO A 295     153.774 140.224 162.425  1.00 11.11           C  
ATOM   1665  O   PRO A 295     154.815 139.686 162.814  1.00 11.11           O  
ATOM   1666  CB  PRO A 295     153.876 142.408 161.139  1.00 11.11           C  
ATOM   1667  CG  PRO A 295     153.116 142.914 159.993  1.00 11.11           C  
ATOM   1668  CD  PRO A 295     151.942 141.991 159.855  1.00 11.11           C  
ATOM   1669  N   ILE A 296     152.678 140.240 163.179  1.00 11.38           N  
ATOM   1670  CA  ILE A 296     152.678 139.540 164.459  1.00 11.38           C  
ATOM   1671  C   ILE A 296     152.839 138.038 164.241  1.00 11.38           C  
ATOM   1672  O   ILE A 296     153.531 137.353 165.011  1.00 11.38           O  
ATOM   1673  CB  ILE A 296     151.406 139.904 165.258  1.00 11.38           C  
ATOM   1674  CG1 ILE A 296     151.539 139.596 166.761  1.00 11.38           C  
ATOM   1675  CG2 ILE A 296     150.174 139.226 164.694  1.00 11.38           C  
ATOM   1676  CD1 ILE A 296     152.779 140.134 167.451  1.00 11.38           C  
ATOM   1677  N   HIS A 297     152.231 137.503 163.176  1.00 10.29           N  
ATOM   1678  CA  HIS A 297     152.324 136.069 162.919  1.00 10.29           C  
ATOM   1679  C   HIS A 297     153.745 135.655 162.615  1.00 10.29           C  
ATOM   1680  O   HIS A 297     154.208 134.619 163.096  1.00 10.29           O  
ATOM   1681  CB  HIS A 297     151.435 135.633 161.756  1.00 10.29           C  
ATOM   1682  CG  HIS A 297     149.986 135.530 162.094  1.00 10.29           C  
ATOM   1683  ND1 HIS A 297     149.134 136.606 162.062  1.00 10.29           N  
ATOM   1684  CD2 HIS A 297     149.245 134.472 162.490  1.00 10.29           C  
ATOM   1685  CE1 HIS A 297     147.923 136.213 162.403  1.00 10.29           C  
ATOM   1686  NE2 HIS A 297     147.963 134.922 162.670  1.00 10.29           N  
ATOM   1687  N   ILE A 298     154.454 136.448 161.816  1.00 11.60           N  
ATOM   1688  CA  ILE A 298     155.848 136.129 161.532  1.00 11.60           C  
ATOM   1689  C   ILE A 298     156.707 136.317 162.770  1.00 11.60           C  
ATOM   1690  O   ILE A 298     157.671 135.571 162.985  1.00 11.60           O  
ATOM   1691  CB  ILE A 298     156.364 136.965 160.349  1.00 11.60           C  
ATOM   1692  CG1 ILE A 298     155.443 136.806 159.134  1.00 11.60           C  
ATOM   1693  CG2 ILE A 298     157.786 136.575 160.004  1.00 11.60           C  
ATOM   1694  CD1 ILE A 298     155.182 135.370 158.719  1.00 11.60           C  
ATOM   1695  N   TYR A 299     156.404 137.332 163.582  1.00 12.31           N  
ATOM   1696  CA  TYR A 299     157.222 137.587 164.760  1.00 12.31           C  
ATOM   1697  C   TYR A 299     157.165 136.423 165.731  1.00 12.31           C  
ATOM   1698  O   TYR A 299     158.178 136.061 166.332  1.00 12.31           O  
ATOM   1699  CB  TYR A 299     156.755 138.865 165.450  1.00 12.31           C  
ATOM   1700  N   VAL A 300     155.991 135.815 165.891  1.00 11.92           N  
ATOM   1701  CA  VAL A 300     155.864 134.700 166.830  1.00 11.92           C  
ATOM   1702  C   VAL A 300     156.767 133.531 166.431  1.00 11.92           C  
ATOM   1703  O   VAL A 300     157.456 132.933 167.272  1.00 11.92           O  
ATOM   1704  CB  VAL A 300     154.391 134.277 166.920  1.00 11.92           C  
ATOM   1705  CG1 VAL A 300     154.247 132.943 167.633  1.00 11.92           C  
ATOM   1706  CG2 VAL A 300     153.583 135.364 167.601  1.00 11.92           C  
ATOM   1707  N   ILE A 301     156.819 133.228 165.133  1.00 13.09           N  
ATOM   1708  CA  ILE A 301     157.665 132.150 164.632  1.00 13.09           C  
ATOM   1709  C   ILE A 301     159.140 132.511 164.761  1.00 13.09           C  
ATOM   1710  O   ILE A 301     159.948 131.702 165.223  1.00 13.09           O  
ATOM   1711  CB  ILE A 301     157.282 131.807 163.180  1.00 13.09           C  
ATOM   1712  CG1 ILE A 301     155.765 131.752 163.016  1.00 13.09           C  
ATOM   1713  CG2 ILE A 301     157.894 130.487 162.750  1.00 13.09           C  
ATOM   1714  CD1 ILE A 301     155.065 130.835 163.995  1.00 13.09           C  
ATOM   1715  N   ILE A 302     159.523 133.720 164.344  1.00 14.29           N  
ATOM   1716  CA  ILE A 302     160.943 134.056 164.367  1.00 14.29           C  
ATOM   1717  C   ILE A 302     161.447 134.162 165.795  1.00 14.29           C  
ATOM   1718  O   ILE A 302     162.639 133.969 166.053  1.00 14.29           O  
ATOM   1719  CB  ILE A 302     161.240 135.351 163.600  1.00 14.29           C  
ATOM   1720  CG1 ILE A 302     160.843 135.234 162.132  1.00 14.29           C  
ATOM   1721  CG2 ILE A 302     162.713 135.673 163.709  1.00 14.29           C  
ATOM   1722  CD1 ILE A 302     161.636 134.196 161.349  1.00 14.29           C  
ATOM   1723  N   LYS A 303     160.571 134.493 166.738  1.00 15.33           N  
ATOM   1724  CA  LYS A 303     160.952 134.488 168.144  1.00 15.33           C  
ATOM   1725  C   LYS A 303     161.083 133.066 168.675  1.00 15.33           C  
ATOM   1726  O   LYS A 303     161.944 132.790 169.512  1.00 15.33           O  
ATOM   1727  CB  LYS A 303     159.931 135.298 168.941  1.00 15.33           C  
ATOM   1728  CG  LYS A 303     160.346 135.729 170.323  1.00 15.33           C  
ATOM   1729  CD  LYS A 303     159.185 136.460 170.968  1.00 15.33           C  
ATOM   1730  CE  LYS A 303     159.511 137.001 172.332  1.00 15.33           C  
ATOM   1731  NZ  LYS A 303     158.338 137.691 172.927  1.00 15.33           N  
ATOM   1732  N   ALA A 304     160.242 132.146 168.213  1.00 16.15           N  
ATOM   1733  CA  ALA A 304     160.287 130.795 168.768  1.00 16.15           C  
ATOM   1734  C   ALA A 304     161.634 130.114 168.508  1.00 16.15           C  
ATOM   1735  O   ALA A 304     162.097 129.319 169.334  1.00 16.15           O  
ATOM   1736  CB  ALA A 304     159.150 129.949 168.198  1.00 16.15           C  
ATOM   1737  N   LEU A 305     162.243 130.349 167.346  1.00 17.09           N  
ATOM   1738  CA  LEU A 305     163.405 129.582 166.918  1.00 17.09           C  
ATOM   1739  C   LEU A 305     164.761 130.269 167.081  1.00 17.09           C  
ATOM   1740  O   LEU A 305     165.770 129.667 166.712  1.00 17.09           O  
ATOM   1741  CB  LEU A 305     163.251 129.207 165.443  1.00 17.09           C  
ATOM   1742  CG  LEU A 305     162.041 128.388 165.038  1.00 17.09           C  
ATOM   1743  CD1 LEU A 305     161.853 128.500 163.549  1.00 17.09           C  
ATOM   1744  CD2 LEU A 305     162.199 126.963 165.461  1.00 17.09           C  
ATOM   1745  N   ILE A 306     164.837 131.489 167.609  1.00 20.83           N  
ATOM   1746  CA  ILE A 306     166.099 132.226 167.557  1.00 20.83           C  
ATOM   1747  C   ILE A 306     166.587 132.744 168.900  1.00 20.83           C  
ATOM   1748  O   ILE A 306     167.775 133.103 169.013  1.00 20.83           O  
ATOM   1749  CB  ILE A 306     165.984 133.396 166.556  1.00 20.83           C  
ATOM   1750  N   THR A 307     165.778 132.828 169.953  1.00 22.27           N  
ATOM   1751  CA  THR A 307     166.251 133.391 171.219  1.00 22.27           C  
ATOM   1752  C   THR A 307     166.866 134.777 170.997  1.00 22.27           C  
ATOM   1753  O   THR A 307     168.061 135.000 171.184  1.00 22.27           O  
ATOM   1754  CB  THR A 307     167.253 132.452 171.899  1.00 22.27           C  
ATOM   1755  N   ILE A 308     166.017 135.704 170.561  1.00 20.80           N  
ATOM   1756  CA  ILE A 308     166.442 137.094 170.351  1.00 20.80           C  
ATOM   1757  C   ILE A 308     166.931 137.676 171.669  1.00 20.80           C  
ATOM   1758  O   ILE A 308     166.323 137.408 172.723  1.00 20.80           O  
ATOM   1759  CB  ILE A 308     165.280 137.934 169.797  1.00 20.80           C  
ATOM   1760  CG1 ILE A 308     164.632 137.246 168.596  1.00 20.80           C  
ATOM   1761  CG2 ILE A 308     165.766 139.347 169.442  1.00 20.80           C  
ATOM   1762  CD1 ILE A 308     163.442 137.991 168.035  1.00 20.80           C  
ATOM   1763  N   PRO A 309     168.003 138.467 171.687  1.00 22.92           N  
ATOM   1764  CA  PRO A 309     168.411 139.106 172.940  1.00 22.92           C  
ATOM   1765  C   PRO A 309     167.425 140.186 173.347  1.00 22.92           C  
ATOM   1766  O   PRO A 309     166.819 140.855 172.507  1.00 22.92           O  
ATOM   1767  CB  PRO A 309     169.787 139.697 172.608  1.00 22.92           C  
ATOM   1768  CG  PRO A 309     169.753 139.908 171.135  1.00 22.92           C  
ATOM   1769  CD  PRO A 309     168.938 138.769 170.590  1.00 22.92           C  
ATOM   1770  N   GLU A 310     167.280 140.365 174.658  1.00 22.06           N  
ATOM   1771  CA  GLU A 310     166.373 141.374 175.184  1.00 22.06           C  
ATOM   1772  C   GLU A 310     167.003 142.759 175.104  1.00 22.06           C  
ATOM   1773  O   GLU A 310     168.120 142.974 175.583  1.00 22.06           O  
ATOM   1774  CB  GLU A 310     165.997 141.044 176.627  1.00 22.06           C  
ATOM   1775  N   THR A 311     166.280 143.692 174.491  1.00 18.88           N  
ATOM   1776  CA  THR A 311     166.744 145.054 174.275  1.00 18.88           C  
ATOM   1777  C   THR A 311     165.523 145.925 174.019  1.00 18.88           C  
ATOM   1778  O   THR A 311     164.425 145.425 173.765  1.00 18.88           O  
ATOM   1779  CB  THR A 311     167.726 145.139 173.105  1.00 18.88           C  
ATOM   1780  N   THR A 312     165.729 147.242 174.046  1.00 18.21           N  
ATOM   1781  CA  THR A 312     164.592 148.146 173.947  1.00 18.21           C  
ATOM   1782  C   THR A 312     163.860 147.932 172.632  1.00 18.21           C  
ATOM   1783  O   THR A 312     162.621 147.956 172.580  1.00 18.21           O  
ATOM   1784  CB  THR A 312     165.060 149.594 174.081  1.00 18.21           C  
ATOM   1785  N   PHE A 313     164.619 147.685 171.561  1.00 17.95           N  
ATOM   1786  CA  PHE A 313     164.018 147.517 170.248  1.00 17.95           C  
ATOM   1787  C   PHE A 313     163.035 146.361 170.287  1.00 17.95           C  
ATOM   1788  O   PHE A 313     161.947 146.435 169.705  1.00 17.95           O  
ATOM   1789  CB  PHE A 313     165.109 147.253 169.215  1.00 17.95           C  
ATOM   1790  CG  PHE A 313     164.651 147.377 167.800  1.00 17.95           C  
ATOM   1791  CD1 PHE A 313     163.797 146.442 167.243  1.00 17.95           C  
ATOM   1792  CD2 PHE A 313     165.144 148.383 166.995  1.00 17.95           C  
ATOM   1793  CE1 PHE A 313     163.390 146.547 165.930  1.00 17.95           C  
ATOM   1794  CE2 PHE A 313     164.748 148.489 165.683  1.00 17.95           C  
ATOM   1795  CZ  PHE A 313     163.871 147.563 165.148  1.00 17.95           C  
ATOM   1796  N   GLN A 314     163.390 145.298 171.011  1.00 17.30           N  
ATOM   1797  CA  GLN A 314     162.568 144.097 171.036  1.00 17.30           C  
ATOM   1798  C   GLN A 314     161.214 144.388 171.665  1.00 17.30           C  
ATOM   1799  O   GLN A 314     160.166 144.069 171.089  1.00 17.30           O  
ATOM   1800  CB  GLN A 314     163.314 142.997 171.804  1.00 17.30           C  
ATOM   1801  CG  GLN A 314     162.819 141.574 171.583  1.00 17.30           C  
ATOM   1802  CD  GLN A 314     161.587 141.238 172.405  1.00 17.30           C  
ATOM   1803  OE1 GLN A 314     161.456 141.666 173.549  1.00 17.30           O  
ATOM   1804  NE2 GLN A 314     160.664 140.489 171.813  1.00 17.30           N  
ATOM   1805  N   THR A 315     161.214 145.084 172.803  1.00 14.80           N  
ATOM   1806  CA  THR A 315     159.969 145.345 173.519  1.00 14.80           C  
ATOM   1807  C   THR A 315     159.079 146.295 172.736  1.00 14.80           C  
ATOM   1808  O   THR A 315     157.865 146.059 172.598  1.00 14.80           O  
ATOM   1809  CB  THR A 315     160.267 145.911 174.906  1.00 14.80           C  
ATOM   1810  N   VAL A 316     159.675 147.337 172.150  1.00 14.52           N  
ATOM   1811  CA  VAL A 316     158.862 148.337 171.469  1.00 14.52           C  
ATOM   1812  C   VAL A 316     158.270 147.737 170.205  1.00 14.52           C  
ATOM   1813  O   VAL A 316     157.067 147.864 169.950  1.00 14.52           O  
ATOM   1814  CB  VAL A 316     159.694 149.599 171.172  1.00 14.52           C  
ATOM   1815  CG1 VAL A 316     158.838 150.676 170.560  1.00 14.52           C  
ATOM   1816  CG2 VAL A 316     160.321 150.126 172.435  1.00 14.52           C  
ATOM   1817  N   SER A 317     159.103 147.084 169.389  1.00 14.15           N  
ATOM   1818  CA  SER A 317     158.607 146.453 168.173  1.00 14.15           C  
ATOM   1819  C   SER A 317     157.515 145.433 168.480  1.00 14.15           C  
ATOM   1820  O   SER A 317     156.504 145.356 167.763  1.00 14.15           O  
ATOM   1821  CB  SER A 317     159.768 145.812 167.427  1.00 14.15           C  
ATOM   1822  OG  SER A 317     160.347 144.786 168.200  1.00 14.15           O  
ATOM   1823  N   TRP A 318     157.682 144.658 169.558  1.00 11.70           N  
ATOM   1824  CA  TRP A 318     156.696 143.641 169.888  1.00 11.70           C  
ATOM   1825  C   TRP A 318     155.343 144.277 170.159  1.00 11.70           C  
ATOM   1826  O   TRP A 318     154.307 143.858 169.608  1.00 11.70           O  
ATOM   1827  CB  TRP A 318     157.193 142.879 171.120  1.00 11.70           C  
ATOM   1828  CG  TRP A 318     156.297 141.817 171.652  1.00 11.70           C  
ATOM   1829  CD1 TRP A 318     155.532 141.890 172.760  1.00 11.70           C  
ATOM   1830  CD2 TRP A 318     156.101 140.513 171.112  1.00 11.70           C  
ATOM   1831  NE1 TRP A 318     154.857 140.723 172.946  1.00 11.70           N  
ATOM   1832  CE2 TRP A 318     155.191 139.857 171.942  1.00 11.70           C  
ATOM   1833  CE3 TRP A 318     156.603 139.838 169.997  1.00 11.70           C  
ATOM   1834  CZ2 TRP A 318     154.766 138.564 171.697  1.00 11.70           C  
ATOM   1835  CZ3 TRP A 318     156.183 138.555 169.762  1.00 11.70           C  
ATOM   1836  CH2 TRP A 318     155.279 137.930 170.606  1.00 11.70           C  
ATOM   1837  N   HIS A 319     155.342 145.347 170.958  1.00 11.91           N  
ATOM   1838  CA  HIS A 319     154.075 145.973 171.313  1.00 11.91           C  
ATOM   1839  C   HIS A 319     153.455 146.658 170.108  1.00 11.91           C  
ATOM   1840  O   HIS A 319     152.232 146.676 169.968  1.00 11.91           O  
ATOM   1841  CB  HIS A 319     154.252 146.921 172.490  1.00 11.91           C  
ATOM   1842  CG  HIS A 319     154.425 146.207 173.788  1.00 11.91           C  
ATOM   1843  ND1 HIS A 319     155.643 146.078 174.417  1.00 11.91           N  
ATOM   1844  CD2 HIS A 319     153.529 145.560 174.567  1.00 11.91           C  
ATOM   1845  CE1 HIS A 319     155.487 145.390 175.532  1.00 11.91           C  
ATOM   1846  NE2 HIS A 319     154.215 145.062 175.644  1.00 11.91           N  
ATOM   1847  N   PHE A 320     154.279 147.253 169.247  1.00 12.65           N  
ATOM   1848  CA  PHE A 320     153.758 147.905 168.051  1.00 12.65           C  
ATOM   1849  C   PHE A 320     153.042 146.916 167.132  1.00 12.65           C  
ATOM   1850  O   PHE A 320     151.979 147.229 166.586  1.00 12.65           O  
ATOM   1851  CB  PHE A 320     154.916 148.590 167.325  1.00 12.65           C  
ATOM   1852  CG  PHE A 320     154.529 149.278 166.052  1.00 12.65           C  
ATOM   1853  CD1 PHE A 320     154.427 150.650 166.004  1.00 12.65           C  
ATOM   1854  CD2 PHE A 320     154.305 148.558 164.895  1.00 12.65           C  
ATOM   1855  CE1 PHE A 320     154.081 151.288 164.837  1.00 12.65           C  
ATOM   1856  CE2 PHE A 320     153.960 149.189 163.730  1.00 12.65           C  
ATOM   1857  CZ  PHE A 320     153.853 150.555 163.697  1.00 12.65           C  
ATOM   1858  N   CYS A 321     153.615 145.728 166.925  1.00 11.89           N  
ATOM   1859  CA  CYS A 321     152.935 144.725 166.099  1.00 11.89           C  
ATOM   1860  C   CYS A 321     151.619 144.258 166.731  1.00 11.89           C  
ATOM   1861  O   CYS A 321     150.592 144.131 166.038  1.00 11.89           O  
ATOM   1862  CB  CYS A 321     153.872 143.547 165.835  1.00 11.89           C  
ATOM   1863  SG  CYS A 321     155.345 144.023 164.926  1.00 11.89           S  
ATOM   1864  N   ILE A 322     151.603 144.057 168.049  1.00 10.71           N  
ATOM   1865  CA  ILE A 322     150.322 143.730 168.677  1.00 10.71           C  
ATOM   1866  C   ILE A 322     149.321 144.873 168.503  1.00 10.71           C  
ATOM   1867  O   ILE A 322     148.122 144.644 168.270  1.00 10.71           O  
ATOM   1868  CB  ILE A 322     150.518 143.361 170.162  1.00 10.71           C  
ATOM   1869  CG1 ILE A 322     151.514 142.205 170.301  1.00 10.71           C  
ATOM   1870  CG2 ILE A 322     149.196 143.027 170.818  1.00 10.71           C  
ATOM   1871  CD1 ILE A 322     151.963 141.941 171.707  1.00 10.71           C  
ATOM   1872  N   ALA A 323     149.792 146.118 168.607  1.00 11.42           N  
ATOM   1873  CA  ALA A 323     148.895 147.259 168.477  1.00 11.42           C  
ATOM   1874  C   ALA A 323     148.284 147.341 167.085  1.00 11.42           C  
ATOM   1875  O   ALA A 323     147.097 147.640 166.948  1.00 11.42           O  
ATOM   1876  CB  ALA A 323     149.644 148.544 168.811  1.00 11.42           C  
ATOM   1877  N   LEU A 324     149.071 147.056 166.044  1.00 10.56           N  
ATOM   1878  CA  LEU A 324     148.537 147.065 164.681  1.00 10.56           C  
ATOM   1879  C   LEU A 324     147.433 146.031 164.516  1.00 10.56           C  
ATOM   1880  O   LEU A 324     146.340 146.321 163.980  1.00 10.56           O  
ATOM   1881  CB  LEU A 324     149.656 146.794 163.685  1.00 10.56           C  
ATOM   1882  CG  LEU A 324     149.278 146.786 162.205  1.00 10.56           C  
ATOM   1883  CD1 LEU A 324     148.833 148.149 161.738  1.00 10.56           C  
ATOM   1884  CD2 LEU A 324     150.448 146.296 161.385  1.00 10.56           C  
ATOM   1885  N   GLY A 325     147.695 144.815 165.002  1.00 10.76           N  
ATOM   1886  CA  GLY A 325     146.698 143.773 164.872  1.00 10.76           C  
ATOM   1887  C   GLY A 325     145.397 144.148 165.547  1.00 10.76           C  
ATOM   1888  O   GLY A 325     144.319 143.903 165.007  1.00 10.76           O  
ATOM   1889  N   TYR A 326     145.477 144.759 166.735  1.00 11.48           N  
ATOM   1890  CA  TYR A 326     144.254 145.237 167.383  1.00 11.48           C  
ATOM   1891  C   TYR A 326     143.619 146.414 166.642  1.00 11.48           C  
ATOM   1892  O   TYR A 326     142.391 146.529 166.598  1.00 11.48           O  
ATOM   1893  CB  TYR A 326     144.518 145.602 168.837  1.00 11.48           C  
ATOM   1894  CG  TYR A 326     144.696 144.413 169.748  1.00 11.48           C  
ATOM   1895  CD1 TYR A 326     143.854 143.313 169.646  1.00 11.48           C  
ATOM   1896  CD2 TYR A 326     145.648 144.413 170.751  1.00 11.48           C  
ATOM   1897  CE1 TYR A 326     143.990 142.239 170.475  1.00 11.48           C  
ATOM   1898  CE2 TYR A 326     145.783 143.341 171.591  1.00 11.48           C  
ATOM   1899  CZ  TYR A 326     144.950 142.257 171.452  1.00 11.48           C  
ATOM   1900  OH  TYR A 326     145.079 141.178 172.292  1.00 11.48           O  
ATOM   1901  N   THR A 327     144.430 147.308 166.074  1.00 12.00           N  
ATOM   1902  CA  THR A 327     143.893 148.488 165.402  1.00 12.00           C  
ATOM   1903  C   THR A 327     142.965 148.116 164.261  1.00 12.00           C  
ATOM   1904  O   THR A 327     142.004 148.841 163.988  1.00 12.00           O  
ATOM   1905  CB  THR A 327     145.025 149.361 164.863  1.00 12.00           C  
ATOM   1906  OG1 THR A 327     145.720 149.987 165.945  1.00 12.00           O  
ATOM   1907  CG2 THR A 327     144.482 150.426 163.937  1.00 12.00           C  
ATOM   1908  N   ASN A 328     143.231 147.000 163.583  1.00 11.56           N  
ATOM   1909  CA  ASN A 328     142.372 146.636 162.450  1.00 11.56           C  
ATOM   1910  C   ASN A 328     140.885 146.538 162.826  1.00 11.56           C  
ATOM   1911  O   ASN A 328     140.017 146.689 161.959  1.00 11.56           O  
ATOM   1912  CB  ASN A 328     142.816 145.308 161.849  1.00 11.56           C  
ATOM   1913  CG  ASN A 328     142.307 145.108 160.433  1.00 11.56           C  
ATOM   1914  OD1 ASN A 328     142.303 146.036 159.626  1.00 11.56           O  
ATOM   1915  ND2 ASN A 328     141.781 143.926 160.159  1.00 11.56           N  
ATOM   1916  N   SER A 329     140.566 146.249 164.089  1.00 13.37           N  
ATOM   1917  CA  SER A 329     139.170 146.096 164.500  1.00 13.37           C  
ATOM   1918  C   SER A 329     138.312 147.337 164.250  1.00 13.37           C  
ATOM   1919  O   SER A 329     137.110 147.207 163.987  1.00 13.37           O  
ATOM   1920  CB  SER A 329     139.092 145.709 165.972  1.00 13.37           C  
ATOM   1921  OG  SER A 329     139.675 144.439 166.182  1.00 13.37           O  
ATOM   1922  N   CYS A 330     138.871 148.535 164.365  1.00 12.76           N  
ATOM   1923  CA  CYS A 330     138.094 149.751 164.138  1.00 12.76           C  
ATOM   1924  C   CYS A 330     138.062 150.222 162.687  1.00 12.76           C  
ATOM   1925  O   CYS A 330     137.211 151.049 162.347  1.00 12.76           O  
ATOM   1926  CB  CYS A 330     138.629 150.888 165.027  1.00 12.76           C  
ATOM   1927  SG  CYS A 330     140.073 151.775 164.409  1.00 12.76           S  
ATOM   1928  N   LEU A 331     138.956 149.725 161.830  1.00 12.81           N  
ATOM   1929  CA  LEU A 331     139.067 150.235 160.459  1.00 12.81           C  
ATOM   1930  C   LEU A 331     137.863 149.906 159.567  1.00 12.81           C  
ATOM   1931  O   LEU A 331     137.499 150.716 158.710  1.00 12.81           O  
ATOM   1932  CB  LEU A 331     140.343 149.703 159.811  1.00 12.81           C  
ATOM   1933  CG  LEU A 331     141.677 150.166 160.397  1.00 12.81           C  
ATOM   1934  CD1 LEU A 331     142.841 149.442 159.721  1.00 12.81           C  
ATOM   1935  CD2 LEU A 331     141.858 151.677 160.300  1.00 12.81           C  
ATOM   1936  N   ASN A 332     137.249 148.734 159.714  1.00 13.41           N  
ATOM   1937  CA  ASN A 332     136.257 148.309 158.725  1.00 13.41           C  
ATOM   1938  C   ASN A 332     135.020 149.196 158.611  1.00 13.41           C  
ATOM   1939  O   ASN A 332     134.573 149.432 157.470  1.00 13.41           O  
ATOM   1940  CB  ASN A 332     135.828 146.862 159.005  1.00 13.41           C  
ATOM   1941  CG  ASN A 332     136.768 145.839 158.389  1.00 13.41           C  
ATOM   1942  OD1 ASN A 332     136.996 145.844 157.185  1.00 13.41           O  
ATOM   1943  ND2 ASN A 332     137.277 144.932 159.204  1.00 13.41           N  
ATOM   1944  N   PRO A 333     134.401 149.673 159.695  1.00 14.08           N  
ATOM   1945  CA  PRO A 333     133.208 150.515 159.532  1.00 14.08           C  
ATOM   1946  C   PRO A 333     133.431 151.731 158.654  1.00 14.08           C  
ATOM   1947  O   PRO A 333     132.461 152.264 158.106  1.00 14.08           O  
ATOM   1948  CB  PRO A 333     132.868 150.889 160.976  1.00 14.08           C  
ATOM   1949  CG  PRO A 333     133.240 149.660 161.706  1.00 14.08           C  
ATOM   1950  CD  PRO A 333     134.562 149.276 161.103  1.00 14.08           C  
ATOM   1951  N   VAL A 334     134.671 152.166 158.460  1.00 14.68           N  
ATOM   1952  CA  VAL A 334     134.904 153.365 157.669  1.00 14.68           C  
ATOM   1953  C   VAL A 334     134.904 152.979 156.197  1.00 14.68           C  
ATOM   1954  O   VAL A 334     134.404 153.716 155.331  1.00 14.68           O  
ATOM   1955  CB  VAL A 334     136.228 154.027 158.091  1.00 14.68           C  
ATOM   1956  CG1 VAL A 334     136.564 155.198 157.186  1.00 14.68           C  
ATOM   1957  CG2 VAL A 334     136.183 154.450 159.551  1.00 14.68           C  
ATOM   1958  N   LEU A 335     135.468 151.806 155.905  1.00 14.06           N  
ATOM   1959  CA  LEU A 335     135.478 151.291 154.546  1.00 14.06           C  
ATOM   1960  C   LEU A 335     134.061 150.974 154.082  1.00 14.06           C  
ATOM   1961  O   LEU A 335     133.713 151.242 152.933  1.00 14.06           O  
ATOM   1962  CB  LEU A 335     136.382 150.060 154.460  1.00 14.06           C  
ATOM   1963  N   TYR A 336     133.224 150.402 154.954  1.00 14.60           N  
ATOM   1964  CA  TYR A 336     131.844 150.141 154.541  1.00 14.60           C  
ATOM   1965  C   TYR A 336     131.171 151.415 154.067  1.00 14.60           C  
ATOM   1966  O   TYR A 336     130.372 151.390 153.128  1.00 14.60           O  
ATOM   1967  CB  TYR A 336     131.022 149.520 155.670  1.00 14.60           C  
ATOM   1968  CG  TYR A 336     131.526 148.199 156.149  1.00 14.60           C  
ATOM   1969  CD1 TYR A 336     132.311 147.399 155.332  1.00 14.60           C  
ATOM   1970  CD2 TYR A 336     131.223 147.747 157.413  1.00 14.60           C  
ATOM   1971  CE1 TYR A 336     132.780 146.194 155.763  1.00 14.60           C  
ATOM   1972  CE2 TYR A 336     131.690 146.539 157.857  1.00 14.60           C  
ATOM   1973  CZ  TYR A 336     132.471 145.766 157.026  1.00 14.60           C  
ATOM   1974  OH  TYR A 336     132.935 144.555 157.463  1.00 14.60           O  
ATOM   1975  N   ALA A 337     131.458 152.532 154.718  1.00 15.31           N  
ATOM   1976  CA  ALA A 337     130.739 153.759 154.422  1.00 15.31           C  
ATOM   1977  C   ALA A 337     131.280 154.395 153.151  1.00 15.31           C  
ATOM   1978  O   ALA A 337     130.511 154.838 152.293  1.00 15.31           O  
ATOM   1979  CB  ALA A 337     130.840 154.727 155.596  1.00 15.31           C  
ATOM   1980  N   PHE A 338     132.600 154.461 153.012  1.00 14.79           N  
ATOM   1981  CA  PHE A 338     133.152 154.972 151.763  1.00 14.79           C  
ATOM   1982  C   PHE A 338     132.778 154.102 150.558  1.00 14.79           C  
ATOM   1983  O   PHE A 338     132.514 154.629 149.472  1.00 14.79           O  
ATOM   1984  CB  PHE A 338     134.671 155.103 151.877  1.00 14.79           C  
ATOM   1985  N   LEU A 339     132.762 152.775 150.713  1.00 14.67           N  
ATOM   1986  CA  LEU A 339     132.642 151.868 149.571  1.00 14.67           C  
ATOM   1987  C   LEU A 339     131.247 151.311 149.294  1.00 14.67           C  
ATOM   1988  O   LEU A 339     131.080 150.615 148.290  1.00 14.67           O  
ATOM   1989  CB  LEU A 339     133.592 150.676 149.744  1.00 14.67           C  
ATOM   1990  CG  LEU A 339     135.085 150.957 149.637  1.00 14.67           C  
ATOM   1991  CD1 LEU A 339     135.871 149.788 150.189  1.00 14.67           C  
ATOM   1992  CD2 LEU A 339     135.481 151.234 148.201  1.00 14.67           C  
ATOM   1993  N   ASP A 340     130.251 151.557 150.133  1.00 17.52           N  
ATOM   1994  CA  ASP A 340     128.912 151.050 149.859  1.00 17.52           C  
ATOM   1995  C   ASP A 340     127.897 152.178 149.945  1.00 17.52           C  
ATOM   1996  O   ASP A 340     127.841 152.893 150.949  1.00 17.52           O  
ATOM   1997  CB  ASP A 340     128.546 149.916 150.821  1.00 17.52           C  
ATOM   1998  CG  ASP A 340     127.316 149.164 150.381  1.00 17.52           C  
ATOM   1999  OD1 ASP A 340     126.880 149.364 149.230  1.00 17.52           O  
ATOM   2000  OD2 ASP A 340     126.793 148.356 151.173  1.00 17.52           O  
ATOM   2001  N   GLU A 341     127.092 152.326 148.890  1.00 18.90           N  
ATOM   2002  CA  GLU A 341     126.102 153.394 148.858  1.00 18.90           C  
ATOM   2003  C   GLU A 341     125.036 153.189 149.921  1.00 18.90           C  
ATOM   2004  O   GLU A 341     124.609 154.147 150.574  1.00 18.90           O  
ATOM   2005  CB  GLU A 341     125.476 153.474 147.471  1.00 18.90           C  
ATOM   2006  N   ASN A 342     124.590 151.949 150.109  1.00 19.11           N  
ATOM   2007  CA  ASN A 342     123.530 151.684 151.071  1.00 19.11           C  
ATOM   2008  C   ASN A 342     123.993 151.974 152.494  1.00 19.11           C  
ATOM   2009  O   ASN A 342     123.269 152.606 153.275  1.00 19.11           O  
ATOM   2010  CB  ASN A 342     123.061 150.241 150.931  1.00 19.11           C  
ATOM   2011  CG  ASN A 342     122.259 150.016 149.666  1.00 19.11           C  
ATOM   2012  OD1 ASN A 342     122.342 150.799 148.719  1.00 19.11           O  
ATOM   2013  ND2 ASN A 342     121.477 148.945 149.643  1.00 19.11           N  
ATOM   2014  N   PHE A 343     125.197 151.516 152.856  1.00 16.47           N  
ATOM   2015  CA  PHE A 343     125.710 151.801 154.194  1.00 16.47           C  
ATOM   2016  C   PHE A 343     125.899 153.298 154.394  1.00 16.47           C  
ATOM   2017  O   PHE A 343     125.555 153.834 155.452  1.00 16.47           O  
ATOM   2018  CB  PHE A 343     127.023 151.055 154.449  1.00 16.47           C  
ATOM   2019  CG  PHE A 343     126.834 149.655 154.961  1.00 16.47           C  
ATOM   2020  CD1 PHE A 343     126.301 149.427 156.214  1.00 16.47           C  
ATOM   2021  CD2 PHE A 343     127.225 148.569 154.203  1.00 16.47           C  
ATOM   2022  CE1 PHE A 343     126.127 148.137 156.689  1.00 16.47           C  
ATOM   2023  CE2 PHE A 343     127.059 147.282 154.672  1.00 16.47           C  
ATOM   2024  CZ  PHE A 343     126.506 147.066 155.918  1.00 16.47           C  
ATOM   2025  N   LYS A 344     126.459 153.987 153.397  1.00 18.50           N  
ATOM   2026  CA  LYS A 344     126.683 155.423 153.524  1.00 18.50           C  
ATOM   2027  C   LYS A 344     125.361 156.140 153.763  1.00 18.50           C  
ATOM   2028  O   LYS A 344     125.248 157.006 154.643  1.00 18.50           O  
ATOM   2029  CB  LYS A 344     127.374 155.967 152.270  1.00 18.50           C  
ATOM   2030  N   ARG A 345     124.339 155.767 152.992  1.00 19.85           N  
ATOM   2031  CA  ARG A 345     123.036 156.403 153.119  1.00 19.85           C  
ATOM   2032  C   ARG A 345     122.458 156.153 154.505  1.00 19.85           C  
ATOM   2033  O   ARG A 345     121.966 157.079 155.158  1.00 19.85           O  
ATOM   2034  CB  ARG A 345     122.097 155.889 152.026  1.00 19.85           C  
ATOM   2035  N   CYS A 346     122.493 154.900 154.969  1.00 18.76           N  
ATOM   2036  CA  CYS A 346     121.903 154.602 156.273  1.00 18.76           C  
ATOM   2037  C   CYS A 346     122.651 155.333 157.380  1.00 18.76           C  
ATOM   2038  O   CYS A 346     122.035 155.794 158.343  1.00 18.76           O  
ATOM   2039  CB  CYS A 346     121.875 153.096 156.537  1.00 18.76           C  
ATOM   2040  SG  CYS A 346     121.015 152.137 155.293  1.00 18.76           S  
ATOM   2041  N   PHE A 347     123.982 155.433 157.282  1.00 16.87           N  
ATOM   2042  CA  PHE A 347     124.724 156.149 158.315  1.00 16.87           C  
ATOM   2043  C   PHE A 347     124.323 157.615 158.334  1.00 16.87           C  
ATOM   2044  O   PHE A 347     124.134 158.198 159.408  1.00 16.87           O  
ATOM   2045  CB  PHE A 347     126.239 156.025 158.114  1.00 16.87           C  
ATOM   2046  CG  PHE A 347     126.786 154.640 158.321  1.00 16.87           C  
ATOM   2047  CD1 PHE A 347     126.161 153.741 159.166  1.00 16.87           C  
ATOM   2048  CD2 PHE A 347     127.928 154.235 157.666  1.00 16.87           C  
ATOM   2049  CE1 PHE A 347     126.668 152.481 159.352  1.00 16.87           C  
ATOM   2050  CE2 PHE A 347     128.433 152.972 157.853  1.00 16.87           C  
ATOM   2051  CZ  PHE A 347     127.804 152.100 158.698  1.00 16.87           C  
ATOM   2052  N   ARG A 348     124.182 158.234 157.159  1.00 22.42           N  
ATOM   2053  CA  ARG A 348     123.797 159.642 157.152  1.00 22.42           C  
ATOM   2054  C   ARG A 348     122.405 159.816 157.747  1.00 22.42           C  
ATOM   2055  O   ARG A 348     122.182 160.706 158.574  1.00 22.42           O  
ATOM   2056  CB  ARG A 348     123.854 160.207 155.732  1.00 22.42           C  
ATOM   2057  N   GLU A 349     121.464 158.953 157.364  1.00 23.21           N  
ATOM   2058  CA  GLU A 349     120.111 159.048 157.902  1.00 23.21           C  
ATOM   2059  C   GLU A 349     120.085 158.802 159.405  1.00 23.21           C  
ATOM   2060  O   GLU A 349     119.270 159.399 160.117  1.00 23.21           O  
ATOM   2061  CB  GLU A 349     119.199 158.053 157.187  1.00 23.21           C  
ATOM   2062  N   PHE A 350     120.945 157.908 159.900  1.00 24.05           N  
ATOM   2063  CA  PHE A 350     121.039 157.656 161.333  1.00 24.05           C  
ATOM   2064  C   PHE A 350     121.557 158.879 162.068  1.00 24.05           C  
ATOM   2065  O   PHE A 350     121.013 159.274 163.105  1.00 24.05           O  
ATOM   2066  CB  PHE A 350     121.951 156.457 161.594  1.00 24.05           C  
ATOM   2067  N   CYS A 351     122.628 159.479 161.556  1.00 26.30           N  
ATOM   2068  CA  CYS A 351     123.211 160.616 162.248  1.00 26.30           C  
ATOM   2069  C   CYS A 351     122.242 161.786 162.247  1.00 26.30           C  
ATOM   2070  O   CYS A 351     122.068 162.459 163.270  1.00 26.30           O  
ATOM   2071  CB  CYS A 351     124.539 161.003 161.601  1.00 26.30           C  
ATOM   2072  N   ILE A 352     121.604 162.041 161.110  1.00 29.32           N  
ATOM   2073  CA  ILE A 352     120.665 163.148 160.982  1.00 29.32           C  
ATOM   2074  C   ILE A 352     119.237 162.616 160.938  1.00 29.32           C  
ATOM   2075  O   ILE A 352     118.937 161.562 161.499  1.00 29.32           O  
ATOM   2076  CB  ILE A 352     120.969 163.991 159.733  1.00 29.32           C  
TER    2077      ILE A 352                                                      
ATOM   2078  N   LEU D 405     133.571 152.715 104.797  1.00 61.71           N  
ATOM   2079  CA  LEU D 405     133.030 153.375 105.979  1.00 61.71           C  
ATOM   2080  C   LEU D 405     133.340 152.571 107.233  1.00 61.71           C  
ATOM   2081  O   LEU D 405     132.694 151.561 107.512  1.00 61.71           O  
ATOM   2082  CB  LEU D 405     131.517 153.566 105.841  1.00 61.71           C  
ATOM   2083  N   SER D 406     134.333 153.029 107.984  1.00 62.14           N  
ATOM   2084  CA  SER D 406     134.794 152.359 109.188  1.00 62.14           C  
ATOM   2085  C   SER D 406     134.405 153.167 110.417  1.00 62.14           C  
ATOM   2086  O   SER D 406     134.108 154.362 110.335  1.00 62.14           O  
ATOM   2087  CB  SER D 406     136.313 152.158 109.156  1.00 62.14           C  
ATOM   2088  N   CYS D 407     134.408 152.497 111.567  1.00 59.04           N  
ATOM   2089  CA  CYS D 407     134.065 153.112 112.844  1.00 59.04           C  
ATOM   2090  C   CYS D 407     135.190 152.798 113.827  1.00 59.04           C  
ATOM   2091  O   CYS D 407     135.043 151.960 114.716  1.00 59.04           O  
ATOM   2092  CB  CYS D 407     132.714 152.618 113.359  1.00 59.04           C  
ATOM   2093  N   ALA D 408     136.310 153.497 113.671  1.00 61.07           N  
ATOM   2094  CA  ALA D 408     137.469 153.240 114.508  1.00 61.07           C  
ATOM   2095  C   ALA D 408     137.244 153.784 115.913  1.00 61.07           C  
ATOM   2096  O   ALA D 408     136.438 154.690 116.142  1.00 61.07           O  
ATOM   2097  CB  ALA D 408     138.722 153.865 113.900  1.00 61.07           C  
ATOM   2098  N   ALA D 409     137.973 153.209 116.864  1.00 56.80           N  
ATOM   2099  CA  ALA D 409     137.864 153.567 118.269  1.00 56.80           C  
ATOM   2100  C   ALA D 409     139.245 153.868 118.823  1.00 56.80           C  
ATOM   2101  O   ALA D 409     140.226 153.210 118.465  1.00 56.80           O  
ATOM   2102  CB  ALA D 409     137.210 152.441 119.078  1.00 56.80           C  
ATOM   2103  N   SER D 410     139.316 154.866 119.698  1.00 59.16           N  
ATOM   2104  CA  SER D 410     140.561 155.241 120.353  1.00 59.16           C  
ATOM   2105  C   SER D 410     140.244 155.536 121.812  1.00 59.16           C  
ATOM   2106  O   SER D 410     139.123 155.319 122.280  1.00 59.16           O  
ATOM   2107  CB  SER D 410     141.211 156.435 119.642  1.00 59.16           C  
ATOM   2108  N   GLY D 411     141.236 156.037 122.541  1.00 54.13           N  
ATOM   2109  CA  GLY D 411     141.019 156.432 123.915  1.00 54.13           C  
ATOM   2110  C   GLY D 411     141.379 155.318 124.874  1.00 54.13           C  
ATOM   2111  O   GLY D 411     141.852 154.243 124.496  1.00 54.13           O  
ATOM   2112  N   THR D 412     141.142 155.583 126.154  1.00 45.90           N  
ATOM   2113  CA  THR D 412     141.493 154.646 127.214  1.00 45.90           C  
ATOM   2114  C   THR D 412     140.306 153.715 127.428  1.00 45.90           C  
ATOM   2115  O   THR D 412     139.299 154.109 128.024  1.00 45.90           O  
ATOM   2116  CB  THR D 412     141.849 155.387 128.500  1.00 45.90           C  
ATOM   2117  N   ILE D 413     140.428 152.478 126.952  1.00 32.78           N  
ATOM   2118  CA  ILE D 413     139.388 151.467 127.099  1.00 32.78           C  
ATOM   2119  C   ILE D 413     140.037 150.195 127.618  1.00 32.78           C  
ATOM   2120  O   ILE D 413     141.003 149.699 127.028  1.00 32.78           O  
ATOM   2121  CB  ILE D 413     138.658 151.197 125.769  1.00 32.78           C  
ATOM   2122  N   PHE D 414     139.503 149.667 128.717  1.00 21.34           N  
ATOM   2123  CA  PHE D 414     139.964 148.377 129.214  1.00 21.34           C  
ATOM   2124  C   PHE D 414     139.571 147.252 128.258  1.00 21.34           C  
ATOM   2125  O   PHE D 414     140.416 146.437 127.870  1.00 21.34           O  
ATOM   2126  CB  PHE D 414     139.418 148.171 130.628  1.00 21.34           C  
ATOM   2127  CG  PHE D 414     139.208 146.751 131.028  1.00 21.34           C  
ATOM   2128  CD1 PHE D 414     140.278 145.971 131.410  1.00 21.34           C  
ATOM   2129  CD2 PHE D 414     137.945 146.222 131.124  1.00 21.34           C  
ATOM   2130  CE1 PHE D 414     140.093 144.679 131.823  1.00 21.34           C  
ATOM   2131  CE2 PHE D 414     137.755 144.923 131.542  1.00 21.34           C  
ATOM   2132  CZ  PHE D 414     138.831 144.153 131.890  1.00 21.34           C  
ATOM   2133  N   ARG D 415     138.302 147.203 127.841  1.00 24.18           N  
ATOM   2134  CA  ARG D 415     137.855 146.192 126.889  1.00 24.18           C  
ATOM   2135  C   ARG D 415     136.761 146.768 126.004  1.00 24.18           C  
ATOM   2136  O   ARG D 415     135.901 147.511 126.475  1.00 24.18           O  
ATOM   2137  CB  ARG D 415     137.343 144.933 127.596  1.00 24.18           C  
ATOM   2138  N   LEU D 416     136.809 146.429 124.720  1.00 30.25           N  
ATOM   2139  CA  LEU D 416     135.810 146.839 123.742  1.00 30.25           C  
ATOM   2140  C   LEU D 416     134.940 145.621 123.428  1.00 30.25           C  
ATOM   2141  O   LEU D 416     135.475 144.549 123.137  1.00 30.25           O  
ATOM   2142  CB  LEU D 416     136.526 147.357 122.495  1.00 30.25           C  
ATOM   2143  CG  LEU D 416     135.779 147.937 121.307  1.00 30.25           C  
ATOM   2144  CD1 LEU D 416     135.041 149.185 121.744  1.00 30.25           C  
ATOM   2145  CD2 LEU D 416     136.739 148.236 120.174  1.00 30.25           C  
ATOM   2146  N   TYR D 417     133.612 145.770 123.471  1.00 29.33           N  
ATOM   2147  CA  TYR D 417     132.774 144.572 123.403  1.00 29.33           C  
ATOM   2148  C   TYR D 417     132.023 144.323 122.090  1.00 29.33           C  
ATOM   2149  O   TYR D 417     132.452 143.491 121.292  1.00 29.33           O  
ATOM   2150  CB  TYR D 417     131.760 144.628 124.547  1.00 29.33           C  
ATOM   2151  N   ASP D 418     130.910 145.014 121.852  1.00 32.38           N  
ATOM   2152  CA  ASP D 418     130.107 144.866 120.637  1.00 32.38           C  
ATOM   2153  C   ASP D 418     130.153 146.138 119.810  1.00 32.38           C  
ATOM   2154  O   ASP D 418     129.909 147.224 120.337  1.00 32.38           O  
ATOM   2155  CB  ASP D 418     128.642 144.537 120.939  1.00 32.38           C  
ATOM   2156  CG  ASP D 418     128.447 143.157 121.505  1.00 32.38           C  
ATOM   2157  OD1 ASP D 418     129.252 142.261 121.200  1.00 32.38           O  
ATOM   2158  OD2 ASP D 418     127.460 142.950 122.235  1.00 32.38           O  
ATOM   2159  N   MET D 419     130.486 146.021 118.535  1.00 38.80           N  
ATOM   2160  CA  MET D 419     130.538 147.194 117.680  1.00 38.80           C  
ATOM   2161  C   MET D 419     129.418 147.109 116.653  1.00 38.80           C  
ATOM   2162  O   MET D 419     128.932 146.023 116.337  1.00 38.80           O  
ATOM   2163  CB  MET D 419     131.902 147.319 117.006  1.00 38.80           C  
ATOM   2164  CG  MET D 419     132.992 147.725 117.978  1.00 38.80           C  
ATOM   2165  SD  MET D 419     134.591 147.949 117.207  1.00 38.80           S  
ATOM   2166  CE  MET D 419     134.216 149.330 116.142  1.00 38.80           C  
ATOM   2167  N   GLY D 420     128.990 148.260 116.136  1.00 45.57           N  
ATOM   2168  CA  GLY D 420     127.843 148.231 115.244  1.00 45.57           C  
ATOM   2169  C   GLY D 420     127.634 149.520 114.484  1.00 45.57           C  
ATOM   2170  O   GLY D 420     128.220 150.560 114.788  1.00 45.57           O  
ATOM   2171  N   TRP D 421     126.767 149.421 113.481  1.00 56.46           N  
ATOM   2172  CA  TRP D 421     126.315 150.538 112.659  1.00 56.46           C  
ATOM   2173  C   TRP D 421     124.821 150.739 112.824  1.00 56.46           C  
ATOM   2174  O   TRP D 421     124.046 149.790 112.674  1.00 56.46           O  
ATOM   2175  CB  TRP D 421     126.643 150.310 111.190  1.00 56.46           C  
ATOM   2176  CG  TRP D 421     128.085 150.149 110.925  1.00 56.46           C  
ATOM   2177  CD1 TRP D 421     128.794 148.990 110.862  1.00 56.46           C  
ATOM   2178  CD2 TRP D 421     128.995 151.197 110.617  1.00 56.46           C  
ATOM   2179  NE1 TRP D 421     130.106 149.257 110.571  1.00 56.46           N  
ATOM   2180  CE2 TRP D 421     130.255 150.609 110.412  1.00 56.46           C  
ATOM   2181  CE3 TRP D 421     128.871 152.584 110.512  1.00 56.46           C  
ATOM   2182  CZ2 TRP D 421     131.385 151.357 110.105  1.00 56.46           C  
ATOM   2183  CZ3 TRP D 421     129.989 153.326 110.208  1.00 56.46           C  
ATOM   2184  CH2 TRP D 421     131.232 152.712 110.004  1.00 56.46           C  
ATOM   2185  N   TYR D 422     124.418 151.970 113.141  1.00 52.88           N  
ATOM   2186  CA  TYR D 422     123.021 152.292 113.386  1.00 52.88           C  
ATOM   2187  C   TYR D 422     122.606 153.468 112.522  1.00 52.88           C  
ATOM   2188  O   TYR D 422     123.248 154.519 112.553  1.00 52.88           O  
ATOM   2189  CB  TYR D 422     122.809 152.620 114.856  1.00 52.88           C  
ATOM   2190  CG  TYR D 422     122.631 151.412 115.736  1.00 52.88           C  
ATOM   2191  CD1 TYR D 422     123.725 150.725 116.235  1.00 52.88           C  
ATOM   2192  CD2 TYR D 422     121.368 150.968 116.080  1.00 52.88           C  
ATOM   2193  CE1 TYR D 422     123.565 149.624 117.045  1.00 52.88           C  
ATOM   2194  CE2 TYR D 422     121.196 149.873 116.888  1.00 52.88           C  
ATOM   2195  CZ  TYR D 422     122.294 149.204 117.370  1.00 52.88           C  
ATOM   2196  OH  TYR D 422     122.113 148.108 118.177  1.00 52.88           O  
ATOM   2197  N   ARG D 423     121.512 153.309 111.789  1.00 58.69           N  
ATOM   2198  CA  ARG D 423     121.052 154.342 110.872  1.00 58.69           C  
ATOM   2199  C   ARG D 423     120.639 155.610 111.606  1.00 58.69           C  
ATOM   2200  O   ARG D 423     120.706 156.705 111.045  1.00 58.69           O  
ATOM   2201  CB  ARG D 423     119.881 153.824 110.033  1.00 58.69           C  
ATOM   2202  N   LEU D 432     120.515 149.924 112.948  1.00 58.68           N  
ATOM   2203  CA  LEU D 432     120.621 148.510 113.280  1.00 58.68           C  
ATOM   2204  C   LEU D 432     121.102 147.705 112.081  1.00 58.68           C  
ATOM   2205  O   LEU D 432     120.841 146.508 111.986  1.00 58.68           O  
ATOM   2206  CB  LEU D 432     119.274 147.973 113.767  1.00 58.68           C  
ATOM   2207  N   VAL D 433     121.803 148.374 111.163  1.00 55.59           N  
ATOM   2208  CA  VAL D 433     122.194 147.728 109.913  1.00 55.59           C  
ATOM   2209  C   VAL D 433     123.087 146.518 110.177  1.00 55.59           C  
ATOM   2210  O   VAL D 433     122.905 145.457 109.570  1.00 55.59           O  
ATOM   2211  CB  VAL D 433     122.882 148.746 108.987  1.00 55.59           C  
ATOM   2212  N   ALA D 434     124.058 146.648 111.079  1.00 52.53           N  
ATOM   2213  CA  ALA D 434     124.998 145.559 111.305  1.00 52.53           C  
ATOM   2214  C   ALA D 434     125.520 145.591 112.733  1.00 52.53           C  
ATOM   2215  O   ALA D 434     125.691 146.660 113.329  1.00 52.53           O  
ATOM   2216  CB  ALA D 434     126.174 145.632 110.326  1.00 52.53           C  
ATOM   2217  N   SER D 435     125.839 144.399 113.237  1.00 47.92           N  
ATOM   2218  CA  SER D 435     126.470 144.187 114.536  1.00 47.92           C  
ATOM   2219  C   SER D 435     127.600 143.176 114.392  1.00 47.92           C  
ATOM   2220  O   SER D 435     127.406 142.120 113.784  1.00 47.92           O  
ATOM   2221  CB  SER D 435     125.450 143.696 115.568  1.00 47.92           C  
ATOM   2222  N   ILE D 436     128.772 143.493 114.945  1.00 42.63           N  
ATOM   2223  CA  ILE D 436     129.908 142.572 115.001  1.00 42.63           C  
ATOM   2224  C   ILE D 436     130.313 142.389 116.459  1.00 42.63           C  
ATOM   2225  O   ILE D 436     130.680 143.360 117.139  1.00 42.63           O  
ATOM   2226  CB  ILE D 436     131.097 143.081 114.173  1.00 42.63           C  
ATOM   2227  N   THR D 437     130.247 141.145 116.935  1.00 41.80           N  
ATOM   2228  CA  THR D 437     130.716 140.802 118.269  1.00 41.80           C  
ATOM   2229  C   THR D 437     132.237 140.637 118.278  1.00 41.80           C  
ATOM   2230  O   THR D 437     132.878 140.457 117.240  1.00 41.80           O  
ATOM   2231  CB  THR D 437     130.023 139.517 118.742  1.00 41.80           C  
ATOM   2232  OG1 THR D 437     128.605 139.704 118.726  1.00 41.80           O  
ATOM   2233  CG2 THR D 437     130.423 139.140 120.152  1.00 41.80           C  
ATOM   2234  N   SER D 438     132.814 140.667 119.480  1.00 42.64           N  
ATOM   2235  CA  SER D 438     134.267 140.593 119.600  1.00 42.64           C  
ATOM   2236  C   SER D 438     134.799 139.287 119.031  1.00 42.64           C  
ATOM   2237  O   SER D 438     135.854 139.264 118.387  1.00 42.64           O  
ATOM   2238  CB  SER D 438     134.674 140.745 121.064  1.00 42.64           C  
ATOM   2239  N   GLY D 439     134.085 138.185 119.265  1.00 46.28           N  
ATOM   2240  CA  GLY D 439     134.474 136.918 118.673  1.00 46.28           C  
ATOM   2241  C   GLY D 439     134.446 136.946 117.159  1.00 46.28           C  
ATOM   2242  O   GLY D 439     135.267 136.299 116.505  1.00 46.28           O  
ATOM   2243  N   GLY D 440     133.514 137.700 116.586  1.00 45.04           N  
ATOM   2244  CA  GLY D 440     133.296 137.738 115.153  1.00 45.04           C  
ATOM   2245  C   GLY D 440     131.912 137.302 114.728  1.00 45.04           C  
ATOM   2246  O   GLY D 440     131.635 137.279 113.521  1.00 45.04           O  
ATOM   2247  N   SER D 441     131.029 136.951 115.657  1.00 46.46           N  
ATOM   2248  CA  SER D 441     129.640 136.693 115.311  1.00 46.46           C  
ATOM   2249  C   SER D 441     129.026 137.963 114.743  1.00 46.46           C  
ATOM   2250  O   SER D 441     129.234 139.058 115.272  1.00 46.46           O  
ATOM   2251  CB  SER D 441     128.859 136.226 116.539  1.00 46.46           C  
ATOM   2252  N   THR D 442     128.267 137.828 113.662  1.00 49.73           N  
ATOM   2253  CA  THR D 442     127.758 138.996 112.964  1.00 49.73           C  
ATOM   2254  C   THR D 442     126.258 138.890 112.742  1.00 49.73           C  
ATOM   2255  O   THR D 442     125.725 137.806 112.485  1.00 49.73           O  
ATOM   2256  CB  THR D 442     128.453 139.169 111.608  1.00 49.73           C  
ATOM   2257  N   LYS D 443     125.593 140.036 112.857  1.00 51.30           N  
ATOM   2258  CA  LYS D 443     124.167 140.162 112.594  1.00 51.30           C  
ATOM   2259  C   LYS D 443     123.968 141.238 111.536  1.00 51.30           C  
ATOM   2260  O   LYS D 443     124.588 142.302 111.611  1.00 51.30           O  
ATOM   2261  CB  LYS D 443     123.397 140.509 113.867  1.00 51.30           C  
ATOM   2262  N   THR D 453     127.966 142.061 107.282  1.00 56.30           N  
ATOM   2263  CA  THR D 453     129.131 142.295 106.435  1.00 56.30           C  
ATOM   2264  C   THR D 453     130.126 143.218 107.125  1.00 56.30           C  
ATOM   2265  O   THR D 453     130.715 144.090 106.494  1.00 56.30           O  
ATOM   2266  CB  THR D 453     128.734 142.913 105.084  1.00 56.30           C  
ATOM   2267  N   ILE D 454     130.307 143.016 108.426  1.00 57.07           N  
ATOM   2268  CA  ILE D 454     131.172 143.844 109.253  1.00 57.07           C  
ATOM   2269  C   ILE D 454     132.377 143.018 109.674  1.00 57.07           C  
ATOM   2270  O   ILE D 454     132.225 141.912 110.205  1.00 57.07           O  
ATOM   2271  CB  ILE D 454     130.420 144.377 110.483  1.00 57.07           C  
ATOM   2272  N   SER D 455     133.572 143.562 109.455  1.00 58.35           N  
ATOM   2273  CA  SER D 455     134.823 142.925 109.844  1.00 58.35           C  
ATOM   2274  C   SER D 455     135.519 143.793 110.883  1.00 58.35           C  
ATOM   2275  O   SER D 455     135.774 144.975 110.635  1.00 58.35           O  
ATOM   2276  CB  SER D 455     135.728 142.712 108.629  1.00 58.35           C  
ATOM   2277  N   ARG D 456     135.851 143.203 112.027  1.00 56.41           N  
ATOM   2278  CA  ARG D 456     136.458 143.920 113.141  1.00 56.41           C  
ATOM   2279  C   ARG D 456     137.824 143.332 113.454  1.00 56.41           C  
ATOM   2280  O   ARG D 456     137.968 142.110 113.564  1.00 56.41           O  
ATOM   2281  CB  ARG D 456     135.571 143.849 114.386  1.00 56.41           C  
ATOM   2282  N   ASP D 457     138.825 144.202 113.594  1.00 56.03           N  
ATOM   2283  CA  ASP D 457     140.167 143.798 113.997  1.00 56.03           C  
ATOM   2284  C   ASP D 457     140.430 144.298 115.409  1.00 56.03           C  
ATOM   2285  O   ASP D 457     140.380 145.506 115.662  1.00 56.03           O  
ATOM   2286  CB  ASP D 457     141.220 144.343 113.033  1.00 56.03           C  
ATOM   2287  N   ASN D 458     140.711 143.374 116.320  1.00 55.63           N  
ATOM   2288  CA  ASN D 458     140.982 143.722 117.709  1.00 55.63           C  
ATOM   2289  C   ASN D 458     142.232 144.589 117.812  1.00 55.63           C  
ATOM   2290  O   ASN D 458     142.167 145.741 118.240  1.00 55.63           O  
ATOM   2291  CB  ASN D 458     141.144 142.460 118.556  1.00 55.63           C  
ATOM   2292  N   ASN D 461     141.726 147.699 116.198  1.00 55.11           N  
ATOM   2293  CA  ASN D 461     140.816 148.343 117.139  1.00 55.11           C  
ATOM   2294  C   ASN D 461     139.669 149.031 116.412  1.00 55.11           C  
ATOM   2295  O   ASN D 461     139.041 149.938 116.959  1.00 55.11           O  
ATOM   2296  CB  ASN D 461     141.565 149.359 117.999  1.00 55.11           C  
ATOM   2297  N   THR D 462     139.406 148.607 115.177  1.00 56.13           N  
ATOM   2298  CA  THR D 462     138.390 149.233 114.346  1.00 56.13           C  
ATOM   2299  C   THR D 462     137.538 148.174 113.656  1.00 56.13           C  
ATOM   2300  O   THR D 462     137.968 147.035 113.441  1.00 56.13           O  
ATOM   2301  CB  THR D 462     139.023 150.150 113.293  1.00 56.13           C  
ATOM   2302  N   VAL D 463     136.315 148.573 113.303  1.00 54.35           N  
ATOM   2303  CA  VAL D 463     135.418 147.761 112.494  1.00 54.35           C  
ATOM   2304  C   VAL D 463     135.188 148.483 111.174  1.00 54.35           C  
ATOM   2305  O   VAL D 463     135.109 149.715 111.135  1.00 54.35           O  
ATOM   2306  CB  VAL D 463     134.076 147.505 113.208  1.00 54.35           C  
ATOM   2307  N   TYR D 464     135.076 147.711 110.096  1.00 58.73           N  
ATOM   2308  CA  TYR D 464     134.756 148.205 108.764  1.00 58.73           C  
ATOM   2309  C   TYR D 464     133.537 147.455 108.236  1.00 58.73           C  
ATOM   2310  O   TYR D 464     133.501 146.220 108.281  1.00 58.73           O  
ATOM   2311  CB  TYR D 464     135.946 148.031 107.816  1.00 58.73           C  
ATOM   2312  N   LEU D 465     132.546 148.191 107.737  1.00 58.45           N  
ATOM   2313  CA  LEU D 465     131.309 147.573 107.250  1.00 58.45           C  
ATOM   2314  C   LEU D 465     131.323 147.425 105.733  1.00 58.45           C  
ATOM   2315  O   LEU D 465     131.892 148.254 105.024  1.00 58.45           O  
ATOM   2316  CB  LEU D 465     130.088 148.394 107.671  1.00 58.45           C  
ATOM   2317  N   ALA D 476     120.733 158.164 103.907  1.00 67.34           N  
ATOM   2318  CA  ALA D 476     120.558 158.453 105.323  1.00 67.34           C  
ATOM   2319  C   ALA D 476     121.880 158.338 106.062  1.00 67.34           C  
ATOM   2320  O   ALA D 476     122.662 157.422 105.814  1.00 67.34           O  
ATOM   2321  CB  ALA D 476     119.534 157.512 105.934  1.00 67.34           C  
ATOM   2322  N   VAL D 477     122.134 159.284 106.965  1.00 66.09           N  
ATOM   2323  CA  VAL D 477     123.371 159.262 107.732  1.00 66.09           C  
ATOM   2324  C   VAL D 477     123.379 158.033 108.628  1.00 66.09           C  
ATOM   2325  O   VAL D 477     122.341 157.631 109.174  1.00 66.09           O  
ATOM   2326  CB  VAL D 477     123.518 160.554 108.554  1.00 66.09           C  
ATOM   2327  N   TYR D 478     124.552 157.427 108.784  1.00 61.63           N  
ATOM   2328  CA  TYR D 478     124.730 156.270 109.646  1.00 61.63           C  
ATOM   2329  C   TYR D 478     125.756 156.594 110.717  1.00 61.63           C  
ATOM   2330  O   TYR D 478     126.679 157.381 110.492  1.00 61.63           O  
ATOM   2331  CB  TYR D 478     125.167 155.041 108.841  1.00 61.63           C  
ATOM   2332  CG  TYR D 478     124.215 154.666 107.728  1.00 61.63           C  
ATOM   2333  CD1 TYR D 478     123.047 153.971 108.005  1.00 61.63           C  
ATOM   2334  CD2 TYR D 478     124.484 154.987 106.409  1.00 61.63           C  
ATOM   2335  CE1 TYR D 478     122.171 153.606 107.006  1.00 61.63           C  
ATOM   2336  CE2 TYR D 478     123.612 154.632 105.399  1.00 61.63           C  
ATOM   2337  CZ  TYR D 478     122.454 153.941 105.707  1.00 61.63           C  
ATOM   2338  OH  TYR D 478     121.574 153.583 104.716  1.00 61.63           O  
ATOM   2339  N   TYR D 479     125.592 155.979 111.886  1.00 57.84           N  
ATOM   2340  CA  TYR D 479     126.417 156.297 113.041  1.00 57.84           C  
ATOM   2341  C   TYR D 479     127.065 155.064 113.655  1.00 57.84           C  
ATOM   2342  O   TYR D 479     126.424 154.021 113.824  1.00 57.84           O  
ATOM   2343  CB  TYR D 479     125.606 157.018 114.119  1.00 57.84           C  
ATOM   2344  CG  TYR D 479     125.077 158.369 113.709  1.00 57.84           C  
ATOM   2345  CD1 TYR D 479     125.941 159.421 113.448  1.00 57.84           C  
ATOM   2346  CD2 TYR D 479     123.711 158.599 113.601  1.00 57.84           C  
ATOM   2347  CE1 TYR D 479     125.463 160.662 113.076  1.00 57.84           C  
ATOM   2348  CE2 TYR D 479     123.222 159.835 113.235  1.00 57.84           C  
ATOM   2349  CZ  TYR D 479     124.102 160.865 112.977  1.00 57.84           C  
ATOM   2350  OH  TYR D 479     123.618 162.099 112.611  1.00 57.84           O  
ATOM   2351  N   CYS D 480     128.362 155.199 113.917  1.00 51.65           N  
ATOM   2352  CA  CYS D 480     129.153 154.239 114.674  1.00 51.65           C  
ATOM   2353  C   CYS D 480     128.631 154.089 116.098  1.00 51.65           C  
ATOM   2354  O   CYS D 480     128.309 155.081 116.754  1.00 51.65           O  
ATOM   2355  CB  CYS D 480     130.616 154.678 114.699  1.00 51.65           C  
ATOM   2356  N   ASN D 481     128.510 152.852 116.567  1.00 41.54           N  
ATOM   2357  CA  ASN D 481     128.188 152.576 117.960  1.00 41.54           C  
ATOM   2358  C   ASN D 481     129.198 151.568 118.486  1.00 41.54           C  
ATOM   2359  O   ASN D 481     129.575 150.637 117.770  1.00 41.54           O  
ATOM   2360  CB  ASN D 481     126.776 152.024 118.129  1.00 41.54           C  
ATOM   2361  CG  ASN D 481     126.383 151.885 119.582  1.00 41.54           C  
ATOM   2362  OD1 ASN D 481     126.587 152.796 120.377  1.00 41.54           O  
ATOM   2363  ND2 ASN D 481     125.817 150.746 119.937  1.00 41.54           N  
ATOM   2364  N   ALA D 482     129.656 151.761 119.726  1.00 33.37           N  
ATOM   2365  CA  ALA D 482     130.543 150.770 120.326  1.00 33.37           C  
ATOM   2366  C   ALA D 482     130.327 150.668 121.829  1.00 33.37           C  
ATOM   2367  O   ALA D 482     130.199 151.678 122.515  1.00 33.37           O  
ATOM   2368  CB  ALA D 482     132.004 151.107 120.038  1.00 33.37           C  
ATOM   2369  N   GLU D 483     130.366 149.444 122.339  1.00 26.47           N  
ATOM   2370  CA  GLU D 483     130.241 149.142 123.758  1.00 26.47           C  
ATOM   2371  C   GLU D 483     131.616 148.948 124.383  1.00 26.47           C  
ATOM   2372  O   GLU D 483     132.544 148.464 123.733  1.00 26.47           O  
ATOM   2373  CB  GLU D 483     129.436 147.865 123.951  1.00 26.47           C  
ATOM   2374  CG  GLU D 483     128.105 147.879 123.290  1.00 26.47           C  
ATOM   2375  CD  GLU D 483     127.306 146.641 123.594  1.00 26.47           C  
ATOM   2376  OE1 GLU D 483     127.727 145.864 124.465  1.00 26.47           O  
ATOM   2377  OE2 GLU D 483     126.254 146.442 122.959  1.00 26.47           O  
ATOM   2378  N   TYR D 484     131.754 149.345 125.646  1.00 23.73           N  
ATOM   2379  CA  TYR D 484     133.074 149.301 126.263  1.00 23.73           C  
ATOM   2380  C   TYR D 484     132.960 149.292 127.782  1.00 23.73           C  
ATOM   2381  O   TYR D 484     131.903 149.568 128.353  1.00 23.73           O  
ATOM   2382  CB  TYR D 484     133.958 150.466 125.813  1.00 23.73           C  
ATOM   2383  CG  TYR D 484     133.451 151.829 126.207  1.00 23.73           C  
ATOM   2384  CD1 TYR D 484     132.578 152.527 125.400  1.00 23.73           C  
ATOM   2385  CD2 TYR D 484     133.860 152.420 127.392  1.00 23.73           C  
ATOM   2386  CE1 TYR D 484     132.128 153.763 125.757  1.00 23.73           C  
ATOM   2387  CE2 TYR D 484     133.414 153.648 127.754  1.00 23.73           C  
ATOM   2388  CZ  TYR D 484     132.545 154.322 126.931  1.00 23.73           C  
ATOM   2389  OH  TYR D 484     132.085 155.567 127.290  1.00 23.73           O  
ATOM   2390  N   ARG D 485     134.081 148.939 128.416  1.00 18.71           N  
ATOM   2391  CA  ARG D 485     134.289 148.996 129.861  1.00 18.71           C  
ATOM   2392  C   ARG D 485     135.633 149.658 130.118  1.00 18.71           C  
ATOM   2393  O   ARG D 485     136.648 149.234 129.562  1.00 18.71           O  
ATOM   2394  CB  ARG D 485     134.249 147.599 130.497  1.00 18.71           C  
ATOM   2395  CG  ARG D 485     133.844 147.599 131.962  1.00 18.71           C  
ATOM   2396  CD  ARG D 485     133.549 146.225 132.543  1.00 18.71           C  
ATOM   2397  NE  ARG D 485     132.173 145.782 132.359  1.00 18.71           N  
ATOM   2398  CZ  ARG D 485     131.779 144.769 131.600  1.00 18.71           C  
ATOM   2399  NH1 ARG D 485     132.637 144.039 130.908  1.00 18.71           N  
ATOM   2400  NH2 ARG D 485     130.490 144.455 131.562  1.00 18.71           N  
ATOM   2401  N   THR D 486     135.628 150.725 130.921  1.00 20.61           N  
ATOM   2402  CA  THR D 486     136.864 151.425 131.271  1.00 20.61           C  
ATOM   2403  C   THR D 486     137.750 150.617 132.218  1.00 20.61           C  
ATOM   2404  O   THR D 486     138.979 150.719 132.147  1.00 20.61           O  
ATOM   2405  CB  THR D 486     136.532 152.781 131.890  1.00 20.61           C  
ATOM   2406  N   GLY D 487     137.161 149.854 133.145  1.00 18.73           N  
ATOM   2407  CA  GLY D 487     137.944 149.080 134.092  1.00 18.73           C  
ATOM   2408  C   GLY D 487     137.283 147.767 134.449  1.00 18.73           C  
ATOM   2409  O   GLY D 487     136.116 147.534 134.146  1.00 18.73           O  
ATOM   2410  N   ILE D 488     138.045 146.910 135.133  1.00 16.72           N  
ATOM   2411  CA  ILE D 488     137.557 145.565 135.447  1.00 16.72           C  
ATOM   2412  C   ILE D 488     136.311 145.642 136.314  1.00 16.72           C  
ATOM   2413  O   ILE D 488     135.402 144.817 136.193  1.00 16.72           O  
ATOM   2414  CB  ILE D 488     138.661 144.736 136.124  1.00 16.72           C  
ATOM   2415  N   TRP D 489     136.275 146.587 137.241  1.00 14.07           N  
ATOM   2416  CA  TRP D 489     135.172 146.728 138.177  1.00 14.07           C  
ATOM   2417  C   TRP D 489     134.142 147.746 137.719  1.00 14.07           C  
ATOM   2418  O   TRP D 489     133.165 147.974 138.431  1.00 14.07           O  
ATOM   2419  CB  TRP D 489     135.699 147.125 139.559  1.00 14.07           C  
ATOM   2420  CG  TRP D 489     136.885 146.349 140.030  1.00 14.07           C  
ATOM   2421  CD1 TRP D 489     138.181 146.754 140.039  1.00 14.07           C  
ATOM   2422  CD2 TRP D 489     136.870 145.041 140.607  1.00 14.07           C  
ATOM   2423  NE1 TRP D 489     138.981 145.772 140.569  1.00 14.07           N  
ATOM   2424  CE2 TRP D 489     138.195 144.709 140.927  1.00 14.07           C  
ATOM   2425  CE3 TRP D 489     135.861 144.113 140.875  1.00 14.07           C  
ATOM   2426  CZ2 TRP D 489     138.538 143.491 141.499  1.00 14.07           C  
ATOM   2427  CZ3 TRP D 489     136.201 142.910 141.435  1.00 14.07           C  
ATOM   2428  CH2 TRP D 489     137.527 142.607 141.747  1.00 14.07           C  
ATOM   2429  N   GLU D 490     134.324 148.350 136.547  1.00 17.23           N  
ATOM   2430  CA  GLU D 490     133.426 149.394 136.074  1.00 17.23           C  
ATOM   2431  C   GLU D 490     132.203 148.782 135.383  1.00 17.23           C  
ATOM   2432  O   GLU D 490     132.001 147.566 135.370  1.00 17.23           O  
ATOM   2433  CB  GLU D 490     134.191 150.346 135.161  1.00 17.23           C  
ATOM   2434  N   GLU D 491     131.366 149.636 134.803  1.00 19.63           N  
ATOM   2435  CA  GLU D 491     130.063 149.262 134.270  1.00 19.63           C  
ATOM   2436  C   GLU D 491     130.051 149.439 132.753  1.00 19.63           C  
ATOM   2437  O   GLU D 491     130.768 150.279 132.205  1.00 19.63           O  
ATOM   2438  CB  GLU D 491     128.943 150.044 134.965  1.00 19.63           C  
ATOM   2439  CG  GLU D 491     128.982 151.531 134.825  1.00 19.63           C  
ATOM   2440  CD  GLU D 491     128.310 152.029 133.582  1.00 19.63           C  
ATOM   2441  OE1 GLU D 491     127.566 151.267 132.940  1.00 19.63           O  
ATOM   2442  OE2 GLU D 491     128.511 153.209 133.261  1.00 19.63           O  
ATOM   2443  N   LEU D 492     129.244 148.621 132.079  1.00 20.00           N  
ATOM   2444  CA  LEU D 492     129.170 148.644 130.622  1.00 20.00           C  
ATOM   2445  C   LEU D 492     128.573 149.941 130.096  1.00 20.00           C  
ATOM   2446  O   LEU D 492     127.466 150.328 130.473  1.00 20.00           O  
ATOM   2447  CB  LEU D 492     128.316 147.476 130.129  1.00 20.00           C  
ATOM   2448  CG  LEU D 492     128.400 147.024 128.658  1.00 20.00           C  
ATOM   2449  CD1 LEU D 492     129.808 146.744 128.196  1.00 20.00           C  
ATOM   2450  CD2 LEU D 492     127.528 145.826 128.448  1.00 20.00           C  
ATOM   2451  N   LEU D 493     129.295 150.580 129.179  1.00 23.00           N  
ATOM   2452  CA  LEU D 493     128.908 151.839 128.560  1.00 23.00           C  
ATOM   2453  C   LEU D 493     128.835 151.686 127.050  1.00 23.00           C  
ATOM   2454  O   LEU D 493     129.292 150.697 126.480  1.00 23.00           O  
ATOM   2455  CB  LEU D 493     129.903 152.955 128.891  1.00 23.00           C  
ATOM   2456  CG  LEU D 493     130.047 153.415 130.328  1.00 23.00           C  
ATOM   2457  CD1 LEU D 493     131.283 154.253 130.469  1.00 23.00           C  
ATOM   2458  CD2 LEU D 493     128.813 154.219 130.677  1.00 23.00           C  
ATOM   2459  N   ASP D 494     128.310 152.726 126.408  1.00 26.82           N  
ATOM   2460  CA  ASP D 494     128.194 152.801 124.961  1.00 26.82           C  
ATOM   2461  C   ASP D 494     128.626 154.182 124.499  1.00 26.82           C  
ATOM   2462  O   ASP D 494     128.358 155.183 125.165  1.00 26.82           O  
ATOM   2463  CB  ASP D 494     126.759 152.532 124.506  1.00 26.82           C  
ATOM   2464  N   GLY D 495     129.309 154.221 123.363  1.00 36.23           N  
ATOM   2465  CA  GLY D 495     129.759 155.453 122.753  1.00 36.23           C  
ATOM   2466  C   GLY D 495     129.353 155.569 121.300  1.00 36.23           C  
ATOM   2467  O   GLY D 495     129.657 154.677 120.493  1.00 36.23           O  
ATOM   2468  N   TRP D 496     128.606 156.627 120.978  1.00 47.23           N  
ATOM   2469  CA  TRP D 496     128.185 156.907 119.618  1.00 47.23           C  
ATOM   2470  C   TRP D 496     129.226 157.768 118.911  1.00 47.23           C  
ATOM   2471  O   TRP D 496     130.263 158.127 119.468  1.00 47.23           O  
ATOM   2472  CB  TRP D 496     126.825 157.600 119.604  1.00 47.23           C  
ATOM   2473  CG  TRP D 496     125.728 156.751 120.106  1.00 47.23           C  
ATOM   2474  CD1 TRP D 496     125.299 156.647 121.388  1.00 47.23           C  
ATOM   2475  CD2 TRP D 496     124.909 155.869 119.334  1.00 47.23           C  
ATOM   2476  NE1 TRP D 496     124.262 155.755 121.468  1.00 47.23           N  
ATOM   2477  CE2 TRP D 496     124.003 155.265 120.216  1.00 47.23           C  
ATOM   2478  CE3 TRP D 496     124.856 155.532 117.979  1.00 47.23           C  
ATOM   2479  CZ2 TRP D 496     123.057 154.341 119.790  1.00 47.23           C  
ATOM   2480  CZ3 TRP D 496     123.919 154.622 117.559  1.00 47.23           C  
ATOM   2481  CH2 TRP D 496     123.033 154.035 118.458  1.00 47.23           C  
ATOM   2482  N   GLY D 497     128.931 158.113 117.657  1.00 57.46           N  
ATOM   2483  CA  GLY D 497     129.849 158.865 116.834  1.00 57.46           C  
ATOM   2484  C   GLY D 497     129.150 160.044 116.182  1.00 57.46           C  
ATOM   2485  O   GLY D 497     127.927 160.192 116.257  1.00 57.46           O  
ATOM   2486  N   GLN D 498     129.951 160.875 115.528  1.00 66.71           N  
ATOM   2487  CA  GLN D 498     129.433 162.051 114.847  1.00 66.71           C  
ATOM   2488  C   GLN D 498     128.669 161.640 113.593  1.00 66.71           C  
ATOM   2489  O   GLN D 498     128.982 160.628 112.967  1.00 66.71           O  
ATOM   2490  CB  GLN D 498     130.569 163.009 114.484  1.00 66.71           C  
TER    2491      GLN D 498                                                      
HETATM 2492  N1  NG0 A 900     148.234 138.484 172.544  1.00 12.12           N  
HETATM 2493  C4  NG0 A 900     149.611 135.669 166.631  1.00 12.12           C  
HETATM 2494  C5  NG0 A 900     149.543 136.555 167.615  1.00 12.12           C  
HETATM 2495  C6  NG0 A 900     149.569 136.098 169.080  1.00 12.12           C  
HETATM 2496  C7  NG0 A 900     149.522 137.157 170.227  1.00 12.12           C  
HETATM 2497  C8  NG0 A 900     149.290 136.483 171.576  1.00 12.12           C  
HETATM 2498  C10 NG0 A 900     148.377 139.160 171.254  1.00 12.12           C  
HETATM 2499  C13 NG0 A 900     147.071 137.616 169.788  1.00 12.12           C  
HETATM 2500  C15 NG0 A 900     147.471 139.144 174.800  1.00 12.12           C  
HETATM 2501  C17 NG0 A 900     146.643 140.481 176.853  1.00 12.12           C  
HETATM 2502  C20 NG0 A 900     146.423 140.648 179.670  1.00 12.12           C  
HETATM 2503  C21 NG0 A 900     147.390 141.566 178.932  1.00 12.12           C  
HETATM 2504  C22 NG0 A 900     147.491 141.483 177.616  1.00 12.12           C  
HETATM 2505  C24 NG0 A 900     149.127 136.507 177.169  1.00 12.12           C  
HETATM 2506  C1  NG0 A 900     149.674 134.803 169.356  1.00 12.12           C  
HETATM 2507  C11 NG0 A 900     148.450 138.216 170.012  1.00 12.12           C  
HETATM 2508  C12 NG0 A 900     150.906 137.835 170.207  1.00 12.12           C  
HETATM 2509  C14 NG0 A 900     148.348 139.518 173.585  1.00 12.12           C  
HETATM 2510  C16 NG0 A 900     146.762 140.405 175.300  1.00 12.12           C  
HETATM 2511  C18 NG0 A 900     145.798 139.700 177.493  1.00 12.12           C  
HETATM 2512  C19 NG0 A 900     145.688 139.784 179.010  1.00 12.12           C  
HETATM 2513  C2  NG0 A 900     149.748 133.780 168.223  1.00 12.12           C  
HETATM 2514  C23 NG0 A 900     148.380 138.510 175.841  1.00 12.12           C  
HETATM 2515  C25 NG0 A 900     149.002 134.993 177.062  1.00 12.12           C  
HETATM 2516  C3  NG0 A 900     149.720 134.177 166.967  1.00 12.12           C  
HETATM 2517  C9  NG0 A 900     149.245 137.480 172.758  1.00 12.12           C  
HETATM 2518  N2  NG0 A 900     148.235 137.109 176.178  1.00 12.12           N  
HETATM 2519  O1  NG0 A 900     149.850 132.423 168.533  1.00 12.12           O  
HETATM 2520  O2  NG0 A 900     149.239 139.133 176.348  1.00 12.12           O  
HETATM 2521  O3  NG0 A 900     147.880 134.429 177.186  1.00 12.12           O  
HETATM 2522  O4  NG0 A 900     150.034 134.303 176.856  1.00 12.12           O  
HETATM 2523  O   HOH A1001     143.170 138.034 168.522  1.00  9.97           O  
HETATM 2524  O   HOH A1002     152.370 132.769 164.237  1.00 10.35           O  
HETATM 2525  O   HOH A1003     148.185 133.864 174.407  1.00 11.23           O  
HETATM 2526  O   HOH A1004     141.147 140.142 170.767  1.00  9.46           O  
CONECT  535 1093                                                                
CONECT 1093  535                                                                
CONECT 2492 2498 2509 2517                                                      
CONECT 2493 2494 2516                                                           
CONECT 2494 2493 2495                                                           
CONECT 2495 2494 2496 2506                                                      
CONECT 2496 2495 2497 2507 2508                                                 
CONECT 2497 2496 2517                                                           
CONECT 2498 2492 2507                                                           
CONECT 2499 2507                                                                
CONECT 2500 2509 2510 2514                                                      
CONECT 2501 2504 2510 2511                                                      
CONECT 2502 2503 2512                                                           
CONECT 2503 2502 2504                                                           
CONECT 2504 2501 2503                                                           
CONECT 2505 2515 2518                                                           
CONECT 2506 2495 2513                                                           
CONECT 2507 2496 2498 2499                                                      
CONECT 2508 2496                                                                
CONECT 2509 2492 2500                                                           
CONECT 2510 2500 2501                                                           
CONECT 2511 2501 2512                                                           
CONECT 2512 2502 2511                                                           
CONECT 2513 2506 2516 2519                                                      
CONECT 2514 2500 2518 2520                                                      
CONECT 2515 2505 2521 2522                                                      
CONECT 2516 2493 2513                                                           
CONECT 2517 2492 2497                                                           
CONECT 2518 2505 2514                                                           
CONECT 2519 2513                                                                
CONECT 2520 2514                                                                
CONECT 2521 2515                                                                
CONECT 2522 2515                                                                
MASTER      817    0    1   11   10    0    0    6 2524    2   33   73          
END