HEADER    PROTEIN TRANSPORT                       22-JUL-14   4UTQ              
TITLE     A STRUCTURAL MODEL OF THE ACTIVE RIBOSOME-BOUND MEMBRANE PROTEIN      
TITLE    2 INSERTASE YIDC                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MEMBRANE PROTEIN INSERTASE YIDC;                           
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: FOLDASE YIDC, INNER MEMBRANE PROTEIN YIDC, MEMBRANE         
COMPND   5 INTEGRASE YIDC, OXA1EC;                                              
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: ATP SYNTHASE SUBUNIT C;                                    
COMPND   8 CHAIN: Z;                                                            
COMPND   9 FRAGMENT: MEMBRANE DOMAIN;                                           
COMPND  10 SYNONYM: ATP SYNTHASE F(0) SECTOR SUBUNIT C,                         
COMPND  11 DICYCLOHEXYLCARBODIIMIDE-BINDING PROTEIN, F-TYPE ATPASE SUBUNIT C, F-
COMPND  12 ATPASE SUBUNIT C, LIPID-BINDING PROTEIN                              
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   3 ORGANISM_TAXID: 562;                                                 
SOURCE   4 MOL_ID: 2;                                                           
SOURCE   5 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI;                               
SOURCE   6 ORGANISM_TAXID: 562                                                  
KEYWDS    PROTEIN TRANSPORT, PROTEIN TRANSLOCATION, BIOINFORMATICS, MD          
KEYWDS   2 SIMULATION, MEMBRANE                                                 
EXPDTA    ELECTRON MICROSCOPY                                                   
AUTHOR    S.WICKLES,A.SINGHAROY,J.ANDREANI,S.SEEMAYER,L.BISCHOFF,               
AUTHOR   2 O.BERNINGHAUSEN,J.SOEDING,K.SCHULTEN,E.O.VANDERSLUIS,R.BECKMANN      
REVDAT   3   03-OCT-18 4UTQ    1       REMARK                                   
REVDAT   2   20-AUG-14 4UTQ    1       JRNL                                     
REVDAT   1   30-JUL-14 4UTQ    0                                                
JRNL        AUTH   S.WICKLES,A.SINGHAROY,J.ANDREANI,S.SEEMAYER,L.BISCHOFF,      
JRNL        AUTH 2 O.BERNINGHAUSEN,J.SOEDING,K.SCHULTEN,E.O.VAN DER SLUIS,      
JRNL        AUTH 3 R.BECKMANN                                                   
JRNL        TITL   A STRUCTURAL MODEL OF THE ACTIVE RIBOSOME-BOUND MEMBRANE     
JRNL        TITL 2 PROTEIN INSERTASE YIDC.                                      
JRNL        REF    ELIFE                         V.   3  3035 2014              
JRNL        REFN                   ESSN 2050-084X                               
JRNL        PMID   25012291                                                     
JRNL        DOI    10.7554/ELIFE.03035                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    8.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : SPIDER                                    
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)    : 1.035                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 8.000                          
REMARK   3   NUMBER OF PARTICLES               : 58960                          
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL                    
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: ONLY THE MEMBRANE PART WAS MODELED SUBMISSION BASED   
REMARK   3  ON EXPERIMENTAL DATA FROM EMDB EMD-2705. (DEPOSITION ID: 12685).    
REMARK   4                                                                      
REMARK   4 4UTQ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1290061298.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : SINGLE PARTICLE                   
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE                      
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : PARTICLE                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : MONOMERIC YIDC BOUND TO           
REMARK 245                                    RIBOSOME NASCENT CHAIN            
REMARK 245                                    COMPLEX(F0C)                      
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : CARBON                            
REMARK 245   SAMPLE VITRIFICATION DETAILS   : VITRIFICATION 1 -- CRYOGEN-       
REMARK 245                                    ETHANE, INSTRUMENT- FEI           
REMARK 245                                    VITROBOT MARK IV,                 
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : NULL                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 01-JUN-13                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : NULL                           
REMARK 245   MICROSCOPE MODEL                  : FEI TITAN KRIOS                
REMARK 245   DETECTOR TYPE                     : TVIPS TEMCAM-F416 (4K X 4K)    
REMARK 245   MINIMUM DEFOCUS (NM)              : 1300.00                        
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3500.00                        
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)  : 20.00                          
REMARK 245   ILLUMINATION MODE                 : SPOT SCAN                      
REMARK 245   NOMINAL MAGNIFICATION             : NULL                           
REMARK 245   CALIBRATED MAGNIFICATION          : NULL                           
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 200                            
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, Z                                  
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     1                                                      
REMARK 465     ASP A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     GLN A     4                                                      
REMARK 465     GLU A    24                                                      
REMARK 465     GLN A    25                                                      
REMARK 465     ASP A    26                                                      
REMARK 465     LYS A    27                                                      
REMARK 465     ASN A    28                                                      
REMARK 465     PRO A    29                                                      
REMARK 465     GLN A    30                                                      
REMARK 465     PRO A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     ALA A    33                                                      
REMARK 465     GLN A    34                                                      
REMARK 465     GLN A    35                                                      
REMARK 465     THR A    36                                                      
REMARK 465     THR A    37                                                      
REMARK 465     GLN A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     THR A    40                                                      
REMARK 465     THR A    41                                                      
REMARK 465     THR A    42                                                      
REMARK 465     ALA A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     SER A    46                                                      
REMARK 465     ALA A    47                                                      
REMARK 465     ALA A    48                                                      
REMARK 465     ASP A    49                                                      
REMARK 465     GLN A    50                                                      
REMARK 465     GLY A    51                                                      
REMARK 465     VAL A    52                                                      
REMARK 465     PRO A    53                                                      
REMARK 465     ALA A    54                                                      
REMARK 465     SER A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     GLN A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     LYS A    59                                                      
REMARK 465     LEU A    60                                                      
REMARK 465     ILE A    61                                                      
REMARK 465     SER A    62                                                      
REMARK 465     VAL A    63                                                      
REMARK 465     LYS A    64                                                      
REMARK 465     THR A    65                                                      
REMARK 465     ASP A    66                                                      
REMARK 465     VAL A    67                                                      
REMARK 465     LEU A    68                                                      
REMARK 465     ASP A    69                                                      
REMARK 465     LEU A    70                                                      
REMARK 465     THR A    71                                                      
REMARK 465     ILE A    72                                                      
REMARK 465     ASN A    73                                                      
REMARK 465     THR A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     GLY A    76                                                      
REMARK 465     GLY A    77                                                      
REMARK 465     ASP A    78                                                      
REMARK 465     VAL A    79                                                      
REMARK 465     GLU A    80                                                      
REMARK 465     GLN A    81                                                      
REMARK 465     ALA A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     LEU A    84                                                      
REMARK 465     PRO A    85                                                      
REMARK 465     ALA A    86                                                      
REMARK 465     TYR A    87                                                      
REMARK 465     PRO A    88                                                      
REMARK 465     LYS A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     LEU A    91                                                      
REMARK 465     ASN A    92                                                      
REMARK 465     SER A    93                                                      
REMARK 465     THR A    94                                                      
REMARK 465     GLN A    95                                                      
REMARK 465     PRO A    96                                                      
REMARK 465     PHE A    97                                                      
REMARK 465     GLN A    98                                                      
REMARK 465     LEU A    99                                                      
REMARK 465     LEU A   100                                                      
REMARK 465     GLU A   101                                                      
REMARK 465     THR A   102                                                      
REMARK 465     SER A   103                                                      
REMARK 465     PRO A   104                                                      
REMARK 465     GLN A   105                                                      
REMARK 465     PHE A   106                                                      
REMARK 465     ILE A   107                                                      
REMARK 465     TYR A   108                                                      
REMARK 465     GLN A   109                                                      
REMARK 465     ALA A   110                                                      
REMARK 465     GLN A   111                                                      
REMARK 465     SER A   112                                                      
REMARK 465     GLY A   113                                                      
REMARK 465     LEU A   114                                                      
REMARK 465     THR A   115                                                      
REMARK 465     GLY A   116                                                      
REMARK 465     ARG A   117                                                      
REMARK 465     ASP A   118                                                      
REMARK 465     GLY A   119                                                      
REMARK 465     PRO A   120                                                      
REMARK 465     ASP A   121                                                      
REMARK 465     ASN A   122                                                      
REMARK 465     PRO A   123                                                      
REMARK 465     ALA A   124                                                      
REMARK 465     ASN A   125                                                      
REMARK 465     GLY A   126                                                      
REMARK 465     PRO A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     PRO A   129                                                      
REMARK 465     LEU A   130                                                      
REMARK 465     TYR A   131                                                      
REMARK 465     ASN A   132                                                      
REMARK 465     VAL A   133                                                      
REMARK 465     GLU A   134                                                      
REMARK 465     LYS A   135                                                      
REMARK 465     ASP A   136                                                      
REMARK 465     ALA A   137                                                      
REMARK 465     TYR A   138                                                      
REMARK 465     VAL A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     ALA A   141                                                      
REMARK 465     GLU A   142                                                      
REMARK 465     GLY A   143                                                      
REMARK 465     GLN A   144                                                      
REMARK 465     ASN A   145                                                      
REMARK 465     GLU A   146                                                      
REMARK 465     LEU A   147                                                      
REMARK 465     GLN A   148                                                      
REMARK 465     VAL A   149                                                      
REMARK 465     PRO A   150                                                      
REMARK 465     MET A   151                                                      
REMARK 465     THR A   152                                                      
REMARK 465     TYR A   153                                                      
REMARK 465     THR A   154                                                      
REMARK 465     ASP A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     ALA A   157                                                      
REMARK 465     GLY A   158                                                      
REMARK 465     ASN A   159                                                      
REMARK 465     THR A   160                                                      
REMARK 465     PHE A   161                                                      
REMARK 465     THR A   162                                                      
REMARK 465     LYS A   163                                                      
REMARK 465     THR A   164                                                      
REMARK 465     PHE A   165                                                      
REMARK 465     VAL A   166                                                      
REMARK 465     LEU A   167                                                      
REMARK 465     LYS A   168                                                      
REMARK 465     ARG A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     ASP A   171                                                      
REMARK 465     TYR A   172                                                      
REMARK 465     ALA A   173                                                      
REMARK 465     VAL A   174                                                      
REMARK 465     ASN A   175                                                      
REMARK 465     VAL A   176                                                      
REMARK 465     ASN A   177                                                      
REMARK 465     TYR A   178                                                      
REMARK 465     ASN A   179                                                      
REMARK 465     VAL A   180                                                      
REMARK 465     GLN A   181                                                      
REMARK 465     ASN A   182                                                      
REMARK 465     ALA A   183                                                      
REMARK 465     GLY A   184                                                      
REMARK 465     GLU A   185                                                      
REMARK 465     LYS A   186                                                      
REMARK 465     PRO A   187                                                      
REMARK 465     LEU A   188                                                      
REMARK 465     GLU A   189                                                      
REMARK 465     ILE A   190                                                      
REMARK 465     SER A   191                                                      
REMARK 465     SER A   192                                                      
REMARK 465     PHE A   193                                                      
REMARK 465     GLY A   194                                                      
REMARK 465     GLN A   195                                                      
REMARK 465     LEU A   196                                                      
REMARK 465     LYS A   197                                                      
REMARK 465     GLN A   198                                                      
REMARK 465     SER A   199                                                      
REMARK 465     ILE A   200                                                      
REMARK 465     THR A   201                                                      
REMARK 465     LEU A   202                                                      
REMARK 465     PRO A   203                                                      
REMARK 465     PRO A   204                                                      
REMARK 465     HIS A   205                                                      
REMARK 465     LEU A   206                                                      
REMARK 465     ASP A   207                                                      
REMARK 465     THR A   208                                                      
REMARK 465     GLY A   209                                                      
REMARK 465     SER A   210                                                      
REMARK 465     SER A   211                                                      
REMARK 465     ASN A   212                                                      
REMARK 465     PHE A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     LEU A   215                                                      
REMARK 465     HIS A   216                                                      
REMARK 465     THR A   217                                                      
REMARK 465     PHE A   218                                                      
REMARK 465     ARG A   219                                                      
REMARK 465     GLY A   220                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     ALA A   222                                                      
REMARK 465     TYR A   223                                                      
REMARK 465     SER A   224                                                      
REMARK 465     THR A   225                                                      
REMARK 465     PRO A   226                                                      
REMARK 465     ASP A   227                                                      
REMARK 465     GLU A   228                                                      
REMARK 465     LYS A   229                                                      
REMARK 465     TYR A   230                                                      
REMARK 465     GLU A   231                                                      
REMARK 465     LYS A   232                                                      
REMARK 465     TYR A   233                                                      
REMARK 465     LYS A   234                                                      
REMARK 465     PHE A   235                                                      
REMARK 465     ASP A   236                                                      
REMARK 465     THR A   237                                                      
REMARK 465     ILE A   238                                                      
REMARK 465     ALA A   239                                                      
REMARK 465     ASP A   240                                                      
REMARK 465     ASN A   241                                                      
REMARK 465     GLU A   242                                                      
REMARK 465     ASN A   243                                                      
REMARK 465     LEU A   244                                                      
REMARK 465     ASN A   245                                                      
REMARK 465     ILE A   246                                                      
REMARK 465     SER A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     LYS A   249                                                      
REMARK 465     GLY A   250                                                      
REMARK 465     GLY A   251                                                      
REMARK 465     TRP A   252                                                      
REMARK 465     VAL A   253                                                      
REMARK 465     ALA A   254                                                      
REMARK 465     MET A   255                                                      
REMARK 465     LEU A   256                                                      
REMARK 465     GLN A   257                                                      
REMARK 465     GLN A   258                                                      
REMARK 465     TYR A   259                                                      
REMARK 465     PHE A   260                                                      
REMARK 465     ALA A   261                                                      
REMARK 465     THR A   262                                                      
REMARK 465     ALA A   263                                                      
REMARK 465     TRP A   264                                                      
REMARK 465     ILE A   265                                                      
REMARK 465     PRO A   266                                                      
REMARK 465     HIS A   267                                                      
REMARK 465     ASN A   268                                                      
REMARK 465     ASP A   269                                                      
REMARK 465     GLY A   270                                                      
REMARK 465     THR A   271                                                      
REMARK 465     ASN A   272                                                      
REMARK 465     ASN A   273                                                      
REMARK 465     PHE A   274                                                      
REMARK 465     TYR A   275                                                      
REMARK 465     THR A   276                                                      
REMARK 465     ALA A   277                                                      
REMARK 465     ASN A   278                                                      
REMARK 465     LEU A   279                                                      
REMARK 465     GLY A   280                                                      
REMARK 465     ASN A   281                                                      
REMARK 465     GLY A   282                                                      
REMARK 465     ILE A   283                                                      
REMARK 465     ALA A   284                                                      
REMARK 465     ALA A   285                                                      
REMARK 465     ILE A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     TYR A   288                                                      
REMARK 465     LYS A   289                                                      
REMARK 465     SER A   290                                                      
REMARK 465     GLN A   291                                                      
REMARK 465     PRO A   292                                                      
REMARK 465     VAL A   293                                                      
REMARK 465     LEU A   294                                                      
REMARK 465     VAL A   295                                                      
REMARK 465     GLN A   296                                                      
REMARK 465     PRO A   297                                                      
REMARK 465     GLY A   298                                                      
REMARK 465     GLN A   299                                                      
REMARK 465     THR A   300                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     ALA A   302                                                      
REMARK 465     MET A   303                                                      
REMARK 465     ASN A   304                                                      
REMARK 465     SER A   305                                                      
REMARK 465     THR A   306                                                      
REMARK 465     LEU A   307                                                      
REMARK 465     TRP A   308                                                      
REMARK 465     VAL A   309                                                      
REMARK 465     GLY A   310                                                      
REMARK 465     PRO A   311                                                      
REMARK 465     GLU A   312                                                      
REMARK 465     ILE A   313                                                      
REMARK 465     GLN A   314                                                      
REMARK 465     ASP A   315                                                      
REMARK 465     LYS A   316                                                      
REMARK 465     MET A   317                                                      
REMARK 465     ALA A   318                                                      
REMARK 465     ALA A   319                                                      
REMARK 465     VAL A   320                                                      
REMARK 465     ALA A   321                                                      
REMARK 465     PRO A   322                                                      
REMARK 465     HIS A   323                                                      
REMARK 465     LEU A   324                                                      
REMARK 465     ASP A   325                                                      
REMARK 465     LEU A   326                                                      
REMARK 465     THR A   327                                                      
REMARK 465     VAL A   328                                                      
REMARK 465     ASP A   329                                                      
REMARK 465     TYR A   330                                                      
REMARK 465     GLY A   331                                                      
REMARK 465     TRP A   332                                                      
REMARK 465     LEU A   333                                                      
REMARK 465     TRP A   334                                                      
REMARK 465     PHE A   335                                                      
REMARK 465     ILE A   336                                                      
REMARK 465     SER A   337                                                      
REMARK 465     GLN A   338                                                      
REMARK 465     PRO A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     PHE A   341                                                      
REMARK 465     LYS A   342                                                      
REMARK 465     LEU A   343                                                      
REMARK 465     LEU A   344                                                      
REMARK 465     LYS A   345                                                      
REMARK 465     TRP A   346                                                      
REMARK 465     ILE A   347                                                      
REMARK 465     HIS A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     PHE A   350                                                      
REMARK 465     VAL A   351                                                      
REMARK 465     LEU A   372                                                      
REMARK 465     THR A   373                                                      
REMARK 465     LYS A   374                                                      
REMARK 465     ALA A   375                                                      
REMARK 465     GLN A   376                                                      
REMARK 465     TYR A   377                                                      
REMARK 465     THR A   378                                                      
REMARK 465     SER A   379                                                      
REMARK 465     MET A   380                                                      
REMARK 465     ALA A   381                                                      
REMARK 465     LYS A   382                                                      
REMARK 465     MET A   383                                                      
REMARK 465     ARG A   384                                                      
REMARK 465     MET A   385                                                      
REMARK 465     LEU A   386                                                      
REMARK 465     GLN A   387                                                      
REMARK 465     PRO A   388                                                      
REMARK 465     LYS A   389                                                      
REMARK 465     ILE A   390                                                      
REMARK 465     GLN A   391                                                      
REMARK 465     ALA A   392                                                      
REMARK 465     MET A   393                                                      
REMARK 465     ARG A   394                                                      
REMARK 465     GLU A   395                                                      
REMARK 465     ARG A   396                                                      
REMARK 465     LEU A   397                                                      
REMARK 465     GLY A   398                                                      
REMARK 465     ASP A   399                                                      
REMARK 465     ASP A   400                                                      
REMARK 465     LYS A   401                                                      
REMARK 465     GLN A   402                                                      
REMARK 465     ARG A   403                                                      
REMARK 465     ILE A   404                                                      
REMARK 465     SER A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     GLU A   407                                                      
REMARK 465     MET A   408                                                      
REMARK 465     MET A   409                                                      
REMARK 465     ALA A   410                                                      
REMARK 465     LEU A   411                                                      
REMARK 465     TYR A   412                                                      
REMARK 465     LYS A   413                                                      
REMARK 465     ALA A   414                                                      
REMARK 465     GLU A   415                                                      
REMARK 465     LYS A   416                                                      
REMARK 465     VAL A   417                                                      
REMARK 465     ASN A   418                                                      
REMARK 465     LEU A   440                                                      
REMARK 465     MET A   441                                                      
REMARK 465     GLY A   442                                                      
REMARK 465     SER A   443                                                      
REMARK 465     VAL A   444                                                      
REMARK 465     GLU A   445                                                      
REMARK 465     LEU A   446                                                      
REMARK 465     ARG A   447                                                      
REMARK 465     GLN A   448                                                      
REMARK 465     ALA A   449                                                      
REMARK 465     PRO A   450                                                      
REMARK 465     PHE A   451                                                      
REMARK 465     ALA A   452                                                      
REMARK 465     LEU A   453                                                      
REMARK 465     TRP A   454                                                      
REMARK 465     ILE A   455                                                      
REMARK 465     HIS A   456                                                      
REMARK 465     ASP A   457                                                      
REMARK 465     LEU A   458                                                      
REMARK 465     SER A   459                                                      
REMARK 465     ALA A   460                                                      
REMARK 465     GLN A   461                                                      
REMARK 465     ASP A   462                                                      
REMARK 465     PRO A   463                                                      
REMARK 465     TYR A   464                                                      
REMARK 465     MET A   481                                                      
REMARK 465     SER A   482                                                      
REMARK 465     PRO A   483                                                      
REMARK 465     THR A   484                                                      
REMARK 465     THR A   485                                                      
REMARK 465     VAL A   486                                                      
REMARK 465     THR A   487                                                      
REMARK 465     ASP A   488                                                      
REMARK 465     PRO A   489                                                      
REMARK 465     MET A   490                                                      
REMARK 465     GLN A   491                                                      
REMARK 465     GLN A   492                                                      
REMARK 465     LYS A   493                                                      
REMARK 465     ARG A   533                                                      
REMARK 465     GLY A   534                                                      
REMARK 465     LEU A   535                                                      
REMARK 465     GLU A   536                                                      
REMARK 465     LYS A   537                                                      
REMARK 465     ARG A   538                                                      
REMARK 465     GLY A   539                                                      
REMARK 465     LEU A   540                                                      
REMARK 465     HIS A   541                                                      
REMARK 465     SER A   542                                                      
REMARK 465     ARG A   543                                                      
REMARK 465     GLU A   544                                                      
REMARK 465     LYS A   545                                                      
REMARK 465     LYS A   546                                                      
REMARK 465     LYS A   547                                                      
REMARK 465     SER A   548                                                      
REMARK 465     MET Z     1                                                      
REMARK 465     GLU Z     2                                                      
REMARK 465     ASN Z     3                                                      
REMARK 465     LEU Z     4                                                      
REMARK 465     ASN Z     5                                                      
REMARK 465     MET Z     6                                                      
REMARK 465     ASP Z     7                                                      
REMARK 465     LEU Z     8                                                      
REMARK 465     LEU Z     9                                                      
REMARK 465     TYR Z    10                                                      
REMARK 465     LYS Z    34                                                      
REMARK 465     PHE Z    35                                                      
REMARK 465     LEU Z    36                                                      
REMARK 465     GLU Z    37                                                      
REMARK 465     GLY Z    38                                                      
REMARK 465     ALA Z    39                                                      
REMARK 465     ALA Z    40                                                      
REMARK 465     ARG Z    41                                                      
REMARK 465     GLN Z    42                                                      
REMARK 465     PRO Z    43                                                      
REMARK 465     ASP Z    44                                                      
REMARK 465     LEU Z    45                                                      
REMARK 465     ILE Z    46                                                      
REMARK 465     PRO Z    47                                                      
REMARK 465     LEU Z    48                                                      
REMARK 465     LEU Z    49                                                      
REMARK 465     ARG Z    50                                                      
REMARK 465     THR Z    51                                                      
REMARK 465     GLN Z    52                                                      
REMARK 465     PHE Z    53                                                      
REMARK 465     PHE Z    54                                                      
REMARK 465     ILE Z    55                                                      
REMARK 465     VAL Z    56                                                      
REMARK 465     MET Z    57                                                      
REMARK 465     GLY Z    58                                                      
REMARK 465     LEU Z    59                                                      
REMARK 465     VAL Z    60                                                      
REMARK 465     ASP Z    61                                                      
REMARK 465     ALA Z    62                                                      
REMARK 465     ILE Z    63                                                      
REMARK 465     PRO Z    64                                                      
REMARK 465     MET Z    65                                                      
REMARK 465     ILE Z    66                                                      
REMARK 465     ALA Z    67                                                      
REMARK 465     VAL Z    68                                                      
REMARK 465     GLY Z    69                                                      
REMARK 465     LEU Z    70                                                      
REMARK 465     GLY Z    71                                                      
REMARK 465     LEU Z    72                                                      
REMARK 465     TYR Z    73                                                      
REMARK 465     VAL Z    74                                                      
REMARK 465     MET Z    75                                                      
REMARK 465     PHE Z    76                                                      
REMARK 465     ALA Z    77                                                      
REMARK 465     VAL Z    78                                                      
REMARK 465     ALA Z    79                                                      
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     ARG A   5    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ASN A   6    CB   CG   OD1  ND2                                  
REMARK 470     LEU A   7    CB   CG   CD1  CD2                                  
REMARK 470     LEU A   8    CB   CG   CD1  CD2                                  
REMARK 470     VAL A   9    CB   CG1  CG2                                       
REMARK 470     ILE A  10    CB   CG1  CG2  CD1                                  
REMARK 470     ALA A  11    CB                                                  
REMARK 470     LEU A  12    CB   CG   CD1  CD2                                  
REMARK 470     LEU A  13    CB   CG   CD1  CD2                                  
REMARK 470     PHE A  14    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     VAL A  15    CB   CG1  CG2                                       
REMARK 470     SER A  16    CB   OG                                             
REMARK 470     PHE A  17    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     MET A  18    CB   CG   SD   CE                                   
REMARK 470     ILE A  19    CB   CG1  CG2  CD1                                  
REMARK 470     TRP A  20    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A  20    CZ2  CZ3  CH2                                       
REMARK 470     GLN A  21    CB   CG   CD   OE1  NE2                             
REMARK 470     ALA A  22    CB                                                  
REMARK 470     TRP A  23    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A  23    CZ2  CZ3  CH2                                       
REMARK 470     ASN A 353    CB   CG   OD1  ND2                                  
REMARK 470     TRP A 354    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A 354    CZ2  CZ3  CH2                                       
REMARK 470     PHE A 356    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     SER A 357    CB   OG                                             
REMARK 470     ILE A 358    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A 359    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A 360    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A 361    CB   CG1  CG2  CD1                                  
REMARK 470     THR A 362    CB   OG1  CG2                                       
REMARK 470     PHE A 363    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ILE A 364    CB   CG1  CG2  CD1                                  
REMARK 470     VAL A 365    CB   CG1  CG2                                       
REMARK 470     ARG A 366    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     ILE A 368    CB   CG1  CG2  CD1                                  
REMARK 470     MET A 369    CB   CG   SD   CE                                   
REMARK 470     TYR A 370    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 370    OH                                                  
REMARK 470     PRO A 371    CB   CG   CD                                        
REMARK 470     PRO A 419    CB   CG   CD                                        
REMARK 470     LEU A 420    CB   CG   CD1  CD2                                  
REMARK 470     CYS A 423    CB   SG                                             
REMARK 470     PHE A 424    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     PRO A 425    CB   CG   CD                                        
REMARK 470     LEU A 426    CB   CG   CD1  CD2                                  
REMARK 470     LEU A 427    CB   CG   CD1  CD2                                  
REMARK 470     ILE A 428    CB   CG1  CG2  CD1                                  
REMARK 470     GLN A 429    CB   CG   CD   OE1  NE2                             
REMARK 470     MET A 430    CB   CG   SD   CE                                   
REMARK 470     PRO A 431    CB   CG   CD                                        
REMARK 470     ILE A 432    CB   CG1  CG2  CD1                                  
REMARK 470     PHE A 433    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     LEU A 434    CB   CG   CD1  CD2                                  
REMARK 470     ALA A 435    CB                                                  
REMARK 470     LEU A 436    CB   CG   CD1  CD2                                  
REMARK 470     TYR A 437    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 437    OH                                                  
REMARK 470     TYR A 438    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 438    OH                                                  
REMARK 470     MET A 439    CB   CG   SD   CE                                   
REMARK 470     TYR A 465    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 465    OH                                                  
REMARK 470     ILE A 466    CB   CG1  CG2  CD1                                  
REMARK 470     LEU A 467    CB   CG   CD1  CD2                                  
REMARK 470     PRO A 468    CB   CG   CD                                        
REMARK 470     ILE A 469    CB   CG1  CG2  CD1                                  
REMARK 470     LEU A 470    CB   CG   CD1  CD2                                  
REMARK 470     MET A 471    CB   CG   SD   CE                                   
REMARK 470     VAL A 473    CB   CG1  CG2                                       
REMARK 470     THR A 474    CB   OG1  CG2                                       
REMARK 470     MET A 475    CB   CG   SD   CE                                   
REMARK 470     PHE A 476    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     PHE A 477    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     ILE A 478    CB   CG1  CG2  CD1                                  
REMARK 470     GLN A 479    CB   CG   CD   OE1  NE2                             
REMARK 470     LYS A 480    CB   CG   CD   CE   NZ                              
REMARK 470     ILE A 494    CB   CG1  CG2  CD1                                  
REMARK 470     MET A 495    CB   CG   SD   CE                                   
REMARK 470     THR A 496    CB   OG1  CG2                                       
REMARK 470     PHE A 497    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     MET A 498    CB   CG   SD   CE                                   
REMARK 470     PRO A 499    CB   CG   CD                                        
REMARK 470     VAL A 500    CB   CG1  CG2                                       
REMARK 470     ILE A 501    CB   CG1  CG2  CD1                                  
REMARK 470     PHE A 502    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     THR A 503    CB   OG1  CG2                                       
REMARK 470     VAL A 504    CB   CG1  CG2                                       
REMARK 470     PHE A 505    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     PHE A 506    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     LEU A 507    CB   CG   CD1  CD2                                  
REMARK 470     TRP A 508    CB   CG   CD1  CD2  NE1  CE2  CE3                   
REMARK 470     TRP A 508    CZ2  CZ3  CH2                                       
REMARK 470     PHE A 509    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     PRO A 510    CB   CG   CD                                        
REMARK 470     SER A 511    CB   OG                                             
REMARK 470     LEU A 513    CB   CG   CD1  CD2                                  
REMARK 470     VAL A 514    CB   CG1  CG2                                       
REMARK 470     LEU A 515    CB   CG   CD1  CD2                                  
REMARK 470     TYR A 516    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 516    OH                                                  
REMARK 470     TYR A 517    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 517    OH                                                  
REMARK 470     ILE A 518    CB   CG1  CG2  CD1                                  
REMARK 470     VAL A 519    CB   CG1  CG2                                       
REMARK 470     SER A 520    CB   OG                                             
REMARK 470     ASN A 521    CB   CG   OD1  ND2                                  
REMARK 470     LEU A 522    CB   CG   CD1  CD2                                  
REMARK 470     VAL A 523    CB   CG1  CG2                                       
REMARK 470     THR A 524    CB   OG1  CG2                                       
REMARK 470     ILE A 525    CB   CG1  CG2  CD1                                  
REMARK 470     ILE A 526    CB   CG1  CG2  CD1                                  
REMARK 470     GLN A 527    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN A 528    CB   CG   CD   OE1  NE2                             
REMARK 470     GLN A 529    CB   CG   CD   OE1  NE2                             
REMARK 470     LEU A 530    CB   CG   CD1  CD2                                  
REMARK 470     ILE A 531    CB   CG1  CG2  CD1                                  
REMARK 470     TYR A 532    CB   CG   CD1  CD2  CE1  CE2  CZ                    
REMARK 470     TYR A 532    OH                                                  
REMARK 470     MET Z  11    CB   CG   SD   CE                                   
REMARK 470     ALA Z  12    CB                                                  
REMARK 470     ALA Z  13    CB                                                  
REMARK 470     ALA Z  14    CB                                                  
REMARK 470     VAL Z  15    CB   CG1  CG2                                       
REMARK 470     MET Z  16    CB   CG   SD   CE                                   
REMARK 470     MET Z  17    CB   CG   SD   CE                                   
REMARK 470     LEU Z  19    CB   CG   CD1  CD2                                  
REMARK 470     ALA Z  20    CB                                                  
REMARK 470     ALA Z  21    CB                                                  
REMARK 470     ILE Z  22    CB   CG1  CG2  CD1                                  
REMARK 470     ALA Z  24    CB                                                  
REMARK 470     ALA Z  25    CB                                                  
REMARK 470     ILE Z  26    CB   CG1  CG2  CD1                                  
REMARK 470     ILE Z  28    CB   CG1  CG2  CD1                                  
REMARK 470     ILE Z  30    CB   CG1  CG2  CD1                                  
REMARK 470     LEU Z  31    CB   CG   CD1  CD2                                  
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    TYR A 370      -78.37    -71.50                                   
REMARK 500    MET Z  16      -77.11    -76.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: EMD-2705   RELATED DB: EMDB                              
DBREF  4UTQ A    1   548  UNP    P25714   YIDC_ECOLI       1    548             
DBREF  4UTQ Z    1    79  UNP    P68699   ATPL_ECOLI       1     79             
SEQRES   1 A  548  MET ASP SER GLN ARG ASN LEU LEU VAL ILE ALA LEU LEU          
SEQRES   2 A  548  PHE VAL SER PHE MET ILE TRP GLN ALA TRP GLU GLN ASP          
SEQRES   3 A  548  LYS ASN PRO GLN PRO GLN ALA GLN GLN THR THR GLN THR          
SEQRES   4 A  548  THR THR THR ALA ALA GLY SER ALA ALA ASP GLN GLY VAL          
SEQRES   5 A  548  PRO ALA SER GLY GLN GLY LYS LEU ILE SER VAL LYS THR          
SEQRES   6 A  548  ASP VAL LEU ASP LEU THR ILE ASN THR ARG GLY GLY ASP          
SEQRES   7 A  548  VAL GLU GLN ALA LEU LEU PRO ALA TYR PRO LYS GLU LEU          
SEQRES   8 A  548  ASN SER THR GLN PRO PHE GLN LEU LEU GLU THR SER PRO          
SEQRES   9 A  548  GLN PHE ILE TYR GLN ALA GLN SER GLY LEU THR GLY ARG          
SEQRES  10 A  548  ASP GLY PRO ASP ASN PRO ALA ASN GLY PRO ARG PRO LEU          
SEQRES  11 A  548  TYR ASN VAL GLU LYS ASP ALA TYR VAL LEU ALA GLU GLY          
SEQRES  12 A  548  GLN ASN GLU LEU GLN VAL PRO MET THR TYR THR ASP ALA          
SEQRES  13 A  548  ALA GLY ASN THR PHE THR LYS THR PHE VAL LEU LYS ARG          
SEQRES  14 A  548  GLY ASP TYR ALA VAL ASN VAL ASN TYR ASN VAL GLN ASN          
SEQRES  15 A  548  ALA GLY GLU LYS PRO LEU GLU ILE SER SER PHE GLY GLN          
SEQRES  16 A  548  LEU LYS GLN SER ILE THR LEU PRO PRO HIS LEU ASP THR          
SEQRES  17 A  548  GLY SER SER ASN PHE ALA LEU HIS THR PHE ARG GLY ALA          
SEQRES  18 A  548  ALA TYR SER THR PRO ASP GLU LYS TYR GLU LYS TYR LYS          
SEQRES  19 A  548  PHE ASP THR ILE ALA ASP ASN GLU ASN LEU ASN ILE SER          
SEQRES  20 A  548  SER LYS GLY GLY TRP VAL ALA MET LEU GLN GLN TYR PHE          
SEQRES  21 A  548  ALA THR ALA TRP ILE PRO HIS ASN ASP GLY THR ASN ASN          
SEQRES  22 A  548  PHE TYR THR ALA ASN LEU GLY ASN GLY ILE ALA ALA ILE          
SEQRES  23 A  548  GLY TYR LYS SER GLN PRO VAL LEU VAL GLN PRO GLY GLN          
SEQRES  24 A  548  THR GLY ALA MET ASN SER THR LEU TRP VAL GLY PRO GLU          
SEQRES  25 A  548  ILE GLN ASP LYS MET ALA ALA VAL ALA PRO HIS LEU ASP          
SEQRES  26 A  548  LEU THR VAL ASP TYR GLY TRP LEU TRP PHE ILE SER GLN          
SEQRES  27 A  548  PRO LEU PHE LYS LEU LEU LYS TRP ILE HIS SER PHE VAL          
SEQRES  28 A  548  GLY ASN TRP GLY PHE SER ILE ILE ILE ILE THR PHE ILE          
SEQRES  29 A  548  VAL ARG GLY ILE MET TYR PRO LEU THR LYS ALA GLN TYR          
SEQRES  30 A  548  THR SER MET ALA LYS MET ARG MET LEU GLN PRO LYS ILE          
SEQRES  31 A  548  GLN ALA MET ARG GLU ARG LEU GLY ASP ASP LYS GLN ARG          
SEQRES  32 A  548  ILE SER GLN GLU MET MET ALA LEU TYR LYS ALA GLU LYS          
SEQRES  33 A  548  VAL ASN PRO LEU GLY GLY CYS PHE PRO LEU LEU ILE GLN          
SEQRES  34 A  548  MET PRO ILE PHE LEU ALA LEU TYR TYR MET LEU MET GLY          
SEQRES  35 A  548  SER VAL GLU LEU ARG GLN ALA PRO PHE ALA LEU TRP ILE          
SEQRES  36 A  548  HIS ASP LEU SER ALA GLN ASP PRO TYR TYR ILE LEU PRO          
SEQRES  37 A  548  ILE LEU MET GLY VAL THR MET PHE PHE ILE GLN LYS MET          
SEQRES  38 A  548  SER PRO THR THR VAL THR ASP PRO MET GLN GLN LYS ILE          
SEQRES  39 A  548  MET THR PHE MET PRO VAL ILE PHE THR VAL PHE PHE LEU          
SEQRES  40 A  548  TRP PHE PRO SER GLY LEU VAL LEU TYR TYR ILE VAL SER          
SEQRES  41 A  548  ASN LEU VAL THR ILE ILE GLN GLN GLN LEU ILE TYR ARG          
SEQRES  42 A  548  GLY LEU GLU LYS ARG GLY LEU HIS SER ARG GLU LYS LYS          
SEQRES  43 A  548  LYS SER                                                      
SEQRES   1 Z   79  MET GLU ASN LEU ASN MET ASP LEU LEU TYR MET ALA ALA          
SEQRES   2 Z   79  ALA VAL MET MET GLY LEU ALA ALA ILE GLY ALA ALA ILE          
SEQRES   3 Z   79  GLY ILE GLY ILE LEU GLY GLY LYS PHE LEU GLU GLY ALA          
SEQRES   4 Z   79  ALA ARG GLN PRO ASP LEU ILE PRO LEU LEU ARG THR GLN          
SEQRES   5 Z   79  PHE PHE ILE VAL MET GLY LEU VAL ASP ALA ILE PRO MET          
SEQRES   6 Z   79  ILE ALA VAL GLY LEU GLY LEU TYR VAL MET PHE ALA VAL          
SEQRES   7 Z   79  ALA                                                          
HELIX    1   1 ARG A    5  TRP A   23  1                                  19    
HELIX    2   2 GLY A  352  MET A  369  1                                  18    
HELIX    3   3 PRO A  419  MET A  439  1                                  21    
HELIX    4   4 TYR A  465  LYS A  480  1                                  16    
HELIX    5   5 THR A  496  PHE A  509  1                                  14    
HELIX    6   6 LEU A  513  TYR A  532  1                                  20    
HELIX    7   7 MET Z   11  LEU Z   31  1                                  21    
CRYST1    1.000    1.000    1.000  90.00  90.00  90.00 P 1           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   ARG A   5      -9.564 104.055 -30.067  1.00  0.00           N  
ATOM      2  CA  ARG A   5      -9.132 104.911 -31.200  1.00  0.00           C  
ATOM      3  C   ARG A   5      -9.956 106.177 -31.252  1.00  0.00           C  
ATOM      4  O   ARG A   5      -9.354 107.235 -31.237  1.00  0.00           O  
ATOM      5  N   ASN A   6     -11.287 106.069 -31.166  1.00  0.00           N  
ATOM      6  CA  ASN A   6     -12.154 107.242 -31.181  1.00  0.00           C  
ATOM      7  C   ASN A   6     -11.846 108.228 -30.057  1.00  0.00           C  
ATOM      8  O   ASN A   6     -11.597 109.386 -30.303  1.00  0.00           O  
ATOM      9  N   LEU A   7     -11.582 107.722 -28.859  1.00  0.00           N  
ATOM     10  CA  LEU A   7     -11.216 108.606 -27.754  1.00  0.00           C  
ATOM     11  C   LEU A   7      -9.895 109.305 -27.965  1.00  0.00           C  
ATOM     12  O   LEU A   7      -9.768 110.480 -27.648  1.00  0.00           O  
ATOM     13  N   LEU A   8      -8.948 108.601 -28.584  1.00  0.00           N  
ATOM     14  CA  LEU A   8      -7.716 109.245 -28.949  1.00  0.00           C  
ATOM     15  C   LEU A   8      -7.951 110.341 -29.974  1.00  0.00           C  
ATOM     16  O   LEU A   8      -7.519 111.468 -29.745  1.00  0.00           O  
ATOM     17  N   VAL A   9      -8.755 110.031 -31.006  1.00  0.00           N  
ATOM     18  CA  VAL A   9      -9.227 111.046 -31.944  1.00  0.00           C  
ATOM     19  C   VAL A   9      -9.932 112.235 -31.264  1.00  0.00           C  
ATOM     20  O   VAL A   9     -10.140 113.255 -31.897  1.00  0.00           O  
ATOM     21  N   ILE A  10     -10.467 112.046 -30.055  1.00  0.00           N  
ATOM     22  CA  ILE A  10     -11.104 113.107 -29.267  1.00  0.00           C  
ATOM     23  C   ILE A  10     -10.144 113.870 -28.324  1.00  0.00           C  
ATOM     24  O   ILE A  10     -10.381 114.982 -27.857  1.00  0.00           O  
ATOM     25  N   ALA A  11      -8.972 113.321 -28.096  1.00  0.00           N  
ATOM     26  CA  ALA A  11      -7.940 114.019 -27.367  1.00  0.00           C  
ATOM     27  C   ALA A  11      -7.082 114.942 -28.266  1.00  0.00           C  
ATOM     28  O   ALA A  11      -6.998 116.134 -27.994  1.00  0.00           O  
ATOM     29  N   LEU A  12      -6.610 114.473 -29.433  1.00  0.00           N  
ATOM     30  CA  LEU A  12      -5.839 115.295 -30.410  1.00  0.00           C  
ATOM     31  C   LEU A  12      -6.580 116.559 -30.885  1.00  0.00           C  
ATOM     32  O   LEU A  12      -5.943 117.596 -30.987  1.00  0.00           O  
ATOM     33  N   LEU A  13      -7.873 116.485 -31.254  1.00  0.00           N  
ATOM     34  CA  LEU A  13      -8.634 117.652 -31.733  1.00  0.00           C  
ATOM     35  C   LEU A  13      -8.610 118.690 -30.624  1.00  0.00           C  
ATOM     36  O   LEU A  13      -8.269 119.826 -30.890  1.00  0.00           O  
ATOM     37  N   PHE A  14      -8.845 118.266 -29.377  1.00  0.00           N  
ATOM     38  CA  PHE A  14      -8.956 119.162 -28.241  1.00  0.00           C  
ATOM     39  C   PHE A  14      -7.642 119.885 -27.971  1.00  0.00           C  
ATOM     40  O   PHE A  14      -7.619 121.106 -27.858  1.00  0.00           O  
ATOM     41  N   VAL A  15      -6.540 119.142 -28.114  1.00  0.00           N  
ATOM     42  CA  VAL A  15      -5.187 119.697 -28.135  1.00  0.00           C  
ATOM     43  C   VAL A  15      -5.060 120.722 -29.263  1.00  0.00           C  
ATOM     44  O   VAL A  15      -4.705 121.858 -28.980  1.00  0.00           O  
ATOM     45  N   SER A  16      -5.423 120.385 -30.503  1.00  0.00           N  
ATOM     46  CA  SER A  16      -5.338 121.308 -31.643  1.00  0.00           C  
ATOM     47  C   SER A  16      -6.153 122.587 -31.438  1.00  0.00           C  
ATOM     48  O   SER A  16      -5.648 123.679 -31.684  1.00  0.00           O  
ATOM     49  N   PHE A  17      -7.378 122.459 -30.917  1.00  0.00           N  
ATOM     50  CA  PHE A  17      -8.206 123.588 -30.498  1.00  0.00           C  
ATOM     51  C   PHE A  17      -7.580 124.499 -29.475  1.00  0.00           C  
ATOM     52  O   PHE A  17      -7.647 125.715 -29.623  1.00  0.00           O  
ATOM     53  N   MET A  18      -7.013 123.886 -28.431  1.00  0.00           N  
ATOM     54  CA  MET A  18      -6.245 124.624 -27.454  1.00  0.00           C  
ATOM     55  C   MET A  18      -5.152 125.382 -28.199  1.00  0.00           C  
ATOM     56  O   MET A  18      -5.254 126.593 -28.253  1.00  0.00           O  
ATOM     57  N   ILE A  19      -4.269 124.717 -28.957  1.00  0.00           N  
ATOM     58  CA  ILE A  19      -3.119 125.380 -29.611  1.00  0.00           C  
ATOM     59  C   ILE A  19      -3.545 126.612 -30.402  1.00  0.00           C  
ATOM     60  O   ILE A  19      -2.915 127.661 -30.298  1.00  0.00           O  
ATOM     61  N   TRP A  20      -4.639 126.480 -31.148  1.00  0.00           N  
ATOM     62  CA  TRP A  20      -5.204 127.586 -31.897  1.00  0.00           C  
ATOM     63  C   TRP A  20      -5.646 128.754 -31.011  1.00  0.00           C  
ATOM     64  O   TRP A  20      -5.366 129.890 -31.351  1.00  0.00           O  
ATOM     65  N   GLN A  21      -6.304 128.494 -29.880  1.00  0.00           N  
ATOM     66  CA  GLN A  21      -6.619 129.529 -28.896  1.00  0.00           C  
ATOM     67  C   GLN A  21      -5.367 130.265 -28.389  1.00  0.00           C  
ATOM     68  O   GLN A  21      -5.454 131.458 -28.113  1.00  0.00           O  
ATOM     69  N   ALA A  22      -4.296 129.530 -28.051  1.00  0.00           N  
ATOM     70  CA  ALA A  22      -3.049 130.161 -27.586  1.00  0.00           C  
ATOM     71  C   ALA A  22      -2.490 131.140 -28.618  1.00  0.00           C  
ATOM     72  O   ALA A  22      -1.878 132.129 -28.219  1.00  0.00           O  
ATOM     73  N   TRP A  23      -2.482 130.708 -29.886  1.00  0.00           N  
ATOM     74  CA  TRP A  23      -2.020 131.495 -31.020  1.00  0.00           C  
ATOM     75  C   TRP A  23      -2.713 132.865 -31.138  1.00  0.00           C  
ATOM     76  O   TRP A  23      -2.041 133.825 -31.345  1.00  0.00           O  
ATOM     77  N   GLY A 352      16.784 132.339  -8.706  1.00  0.00           N  
ATOM     78  CA  GLY A 352      17.997 131.558  -8.935  1.00  0.00           C  
ATOM     79  C   GLY A 352      18.070 130.312  -8.047  1.00  0.00           C  
ATOM     80  O   GLY A 352      17.308 129.366  -8.229  1.00  0.00           O  
ATOM     81  N   ASN A 353      18.957 130.319  -7.046  1.00  0.00           N  
ATOM     82  CA  ASN A 353      19.271 129.153  -6.202  1.00  0.00           C  
ATOM     83  C   ASN A 353      18.043 128.454  -5.587  1.00  0.00           C  
ATOM     84  O   ASN A 353      17.928 127.235  -5.678  1.00  0.00           O  
ATOM     85  N   TRP A 354      17.083 129.225  -5.062  1.00  0.00           N  
ATOM     86  CA  TRP A 354      15.807 128.706  -4.546  1.00  0.00           C  
ATOM     87  C   TRP A 354      14.978 127.910  -5.566  1.00  0.00           C  
ATOM     88  O   TRP A 354      14.459 126.845  -5.238  1.00  0.00           O  
ATOM     89  N   GLY A 355      15.081 128.267  -6.846  1.00  0.00           N  
ATOM     90  CA  GLY A 355      14.505 127.490  -7.933  1.00  0.00           C  
ATOM     91  C   GLY A 355      15.258 126.213  -8.261  1.00  0.00           C  
ATOM     92  O   GLY A 355      14.647 125.147  -8.306  1.00  0.00           O  
ATOM     93  N   PHE A 356      16.589 126.269  -8.311  1.00  0.00           N  
ATOM     94  CA  PHE A 356      17.407 125.072  -8.515  1.00  0.00           C  
ATOM     95  C   PHE A 356      17.241 123.987  -7.433  1.00  0.00           C  
ATOM     96  O   PHE A 356      17.107 122.810  -7.768  1.00  0.00           O  
ATOM     97  N   SER A 357      16.931 124.403  -6.200  1.00  0.00           N  
ATOM     98  CA  SER A 357      16.455 123.512  -5.132  1.00  0.00           C  
ATOM     99  C   SER A 357      15.122 122.825  -5.454  1.00  0.00           C  
ATOM    100  O   SER A 357      15.027 121.606  -5.335  1.00  0.00           O  
ATOM    101  N   ILE A 358      14.118 123.550  -5.959  1.00  0.00           N  
ATOM    102  CA  ILE A 358      12.816 122.979  -6.359  1.00  0.00           C  
ATOM    103  C   ILE A 358      12.933 122.004  -7.549  1.00  0.00           C  
ATOM    104  O   ILE A 358      12.267 120.960  -7.550  1.00  0.00           O  
ATOM    105  N   ILE A 359      13.878 122.240  -8.469  1.00  0.00           N  
ATOM    106  CA  ILE A 359      14.240 121.278  -9.524  1.00  0.00           C  
ATOM    107  C   ILE A 359      14.778 119.971  -8.910  1.00  0.00           C  
ATOM    108  O   ILE A 359      14.342 118.882  -9.286  1.00  0.00           O  
ATOM    109  N   ILE A 360      15.636 120.059  -7.890  1.00  0.00           N  
ATOM    110  CA  ILE A 360      16.220 118.883  -7.226  1.00  0.00           C  
ATOM    111  C   ILE A 360      15.185 118.109  -6.394  1.00  0.00           C  
ATOM    112  O   ILE A 360      15.080 116.892  -6.552  1.00  0.00           O  
ATOM    113  N   ILE A 361      14.317 118.795  -5.639  1.00  0.00           N  
ATOM    114  CA  ILE A 361      13.224 118.151  -4.882  1.00  0.00           C  
ATOM    115  C   ILE A 361      12.264 117.405  -5.821  1.00  0.00           C  
ATOM    116  O   ILE A 361      11.955 116.236  -5.584  1.00  0.00           O  
ATOM    117  N   THR A 362      11.972 117.985  -6.990  1.00  0.00           N  
ATOM    118  CA  THR A 362      11.188 117.332  -8.049  1.00  0.00           C  
ATOM    119  C   THR A 362      11.871 116.049  -8.535  1.00  0.00           C  
ATOM    120  O   THR A 362      11.198 115.026  -8.668  1.00  0.00           O  
ATOM    121  N   PHE A 363      13.193 116.035  -8.727  1.00  0.00           N  
ATOM    122  CA  PHE A 363      13.906 114.800  -9.065  1.00  0.00           C  
ATOM    123  C   PHE A 363      13.887 113.667  -8.045  1.00  0.00           C  
ATOM    124  O   PHE A 363      13.645 112.521  -8.422  1.00  0.00           O  
ATOM    125  N   ILE A 364      13.996 113.996  -6.756  1.00  0.00           N  
ATOM    126  CA  ILE A 364      13.858 113.018  -5.664  1.00  0.00           C  
ATOM    127  C   ILE A 364      12.464 112.378  -5.686  1.00  0.00           C  
ATOM    128  O   ILE A 364      12.341 111.154  -5.710  1.00  0.00           O  
ATOM    129  N   VAL A 365      11.432 113.191  -5.919  1.00  0.00           N  
ATOM    130  CA  VAL A 365      10.041 112.737  -6.037  1.00  0.00           C  
ATOM    131  C   VAL A 365       9.825 111.878  -7.296  1.00  0.00           C  
ATOM    132  O   VAL A 365       9.281 110.777  -7.188  1.00  0.00           O  
ATOM    133  N   ARG A 366      10.369 112.269  -8.461  1.00  0.00           N  
ATOM    134  CA  ARG A 366      10.361 111.432  -9.680  1.00  0.00           C  
ATOM    135  C   ARG A 366      11.119 110.110  -9.516  1.00  0.00           C  
ATOM    136  O   ARG A 366      10.721 109.119 -10.127  1.00  0.00           O  
ATOM    137  N   GLY A 367      12.168 110.093  -8.693  1.00  0.00           N  
ATOM    138  CA  GLY A 367      12.988 108.921  -8.386  1.00  0.00           C  
ATOM    139  C   GLY A 367      12.298 107.887  -7.494  1.00  0.00           C  
ATOM    140  O   GLY A 367      12.398 106.699  -7.786  1.00  0.00           O  
ATOM    141  N   ILE A 368      11.428 108.314  -6.569  1.00  0.00           N  
ATOM    142  CA  ILE A 368      10.605 107.387  -5.762  1.00  0.00           C  
ATOM    143  C   ILE A 368       9.624 106.598  -6.647  1.00  0.00           C  
ATOM    144  O   ILE A 368       9.373 105.425  -6.393  1.00  0.00           O  
ATOM    145  N   MET A 369       9.153 107.191  -7.750  1.00  0.00           N  
ATOM    146  CA  MET A 369       8.278 106.516  -8.720  1.00  0.00           C  
ATOM    147  C   MET A 369       8.993 105.484  -9.621  1.00  0.00           C  
ATOM    148  O   MET A 369       8.332 104.939 -10.501  1.00  0.00           O  
ATOM    149  N   TYR A 370      10.336 105.416  -9.623  1.00  0.00           N  
ATOM    150  CA  TYR A 370      11.089 104.922 -10.787  1.00  0.00           C  
ATOM    151  C   TYR A 370      11.052 103.414 -11.133  1.00  0.00           C  
ATOM    152  O   TYR A 370      10.367 103.061 -12.095  1.00  0.00           O  
ATOM    153  N   PRO A 371      11.795 102.510 -10.456  1.00  0.00           N  
ATOM    154  CA  PRO A 371      11.720 101.078 -10.749  1.00  0.00           C  
ATOM    155  C   PRO A 371      10.315 100.500 -10.540  1.00  0.00           C  
ATOM    156  O   PRO A 371       9.774 100.536  -9.435  1.00  0.00           O  
ATOM    157  N   PRO A 419      -5.506 100.847 -11.838  1.00  0.00           N  
ATOM    158  CA  PRO A 419      -5.331 102.266 -12.113  1.00  0.00           C  
ATOM    159  C   PRO A 419      -4.452 102.985 -11.094  1.00  0.00           C  
ATOM    160  O   PRO A 419      -3.770 103.941 -11.448  1.00  0.00           O  
ATOM    161  N   LEU A 420      -4.361 102.449  -9.874  1.00  0.00           N  
ATOM    162  CA  LEU A 420      -3.605 102.997  -8.744  1.00  0.00           C  
ATOM    163  C   LEU A 420      -2.108 103.191  -9.039  1.00  0.00           C  
ATOM    164  O   LEU A 420      -1.548 104.247  -8.753  1.00  0.00           O  
ATOM    165  N   GLY A 421      -1.491 102.194  -9.679  1.00  0.00           N  
ATOM    166  CA  GLY A 421      -0.051 102.180  -9.956  1.00  0.00           C  
ATOM    167  C   GLY A 421       0.385 103.208 -11.004  1.00  0.00           C  
ATOM    168  O   GLY A 421       1.506 103.691 -10.941  1.00  0.00           O  
ATOM    169  N   GLY A 422      -0.542 103.665 -11.855  1.00  0.00           N  
ATOM    170  CA  GLY A 422      -0.367 104.878 -12.658  1.00  0.00           C  
ATOM    171  C   GLY A 422      -0.832 106.143 -11.930  1.00  0.00           C  
ATOM    172  O   GLY A 422      -0.133 107.148 -11.930  1.00  0.00           O  
ATOM    173  N   CYS A 423      -1.952 106.069 -11.208  1.00  0.00           N  
ATOM    174  CA  CYS A 423      -2.567 107.169 -10.465  1.00  0.00           C  
ATOM    175  C   CYS A 423      -1.653 107.868  -9.447  1.00  0.00           C  
ATOM    176  O   CYS A 423      -1.637 109.095  -9.439  1.00  0.00           O  
ATOM    177  N   PHE A 424      -0.817 107.153  -8.682  1.00  0.00           N  
ATOM    178  CA  PHE A 424       0.063 107.825  -7.713  1.00  0.00           C  
ATOM    179  C   PHE A 424       1.242 108.587  -8.349  1.00  0.00           C  
ATOM    180  O   PHE A 424       1.296 109.804  -8.156  1.00  0.00           O  
ATOM    181  N   PRO A 425       1.952 108.006  -9.345  1.00  0.00           N  
ATOM    182  CA  PRO A 425       2.856 108.759 -10.215  1.00  0.00           C  
ATOM    183  C   PRO A 425       2.186 109.921 -10.957  1.00  0.00           C  
ATOM    184  O   PRO A 425       2.763 111.003 -11.018  1.00  0.00           O  
ATOM    185  N   LEU A 426       0.965 109.743 -11.474  1.00  0.00           N  
ATOM    186  CA  LEU A 426       0.232 110.783 -12.209  1.00  0.00           C  
ATOM    187  C   LEU A 426      -0.262 111.930 -11.312  1.00  0.00           C  
ATOM    188  O   LEU A 426      -0.146 113.083 -11.718  1.00  0.00           O  
ATOM    189  N   LEU A 427      -0.714 111.655 -10.084  1.00  0.00           N  
ATOM    190  CA  LEU A 427      -1.016 112.690  -9.089  1.00  0.00           C  
ATOM    191  C   LEU A 427       0.256 113.446  -8.699  1.00  0.00           C  
ATOM    192  O   LEU A 427       0.288 114.671  -8.767  1.00  0.00           O  
ATOM    193  N   ILE A 428       1.332 112.718  -8.397  1.00  0.00           N  
ATOM    194  CA  ILE A 428       2.619 113.289  -7.988  1.00  0.00           C  
ATOM    195  C   ILE A 428       3.255 114.157  -9.085  1.00  0.00           C  
ATOM    196  O   ILE A 428       3.851 115.191  -8.782  1.00  0.00           O  
ATOM    197  N   GLN A 429       3.025 113.811 -10.353  1.00  0.00           N  
ATOM    198  CA  GLN A 429       3.485 114.569 -11.517  1.00  0.00           C  
ATOM    199  C   GLN A 429       2.960 116.020 -11.509  1.00  0.00           C  
ATOM    200  O   GLN A 429       3.697 116.918 -11.904  1.00  0.00           O  
ATOM    201  N   MET A 430       1.773 116.288 -10.943  1.00  0.00           N  
ATOM    202  CA  MET A 430       1.187 117.636 -10.919  1.00  0.00           C  
ATOM    203  C   MET A 430       1.867 118.630  -9.955  1.00  0.00           C  
ATOM    204  O   MET A 430       2.368 119.645 -10.446  1.00  0.00           O  
ATOM    205  N   PRO A 431       1.985 118.380  -8.631  1.00  0.00           N  
ATOM    206  CA  PRO A 431       2.683 119.303  -7.736  1.00  0.00           C  
ATOM    207  C   PRO A 431       4.140 119.549  -8.132  1.00  0.00           C  
ATOM    208  O   PRO A 431       4.607 120.681  -8.018  1.00  0.00           O  
ATOM    209  N   ILE A 432       4.818 118.551  -8.716  1.00  0.00           N  
ATOM    210  CA  ILE A 432       6.188 118.744  -9.199  1.00  0.00           C  
ATOM    211  C   ILE A 432       6.245 119.542 -10.510  1.00  0.00           C  
ATOM    212  O   ILE A 432       7.052 120.467 -10.560  1.00  0.00           O  
ATOM    213  N   PHE A 433       5.361 119.354 -11.511  1.00  0.00           N  
ATOM    214  CA  PHE A 433       5.427 120.233 -12.697  1.00  0.00           C  
ATOM    215  C   PHE A 433       5.021 121.678 -12.396  1.00  0.00           C  
ATOM    216  O   PHE A 433       5.607 122.606 -12.953  1.00  0.00           O  
ATOM    217  N   LEU A 434       4.111 121.871 -11.433  1.00  0.00           N  
ATOM    218  CA  LEU A 434       3.739 123.191 -10.929  1.00  0.00           C  
ATOM    219  C   LEU A 434       4.925 123.863 -10.234  1.00  0.00           C  
ATOM    220  O   LEU A 434       5.316 124.951 -10.646  1.00  0.00           O  
ATOM    221  N   ALA A 435       5.607 123.165  -9.321  1.00  0.00           N  
ATOM    222  CA  ALA A 435       6.790 123.701  -8.652  1.00  0.00           C  
ATOM    223  C   ALA A 435       7.934 124.010  -9.641  1.00  0.00           C  
ATOM    224  O   ALA A 435       8.459 125.124  -9.623  1.00  0.00           O  
ATOM    225  N   LEU A 436       8.197 123.119 -10.608  1.00  0.00           N  
ATOM    226  CA  LEU A 436       9.192 123.331 -11.668  1.00  0.00           C  
ATOM    227  C   LEU A 436       8.922 124.591 -12.492  1.00  0.00           C  
ATOM    228  O   LEU A 436       9.862 125.327 -12.793  1.00  0.00           O  
ATOM    229  N   TYR A 437       7.693 124.739 -12.993  1.00  0.00           N  
ATOM    230  CA  TYR A 437       7.405 125.642 -14.109  1.00  0.00           C  
ATOM    231  C   TYR A 437       6.614 126.909 -13.752  1.00  0.00           C  
ATOM    232  O   TYR A 437       6.658 127.877 -14.508  1.00  0.00           O  
ATOM    233  N   TYR A 438       6.167 127.014 -12.496  1.00  0.00           N  
ATOM    234  CA  TYR A 438       5.967 128.296 -11.810  1.00  0.00           C  
ATOM    235  C   TYR A 438       7.299 129.017 -11.560  1.00  0.00           C  
ATOM    236  O   TYR A 438       7.446 130.200 -11.845  1.00  0.00           O  
ATOM    237  N   MET A 439       8.309 128.268 -11.106  1.00  0.00           N  
ATOM    238  CA  MET A 439       9.643 128.781 -10.811  1.00  0.00           C  
ATOM    239  C   MET A 439      10.338 129.316 -12.073  1.00  0.00           C  
ATOM    240  O   MET A 439      11.282 130.105 -11.993  1.00  0.00           O  
ATOM    241  N   TYR A 465       6.706 128.259 -28.402  1.00  0.00           N  
ATOM    242  CA  TYR A 465       6.538 127.274 -29.471  1.00  0.00           C  
ATOM    243  C   TYR A 465       7.324 125.967 -29.312  1.00  0.00           C  
ATOM    244  O   TYR A 465       6.805 124.868 -29.509  1.00  0.00           O  
ATOM    245  N   ILE A 466       8.540 126.075 -28.767  1.00  0.00           N  
ATOM    246  CA  ILE A 466       9.492 124.958 -28.745  1.00  0.00           C  
ATOM    247  C   ILE A 466       9.232 123.957 -27.607  1.00  0.00           C  
ATOM    248  O   ILE A 466       9.394 122.753 -27.805  1.00  0.00           O  
ATOM    249  N   LEU A 467       8.753 124.411 -26.442  1.00  0.00           N  
ATOM    250  CA  LEU A 467       8.432 123.510 -25.326  1.00  0.00           C  
ATOM    251  C   LEU A 467       7.181 122.641 -25.604  1.00  0.00           C  
ATOM    252  O   LEU A 467       7.286 121.425 -25.427  1.00  0.00           O  
ATOM    253  N   PRO A 468       6.126 123.157 -26.275  1.00  0.00           N  
ATOM    254  CA  PRO A 468       5.063 122.323 -26.842  1.00  0.00           C  
ATOM    255  C   PRO A 468       5.522 121.297 -27.888  1.00  0.00           C  
ATOM    256  O   PRO A 468       5.052 120.164 -27.828  1.00  0.00           O  
ATOM    257  N   ILE A 469       6.527 121.589 -28.729  1.00  0.00           N  
ATOM    258  CA  ILE A 469       7.110 120.566 -29.626  1.00  0.00           C  
ATOM    259  C   ILE A 469       7.787 119.451 -28.824  1.00  0.00           C  
ATOM    260  O   ILE A 469       7.513 118.273 -29.052  1.00  0.00           O  
ATOM    261  N   LEU A 470       8.631 119.810 -27.853  1.00  0.00           N  
ATOM    262  CA  LEU A 470       9.355 118.843 -27.023  1.00  0.00           C  
ATOM    263  C   LEU A 470       8.391 117.951 -26.226  1.00  0.00           C  
ATOM    264  O   LEU A 470       8.532 116.724 -26.242  1.00  0.00           O  
ATOM    265  N   MET A 471       7.326 118.523 -25.658  1.00  0.00           N  
ATOM    266  CA  MET A 471       6.292 117.750 -24.967  1.00  0.00           C  
ATOM    267  C   MET A 471       5.384 116.963 -25.928  1.00  0.00           C  
ATOM    268  O   MET A 471       5.066 115.814 -25.639  1.00  0.00           O  
ATOM    269  N   GLY A 472       5.147 117.456 -27.145  1.00  0.00           N  
ATOM    270  CA  GLY A 472       4.400 116.759 -28.197  1.00  0.00           C  
ATOM    271  C   GLY A 472       5.122 115.531 -28.762  1.00  0.00           C  
ATOM    272  O   GLY A 472       4.530 114.456 -28.837  1.00  0.00           O  
ATOM    273  N   VAL A 473       6.442 115.610 -28.956  1.00  0.00           N  
ATOM    274  CA  VAL A 473       7.291 114.457 -29.318  1.00  0.00           C  
ATOM    275  C   VAL A 473       7.380 113.467 -28.148  1.00  0.00           C  
ATOM    276  O   VAL A 473       7.141 112.275 -28.348  1.00  0.00           O  
ATOM    277  N   THR A 474       7.488 113.966 -26.909  1.00  0.00           N  
ATOM    278  CA  THR A 474       7.325 113.139 -25.697  1.00  0.00           C  
ATOM    279  C   THR A 474       5.978 112.406 -25.619  1.00  0.00           C  
ATOM    280  O   THR A 474       5.941 111.196 -25.394  1.00  0.00           O  
ATOM    281  N   MET A 475       4.889 113.079 -25.996  1.00  0.00           N  
ATOM    282  CA  MET A 475       3.544 112.509 -26.067  1.00  0.00           C  
ATOM    283  C   MET A 475       3.386 111.484 -27.193  1.00  0.00           C  
ATOM    284  O   MET A 475       2.814 110.425 -26.954  1.00  0.00           O  
ATOM    285  N   PHE A 476       3.989 111.686 -28.367  1.00  0.00           N  
ATOM    286  CA  PHE A 476       3.964 110.667 -29.417  1.00  0.00           C  
ATOM    287  C   PHE A 476       4.654 109.340 -29.085  1.00  0.00           C  
ATOM    288  O   PHE A 476       4.079 108.285 -29.356  1.00  0.00           O  
ATOM    289  N   PHE A 477       5.735 109.373 -28.297  1.00  0.00           N  
ATOM    290  CA  PHE A 477       6.316 108.157 -27.715  1.00  0.00           C  
ATOM    291  C   PHE A 477       5.418 107.493 -26.660  1.00  0.00           C  
ATOM    292  O   PHE A 477       5.257 106.275 -26.682  1.00  0.00           O  
ATOM    293  N   ILE A 478       4.748 108.289 -25.815  1.00  0.00           N  
ATOM    294  CA  ILE A 478       3.799 107.800 -24.796  1.00  0.00           C  
ATOM    295  C   ILE A 478       2.547 107.176 -25.443  1.00  0.00           C  
ATOM    296  O   ILE A 478       2.056 106.145 -24.990  1.00  0.00           O  
ATOM    297  N   GLN A 479       2.075 107.755 -26.547  1.00  0.00           N  
ATOM    298  CA  GLN A 479       0.943 107.278 -27.340  1.00  0.00           C  
ATOM    299  C   GLN A 479       1.276 106.014 -28.151  1.00  0.00           C  
ATOM    300  O   GLN A 479       0.441 105.123 -28.301  1.00  0.00           O  
ATOM    301  N   LYS A 480       2.472 105.955 -28.750  1.00  0.00           N  
ATOM    302  CA  LYS A 480       2.926 104.852 -29.610  1.00  0.00           C  
ATOM    303  C   LYS A 480       2.926 103.519 -28.843  1.00  0.00           C  
ATOM    304  O   LYS A 480       3.045 102.462 -29.479  1.00  0.00           O  
ATOM    305  N   ILE A 494      -7.474 105.856 -19.190  1.00  0.00           N  
ATOM    306  CA  ILE A 494      -7.130 107.051 -18.415  1.00  0.00           C  
ATOM    307  C   ILE A 494      -5.613 107.298 -18.324  1.00  0.00           C  
ATOM    308  O   ILE A 494      -5.207 108.456 -18.408  1.00  0.00           O  
ATOM    309  N   MET A 495      -4.762 106.261 -18.367  1.00  0.00           N  
ATOM    310  CA  MET A 495      -3.316 106.439 -18.102  1.00  0.00           C  
ATOM    311  C   MET A 495      -2.559 107.246 -19.169  1.00  0.00           C  
ATOM    312  O   MET A 495      -1.632 107.967 -18.825  1.00  0.00           O  
ATOM    313  N   THR A 496      -3.036 107.260 -20.417  1.00  0.00           N  
ATOM    314  CA  THR A 496      -2.640 108.235 -21.455  1.00  0.00           C  
ATOM    315  C   THR A 496      -3.388 109.566 -21.429  1.00  0.00           C  
ATOM    316  O   THR A 496      -2.826 110.621 -21.697  1.00  0.00           O  
ATOM    317  N   PHE A 497      -4.678 109.511 -21.101  1.00  0.00           N  
ATOM    318  CA  PHE A 497      -5.599 110.648 -21.111  1.00  0.00           C  
ATOM    319  C   PHE A 497      -5.291 111.764 -20.100  1.00  0.00           C  
ATOM    320  O   PHE A 497      -5.305 112.932 -20.474  1.00  0.00           O  
ATOM    321  N   MET A 498      -4.767 111.410 -18.921  1.00  0.00           N  
ATOM    322  CA  MET A 498      -4.298 112.394 -17.929  1.00  0.00           C  
ATOM    323  C   MET A 498      -2.988 113.108 -18.325  1.00  0.00           C  
ATOM    324  O   MET A 498      -3.022 114.332 -18.422  1.00  0.00           O  
ATOM    325  N   PRO A 499      -1.960 112.411 -18.857  1.00  0.00           N  
ATOM    326  CA  PRO A 499      -0.837 113.045 -19.554  1.00  0.00           C  
ATOM    327  C   PRO A 499      -1.219 113.913 -20.757  1.00  0.00           C  
ATOM    328  O   PRO A 499      -0.562 114.923 -21.007  1.00  0.00           O  
ATOM    329  N   VAL A 500      -2.295 113.586 -21.479  1.00  0.00           N  
ATOM    330  CA  VAL A 500      -2.812 114.460 -22.540  1.00  0.00           C  
ATOM    331  C   VAL A 500      -3.472 115.714 -21.949  1.00  0.00           C  
ATOM    332  O   VAL A 500      -3.124 116.800 -22.395  1.00  0.00           O  
ATOM    333  N   ILE A 501      -4.264 115.631 -20.874  1.00  0.00           N  
ATOM    334  CA  ILE A 501      -4.806 116.828 -20.195  1.00  0.00           C  
ATOM    335  C   ILE A 501      -3.685 117.703 -19.600  1.00  0.00           C  
ATOM    336  O   ILE A 501      -3.679 118.911 -19.828  1.00  0.00           O  
ATOM    337  N   PHE A 502      -2.642 117.095 -19.021  1.00  0.00           N  
ATOM    338  CA  PHE A 502      -1.437 117.811 -18.581  1.00  0.00           C  
ATOM    339  C   PHE A 502      -0.711 118.514 -19.736  1.00  0.00           C  
ATOM    340  O   PHE A 502      -0.323 119.673 -19.612  1.00  0.00           O  
ATOM    341  N   THR A 503      -0.644 117.855 -20.899  1.00  0.00           N  
ATOM    342  CA  THR A 503      -0.141 118.459 -22.139  1.00  0.00           C  
ATOM    343  C   THR A 503      -0.985 119.651 -22.565  1.00  0.00           C  
ATOM    344  O   THR A 503      -0.409 120.713 -22.748  1.00  0.00           O  
ATOM    345  N   VAL A 504      -2.320 119.561 -22.545  1.00  0.00           N  
ATOM    346  CA  VAL A 504      -3.201 120.684 -22.917  1.00  0.00           C  
ATOM    347  C   VAL A 504      -3.027 121.894 -22.005  1.00  0.00           C  
ATOM    348  O   VAL A 504      -2.865 123.000 -22.514  1.00  0.00           O  
ATOM    349  N   PHE A 505      -2.915 121.699 -20.690  1.00  0.00           N  
ATOM    350  CA  PHE A 505      -2.551 122.805 -19.801  1.00  0.00           C  
ATOM    351  C   PHE A 505      -1.212 123.475 -20.144  1.00  0.00           C  
ATOM    352  O   PHE A 505      -1.091 124.697 -20.103  1.00  0.00           O  
ATOM    353  N   PHE A 506      -0.229 122.683 -20.576  1.00  0.00           N  
ATOM    354  CA  PHE A 506       1.109 123.172 -20.907  1.00  0.00           C  
ATOM    355  C   PHE A 506       1.161 123.880 -22.273  1.00  0.00           C  
ATOM    356  O   PHE A 506       2.028 124.721 -22.490  1.00  0.00           O  
ATOM    357  N   LEU A 507       0.217 123.614 -23.177  1.00  0.00           N  
ATOM    358  CA  LEU A 507       0.061 124.393 -24.405  1.00  0.00           C  
ATOM    359  C   LEU A 507      -0.428 125.833 -24.133  1.00  0.00           C  
ATOM    360  O   LEU A 507      -0.044 126.748 -24.854  1.00  0.00           O  
ATOM    361  N   TRP A 508      -1.250 126.024 -23.092  1.00  0.00           N  
ATOM    362  CA  TRP A 508      -1.753 127.329 -22.637  1.00  0.00           C  
ATOM    363  C   TRP A 508      -0.755 128.080 -21.739  1.00  0.00           C  
ATOM    364  O   TRP A 508      -0.630 129.298 -21.847  1.00  0.00           O  
ATOM    365  N   PHE A 509       0.077 127.347 -20.989  1.00  0.00           N  
ATOM    366  CA  PHE A 509       1.062 127.916 -20.062  1.00  0.00           C  
ATOM    367  C   PHE A 509       2.545 127.529 -20.330  1.00  0.00           C  
ATOM    368  O   PHE A 509       3.208 127.051 -19.401  1.00  0.00           O  
ATOM    369  N   PRO A 510       3.123 127.686 -21.546  1.00  0.00           N  
ATOM    370  CA  PRO A 510       4.537 127.376 -21.774  1.00  0.00           C  
ATOM    371  C   PRO A 510       5.479 128.156 -20.843  1.00  0.00           C  
ATOM    372  O   PRO A 510       5.552 129.381 -20.886  1.00  0.00           O  
ATOM    373  N   SER A 511       6.302 127.423 -20.094  1.00  0.00           N  
ATOM    374  CA  SER A 511       7.281 127.962 -19.146  1.00  0.00           C  
ATOM    375  C   SER A 511       8.437 126.974 -18.947  1.00  0.00           C  
ATOM    376  O   SER A 511       8.277 125.769 -19.160  1.00  0.00           O  
ATOM    377  N   GLY A 512       9.624 127.485 -18.609  1.00  0.00           N  
ATOM    378  CA  GLY A 512      10.871 126.721 -18.525  1.00  0.00           C  
ATOM    379  C   GLY A 512      11.957 127.183 -19.504  1.00  0.00           C  
ATOM    380  O   GLY A 512      11.775 128.104 -20.296  1.00  0.00           O  
ATOM    381  N   LEU A 513      13.104 126.501 -19.463  1.00  0.00           N  
ATOM    382  CA  LEU A 513      14.276 126.763 -20.306  1.00  0.00           C  
ATOM    383  C   LEU A 513      14.680 125.477 -21.038  1.00  0.00           C  
ATOM    384  O   LEU A 513      14.750 124.411 -20.425  1.00  0.00           O  
ATOM    385  N   VAL A 514      15.008 125.597 -22.330  1.00  0.00           N  
ATOM    386  CA  VAL A 514      15.098 124.470 -23.283  1.00  0.00           C  
ATOM    387  C   VAL A 514      16.014 123.344 -22.796  1.00  0.00           C  
ATOM    388  O   VAL A 514      15.554 122.209 -22.702  1.00  0.00           O  
ATOM    389  N   LEU A 515      17.246 123.651 -22.368  1.00  0.00           N  
ATOM    390  CA  LEU A 515      18.203 122.635 -21.907  1.00  0.00           C  
ATOM    391  C   LEU A 515      17.660 121.818 -20.725  1.00  0.00           C  
ATOM    392  O   LEU A 515      17.680 120.589 -20.762  1.00  0.00           O  
ATOM    393  N   TYR A 516      17.100 122.489 -19.715  1.00  0.00           N  
ATOM    394  CA  TYR A 516      16.514 121.796 -18.572  1.00  0.00           C  
ATOM    395  C   TYR A 516      15.224 121.018 -18.871  1.00  0.00           C  
ATOM    396  O   TYR A 516      15.059 119.881 -18.429  1.00  0.00           O  
ATOM    397  N   TYR A 517      14.382 121.560 -19.755  1.00  0.00           N  
ATOM    398  CA  TYR A 517      13.122 120.924 -20.145  1.00  0.00           C  
ATOM    399  C   TYR A 517      13.447 119.645 -20.945  1.00  0.00           C  
ATOM    400  O   TYR A 517      12.845 118.605 -20.678  1.00  0.00           O  
ATOM    401  N   ILE A 518      14.501 119.649 -21.777  1.00  0.00           N  
ATOM    402  CA  ILE A 518      15.016 118.439 -22.441  1.00  0.00           C  
ATOM    403  C   ILE A 518      15.497 117.400 -21.422  1.00  0.00           C  
ATOM    404  O   ILE A 518      15.114 116.243 -21.543  1.00  0.00           O  
ATOM    405  N   VAL A 519      16.245 117.789 -20.381  1.00  0.00           N  
ATOM    406  CA  VAL A 519      16.712 116.850 -19.338  1.00  0.00           C  
ATOM    407  C   VAL A 519      15.522 116.248 -18.577  1.00  0.00           C  
ATOM    408  O   VAL A 519      15.432 115.025 -18.469  1.00  0.00           O  
ATOM    409  N   SER A 520      14.542 117.058 -18.167  1.00  0.00           N  
ATOM    410  CA  SER A 520      13.353 116.574 -17.449  1.00  0.00           C  
ATOM    411  C   SER A 520      12.492 115.636 -18.310  1.00  0.00           C  
ATOM    412  O   SER A 520      12.118 114.550 -17.858  1.00  0.00           O  
ATOM    413  N   ASN A 521      12.337 115.936 -19.605  1.00  0.00           N  
ATOM    414  CA  ASN A 521      11.618 115.072 -20.545  1.00  0.00           C  
ATOM    415  C   ASN A 521      12.410 113.848 -21.028  1.00  0.00           C  
ATOM    416  O   ASN A 521      11.803 112.802 -21.245  1.00  0.00           O  
ATOM    417  N   LEU A 522      13.743 113.886 -21.034  1.00  0.00           N  
ATOM    418  CA  LEU A 522      14.589 112.714 -21.274  1.00  0.00           C  
ATOM    419  C   LEU A 522      14.523 111.719 -20.109  1.00  0.00           C  
ATOM    420  O   LEU A 522      14.328 110.525 -20.341  1.00  0.00           O  
ATOM    421  N   VAL A 523      14.447 112.220 -18.872  1.00  0.00           N  
ATOM    422  CA  VAL A 523      14.107 111.390 -17.707  1.00  0.00           C  
ATOM    423  C   VAL A 523      12.650 110.901 -17.770  1.00  0.00           C  
ATOM    424  O   VAL A 523      12.422 109.723 -17.527  1.00  0.00           O  
ATOM    425  N   THR A 524      11.713 111.637 -18.384  1.00  0.00           N  
ATOM    426  CA  THR A 524      10.425 111.047 -18.822  1.00  0.00           C  
ATOM    427  C   THR A 524      10.530 109.907 -19.827  1.00  0.00           C  
ATOM    428  O   THR A 524       9.916 108.867 -19.612  1.00  0.00           O  
ATOM    429  N   ILE A 525      11.363 110.033 -20.859  1.00  0.00           N  
ATOM    430  CA  ILE A 525      11.542 108.986 -21.872  1.00  0.00           C  
ATOM    431  C   ILE A 525      12.114 107.705 -21.255  1.00  0.00           C  
ATOM    432  O   ILE A 525      11.509 106.655 -21.450  1.00  0.00           O  
ATOM    433  N   ILE A 526      13.144 107.779 -20.401  1.00  0.00           N  
ATOM    434  CA  ILE A 526      13.702 106.580 -19.740  1.00  0.00           C  
ATOM    435  C   ILE A 526      12.807 106.049 -18.609  1.00  0.00           C  
ATOM    436  O   ILE A 526      12.817 104.844 -18.375  1.00  0.00           O  
ATOM    437  N   GLN A 527      11.962 106.871 -17.971  1.00  0.00           N  
ATOM    438  CA  GLN A 527      10.937 106.369 -17.043  1.00  0.00           C  
ATOM    439  C   GLN A 527       9.798 105.648 -17.780  1.00  0.00           C  
ATOM    440  O   GLN A 527       9.454 104.531 -17.408  1.00  0.00           O  
ATOM    441  N   GLN A 528       9.372 106.149 -18.944  1.00  0.00           N  
ATOM    442  CA  GLN A 528       8.416 105.456 -19.817  1.00  0.00           C  
ATOM    443  C   GLN A 528       8.997 104.185 -20.447  1.00  0.00           C  
ATOM    444  O   GLN A 528       8.317 103.163 -20.460  1.00  0.00           O  
ATOM    445  N   GLN A 529      10.265 104.202 -20.873  1.00  0.00           N  
ATOM    446  CA  GLN A 529      10.971 102.994 -21.316  1.00  0.00           C  
ATOM    447  C   GLN A 529      11.277 102.003 -20.183  1.00  0.00           C  
ATOM    448  O   GLN A 529      11.535 100.849 -20.498  1.00  0.00           O  
ATOM    449  N   LEU A 530      11.181 102.398 -18.903  1.00  0.00           N  
ATOM    450  CA  LEU A 530      11.207 101.447 -17.784  1.00  0.00           C  
ATOM    451  C   LEU A 530       9.819 100.930 -17.364  1.00  0.00           C  
ATOM    452  O   LEU A 530       9.688  99.756 -17.035  1.00  0.00           O  
ATOM    453  N   ILE A 531       8.758 101.749 -17.426  1.00  0.00           N  
ATOM    454  CA  ILE A 531       7.388 101.210 -17.305  1.00  0.00           C  
ATOM    455  C   ILE A 531       7.080 100.272 -18.490  1.00  0.00           C  
ATOM    456  O   ILE A 531       6.344  99.295 -18.345  1.00  0.00           O  
ATOM    457  N   TYR A 532       7.763 100.459 -19.623  1.00  0.00           N  
ATOM    458  CA  TYR A 532       7.884  99.444 -20.661  1.00  0.00           C  
ATOM    459  C   TYR A 532       8.745  98.220 -20.303  1.00  0.00           C  
ATOM    460  O   TYR A 532       9.867  98.326 -19.816  1.00  0.00           O  
TER     461      TYR A 532                                                      
ATOM    462  N   MET Z  11      -1.800 133.891  -4.040  1.00  0.00           N  
ATOM    463  CA  MET Z  11      -2.416 133.346  -5.229  1.00  0.00           C  
ATOM    464  C   MET Z  11      -1.507 132.360  -5.910  1.00  0.00           C  
ATOM    465  O   MET Z  11      -1.971 131.540  -6.694  1.00  0.00           O  
ATOM    466  N   ALA Z  12      -0.185 132.406  -5.601  1.00  0.00           N  
ATOM    467  CA  ALA Z  12       0.812 131.499  -6.093  1.00  0.00           C  
ATOM    468  C   ALA Z  12       0.552 130.112  -5.573  1.00  0.00           C  
ATOM    469  O   ALA Z  12       0.443 129.186  -6.367  1.00  0.00           O  
ATOM    470  N   ALA Z  13       0.416 129.950  -4.231  1.00  0.00           N  
ATOM    471  CA  ALA Z  13       0.013 128.750  -3.542  1.00  0.00           C  
ATOM    472  C   ALA Z  13      -1.331 128.241  -3.945  1.00  0.00           C  
ATOM    473  O   ALA Z  13      -1.579 127.048  -3.840  1.00  0.00           O  
ATOM    474  N   ALA Z  14      -2.245 129.108  -4.424  1.00  0.00           N  
ATOM    475  CA  ALA Z  14      -3.586 128.668  -4.725  1.00  0.00           C  
ATOM    476  C   ALA Z  14      -3.651 128.149  -6.130  1.00  0.00           C  
ATOM    477  O   ALA Z  14      -4.505 127.335  -6.458  1.00  0.00           O  
ATOM    478  N   VAL Z  15      -2.706 128.589  -6.983  1.00  0.00           N  
ATOM    479  CA  VAL Z  15      -2.535 128.114  -8.330  1.00  0.00           C  
ATOM    480  C   VAL Z  15      -1.717 126.847  -8.264  1.00  0.00           C  
ATOM    481  O   VAL Z  15      -1.893 125.953  -9.085  1.00  0.00           O  
ATOM    482  N   MET Z  16      -0.825 126.727  -7.253  1.00  0.00           N  
ATOM    483  CA  MET Z  16       0.043 125.596  -7.071  1.00  0.00           C  
ATOM    484  C   MET Z  16      -0.755 124.473  -6.502  1.00  0.00           C  
ATOM    485  O   MET Z  16      -1.105 123.549  -7.233  1.00  0.00           O  
ATOM    486  N   MET Z  17      -1.059 124.519  -5.182  1.00  0.00           N  
ATOM    487  CA  MET Z  17      -1.685 123.370  -4.543  1.00  0.00           C  
ATOM    488  C   MET Z  17      -3.160 123.311  -4.769  1.00  0.00           C  
ATOM    489  O   MET Z  17      -3.790 122.309  -4.443  1.00  0.00           O  
ATOM    490  N   GLY Z  18      -3.742 124.341  -5.409  1.00  0.00           N  
ATOM    491  CA  GLY Z  18      -5.081 124.240  -5.937  1.00  0.00           C  
ATOM    492  C   GLY Z  18      -5.105 123.266  -7.077  1.00  0.00           C  
ATOM    493  O   GLY Z  18      -5.906 122.333  -7.077  1.00  0.00           O  
ATOM    494  N   LEU Z  19      -4.196 123.464  -8.066  1.00  0.00           N  
ATOM    495  CA  LEU Z  19      -4.151 122.707  -9.293  1.00  0.00           C  
ATOM    496  C   LEU Z  19      -3.839 121.259  -9.045  1.00  0.00           C  
ATOM    497  O   LEU Z  19      -4.588 120.383  -9.471  1.00  0.00           O  
ATOM    498  N   ALA Z  20      -2.681 120.971  -8.404  1.00  0.00           N  
ATOM    499  CA  ALA Z  20      -2.210 119.613  -8.295  1.00  0.00           C  
ATOM    500  C   ALA Z  20      -2.916 118.826  -7.259  1.00  0.00           C  
ATOM    501  O   ALA Z  20      -3.259 117.686  -7.528  1.00  0.00           O  
ATOM    502  N   ALA Z  21      -3.090 119.366  -6.029  1.00  0.00           N  
ATOM    503  CA  ALA Z  21      -3.789 118.668  -4.973  1.00  0.00           C  
ATOM    504  C   ALA Z  21      -5.203 118.236  -5.295  1.00  0.00           C  
ATOM    505  O   ALA Z  21      -5.696 117.289  -4.686  1.00  0.00           O  
ATOM    506  N   ILE Z  22      -5.902 118.911  -6.252  1.00  0.00           N  
ATOM    507  CA  ILE Z  22      -7.196 118.418  -6.698  1.00  0.00           C  
ATOM    508  C   ILE Z  22      -7.049 117.335  -7.724  1.00  0.00           C  
ATOM    509  O   ILE Z  22      -7.877 116.430  -7.774  1.00  0.00           O  
ATOM    510  N   GLY Z  23      -5.993 117.408  -8.565  1.00  0.00           N  
ATOM    511  CA  GLY Z  23      -5.674 116.432  -9.591  1.00  0.00           C  
ATOM    512  C   GLY Z  23      -5.268 115.121  -8.984  1.00  0.00           C  
ATOM    513  O   GLY Z  23      -5.588 114.045  -9.492  1.00  0.00           O  
ATOM    514  N   ALA Z  24      -4.570 115.220  -7.835  1.00  0.00           N  
ATOM    515  CA  ALA Z  24      -4.275 114.190  -6.884  1.00  0.00           C  
ATOM    516  C   ALA Z  24      -5.534 113.579  -6.388  1.00  0.00           C  
ATOM    517  O   ALA Z  24      -5.693 112.370  -6.459  1.00  0.00           O  
ATOM    518  N   ALA Z  25      -6.466 114.429  -5.892  1.00  0.00           N  
ATOM    519  CA  ALA Z  25      -7.660 113.995  -5.190  1.00  0.00           C  
ATOM    520  C   ALA Z  25      -8.529 113.114  -6.046  1.00  0.00           C  
ATOM    521  O   ALA Z  25      -8.979 112.058  -5.603  1.00  0.00           O  
ATOM    522  N   ILE Z  26      -8.755 113.534  -7.314  1.00  0.00           N  
ATOM    523  CA  ILE Z  26      -9.531 112.785  -8.272  1.00  0.00           C  
ATOM    524  C   ILE Z  26      -8.868 111.548  -8.777  1.00  0.00           C  
ATOM    525  O   ILE Z  26      -9.566 110.682  -9.278  1.00  0.00           O  
ATOM    526  N   GLY Z  27      -7.533 111.428  -8.709  1.00  0.00           N  
ATOM    527  CA  GLY Z  27      -6.868 110.294  -9.297  1.00  0.00           C  
ATOM    528  C   GLY Z  27      -6.702 109.187  -8.340  1.00  0.00           C  
ATOM    529  O   GLY Z  27      -6.772 108.025  -8.704  1.00  0.00           O  
ATOM    530  N   ILE Z  28      -6.531 109.509  -7.050  1.00  0.00           N  
ATOM    531  CA  ILE Z  28      -6.648 108.562  -5.961  1.00  0.00           C  
ATOM    532  C   ILE Z  28      -8.024 107.982  -6.002  1.00  0.00           C  
ATOM    533  O   ILE Z  28      -8.227 106.794  -5.749  1.00  0.00           O  
ATOM    534  N   GLY Z  29      -8.998 108.853  -6.359  1.00  0.00           N  
ATOM    535  CA  GLY Z  29     -10.369 108.517  -6.320  1.00  0.00           C  
ATOM    536  C   GLY Z  29     -10.697 107.634  -7.497  1.00  0.00           C  
ATOM    537  O   GLY Z  29     -11.328 106.593  -7.327  1.00  0.00           O  
ATOM    538  N   ILE Z  30     -10.314 108.066  -8.731  1.00  0.00           N  
ATOM    539  CA  ILE Z  30     -10.573 107.348  -9.968  1.00  0.00           C  
ATOM    540  C   ILE Z  30      -9.833 106.052 -10.042  1.00  0.00           C  
ATOM    541  O   ILE Z  30     -10.441 104.984 -10.052  1.00  0.00           O  
ATOM    542  N   LEU Z  31      -8.484 106.150 -10.121  1.00  0.00           N  
ATOM    543  CA  LEU Z  31      -7.577 105.070 -10.337  1.00  0.00           C  
ATOM    544  C   LEU Z  31      -7.637 104.135  -9.180  1.00  0.00           C  
ATOM    545  O   LEU Z  31      -7.994 102.987  -9.394  1.00  0.00           O  
ATOM    546  N   GLY Z  32      -7.360 104.599  -7.939  1.00  0.00           N  
ATOM    547  CA  GLY Z  32      -7.372 103.775  -6.755  1.00  0.00           C  
ATOM    548  C   GLY Z  32      -8.732 103.228  -6.400  1.00  0.00           C  
ATOM    549  O   GLY Z  32      -8.814 102.272  -5.630  1.00  0.00           O  
ATOM    550  N   GLY Z  33      -9.836 103.797  -6.962  1.00  0.00           N  
ATOM    551  CA  GLY Z  33     -11.162 103.260  -6.761  1.00  0.00           C  
ATOM    552  C   GLY Z  33     -11.377 102.048  -7.624  1.00  0.00           C  
ATOM    553  O   GLY Z  33     -11.924 101.044  -7.172  1.00  0.00           O  
TER     554      GLY Z  33                                                      
MASTER      757    0    0    7    0    0    0    6  552    2    0   50          
END                                                                             
