HEADER    VIRAL PROTEIN                           20-MAY-05   2BSG              
TITLE     THE MODELED STRUCTURE OF FIBRITIN (GPWAC) OF BACTERIOPHAGE T4 BASED ON
TITLE    2 CRYO-EM RECONSTRUCTION OF THE EXTENDED TAIL OF BACTERIOPHAGE T4      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: FIBRITIN;                                                  
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 SYNONYM: WHISKER ANTIGEN CONTROL PROTEIN, COLLAR PROTEIN;            
COMPND   5 OTHER_DETAILS: THE PROTEIN WAS MODELED WITH SEGMENTS OF TRIPLE       
COMPND   6 HELICAL COILED COIL ARRANGED ALONG CRYO-EM DENSITY ASSIGNED TO       
COMPND   7 FIBRITIN                                                             
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACTERIOPHAGE T4;                               
SOURCE   3 ORGANISM_TAXID: 10665                                                
KEYWDS    VIRAL PROTEIN, ATTACHMENT PROTEIN, BACTERIOPHAGE ASSEMBLY,            
KEYWDS   2 BACTERIOPHAGE T4, CHAPERONE, FIBRITIN, STRUCTURAL PROTEIN            
EXPDTA    ELECTRON MICROSCOPY                                                   
MDLTYP    CA ATOMS ONLY, CHAIN A, B, C                                          
AUTHOR    V.A.KOSTYUCHENKO,P.R.CHIPMAN,P.G.LEIMAN,F.ARISAKA,V.V.MESYANZHINOV,   
AUTHOR   2 M.G.ROSSMANN                                                         
REVDAT   6   23-OCT-19 2BSG    1       CRYST1                                   
REVDAT   5   30-AUG-17 2BSG    1       REMARK                                   
REVDAT   4   15-JAN-14 2BSG    1       REMARK VERSN  DBREF                      
REVDAT   3   24-FEB-09 2BSG    1       VERSN                                    
REVDAT   2   13-DEC-05 2BSG    1       REMARK SEQRES                            
REVDAT   1   21-SEP-05 2BSG    0                                                
JRNL        AUTH   V.A.KOSTYUCHENKO,P.R.CHIPMAN,P.G.LEIMAN,F.ARISAKA,           
JRNL        AUTH 2 V.V.MESYANZHINOV,M.G.ROSSMANN                                
JRNL        TITL   THE TAIL STRUCTURE OF BACTERIOPHAGE T4 AND ITS MECHANISM OF  
JRNL        TITL 2 CONTRACTION.                                                 
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  12   810 2005              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   16116440                                                     
JRNL        DOI    10.1038/NSMB975                                              
REMARK   2                                                                      
REMARK   2 RESOLUTION.   15.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   SOFTWARE PACKAGES      : XFIT, SPIDER                              
REMARK   3   RECONSTRUCTION SCHEMA  : NULL                                      
REMARK   3                                                                      
REMARK   3 EM MAP-MODEL FITTING AND REFINEMENT                                  
REMARK   3   PDB ENTRY                    : 1AA0                                
REMARK   3   REFINEMENT SPACE             : REAL                                
REMARK   3   REFINEMENT PROTOCOL          : OTHER                               
REMARK   3   REFINEMENT TARGET            : NULL                                
REMARK   3   OVERALL ANISOTROPIC B VALUE  : NULL                                
REMARK   3                                                                      
REMARK   3 FITTING PROCEDURE : REFINEMENT PROTOCOL--MANUAL FITTING              
REMARK   3                                                                      
REMARK   3 EM IMAGE RECONSTRUCTION STATISTICS                                   
REMARK   3   NOMINAL PIXEL SIZE (ANGSTROMS)    : 3.970                          
REMARK   3   ACTUAL PIXEL SIZE  (ANGSTROMS)    : NULL                           
REMARK   3   EFFECTIVE RESOLUTION (ANGSTROMS)  : 15.00                          
REMARK   3   NUMBER OF PARTICLES               : 3029                           
REMARK   3   CTF CORRECTION METHOD             : NULL                           
REMARK   3                                                                      
REMARK   3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: 47000                   
REMARK   3                                                                      
REMARK   3 OTHER DETAILS: EM MAP DEPOSITED AS EMD-1126                          
REMARK   4                                                                      
REMARK   4 2BSG 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_1290024148.                                   
REMARK 245                                                                      
REMARK 245 EXPERIMENTAL DETAILS                                                 
REMARK 245   RECONSTRUCTION METHOD          : HELICAL                           
REMARK 245   SPECIMEN TYPE                  : VITREOUS ICE (CRYO EM)            
REMARK 245                                                                      
REMARK 245 ELECTRON MICROSCOPE SAMPLE                                           
REMARK 245   SAMPLE TYPE                    : FILAMENT                          
REMARK 245   PARTICLE TYPE                  : POINT                             
REMARK 245   NAME OF SAMPLE                 : T4 EXTENDED TAIL                  
REMARK 245   SAMPLE CONCENTRATION (MG ML-1) : NULL                              
REMARK 245   SAMPLE SUPPORT DETAILS         : COPPER GRID                       
REMARK 245   SAMPLE VITRIFICATION DETAILS   : LIQUID ETHANE                     
REMARK 245   SAMPLE BUFFER                  : NULL                              
REMARK 245   PH                             : 7.00                              
REMARK 245   SAMPLE DETAILS                 : NULL                              
REMARK 245                                                                      
REMARK 245 DATA ACQUISITION                                                     
REMARK 245   DATE OF EXPERIMENT                : 10-JAN-03                      
REMARK 245   NUMBER OF MICROGRAPHS-IMAGES      : NULL                           
REMARK 245   TEMPERATURE (KELVIN)              : 100.00                         
REMARK 245   MICROSCOPE MODEL                  : FEI/PHILIPS CM300FEG/T         
REMARK 245   DETECTOR TYPE                     : KODAK SO-163 FILM              
REMARK 245   MINIMUM DEFOCUS (NM)              : 800.00                         
REMARK 245   MAXIMUM DEFOCUS (NM)              : 3200.00                        
REMARK 245   MINIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   MAXIMUM TILT ANGLE (DEGREES)      : NULL                           
REMARK 245   NOMINAL CS                        : 2.00                           
REMARK 245   IMAGING MODE                      : BRIGHT FIELD                   
REMARK 245   ELECTRON DOSE (ELECTRONS NM**-2)  : NULL                           
REMARK 245   ILLUMINATION MODE                 : SPOT SCAN                      
REMARK 245   NOMINAL MAGNIFICATION             : 45000                          
REMARK 245   CALIBRATED MAGNIFICATION          : 47000                          
REMARK 245   SOURCE                            : FIELD EMISSION GUN             
REMARK 245   ACCELERATION VOLTAGE (KV)         : 300                            
REMARK 245   IMAGING DETAILS                   : NULL                           
REMARK 247                                                                      
REMARK 247 ELECTRON MICROSCOPY                                                  
REMARK 247  THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON          
REMARK 247  MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE              
REMARK 247  THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES           
REMARK 247  ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION         
REMARK 247  OF THE STRUCTURE FACTORS.                                           
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     0                                                      
REMARK 465     THR A     1                                                      
REMARK 465     GLY A    81                                                      
REMARK 465     ILE A    82                                                      
REMARK 465     LEU A    83                                                      
REMARK 465     ASP A    84                                                      
REMARK 465     VAL A    85                                                      
REMARK 465     SER A    86                                                      
REMARK 465     GLY A    87                                                      
REMARK 465     ASP A    88                                                      
REMARK 465     ILE A    89                                                      
REMARK 465     GLU A    90                                                      
REMARK 465     ALA A    91                                                      
REMARK 465     LEU A    92                                                      
REMARK 465     ALA A    93                                                      
REMARK 465     GLN A    94                                                      
REMARK 465     ILE A    95                                                      
REMARK 465     GLY A    96                                                      
REMARK 465     GLY A   131                                                      
REMARK 465     PRO A   132                                                      
REMARK 465     PHE A   133                                                      
REMARK 465     ASN A   134                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     GLU A   136                                                      
REMARK 465     ALA A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     SER A   139                                                      
REMARK 465     VAL A   140                                                      
REMARK 465     TYR A   141                                                      
REMARK 465     ARG A   142                                                      
REMARK 465     THR A   143                                                      
REMARK 465     GLY A   156                                                      
REMARK 465     GLN A   157                                                      
REMARK 465     TYR A   158                                                      
REMARK 465     THR A   159                                                      
REMARK 465     GLY A   160                                                      
REMARK 465     GLN A   161                                                      
REMARK 465     ASP A   162                                                      
REMARK 465     ILE A   163                                                      
REMARK 465     ASN A   164                                                      
REMARK 465     GLY A   165                                                      
REMARK 465     LEU A   166                                                      
REMARK 465     PRO A   167                                                      
REMARK 465     VAL A   168                                                      
REMARK 465     VAL A   169                                                      
REMARK 465     GLY A   170                                                      
REMARK 465     ASN A   171                                                      
REMARK 465     PRO A   172                                                      
REMARK 465     SER A   173                                                      
REMARK 465     SER A   174                                                      
REMARK 465     GLY A   175                                                      
REMARK 465     SER A   195                                                      
REMARK 465     GLU A   196                                                      
REMARK 465     LEU A   197                                                      
REMARK 465     GLU A   198                                                      
REMARK 465     THR A   199                                                      
REMARK 465     LYS A   200                                                      
REMARK 465     PHE A   201                                                      
REMARK 465     ILE A   202                                                      
REMARK 465     GLU A   203                                                      
REMARK 465     SER A   204                                                      
REMARK 465     ASP A   205                                                      
REMARK 465     VAL A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     GLY A   221                                                      
REMARK 465     PRO A   222                                                      
REMARK 465     LYS A   223                                                      
REMARK 465     PRO A   224                                                      
REMARK 465     PRO A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     PHE A   227                                                      
REMARK 465     SER A   228                                                      
REMARK 465     GLN A   229                                                      
REMARK 465     ASN A   230                                                      
REMARK 465     GLY A   257                                                      
REMARK 465     TYR A   258                                                      
REMARK 465     PRO A   259                                                      
REMARK 465     GLY A   260                                                      
REMARK 465     ASN A   261                                                      
REMARK 465     ASN A   262                                                      
REMARK 465     LEU A   282                                                      
REMARK 465     ASN A   283                                                      
REMARK 465     GLN A   284                                                      
REMARK 465     SER A   285                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     GLY A   287                                                      
REMARK 465     GLY A   300                                                      
REMARK 465     SER A   301                                                      
REMARK 465     ASP A   302                                                      
REMARK 465     ASP A   303                                                      
REMARK 465     ILE A   304                                                      
REMARK 465     PRO A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     SER A   307                                                      
REMARK 465     GLU A   320                                                      
REMARK 465     SER A   321                                                      
REMARK 465     LEU A   322                                                      
REMARK 465     ASN A   323                                                      
REMARK 465     GLY A   324                                                      
REMARK 465     ILE A   325                                                      
REMARK 465     VAL A   326                                                      
REMARK 465     GLY A   327                                                      
REMARK 465     GLU A   328                                                      
REMARK 465     ASN A   329                                                      
REMARK 465     THR A   330                                                      
REMARK 465     SER A   331                                                      
REMARK 465     SER A   332                                                      
REMARK 465     GLY A   333                                                      
REMARK 465     GLY A   346                                                      
REMARK 465     THR A   347                                                      
REMARK 465     ASP A   348                                                      
REMARK 465     SER A   349                                                      
REMARK 465     SER A   350                                                      
REMARK 465     GLY A   351                                                      
REMARK 465     GLY A   352                                                      
REMARK 465     GLN A   353                                                      
REMARK 465     PRO A   354                                                      
REMARK 465     SER A   355                                                      
REMARK 465     PRO A   356                                                      
REMARK 465     PRO A   357                                                      
REMARK 465     GLY A   358                                                      
REMARK 465     SER A   484                                                      
REMARK 465     PRO A   485                                                      
REMARK 465     ALA A   486                                                      
REMARK 465     MET B     0                                                      
REMARK 465     THR B     1                                                      
REMARK 465     GLY B    81                                                      
REMARK 465     ILE B    82                                                      
REMARK 465     LEU B    83                                                      
REMARK 465     ASP B    84                                                      
REMARK 465     VAL B    85                                                      
REMARK 465     SER B    86                                                      
REMARK 465     GLY B    87                                                      
REMARK 465     ASP B    88                                                      
REMARK 465     ILE B    89                                                      
REMARK 465     GLU B    90                                                      
REMARK 465     ALA B    91                                                      
REMARK 465     LEU B    92                                                      
REMARK 465     ALA B    93                                                      
REMARK 465     GLN B    94                                                      
REMARK 465     ILE B    95                                                      
REMARK 465     GLY B    96                                                      
REMARK 465     GLY B   131                                                      
REMARK 465     PRO B   132                                                      
REMARK 465     PHE B   133                                                      
REMARK 465     ASN B   134                                                      
REMARK 465     ALA B   135                                                      
REMARK 465     GLU B   136                                                      
REMARK 465     ALA B   137                                                      
REMARK 465     ASN B   138                                                      
REMARK 465     SER B   139                                                      
REMARK 465     VAL B   140                                                      
REMARK 465     TYR B   141                                                      
REMARK 465     ARG B   142                                                      
REMARK 465     THR B   143                                                      
REMARK 465     GLY B   156                                                      
REMARK 465     GLN B   157                                                      
REMARK 465     TYR B   158                                                      
REMARK 465     THR B   159                                                      
REMARK 465     GLY B   160                                                      
REMARK 465     GLN B   161                                                      
REMARK 465     ASP B   162                                                      
REMARK 465     ILE B   163                                                      
REMARK 465     ASN B   164                                                      
REMARK 465     GLY B   165                                                      
REMARK 465     LEU B   166                                                      
REMARK 465     PRO B   167                                                      
REMARK 465     VAL B   168                                                      
REMARK 465     VAL B   169                                                      
REMARK 465     GLY B   170                                                      
REMARK 465     ASN B   171                                                      
REMARK 465     PRO B   172                                                      
REMARK 465     SER B   173                                                      
REMARK 465     SER B   174                                                      
REMARK 465     GLY B   175                                                      
REMARK 465     SER B   195                                                      
REMARK 465     GLU B   196                                                      
REMARK 465     LEU B   197                                                      
REMARK 465     GLU B   198                                                      
REMARK 465     THR B   199                                                      
REMARK 465     LYS B   200                                                      
REMARK 465     PHE B   201                                                      
REMARK 465     ILE B   202                                                      
REMARK 465     GLU B   203                                                      
REMARK 465     SER B   204                                                      
REMARK 465     ASP B   205                                                      
REMARK 465     VAL B   206                                                      
REMARK 465     GLY B   207                                                      
REMARK 465     GLY B   221                                                      
REMARK 465     PRO B   222                                                      
REMARK 465     LYS B   223                                                      
REMARK 465     PRO B   224                                                      
REMARK 465     PRO B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     PHE B   227                                                      
REMARK 465     SER B   228                                                      
REMARK 465     GLN B   229                                                      
REMARK 465     ASN B   230                                                      
REMARK 465     GLY B   257                                                      
REMARK 465     TYR B   258                                                      
REMARK 465     PRO B   259                                                      
REMARK 465     GLY B   260                                                      
REMARK 465     ASN B   261                                                      
REMARK 465     ASN B   262                                                      
REMARK 465     LEU B   282                                                      
REMARK 465     ASN B   283                                                      
REMARK 465     GLN B   284                                                      
REMARK 465     SER B   285                                                      
REMARK 465     GLY B   286                                                      
REMARK 465     GLY B   287                                                      
REMARK 465     GLY B   300                                                      
REMARK 465     SER B   301                                                      
REMARK 465     ASP B   302                                                      
REMARK 465     ASP B   303                                                      
REMARK 465     ILE B   304                                                      
REMARK 465     PRO B   305                                                      
REMARK 465     SER B   306                                                      
REMARK 465     SER B   307                                                      
REMARK 465     GLU B   320                                                      
REMARK 465     SER B   321                                                      
REMARK 465     LEU B   322                                                      
REMARK 465     ASN B   323                                                      
REMARK 465     GLY B   324                                                      
REMARK 465     ILE B   325                                                      
REMARK 465     VAL B   326                                                      
REMARK 465     GLY B   327                                                      
REMARK 465     GLU B   328                                                      
REMARK 465     ASN B   329                                                      
REMARK 465     THR B   330                                                      
REMARK 465     SER B   331                                                      
REMARK 465     SER B   332                                                      
REMARK 465     GLY B   333                                                      
REMARK 465     GLY B   346                                                      
REMARK 465     THR B   347                                                      
REMARK 465     ASP B   348                                                      
REMARK 465     SER B   349                                                      
REMARK 465     SER B   350                                                      
REMARK 465     GLY B   351                                                      
REMARK 465     GLY B   352                                                      
REMARK 465     GLN B   353                                                      
REMARK 465     PRO B   354                                                      
REMARK 465     SER B   355                                                      
REMARK 465     PRO B   356                                                      
REMARK 465     PRO B   357                                                      
REMARK 465     GLY B   358                                                      
REMARK 465     SER B   484                                                      
REMARK 465     PRO B   485                                                      
REMARK 465     ALA B   486                                                      
REMARK 465     MET C     0                                                      
REMARK 465     THR C     1                                                      
REMARK 465     GLY C    81                                                      
REMARK 465     ILE C    82                                                      
REMARK 465     LEU C    83                                                      
REMARK 465     ASP C    84                                                      
REMARK 465     VAL C    85                                                      
REMARK 465     SER C    86                                                      
REMARK 465     GLY C    87                                                      
REMARK 465     ASP C    88                                                      
REMARK 465     ILE C    89                                                      
REMARK 465     GLU C    90                                                      
REMARK 465     ALA C    91                                                      
REMARK 465     LEU C    92                                                      
REMARK 465     ALA C    93                                                      
REMARK 465     GLN C    94                                                      
REMARK 465     ILE C    95                                                      
REMARK 465     GLY C    96                                                      
REMARK 465     GLY C   131                                                      
REMARK 465     PRO C   132                                                      
REMARK 465     PHE C   133                                                      
REMARK 465     ASN C   134                                                      
REMARK 465     ALA C   135                                                      
REMARK 465     GLU C   136                                                      
REMARK 465     ALA C   137                                                      
REMARK 465     ASN C   138                                                      
REMARK 465     SER C   139                                                      
REMARK 465     VAL C   140                                                      
REMARK 465     TYR C   141                                                      
REMARK 465     ARG C   142                                                      
REMARK 465     THR C   143                                                      
REMARK 465     GLY C   156                                                      
REMARK 465     GLN C   157                                                      
REMARK 465     TYR C   158                                                      
REMARK 465     THR C   159                                                      
REMARK 465     GLY C   160                                                      
REMARK 465     GLN C   161                                                      
REMARK 465     ASP C   162                                                      
REMARK 465     ILE C   163                                                      
REMARK 465     ASN C   164                                                      
REMARK 465     GLY C   165                                                      
REMARK 465     LEU C   166                                                      
REMARK 465     PRO C   167                                                      
REMARK 465     VAL C   168                                                      
REMARK 465     VAL C   169                                                      
REMARK 465     GLY C   170                                                      
REMARK 465     ASN C   171                                                      
REMARK 465     PRO C   172                                                      
REMARK 465     SER C   173                                                      
REMARK 465     SER C   174                                                      
REMARK 465     GLY C   175                                                      
REMARK 465     SER C   195                                                      
REMARK 465     GLU C   196                                                      
REMARK 465     LEU C   197                                                      
REMARK 465     GLU C   198                                                      
REMARK 465     THR C   199                                                      
REMARK 465     LYS C   200                                                      
REMARK 465     PHE C   201                                                      
REMARK 465     ILE C   202                                                      
REMARK 465     GLU C   203                                                      
REMARK 465     SER C   204                                                      
REMARK 465     ASP C   205                                                      
REMARK 465     VAL C   206                                                      
REMARK 465     GLY C   207                                                      
REMARK 465     GLY C   221                                                      
REMARK 465     PRO C   222                                                      
REMARK 465     LYS C   223                                                      
REMARK 465     PRO C   224                                                      
REMARK 465     PRO C   225                                                      
REMARK 465     SER C   226                                                      
REMARK 465     PHE C   227                                                      
REMARK 465     SER C   228                                                      
REMARK 465     GLN C   229                                                      
REMARK 465     ASN C   230                                                      
REMARK 465     GLY C   257                                                      
REMARK 465     TYR C   258                                                      
REMARK 465     PRO C   259                                                      
REMARK 465     GLY C   260                                                      
REMARK 465     ASN C   261                                                      
REMARK 465     ASN C   262                                                      
REMARK 465     LEU C   282                                                      
REMARK 465     ASN C   283                                                      
REMARK 465     GLN C   284                                                      
REMARK 465     SER C   285                                                      
REMARK 465     GLY C   286                                                      
REMARK 465     GLY C   287                                                      
REMARK 465     GLY C   300                                                      
REMARK 465     SER C   301                                                      
REMARK 465     ASP C   302                                                      
REMARK 465     ASP C   303                                                      
REMARK 465     ILE C   304                                                      
REMARK 465     PRO C   305                                                      
REMARK 465     SER C   306                                                      
REMARK 465     SER C   307                                                      
REMARK 465     GLU C   320                                                      
REMARK 465     SER C   321                                                      
REMARK 465     LEU C   322                                                      
REMARK 465     ASN C   323                                                      
REMARK 465     GLY C   324                                                      
REMARK 465     ILE C   325                                                      
REMARK 465     VAL C   326                                                      
REMARK 465     GLY C   327                                                      
REMARK 465     GLU C   328                                                      
REMARK 465     ASN C   329                                                      
REMARK 465     THR C   330                                                      
REMARK 465     SER C   331                                                      
REMARK 465     SER C   332                                                      
REMARK 465     GLY C   333                                                      
REMARK 465     GLY C   346                                                      
REMARK 465     THR C   347                                                      
REMARK 465     ASP C   348                                                      
REMARK 465     SER C   349                                                      
REMARK 465     SER C   350                                                      
REMARK 465     GLY C   351                                                      
REMARK 465     GLY C   352                                                      
REMARK 465     GLN C   353                                                      
REMARK 465     PRO C   354                                                      
REMARK 465     SER C   355                                                      
REMARK 465     PRO C   356                                                      
REMARK 465     PRO C   357                                                      
REMARK 465     GLY C   358                                                      
REMARK 465     SER C   484                                                      
REMARK 465     PRO C   485                                                      
REMARK 465     ALA C   486                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   CA   SER B   370     CA   SER B   372              1.81            
REMARK 500   CA   ILE A   344     CA   LEU A   360              1.84            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AA0   RELATED DB: PDB                                   
REMARK 900 FIBRITIN DELETION MUTANT E (BACTERIOPHAGE T4)                        
REMARK 900 RELATED ID: 1AVY   RELATED DB: PDB                                   
REMARK 900 FIBRITIN DELETION MUTANT M (BACTERIOPHAGE T4)                        
REMARK 900 RELATED ID: 1OX3   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF MINI-FIBRITIN                                   
REMARK 900 RELATED ID: 1RFO   RELATED DB: PDB                                   
REMARK 900 TRIMERIC FOLDON OF THE T4 PHAGEHEAD FIBRITIN                         
REMARK 900 RELATED ID: 1V1H   RELATED DB: PDB                                   
REMARK 900 ADENOVIRUS FIBRE SHAFT SEQUENCE N-TERMINALLY FUSED TO THE            
REMARK 900 BACTERIOPHAGE T4 FIBRITIN FOLDON TRIMERISATION MOTIF WITH A SHORT    
REMARK 900 LINKER                                                               
REMARK 900 RELATED ID: 1V1I   RELATED DB: PDB                                   
REMARK 900 ADENOVIRUS FIBRE SHAFT SEQUENCE N-TERMINALLY FUSED TO THE            
REMARK 900 BACTERIOPHAGE T4 FIBRITIN FOLDON TRIMERISATION MOTIF WITH A LONG     
REMARK 900 LINKER                                                               
REMARK 900 RELATED ID: EMD-1126   RELATED DB: EMDB                              
REMARK 900 THE TAIL STRUCTURE OF BACTERIOPHAGE T4 AND ITS MECHANISM OF          
REMARK 900 CONTRACTION.                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE MODELED STRUCTURE DOES NOT INCLUDE LOOP REGIONS                  
DBREF  2BSG A    0   486  UNP    P10104   WAC_BPT4         1    487             
DBREF  2BSG B    0   486  UNP    P10104   WAC_BPT4         1    487             
DBREF  2BSG C    0   486  UNP    P10104   WAC_BPT4         1    487             
SEQRES   1 A  487  MET THR ASP ILE VAL LEU ASN ASP LEU PRO PHE VAL ASP          
SEQRES   2 A  487  GLY PRO PRO ALA GLU GLY GLN SER ARG ILE SER TRP ILE          
SEQRES   3 A  487  LYS ASN GLY GLU GLU ILE LEU GLY ALA ASP THR GLN TYR          
SEQRES   4 A  487  GLY SER GLU GLY SER MET ASN ARG PRO THR VAL SER VAL          
SEQRES   5 A  487  LEU ARG ASN VAL GLU VAL LEU ASP LYS ASN ILE GLY ILE          
SEQRES   6 A  487  LEU LYS THR SER LEU GLU THR ALA ASN SER ASP ILE LYS          
SEQRES   7 A  487  THR ILE GLN GLY ILE LEU ASP VAL SER GLY ASP ILE GLU          
SEQRES   8 A  487  ALA LEU ALA GLN ILE GLY ILE ASN LYS LYS ASP ILE SER          
SEQRES   9 A  487  ASP LEU LYS THR LEU THR SER GLU HIS THR GLU ILE LEU          
SEQRES  10 A  487  ASN GLY THR ASN ASN THR VAL ASP SER ILE LEU ALA ASP          
SEQRES  11 A  487  ILE GLY PRO PHE ASN ALA GLU ALA ASN SER VAL TYR ARG          
SEQRES  12 A  487  THR ILE ARG ASN ASP LEU LEU TRP ILE LYS ARG GLU LEU          
SEQRES  13 A  487  GLY GLN TYR THR GLY GLN ASP ILE ASN GLY LEU PRO VAL          
SEQRES  14 A  487  VAL GLY ASN PRO SER SER GLY MET LYS HIS ARG ILE ILE          
SEQRES  15 A  487  ASN ASN THR ASP VAL ILE THR SER GLN GLY ILE ARG LEU          
SEQRES  16 A  487  SER GLU LEU GLU THR LYS PHE ILE GLU SER ASP VAL GLY          
SEQRES  17 A  487  SER LEU THR ILE GLU VAL GLY ASN LEU ARG GLU GLU LEU          
SEQRES  18 A  487  GLY PRO LYS PRO PRO SER PHE SER GLN ASN VAL TYR SER          
SEQRES  19 A  487  ARG LEU ASN GLU ILE ASP THR LYS GLN THR THR VAL GLU          
SEQRES  20 A  487  SER ASP ILE SER ALA ILE LYS THR SER ILE GLY TYR PRO          
SEQRES  21 A  487  GLY ASN ASN SER ILE ILE THR SER VAL ASN THR ASN THR          
SEQRES  22 A  487  ASP ASN ILE ALA SER ILE ASN LEU GLU LEU ASN GLN SER          
SEQRES  23 A  487  GLY GLY ILE LYS GLN ARG LEU THR VAL ILE GLU THR SER          
SEQRES  24 A  487  ILE GLY SER ASP ASP ILE PRO SER SER ILE LYS GLY GLN          
SEQRES  25 A  487  ILE LYS ASP ASN THR THR SER ILE GLU SER LEU ASN GLY          
SEQRES  26 A  487  ILE VAL GLY GLU ASN THR SER SER GLY LEU ARG ALA ASN          
SEQRES  27 A  487  VAL SER TRP LEU ASN GLN ILE VAL GLY THR ASP SER SER          
SEQRES  28 A  487  GLY GLY GLN PRO SER PRO PRO GLY SER LEU LEU ASN ARG          
SEQRES  29 A  487  VAL SER THR ILE GLU THR SER VAL SER GLY LEU ASN ASN          
SEQRES  30 A  487  ALA VAL GLN ASN LEU GLN VAL GLU ILE GLY ASN ASN SER          
SEQRES  31 A  487  ALA GLY ILE LYS GLY GLN VAL VAL ALA LEU ASN THR LEU          
SEQRES  32 A  487  VAL ASN GLY THR ASN PRO ASN GLY SER THR VAL GLU GLU          
SEQRES  33 A  487  ARG GLY LEU THR ASN SER ILE LYS ALA ASN GLU THR ASN          
SEQRES  34 A  487  ILE ALA SER VAL THR GLN GLU VAL ASN THR ALA LYS GLY          
SEQRES  35 A  487  ASN ILE SER SER LEU GLN GLY ASP VAL GLN ALA LEU GLN          
SEQRES  36 A  487  GLU ALA GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN          
SEQRES  37 A  487  ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL PHE LEU SER          
SEQRES  38 A  487  THR PHE LEU SER PRO ALA                                      
SEQRES   1 B  487  MET THR ASP ILE VAL LEU ASN ASP LEU PRO PHE VAL ASP          
SEQRES   2 B  487  GLY PRO PRO ALA GLU GLY GLN SER ARG ILE SER TRP ILE          
SEQRES   3 B  487  LYS ASN GLY GLU GLU ILE LEU GLY ALA ASP THR GLN TYR          
SEQRES   4 B  487  GLY SER GLU GLY SER MET ASN ARG PRO THR VAL SER VAL          
SEQRES   5 B  487  LEU ARG ASN VAL GLU VAL LEU ASP LYS ASN ILE GLY ILE          
SEQRES   6 B  487  LEU LYS THR SER LEU GLU THR ALA ASN SER ASP ILE LYS          
SEQRES   7 B  487  THR ILE GLN GLY ILE LEU ASP VAL SER GLY ASP ILE GLU          
SEQRES   8 B  487  ALA LEU ALA GLN ILE GLY ILE ASN LYS LYS ASP ILE SER          
SEQRES   9 B  487  ASP LEU LYS THR LEU THR SER GLU HIS THR GLU ILE LEU          
SEQRES  10 B  487  ASN GLY THR ASN ASN THR VAL ASP SER ILE LEU ALA ASP          
SEQRES  11 B  487  ILE GLY PRO PHE ASN ALA GLU ALA ASN SER VAL TYR ARG          
SEQRES  12 B  487  THR ILE ARG ASN ASP LEU LEU TRP ILE LYS ARG GLU LEU          
SEQRES  13 B  487  GLY GLN TYR THR GLY GLN ASP ILE ASN GLY LEU PRO VAL          
SEQRES  14 B  487  VAL GLY ASN PRO SER SER GLY MET LYS HIS ARG ILE ILE          
SEQRES  15 B  487  ASN ASN THR ASP VAL ILE THR SER GLN GLY ILE ARG LEU          
SEQRES  16 B  487  SER GLU LEU GLU THR LYS PHE ILE GLU SER ASP VAL GLY          
SEQRES  17 B  487  SER LEU THR ILE GLU VAL GLY ASN LEU ARG GLU GLU LEU          
SEQRES  18 B  487  GLY PRO LYS PRO PRO SER PHE SER GLN ASN VAL TYR SER          
SEQRES  19 B  487  ARG LEU ASN GLU ILE ASP THR LYS GLN THR THR VAL GLU          
SEQRES  20 B  487  SER ASP ILE SER ALA ILE LYS THR SER ILE GLY TYR PRO          
SEQRES  21 B  487  GLY ASN ASN SER ILE ILE THR SER VAL ASN THR ASN THR          
SEQRES  22 B  487  ASP ASN ILE ALA SER ILE ASN LEU GLU LEU ASN GLN SER          
SEQRES  23 B  487  GLY GLY ILE LYS GLN ARG LEU THR VAL ILE GLU THR SER          
SEQRES  24 B  487  ILE GLY SER ASP ASP ILE PRO SER SER ILE LYS GLY GLN          
SEQRES  25 B  487  ILE LYS ASP ASN THR THR SER ILE GLU SER LEU ASN GLY          
SEQRES  26 B  487  ILE VAL GLY GLU ASN THR SER SER GLY LEU ARG ALA ASN          
SEQRES  27 B  487  VAL SER TRP LEU ASN GLN ILE VAL GLY THR ASP SER SER          
SEQRES  28 B  487  GLY GLY GLN PRO SER PRO PRO GLY SER LEU LEU ASN ARG          
SEQRES  29 B  487  VAL SER THR ILE GLU THR SER VAL SER GLY LEU ASN ASN          
SEQRES  30 B  487  ALA VAL GLN ASN LEU GLN VAL GLU ILE GLY ASN ASN SER          
SEQRES  31 B  487  ALA GLY ILE LYS GLY GLN VAL VAL ALA LEU ASN THR LEU          
SEQRES  32 B  487  VAL ASN GLY THR ASN PRO ASN GLY SER THR VAL GLU GLU          
SEQRES  33 B  487  ARG GLY LEU THR ASN SER ILE LYS ALA ASN GLU THR ASN          
SEQRES  34 B  487  ILE ALA SER VAL THR GLN GLU VAL ASN THR ALA LYS GLY          
SEQRES  35 B  487  ASN ILE SER SER LEU GLN GLY ASP VAL GLN ALA LEU GLN          
SEQRES  36 B  487  GLU ALA GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN          
SEQRES  37 B  487  ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL PHE LEU SER          
SEQRES  38 B  487  THR PHE LEU SER PRO ALA                                      
SEQRES   1 C  487  MET THR ASP ILE VAL LEU ASN ASP LEU PRO PHE VAL ASP          
SEQRES   2 C  487  GLY PRO PRO ALA GLU GLY GLN SER ARG ILE SER TRP ILE          
SEQRES   3 C  487  LYS ASN GLY GLU GLU ILE LEU GLY ALA ASP THR GLN TYR          
SEQRES   4 C  487  GLY SER GLU GLY SER MET ASN ARG PRO THR VAL SER VAL          
SEQRES   5 C  487  LEU ARG ASN VAL GLU VAL LEU ASP LYS ASN ILE GLY ILE          
SEQRES   6 C  487  LEU LYS THR SER LEU GLU THR ALA ASN SER ASP ILE LYS          
SEQRES   7 C  487  THR ILE GLN GLY ILE LEU ASP VAL SER GLY ASP ILE GLU          
SEQRES   8 C  487  ALA LEU ALA GLN ILE GLY ILE ASN LYS LYS ASP ILE SER          
SEQRES   9 C  487  ASP LEU LYS THR LEU THR SER GLU HIS THR GLU ILE LEU          
SEQRES  10 C  487  ASN GLY THR ASN ASN THR VAL ASP SER ILE LEU ALA ASP          
SEQRES  11 C  487  ILE GLY PRO PHE ASN ALA GLU ALA ASN SER VAL TYR ARG          
SEQRES  12 C  487  THR ILE ARG ASN ASP LEU LEU TRP ILE LYS ARG GLU LEU          
SEQRES  13 C  487  GLY GLN TYR THR GLY GLN ASP ILE ASN GLY LEU PRO VAL          
SEQRES  14 C  487  VAL GLY ASN PRO SER SER GLY MET LYS HIS ARG ILE ILE          
SEQRES  15 C  487  ASN ASN THR ASP VAL ILE THR SER GLN GLY ILE ARG LEU          
SEQRES  16 C  487  SER GLU LEU GLU THR LYS PHE ILE GLU SER ASP VAL GLY          
SEQRES  17 C  487  SER LEU THR ILE GLU VAL GLY ASN LEU ARG GLU GLU LEU          
SEQRES  18 C  487  GLY PRO LYS PRO PRO SER PHE SER GLN ASN VAL TYR SER          
SEQRES  19 C  487  ARG LEU ASN GLU ILE ASP THR LYS GLN THR THR VAL GLU          
SEQRES  20 C  487  SER ASP ILE SER ALA ILE LYS THR SER ILE GLY TYR PRO          
SEQRES  21 C  487  GLY ASN ASN SER ILE ILE THR SER VAL ASN THR ASN THR          
SEQRES  22 C  487  ASP ASN ILE ALA SER ILE ASN LEU GLU LEU ASN GLN SER          
SEQRES  23 C  487  GLY GLY ILE LYS GLN ARG LEU THR VAL ILE GLU THR SER          
SEQRES  24 C  487  ILE GLY SER ASP ASP ILE PRO SER SER ILE LYS GLY GLN          
SEQRES  25 C  487  ILE LYS ASP ASN THR THR SER ILE GLU SER LEU ASN GLY          
SEQRES  26 C  487  ILE VAL GLY GLU ASN THR SER SER GLY LEU ARG ALA ASN          
SEQRES  27 C  487  VAL SER TRP LEU ASN GLN ILE VAL GLY THR ASP SER SER          
SEQRES  28 C  487  GLY GLY GLN PRO SER PRO PRO GLY SER LEU LEU ASN ARG          
SEQRES  29 C  487  VAL SER THR ILE GLU THR SER VAL SER GLY LEU ASN ASN          
SEQRES  30 C  487  ALA VAL GLN ASN LEU GLN VAL GLU ILE GLY ASN ASN SER          
SEQRES  31 C  487  ALA GLY ILE LYS GLY GLN VAL VAL ALA LEU ASN THR LEU          
SEQRES  32 C  487  VAL ASN GLY THR ASN PRO ASN GLY SER THR VAL GLU GLU          
SEQRES  33 C  487  ARG GLY LEU THR ASN SER ILE LYS ALA ASN GLU THR ASN          
SEQRES  34 C  487  ILE ALA SER VAL THR GLN GLU VAL ASN THR ALA LYS GLY          
SEQRES  35 C  487  ASN ILE SER SER LEU GLN GLY ASP VAL GLN ALA LEU GLN          
SEQRES  36 C  487  GLU ALA GLY TYR ILE PRO GLU ALA PRO ARG ASP GLY GLN          
SEQRES  37 C  487  ALA TYR VAL ARG LYS ASP GLY GLU TRP VAL PHE LEU SER          
SEQRES  38 C  487  THR PHE LEU SER PRO ALA                                      
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  CA  ASP A   2     233.908 458.2661393.954  1.00 46.92           C  
ATOM      2  CA  ILE A   3     231.017 457.8381391.502  1.00 34.11           C  
ATOM      3  CA  VAL A   4     227.535 458.2151393.000  1.00 28.51           C  
ATOM      4  CA  LEU A   5     224.681 456.4621391.192  1.00 24.61           C  
ATOM      5  CA  ASN A   6     220.930 456.4661391.910  1.00 23.35           C  
ATOM      6  CA  ASP A   7     219.357 453.4311393.599  1.00 22.18           C  
ATOM      7  CA  LEU A   8     216.408 451.8331391.747  1.00 18.58           C  
ATOM      8  CA  PRO A   9     213.112 453.2581393.114  1.00 16.95           C  
ATOM      9  CA  PHE A  10     211.113 450.0091392.932  1.00 15.82           C  
ATOM     10  CA  VAL A  11     212.143 446.5291394.113  1.00 14.91           C  
ATOM     11  CA  ASP A  12     210.495 443.1101394.156  1.00 17.94           C  
ATOM     12  CA  GLY A  13     211.288 442.4481397.817  1.00 19.17           C  
ATOM     13  CA  PRO A  14     211.805 444.2791401.177  1.00 19.29           C  
ATOM     14  CA  PRO A  15     212.738 447.8721400.358  1.00 19.60           C  
ATOM     15  CA  ALA A  16     215.749 449.7761401.598  1.00 21.64           C  
ATOM     16  CA  GLU A  17     216.033 453.5331402.161  1.00 23.66           C  
ATOM     17  CA  GLY A  18     214.347 455.5361399.378  1.00 23.60           C  
ATOM     18  CA  GLN A  19     212.761 452.5021397.699  1.00 20.26           C  
ATOM     19  CA  SER A  20     209.238 451.1561397.427  1.00 21.74           C  
ATOM     20  CA  ARG A  21     208.093 447.5771396.939  1.00 20.74           C  
ATOM     21  CA  ILE A  22     206.446 446.8401393.586  1.00 19.44           C  
ATOM     22  CA  SER A  23     202.743 446.0521393.872  1.00 20.45           C  
ATOM     23  CA  TRP A  24     201.889 443.1881391.500  1.00 18.66           C  
ATOM     24  CA  ILE A  25     198.354 442.6551390.211  1.00 22.73           C  
ATOM     25  CA  LYS A  26     196.349 440.6681392.753  1.00 28.17           C  
ATOM     26  CA  ASN A  27     193.362 438.4041392.285  1.00 34.03           C  
ATOM     27  CA  GLY A  28     190.257 439.9561393.791  1.00 39.29           C  
ATOM     28  CA  GLU A  29     191.493 443.3621392.728  1.00 40.23           C  
ATOM     29  CA  GLU A  30     189.586 445.5291390.257  1.00 40.77           C  
ATOM     30  CA  ILE A  31     191.232 445.1551386.806  1.00 37.71           C  
ATOM     31  CA  LEU A  32     191.285 448.6971385.388  1.00 32.76           C  
ATOM     32  CA  GLY A  33     193.142 450.7741382.807  1.00 27.76           C  
ATOM     33  CA  ALA A  34     193.561 454.5441382.297  1.00 27.47           C  
ATOM     34  CA  ASP A  35     190.797 457.0931381.684  1.00 33.69           C  
ATOM     35  CA  THR A  36     192.797 459.6031379.587  1.00 32.87           C  
ATOM     36  CA  GLN A  37     194.684 459.1941376.311  1.00 32.27           C  
ATOM     37  CA  TYR A  38     197.984 459.7331378.119  1.00 30.85           C  
ATOM     38  CA  GLY A  39     197.462 458.6141381.728  1.00 25.38           C  
ATOM     39  CA  SER A  40     199.055 455.5131383.269  1.00 24.14           C  
ATOM     40  CA  GLU A  41     196.557 454.8621386.073  1.00 25.45           C  
ATOM     41  CA  GLY A  42     194.875 451.4961386.574  1.00 25.08           C  
ATOM     42  CA  SER A  43     195.968 448.1921388.096  1.00 23.23           C  
ATOM     43  CA  MET A  44     196.664 446.7201384.656  1.00 23.26           C  
ATOM     44  CA  ASN A  45     199.395 449.3181384.122  1.00 21.52           C  
ATOM     45  CA  ARG A  46     200.739 449.5941387.677  1.00 19.86           C  
ATOM     46  CA  PRO A  47     203.560 447.0751387.792  1.00 18.04           C  
ATOM     47  CA  THR A  48     204.783 448.0601384.295  1.00 15.26           C  
ATOM     48  CA  VAL A  49     204.817 451.7721385.286  1.00 15.15           C  
ATOM     49  CA  SER A  50     207.028 450.8121388.274  1.00 16.25           C  
ATOM     50  CA  VAL A  51     209.449 448.8961386.070  1.00 12.03           C  
ATOM     51  CA  LEU A  52     209.605 451.8551383.626  1.00 12.21           C  
ATOM     52  CA  ARG A  53     210.525 454.1541386.540  1.00 12.71           C  
ATOM     53  CA  ASN A  54     213.506 451.8591387.204  1.00 12.32           C  
ATOM     54  CA  VAL A  55     214.401 451.9511383.497  1.00 12.32           C  
ATOM     55  CA  GLU A  56     214.424 455.7851383.573  1.00 13.65           C  
ATOM     56  CA AVAL A  57     216.820 455.6991386.550  0.60  7.63           C  
ATOM     57  CA  LEU A  58     219.098 453.1911384.818  1.00 12.48           C  
ATOM     58  CA  ASP A  59     219.248 455.4921381.780  1.00 15.15           C  
ATOM     59  CA  LYS A  60     220.395 458.3771384.023  1.00 17.96           C  
ATOM     60  CA  ASN A  61     222.967 456.1701385.755  1.00 14.05           C  
ATOM     61  CA  ILE A  62     224.464 455.2571382.358  1.00 15.66           C  
ATOM     62  CA  GLY A  63     224.661 458.9741381.570  1.00 17.96           C  
ATOM     63  CA  ILE A  64     226.597 459.5511384.801  1.00 19.80           C  
ATOM     64  CA  LEU A  65     229.087 456.7761383.854  1.00 18.59           C  
ATOM     65  CA  LYS A  66     229.400 458.1601380.317  1.00 20.06           C  
ATOM     66  CA  THR A  67     230.396 461.6141381.602  1.00 22.33           C  
ATOM     67  CA  SER A  68     232.992 460.1681383.934  1.00 20.95           C  
ATOM     68  CA  LEU A  69     234.417 457.9111381.221  1.00 19.55           C  
ATOM     69  CA  GLU A  70     234.653 460.8491378.798  1.00 20.63           C  
ATOM     70  CA  THR A  71     236.655 462.7241381.406  1.00 22.04           C  
ATOM     71  CA  ALA A  72     238.981 459.7271381.865  1.00 19.43           C  
ATOM     72  CA  ASN A  73     239.487 459.4171378.104  1.00 20.13           C  
ATOM     73  CA  SER A  74     240.390 463.1071377.941  1.00 20.92           C  
ATOM     74  CA  ASP A  75     242.839 462.7931380.868  1.00 20.16           C  
ATOM     75  CA  ILE A  76     244.490 459.8071379.155  1.00 18.71           C  
ATOM     76  CA  LYS A  77     244.867 461.7251375.898  1.00 22.05           C  
ATOM     77  CA  THR A  78     246.546 464.5601377.849  1.00 22.36           C  
ATOM     78  CA  ILE A  79     249.055 462.1181379.380  1.00 17.58           C  
ATOM     79  CA  GLN A  80     249.801 460.5691375.955  1.00 21.05           C  
ATOM     80  CA  ILE A  97     256.069 460.9541381.792  1.00 36.03           C  
ATOM     81  CA  ASN A  98     255.349 463.1611378.793  1.00 35.85           C  
ATOM     82  CA  LYS A  99     257.446 466.1181379.954  1.00 36.24           C  
ATOM     83  CA  LYS A 100     260.267 463.8401381.037  1.00 33.52           C  
ATOM     84  CA  ASP A 101     260.437 462.1841377.569  1.00 35.45           C  
ATOM     85  CA  ILE A 102     260.348 465.5861375.855  1.00 38.03           C  
ATOM     86  CA  SER A 103     263.190 466.8151378.126  1.00 36.82           C  
ATOM     87  CA  ASP A 104     265.463 463.8051377.577  1.00 34.99           C  
ATOM     88  CA  LEU A 105     264.761 464.4171373.913  1.00 38.90           C  
ATOM     89  CA  LYS A 106     266.159 467.9521373.764  1.00 36.09           C  
ATOM     90  CA  THR A 107     269.015 467.0991376.044  1.00 33.69           C  
ATOM     91  CA  LEU A 108     270.080 464.2311373.840  1.00 31.16           C  
ATOM     92  CA  THR A 109     269.847 466.5151370.842  1.00 34.98           C  
ATOM     93  CA  SER A 110     272.104 469.0181372.641  1.00 38.53           C  
ATOM     94  CA  GLU A 111     274.827 466.6451373.738  1.00 37.38           C  
ATOM     95  CA  HIS A 112     274.824 465.4201370.186  1.00 38.86           C  
ATOM     96  CA  THR A 113     275.598 468.8651368.801  1.00 42.63           C  
ATOM     97  CA  GLU A 114     278.529 469.3351371.166  1.00 41.28           C  
ATOM     98  CA  ILE A 115     279.733 465.8611370.248  1.00 33.70           C  
ATOM     99  CA  LEU A 116     279.643 466.7391366.541  1.00 36.12           C  
ATOM    100  CA  ASN A 117     281.522 469.9491367.183  1.00 38.26           C  
ATOM    101  CA  GLY A 118     284.165 468.2981369.351  1.00 33.42           C  
ATOM    102  CA  THR A 119     284.693 465.5141366.794  1.00 36.12           C  
ATOM    103  CA  ASN A 120     285.525 468.2271364.300  1.00 36.98           C  
ATOM    104  CA  ASN A 121     287.906 469.9531366.666  1.00 34.22           C  
ATOM    105  CA  THR A 122     289.760 466.7881367.276  1.00 31.70           C  
ATOM    106  CA  VAL A 123     290.062 466.1191363.536  1.00 32.29           C  
ATOM    107  CA  ASP A 124     291.767 469.4141363.082  1.00 32.47           C  
ATOM    108  CA  SER A 125     293.891 468.5881366.105  1.00 28.05           C  
ATOM    109  CA  ILE A 126     295.064 465.3181364.630  1.00 29.60           C  
ATOM    110  CA  LEU A 127     296.119 467.0621361.449  1.00 29.46           C  
ATOM    111  CA  ALA A 128     297.942 469.7781363.396  1.00 29.14           C  
ATOM    112  CA  ASP A 129     299.893 467.1271365.327  1.00 32.26           C  
ATOM    113  CA  ILE A 130     300.510 465.1211362.151  1.00 38.22           C  
ATOM    114  CA  ILE A 144     309.114 464.2351380.355  1.00 66.02           C  
ATOM    115  CA  ARG A 145     308.139 462.6381383.728  1.00 64.90           C  
ATOM    116  CA  ASN A 146     307.571 459.2501382.050  1.00 64.92           C  
ATOM    117  CA  ASP A 147     311.086 459.1271380.577  1.00 63.61           C  
ATOM    118  CA  LEU A 148     312.541 460.4461383.866  1.00 63.93           C  
ATOM    119  CA  LEU A 149     310.737 457.4591385.357  1.00 58.57           C  
ATOM    120  CA  TRP A 150     311.917 454.8631382.854  1.00 52.40           C  
ATOM    121  CA  ILE A 151     315.489 456.2601382.946  1.00 52.49           C  
ATOM    122  CA  LYS A 152     315.687 456.0821386.710  1.00 58.67           C  
ATOM    123  CA  ARG A 153     314.447 452.4871386.602  1.00 55.76           C  
ATOM    124  CA  GLU A 154     317.253 451.4301384.334  1.00 51.68           C  
ATOM    125  CA  LEU A 155     319.818 453.0771386.607  1.00 56.38           C  
ATOM    126  CA  MET A 176     332.837 446.0021385.553  1.00 36.03           C  
ATOM    127  CA  LYS A 177     335.815 444.4171383.823  1.00 35.85           C  
ATOM    128  CA  HIS A 178     336.033 441.3721386.097  1.00 36.24           C  
ATOM    129  CA  ARG A 179     332.279 440.9031386.018  1.00 33.52           C  
ATOM    130  CA  ILE A 180     332.234 440.8421382.173  1.00 35.45           C  
ATOM    131  CA  ILE A 181     335.166 438.4071382.101  1.00 38.03           C  
ATOM    132  CA  ASN A 182     333.353 436.1351384.610  1.00 36.82           C  
ATOM    133  CA  ASN A 183     330.023 436.0821382.756  1.00 34.99           C  
ATOM    134  CA  THR A 184     332.144 435.2641379.736  1.00 38.90           C  
ATOM    135  CA  ASP A 185     333.655 432.0481381.097  1.00 36.09           C  
ATOM    136  CA  VAL A 186     330.428 431.0171382.712  1.00 33.69           C  
ATOM    137  CA  ILE A 187     328.551 431.3471379.459  1.00 31.16           C  
ATOM    138  CA  THR A 188     331.262 429.3491377.749  1.00 34.98           C  
ATOM    139  CA  SER A 189     330.851 426.6271380.399  1.00 38.53           C  
ATOM    140  CA  GLN A 190     327.093 426.2921380.295  1.00 37.38           C  
ATOM    141  CA  GLY A 191     327.480 426.0791376.563  1.00 38.86           C  
ATOM    142  CA  ILE A 192     329.763 423.0571376.786  1.00 42.63           C  
ATOM    143  CA  ARG A 193     327.349 421.1981379.049  1.00 41.28           C  
ATOM    144  CA  LEU A 194     324.532 422.1301376.689  1.00 33.70           C  
ATOM    145  CA  SER A 208     318.110 412.0041373.537  1.00 66.02           C  
ATOM    146  CA  LEU A 209     317.714 409.5141370.618  1.00 64.90           C  
ATOM    147  CA  THR A 210     314.814 407.7701372.396  1.00 64.92           C  
ATOM    148  CA  ILE A 211     312.785 410.9801372.741  1.00 63.61           C  
ATOM    149  CA  GLU A 212     313.718 411.9871369.163  1.00 63.93           C  
ATOM    150  CA  VAL A 213     312.239 408.6031368.292  1.00 58.57           C  
ATOM    151  CA  GLY A 214     309.052 408.9111370.326  1.00 52.40           C  
ATOM    152  CA  ASN A 215     308.544 412.5301369.159  1.00 52.49           C  
ATOM    153  CA  LEU A 216     308.865 411.6211365.511  1.00 58.67           C  
ATOM    154  CA  ARG A 217     306.347 408.8101365.994  1.00 55.76           C  
ATOM    155  CA  GLU A 218     303.736 411.1731367.312  1.00 51.68           C  
ATOM    156  CA  GLU A 219     304.262 413.5231364.369  1.00 56.38           C  
ATOM    157  CA  LEU A 220     303.722 410.7591361.874  1.00 57.81           C  
ATOM    158  CA  VAL A 231     294.908 411.0171365.950  1.00 36.03           C  
ATOM    159  CA  TYR A 232     297.557 412.6831363.809  1.00 35.85           C  
ATOM    160  CA  SER A 233     296.659 410.8821360.578  1.00 36.24           C  
ATOM    161  CA  ARG A 234     292.959 411.3771361.199  1.00 33.52           C  
ATOM    162  CA  LEU A 235     293.402 415.1761361.609  1.00 35.45           C  
ATOM    163  CA  ASN A 236     295.563 415.3411358.476  1.00 38.03           C  
ATOM    164  CA  GLU A 237     292.899 413.3801356.524  1.00 36.82           C  
ATOM    165  CA  ILE A 238     289.946 415.5201357.629  1.00 34.99           C  
ATOM    166  CA  ASP A 239     292.148 418.4201356.614  1.00 38.90           C  
ATOM    167  CA  THR A 240     292.559 417.4241352.963  1.00 36.09           C  
ATOM    168  CA  LYS A 241     288.992 416.2861352.698  1.00 33.69           C  
ATOM    169  CA  GLN A 242     287.710 419.6141353.927  1.00 31.16           C  
ATOM    170  CA  THR A 243     289.991 421.3441351.465  1.00 34.98           C  
ATOM    171  CA  THR A 244     288.529 419.1851348.674  1.00 38.53           C  
ATOM    172  CA  VAL A 245     284.864 419.6851349.426  1.00 37.38           C  
ATOM    173  CA  GLU A 246     285.663 423.3531349.557  1.00 38.86           C  
ATOM    174  CA  SER A 247     287.010 423.3771346.010  1.00 42.63           C  
ATOM    175  CA  ASP A 248     283.915 421.6531344.652  1.00 41.28           C  
ATOM    176  CA  ILE A 249     281.780 424.0951346.612  1.00 33.70           C  
ATOM    177  CA  SER A 250     283.609 427.0501345.044  1.00 36.12           C  
ATOM    178  CA  ALA A 251     283.190 425.5691341.597  1.00 38.26           C  
ATOM    179  CA  ILE A 252     279.500 424.8081342.065  1.00 33.42           C  
ATOM    180  CA  LYS A 253     278.829 428.3111343.424  1.00 36.12           C  
ATOM    181  CA  THR A 254     280.227 429.6301340.172  1.00 36.98           C  
ATOM    182  CA  SER A 255     278.120 427.2961338.084  1.00 34.22           C  
ATOM    183  CA  ILE A 256     275.015 428.3761339.821  1.00 31.70           C  
ATOM    184  CA  SER A 263     274.621 431.5331339.187  1.00 36.03           C  
ATOM    185  CA  ILE A 264     272.353 434.4761339.943  1.00 35.85           C  
ATOM    186  CA  ILE A 265     274.733 437.1601338.669  1.00 36.24           C  
ATOM    187  CA  THR A 266     275.590 435.1061335.608  1.00 33.52           C  
ATOM    188  CA  SER A 267     271.883 434.7451334.649  1.00 35.45           C  
ATOM    189  CA  VAL A 268     271.296 438.4691335.207  1.00 38.03           C  
ATOM    190  CA  ASN A 269     274.329 439.2881333.000  1.00 36.82           C  
ATOM    191  CA  THR A 270     273.337 437.0141330.107  1.00 34.99           C  
ATOM    192  CA  ASN A 271     269.967 438.6961330.432  1.00 38.90           C  
ATOM    193  CA  THR A 272     271.165 442.2481329.782  1.00 36.09           C  
ATOM    194  CA  ASP A 273     273.579 441.1281327.135  1.00 33.69           C  
ATOM    195  CA  ASN A 274     270.855 439.3551325.225  1.00 31.16           C  
ATOM    196  CA  ILE A 275     268.703 442.4431325.526  1.00 34.98           C  
ATOM    197  CA  ALA A 276     271.571 444.5151324.086  1.00 38.53           C  
ATOM    198  CA  SER A 277     272.394 442.3551321.103  1.00 37.38           C  
ATOM    199  CA  ILE A 278     268.705 442.3971320.389  1.00 38.86           C  
ATOM    200  CA  ASN A 279     268.604 446.1821320.162  1.00 42.63           C  
ATOM    201  CA  LEU A 280     271.512 446.2761317.726  1.00 41.28           C  
ATOM    202  CA  GLU A 281     269.832 443.5311315.725  1.00 33.70           C  
ATOM    203  CA  ILE A 288     271.489 444.9861311.676  1.00 66.02           C  
ATOM    204  CA  LYS A 289     269.481 448.2581311.310  1.00 64.90           C  
ATOM    205  CA  GLN A 290     272.642 450.1831310.350  1.00 64.92           C  
ATOM    206  CA  ARG A 291     273.459 447.8551307.444  1.00 63.61           C  
ATOM    207  CA  LEU A 292     269.767 447.7891306.422  1.00 63.93           C  
ATOM    208  CA  THR A 293     270.176 451.5611306.328  1.00 58.57           C  
ATOM    209  CA  VAL A 294     273.412 451.6631304.350  1.00 52.40           C  
ATOM    210  CA  ILE A 295     272.138 448.9611301.943  1.00 52.49           C  
ATOM    211  CA  GLU A 296     268.938 450.8241301.213  1.00 58.67           C  
ATOM    212  CA  THR A 297     270.938 453.9871300.533  1.00 55.76           C  
ATOM    213  CA  SER A 298     272.995 452.2971297.879  1.00 51.68           C  
ATOM    214  CA  ILE A 299     269.861 450.9601296.191  1.00 56.38           C  
ATOM    215  CA  ILE A 308     274.057 454.7851293.028  1.00 66.02           C  
ATOM    216  CA  LYS A 309     272.093 457.7781291.590  1.00 64.90           C  
ATOM    217  CA  GLY A 310     275.328 459.4201290.383  1.00 64.92           C  
ATOM    218  CA  GLN A 311     276.378 456.3851288.329  1.00 63.61           C  
ATOM    219  CA  ILE A 312     272.784 455.9541287.074  1.00 63.93           C  
ATOM    220  CA  LYS A 313     273.207 459.5541285.950  1.00 58.57           C  
ATOM    221  CA  ASP A 314     276.596 459.1631284.291  1.00 52.40           C  
ATOM    222  CA  ASN A 315     275.522 455.8651282.652  1.00 52.49           C  
ATOM    223  CA  THR A 316     272.397 457.3771281.171  1.00 58.67           C  
ATOM    224  CA  THR A 317     274.454 460.2621279.787  1.00 55.76           C  
ATOM    225  CA  SER A 318     276.721 457.9361277.893  1.00 51.68           C  
ATOM    226  CA  ILE A 319     273.735 456.1101276.406  1.00 56.38           C  
ATOM    227  CA  LEU A 334     276.221 458.3171275.647  1.00 66.02           C  
ATOM    228  CA  ARG A 335     273.599 460.6451274.039  1.00 64.90           C  
ATOM    229  CA  ALA A 336     276.311 463.1641273.079  1.00 64.92           C  
ATOM    230  CA  ASN A 337     278.343 460.5901271.136  1.00 63.61           C  
ATOM    231  CA  VAL A 338     275.132 459.1691269.604  1.00 63.93           C  
ATOM    232  CA  SER A 339     274.591 462.7571268.492  1.00 58.57           C  
ATOM    233  CA  TRP A 340     278.068 463.3791267.109  1.00 52.40           C  
ATOM    234  CA  LEU A 341     278.114 459.9391265.412  1.00 52.49           C  
ATOM    235  CA  ASN A 342     274.812 460.5171263.679  1.00 58.67           C  
ATOM    236  CA  GLN A 343     276.056 463.8931262.442  1.00 55.76           C  
ATOM    237  CA  ILE A 344     279.034 462.3441260.750  1.00 51.68           C  
ATOM    238  CA  VAL A 345     276.822 459.7641259.043  1.00 56.38           C  
ATOM    239  CA  SER A 359     281.043 464.2941261.031  1.00 36.03           C  
ATOM    240  CA  LEU A 360     277.707 463.0791259.707  1.00 35.85           C  
ATOM    241  CA  LEU A 361     276.499 466.4711258.472  1.00 36.24           C  
ATOM    242  CA  ASN A 362     279.888 467.2621256.986  1.00 33.52           C  
ATOM    243  CA  ARG A 363     279.902 464.0001254.948  1.00 35.45           C  
ATOM    244  CA  VAL A 364     276.331 464.6281253.773  1.00 38.03           C  
ATOM    245  CA  SER A 365     277.298 468.1891252.708  1.00 36.82           C  
ATOM    246  CA  THR A 366     280.419 467.1851250.765  1.00 34.99           C  
ATOM    247  CA  ILE A 367     278.143 464.6341249.154  1.00 38.90           C  
ATOM    248  CA  GLU A 368     275.656 467.1091247.679  1.00 36.09           C  
ATOM    249  CA  THR A 369     278.365 469.5391246.759  1.00 33.69           C  
ATOM    250  CA  SER A 370     280.241 466.9031244.820  1.00 31.16           C  
ATOM    251  CA  VAL A 371     276.510 467.3501243.776  1.00 66.02           C  
ATOM    252  CA  SER A 372     273.713 467.2761241.121  1.00 64.90           C  
ATOM    253  CA  GLY A 373     274.094 471.0291240.502  1.00 64.92           C  
ATOM    254  CA  LEU A 374     277.808 470.7561239.684  1.00 63.61           C  
ATOM    255  CA  ASN A 375     277.148 467.5991237.615  1.00 63.93           C  
ATOM    256  CA  ASN A 376     274.707 469.8441235.771  1.00 58.57           C  
ATOM    257  CA  ALA A 377     277.019 472.8151235.303  1.00 52.40           C  
ATOM    258  CA  VAL A 378     279.933 470.5171234.331  1.00 52.49           C  
ATOM    259  CA  GLN A 379     277.918 468.7311231.687  1.00 58.67           C  
ATOM    260  CA  ASN A 380     276.837 472.0851230.250  1.00 55.76           C  
ATOM    261  CA  LEU A 381     280.397 473.1841229.743  1.00 51.68           C  
ATOM    262  CA  GLN A 382     281.240 469.9171227.990  1.00 56.38           C  
ATOM    263  CA  VAL A 383     278.406 470.3211225.550  1.00 57.81           C  
ATOM    264  CA  GLU A 384     279.633 473.9361225.304  1.00 56.80           C  
ATOM    265  CA  ILE A 385     283.305 473.3241224.458  1.00 53.25           C  
ATOM    266  CA  GLY A 386     281.911 470.5741222.269  1.00 57.45           C  
ATOM    267  CA  ASN A 387     283.973 468.4151219.952  1.00 61.13           C  
ATOM    268  CA  ASN A 388     285.546 468.6551216.490  1.00 56.21           C  
ATOM    269  CA  SER A 389     282.115 468.7341215.047  1.00 52.91           C  
ATOM    270  CA  ALA A 390     280.265 470.9891217.488  1.00 49.07           C  
ATOM    271  CA  GLY A 391     280.564 473.7471220.042  1.00 46.98           C  
ATOM    272  CA  ILE A 392     283.496 476.0601220.421  1.00 43.17           C  
ATOM    273  CA  LYS A 393     285.902 473.2831219.451  1.00 44.95           C  
ATOM    274  CA  GLY A 394     283.923 472.7521216.249  1.00 41.35           C  
ATOM    275  CA  GLN A 395     283.886 476.4121215.263  1.00 42.54           C  
ATOM    276  CA  VAL A 396     287.659 476.7651215.789  1.00 37.57           C  
ATOM    277  CA  VAL A 397     288.422 473.5811213.815  1.00 36.68           C  
ATOM    278  CA  ALA A 398     286.529 475.0631210.881  1.00 36.11           C  
ATOM    279  CA  LEU A 399     288.401 478.3461211.301  1.00 36.19           C  
ATOM    280  CA  ASN A 400     291.775 476.5781211.084  1.00 41.94           C  
ATOM    281  CA  THR A 401     290.650 474.4671208.175  1.00 42.48           C  
ATOM    282  CA  LEU A 402     289.744 477.5531206.160  1.00 45.15           C  
ATOM    283  CA  VAL A 403     292.909 479.4361207.089  1.00 46.90           C  
ATOM    284  CA  ASN A 404     295.338 476.6211206.290  1.00 55.51           C  
ATOM    285  CA  GLY A 405     293.519 474.8191203.503  1.00 54.83           C  
ATOM    286  CA  THR A 406     292.687 471.2481202.425  1.00 57.60           C  
ATOM    287  CA  ASN A 407     294.788 470.9981199.332  1.00 60.39           C  
ATOM    288  CA  PRO A 408     297.482 473.5861198.644  1.00 64.08           C  
ATOM    289  CA  ASN A 409     297.705 472.7371194.917  1.00 66.30           C  
ATOM    290  CA  GLY A 410     293.945 473.0071194.972  1.00 61.13           C  
ATOM    291  CA  SER A 411     291.785 475.0701192.695  1.00 61.42           C  
ATOM    292  CA  THR A 412     289.608 476.9571195.218  1.00 52.20           C  
ATOM    293  CA  VAL A 413     290.297 479.5661197.874  1.00 48.08           C  
ATOM    294  CA  GLU A 414     288.941 477.1511200.532  1.00 46.50           C  
ATOM    295  CA  GLU A 415     291.118 474.3501199.205  1.00 45.01           C  
ATOM    296  CA  ARG A 416     294.294 476.4351199.259  1.00 40.02           C  
ATOM    297  CA  GLY A 417     293.416 478.1071202.533  1.00 35.39           C  
ATOM    298  CA  LEU A 418     293.078 481.8381203.161  1.00 36.03           C  
ATOM    299  CA  THR A 419     296.779 482.3011203.842  1.00 35.85           C  
ATOM    300  CA  ASN A 420     297.992 480.6391200.640  1.00 36.24           C  
ATOM    301  CA  SER A 421     295.363 482.4221198.585  1.00 33.52           C  
ATOM    302  CA  ILE A 422     296.480 485.8611199.897  1.00 35.45           C  
ATOM    303  CA  LYS A 423     300.138 485.0001199.267  1.00 38.03           C  
ATOM    304  CA  ALA A 424     299.273 483.9041195.689  1.00 36.82           C  
ATOM    305  CA  ASN A 425     297.257 487.0141194.801  1.00 34.99           C  
ATOM    306  CA  GLU A 426     300.237 488.8841196.183  1.00 38.90           C  
ATOM    307  CA  THR A 427     302.816 487.4901193.756  1.00 36.09           C  
ATOM    308  CA  ASN A 428     300.419 487.6221190.871  1.00 33.69           C  
ATOM    309  CA  ILE A 429     299.721 491.2821191.458  1.00 31.16           C  
ATOM    310  CA  ALA A 430     303.439 491.9031191.673  1.00 34.98           C  
ATOM    311  CA  SER A 431     303.875 490.1371188.314  1.00 38.53           C  
ATOM    312  CA  VAL A 432     301.175 491.9251186.375  1.00 37.38           C  
ATOM    313  CA  THR A 433     302.678 495.0951187.718  1.00 38.86           C  
ATOM    314  CA  GLN A 434     306.076 494.3441186.208  1.00 42.63           C  
ATOM    315  CA  GLU A 435     304.585 493.6691182.785  1.00 41.28           C  
ATOM    316  CA  VAL A 436     302.562 496.8571183.116  1.00 33.70           C  
ATOM    317  CA  ASN A 437     305.719 498.8581183.866  1.00 36.12           C  
ATOM    318  CA  THR A 438     307.485 497.3121180.909  1.00 38.26           C  
ATOM    319  CA  ALA A 439     304.596 497.9031178.517  1.00 33.42           C  
ATOM    320  CA  LYS A 440     304.243 501.5301179.653  1.00 36.12           C  
ATOM    321  CA  GLY A 441     307.849 501.9991178.628  1.00 36.98           C  
ATOM    322  CA  ASN A 442     307.322 500.3521175.273  1.00 34.22           C  
ATOM    323  CA  ILE A 443     304.441 502.5771174.516  1.00 31.70           C  
ATOM    324  CA  SER A 444     306.455 505.6771175.444  1.00 32.29           C  
ATOM    325  CA  SER A 445     309.037 504.7641172.902  1.00 32.47           C  
ATOM    326  CA  LEU A 446     306.218 504.0611170.476  1.00 28.05           C  
ATOM    327  CA  GLN A 447     304.724 507.4991170.911  1.00 29.60           C  
ATOM    328  CA  GLY A 448     308.067 509.1081170.194  1.00 29.46           C  
ATOM    329  CA  ASP A 449     308.593 506.9311167.115  1.00 29.14           C  
ATOM    330  CA  VAL A 450     305.188 507.9831165.752  1.00 32.26           C  
ATOM    331  CA  GLN A 451     305.814 511.6151166.703  1.00 38.22           C  
ATOM    332  CA  ALA A 452     308.999 511.4751164.680  1.00 35.96           C  
ATOM    333  CA  LEU A 453     307.295 509.9591161.598  1.00 34.01           C  
ATOM    334  CA  GLN A 454     304.462 512.5151161.841  1.00 34.42           C  
ATOM    335  CA  GLU A 455     306.939 515.4411162.034  1.00 35.15           C  
ATOM    336  CA  ALA A 456     308.996 514.0811159.195  1.00 31.68           C  
ATOM    337  CA  GLY A 457     307.039 515.8371156.437  1.00 32.56           C  
ATOM    338  CA  TYR A 458     306.841 512.9821154.000  1.00 31.35           C  
ATOM    339  CA  ILE A 459     305.099 513.4821150.729  1.00 31.40           C  
ATOM    340  CA  PRO A 460     302.242 511.4101149.349  1.00 32.94           C  
ATOM    341  CA  GLU A 461     302.001 509.7851145.952  1.00 33.93           C  
ATOM    342  CA  ALA A 462     301.745 512.0371142.864  1.00 35.50           C  
ATOM    343  CA  PRO A 463     298.658 511.6641140.583  1.00 37.70           C  
ATOM    344  CA  ARG A 464     298.558 508.4981138.450  1.00 43.46           C  
ATOM    345  CA  ASP A 465     297.350 509.8631135.103  1.00 42.68           C  
ATOM    346  CA  GLY A 466     300.043 509.0201132.558  1.00 41.53           C  
ATOM    347  CA  GLN A 467     301.838 512.2961133.190  1.00 39.66           C  
ATOM    348  CA  ALA A 468     305.222 513.2401134.675  1.00 34.55           C  
ATOM    349  CA  TYR A 469     305.317 515.4271137.796  1.00 33.51           C  
ATOM    350  CA  VAL A 470     308.001 517.3721139.685  1.00 33.42           C  
ATOM    351  CA  ARG A 471     308.036 518.9571143.186  1.00 35.41           C  
ATOM    352  CA  LYS A 472     307.211 522.6751143.686  1.00 39.68           C  
ATOM    353  CA  ASP A 473     305.757 524.5631146.743  1.00 41.29           C  
ATOM    354  CA  GLY A 474     303.870 521.6741148.375  1.00 41.26           C  
ATOM    355  CA  GLU A 475     302.060 520.7731145.119  1.00 40.70           C  
ATOM    356  CA  TRP A 476     302.998 518.2381142.383  1.00 41.16           C  
ATOM    357  CA  VAL A 477     303.386 520.1091139.041  1.00 40.33           C  
ATOM    358  CA  PHE A 478     303.355 518.7681135.488  1.00 34.39           C  
ATOM    359  CA  LEU A 479     306.888 518.4981134.178  1.00 36.69           C  
ATOM    360  CA  SER A 480     305.617 519.4981130.706  1.00 44.11           C  
ATOM    361  CA  THR A 481     304.926 522.9981132.141  1.00 50.73           C  
ATOM    362  CA  PHE A 482     308.710 523.5971132.036  1.00 57.21           C  
ATOM    363  CA  LEU A 483     309.619 521.1421129.236  1.00 61.29           C  
TER     364      LEU A 483                                                      
ATOM    365  CA  ASP B   2     232.941 461.6471372.372  1.00 46.92           C  
ATOM    366  CA  ILE B   3     230.804 458.6121373.251  1.00 34.11           C  
ATOM    367  CA  VAL B   4     227.521 458.3171371.345  1.00 28.51           C  
ATOM    368  CA  LEU B   5     224.731 456.3381373.014  1.00 24.61           C  
ATOM    369  CA  ASN B   6     221.246 455.4281371.741  1.00 23.35           C  
ATOM    370  CA  ASP B   7     218.228 457.3651373.037  1.00 22.18           C  
ATOM    371  CA  LEU B   8     215.427 455.2521374.576  1.00 18.58           C  
ATOM    372  CA  PRO B   9     212.761 454.5221371.909  1.00 16.95           C  
ATOM    373  CA  PHE B  10     209.731 454.8121374.214  1.00 15.82           C  
ATOM    374  CA  VAL B  11     208.955 457.5421376.767  1.00 14.91           C  
ATOM    375  CA  ASP B  12     206.113 458.2281379.188  1.00 17.94           C  
ATOM    376  CA  GLY B  13     205.665 461.8451378.100  1.00 19.17           C  
ATOM    377  CA  PRO B  14     206.050 464.1461375.025  1.00 19.29           C  
ATOM    378  CA  PRO B  15     208.519 462.4631372.673  1.00 19.60           C  
ATOM    379  CA  ALA B  16     211.646 463.9711371.201  1.00 21.64           C  
ATOM    380  CA  GLU B  17     213.273 463.1141367.864  1.00 23.66           C  
ATOM    381  CA  GLY B  18     213.261 459.3541367.182  1.00 23.60           C  
ATOM    382  CA  GLN B  19     211.044 458.4831370.158  1.00 20.26           C  
ATOM    383  CA  SER B  20     207.454 457.3591370.559  1.00 21.74           C  
ATOM    384  CA  ARG B  21     205.121 457.8651373.501  1.00 20.74           C  
ATOM    385  CA  ILE B  22     204.175 454.6991375.389  1.00 19.44           C  
ATOM    386  CA  SER B  23     200.519 453.7521375.004  1.00 20.45           C  
ATOM    387  CA  TRP B  24     199.183 452.5331378.363  1.00 18.66           C  
ATOM    388  CA  ILE B  25     196.157 450.2451378.594  1.00 22.73           C  
ATOM    389  CA  LYS B  26     192.973 452.3201378.487  1.00 28.17           C  
ATOM    390  CA  ASN B  27     189.537 451.5971379.878  1.00 34.03           C  
ATOM    391  CA  GLY B  28     187.057 451.0071377.081  1.00 39.29           C  
ATOM    392  CA  GLU B  29     189.776 449.3161375.083  1.00 40.23           C  
ATOM    393  CA  GLU B  30     189.557 445.6641374.054  1.00 40.77           C  
ATOM    394  CA  ILE B  31     191.692 443.5961376.488  1.00 37.71           C  
ATOM    395  CA  LEU B  32     193.505 441.0821374.266  1.00 32.76           C  
ATOM    396  CA  GLY B  33     196.603 438.8841374.280  1.00 27.76           C  
ATOM    397  CA  ALA B  34     198.613 437.1841371.503  1.00 27.47           C  
ATOM    398  CA  ASP B  35     197.346 434.5861369.021  1.00 33.69           C  
ATOM    399  CA  THR B  36     200.627 432.6831368.467  1.00 32.87           C  
ATOM    400  CA  GLN B  37     202.918 430.8721370.903  1.00 32.27           C  
ATOM    401  CA  TYR B  38     205.615 433.4941370.353  1.00 30.85           C  
ATOM    402  CA  GLY B  39     203.835 436.7151369.351  1.00 25.38           C  
ATOM    403  CA  SER B  40     203.622 439.8251371.544  1.00 24.14           C  
ATOM    404  CA  GLU B  41     200.479 441.4041370.078  1.00 25.45           C  
ATOM    405  CA  GLY B  42     197.518 442.4371372.217  1.00 25.08           C  
ATOM    406  CA  SER B  43     196.788 445.4081374.467  1.00 23.23           C  
ATOM    407  CA  MET B  44     197.636 443.3901377.582  1.00 23.26           C  
ATOM    408  CA  ASN B  45     201.224 443.0441376.351  1.00 21.52           C  
ATOM    409  CA  ARG B  46     201.666 446.4371374.670  1.00 19.86           C  
ATOM    410  CA  PRO B  47     203.116 448.6281377.392  1.00 18.04           C  
ATOM    411  CA  THR B  48     205.435 445.8341378.617  1.00 15.26           C  
ATOM    412  CA  VAL B  49     206.720 445.2501375.044  1.00 15.15           C  
ATOM    413  CA  SER B  50     207.567 448.9911374.885  1.00 16.25           C  
ATOM    414  CA  VAL B  51     209.464 448.8621378.168  1.00 12.03           C  
ATOM    415  CA  LEU B  52     211.382 445.7581376.967  1.00 12.21           C  
ATOM    416  CA  ARG B  53     212.417 447.6711373.821  1.00 12.71           C  
ATOM    417  CA  ASN B  54     213.968 450.2981376.122  1.00 12.32           C  
ATOM    418  CA  VAL B  55     215.688 447.5391378.115  1.00 12.32           C  
ATOM    419  CA  GLU B  56     217.233 446.1421374.898  1.00 13.65           C  
ATOM    420  CA AVAL B  57     218.598 449.6141374.060  0.60  7.63           C  
ATOM    421  CA  LEU B  58     220.017 450.0471377.565  1.00 12.48           C  
ATOM    422  CA  ASP B  59     221.807 446.6981377.208  1.00 15.15           C  
ATOM    423  CA  LYS B  60     223.442 447.9201373.966  1.00 17.96           C  
ATOM    424  CA  ASN B  61     224.408 451.2401375.557  1.00 14.05           C  
ATOM    425  CA  ILE B  62     226.179 449.3631378.379  1.00 15.66           C  
ATOM    426  CA  GLY B  63     228.039 447.3631375.731  1.00 17.96           C  
ATOM    427  CA  ILE B  64     229.204 450.6061374.105  1.00 19.80           C  
ATOM    428  CA  LEU B  65     230.514 451.8811377.490  1.00 18.59           C  
ATOM    429  CA  LYS B  66     232.199 448.5331378.185  1.00 20.06           C  
ATOM    430  CA  THR B  67     234.159 448.6781374.913  1.00 22.33           C  
ATOM    431  CA  SER B  68     235.310 452.2151375.577  1.00 20.95           C  
ATOM    432  CA  LEU B  69     236.313 451.3951379.157  1.00 19.55           C  
ATOM    433  CA  GLU B  70     238.285 448.3481377.984  1.00 20.63           C  
ATOM    434  CA  THR B  71     240.181 450.6031375.607  1.00 22.04           C  
ATOM    435  CA  ALA B  72     240.920 453.0661378.433  1.00 19.43           C  
ATOM    436  CA  ASN B  73     242.146 450.2601380.694  1.00 20.13           C  
ATOM    437  CA  SER B  74     244.469 449.0731377.927  1.00 20.92           C  
ATOM    438  CA  ASP B  75     245.800 452.6101377.319  1.00 20.16           C  
ATOM    439  CA  ILE B  76     246.470 452.9921381.059  1.00 18.71           C  
ATOM    440  CA  LYS B  77     248.357 449.6991381.184  1.00 22.05           C  
ATOM    441  CA  THR B  78     250.512 450.9101378.258  1.00 22.36           C  
ATOM    442  CA  ILE B  79     251.377 454.1271380.132  1.00 17.58           C  
ATOM    443  CA  GLN B  80     252.236 452.1701383.313  1.00 21.05           C  
ATOM    444  CA  ILE B  97     255.328 457.5591374.565  1.00 36.03           C  
ATOM    445  CA  ASN B  98     256.647 454.0611373.941  1.00 35.85           C  
ATOM    446  CA  LYS B  99     258.299 454.8401370.600  1.00 36.24           C  
ATOM    447  CA  LYS B 100     259.722 458.0841371.933  1.00 33.52           C  
ATOM    448  CA  ASP B 101     261.384 456.2871374.901  1.00 35.45           C  
ATOM    449  CA  ILE B 102     262.768 453.5891372.593  1.00 38.03           C  
ATOM    450  CA  SER B 103     264.180 456.2941370.262  1.00 36.82           C  
ATOM    451  CA  ASP B 104     265.868 458.3341373.003  1.00 34.99           C  
ATOM    452  CA  LEU B 105     267.280 455.0031374.096  1.00 38.90           C  
ATOM    453  CA  LYS B 106     269.121 454.2041370.863  1.00 36.09           C  
ATOM    454  CA  THR B 107     270.193 457.7711370.395  1.00 33.69           C  
ATOM    455  CA  LEU B 108     271.749 457.8831373.829  1.00 31.16           C  
ATOM    456  CA  THR B 109     273.488 454.6141373.091  1.00 34.98           C  
ATOM    457  CA  SER B 110     274.868 456.1361369.870  1.00 38.53           C  
ATOM    458  CA  GLU B 111     276.186 459.3761371.290  1.00 37.38           C  
ATOM    459  CA  HIS B 112     277.820 457.2511373.922  1.00 38.86           C  
ATOM    460  CA  THR B 113     279.763 455.2421371.358  1.00 42.63           C  
ATOM    461  CA  GLU B 114     281.074 458.3711369.659  1.00 41.28           C  
ATOM    462  CA  ILE B 115     281.979 459.7561373.070  1.00 33.70           C  
ATOM    463  CA  LEU B 116     283.971 456.6121373.890  1.00 36.12           C  
ATOM    464  CA  ASN B 117     285.751 456.7891370.566  1.00 38.26           C  
ATOM    465  CA  GLY B 118     286.569 460.4831370.882  1.00 33.42           C  
ATOM    466  CA  THR B 119     287.871 460.0111374.438  1.00 36.12           C  
ATOM    467  CA  ASN B 120     290.315 457.5131373.005  1.00 36.98           C  
ATOM    468  CA  ASN B 121     291.375 459.8361370.226  1.00 34.22           C  
ATOM    469  CA  THR B 122     292.083 462.5721372.643  1.00 31.70           C  
ATOM    470  CA  VAL B 123     294.163 460.2451374.830  1.00 32.29           C  
ATOM    471  CA  ASP B 124     296.380 459.4851371.919  1.00 32.47           C  
ATOM    472  CA  SER B 125     296.456 463.1931371.170  1.00 28.05           C  
ATOM    473  CA  ILE B 126     297.659 464.0671374.640  1.00 29.60           C  
ATOM    474  CA  LEU B 127     300.484 461.5741374.354  1.00 29.46           C  
ATOM    475  CA  ALA B 128     301.457 462.8871370.915  1.00 29.14           C  
ATOM    476  CA  ASP B 129     301.649 466.4401372.293  1.00 32.26           C  
ATOM    477  CA  ILE B 130     303.477 465.2441375.411  1.00 38.22           C  
ATOM    478  CA  ILE B 144     315.483 467.2071377.070  1.00 66.02           C  
ATOM    479  CA  ARG B 145     319.302 467.6721377.345  1.00 64.90           C  
ATOM    480  CA  ASN B 146     319.324 466.0821380.823  1.00 64.92           C  
ATOM    481  CA  ASP B 147     317.656 462.8711379.621  1.00 63.61           C  
ATOM    482  CA  LEU B 148     319.865 462.8601376.491  1.00 63.93           C  
ATOM    483  CA  LEU B 149     322.693 462.9911379.018  1.00 58.57           C  
ATOM    484  CA  TRP B 150     321.437 460.2451381.314  1.00 52.40           C  
ATOM    485  CA  ILE B 151     320.507 458.0331378.320  1.00 52.49           C  
ATOM    486  CA  LYS B 152     323.930 458.3421376.763  1.00 58.67           C  
ATOM    487  CA  ARG B 153     325.525 457.4361380.095  1.00 55.76           C  
ATOM    488  CA  GLU B 154     323.630 454.1951380.292  1.00 51.68           C  
ATOM    489  CA  LEU B 155     324.659 453.2851376.746  1.00 56.38           C  
ATOM    490  CA  MET B 176     333.502 446.6641377.590  1.00 36.03           C  
ATOM    491  CA  LYS B 177     330.495 447.6031375.482  1.00 35.85           C  
ATOM    492  CA  HIS B 178     331.072 444.9971372.767  1.00 36.24           C  
ATOM    493  CA  ARG B 179     331.867 442.3341375.337  1.00 33.52           C  
ATOM    494  CA  ILE B 180     328.554 442.9531377.193  1.00 35.45           C  
ATOM    495  CA  ILE B 181     326.617 442.9121373.913  1.00 38.03           C  
ATOM    496  CA  ASN B 182     328.304 439.6011372.947  1.00 36.82           C  
ATOM    497  CA  ASN B 183     327.635 437.8361376.258  1.00 34.99           C  
ATOM    498  CA  THR B 184     324.094 439.0631375.768  1.00 38.90           C  
ATOM    499  CA  ASP B 185     323.448 437.2911372.463  1.00 36.09           C  
ATOM    500  CA  VAL B 186     325.305 434.2171373.557  1.00 33.69           C  
ATOM    501  CA  ILE B 187     323.188 433.8951376.664  1.00 31.16           C  
ATOM    502  CA  THR B 188     320.098 434.3491374.541  1.00 34.98           C  
ATOM    503  CA  SER B 189     321.313 431.5331372.262  1.00 38.53           C  
ATOM    504  CA  GLN B 190     322.144 428.9751374.911  1.00 37.38           C  
ATOM    505  CA  GLY B 191     318.743 429.7231376.324  1.00 38.86           C  
ATOM    506  CA  ILE B 192     316.990 428.7791373.097  1.00 42.63           C  
ATOM    507  CA  ARG B 193     318.813 425.4581372.886  1.00 41.28           C  
ATOM    508  CA  LEU B 194     317.989 424.8561376.537  1.00 33.70           C  
ATOM    509  CA  SER B 208     317.099 419.6011374.744  1.00 66.02           C  
ATOM    510  CA  LEU B 209     315.696 422.9041373.329  1.00 64.90           C  
ATOM    511  CA  THR B 210     314.840 421.2101370.011  1.00 64.92           C  
ATOM    512  CA  ILE B 211     312.697 418.5271371.665  1.00 63.61           C  
ATOM    513  CA  GLU B 212     311.146 421.1531373.983  1.00 63.93           C  
ATOM    514  CA  VAL B 213     310.274 422.8851370.721  1.00 58.57           C  
ATOM    515  CA  GLY B 214     308.860 419.8631368.914  1.00 52.40           C  
ATOM    516  CA  ASN B 215     306.950 418.7601372.054  1.00 52.49           C  
ATOM    517  CA  LEU B 216     305.326 422.1371372.506  1.00 58.67           C  
ATOM    518  CA  ARG B 217     304.278 422.1191368.849  1.00 55.76           C  
ATOM    519  CA  GLU B 218     302.429 418.8691369.238  1.00 51.68           C  
ATOM    520  CA  GLU B 219     300.610 420.1801372.310  1.00 56.38           C  
ATOM    521  CA  LEU B 220     299.402 423.2341370.475  1.00 57.81           C  
ATOM    522  CA  VAL B 231     296.758 418.6941367.342  1.00 36.03           C  
ATOM    523  CA  TYR B 232     294.409 420.9071369.333  1.00 35.85           C  
ATOM    524  CA  SER B 233     294.622 423.9161367.011  1.00 36.24           C  
ATOM    525  CA  ARG B 234     294.337 421.7151363.946  1.00 33.52           C  
ATOM    526  CA  LEU B 235     291.097 420.0991365.245  1.00 35.45           C  
ATOM    527  CA  ASN B 236     289.663 423.5141366.143  1.00 38.03           C  
ATOM    528  CA  GLU B 237     290.518 424.8081362.630  1.00 36.82           C  
ATOM    529  CA  ILE B 238     288.979 421.8741360.745  1.00 34.99           C  
ATOM    530  CA  ASP B 239     285.987 422.5001362.969  1.00 38.90           C  
ATOM    531  CA  THR B 240     285.330 426.0781361.855  1.00 36.09           C  
ATOM    532  CA  LYS B 241     286.142 425.2911358.276  1.00 33.69           C  
ATOM    533  CA  GLN B 242     283.631 422.4791358.196  1.00 31.16           C  
ATOM    534  CA  THR B 243     281.076 424.7841359.750  1.00 34.98           C  
ATOM    535  CA  THR B 244     281.785 427.3371356.998  1.00 38.53           C  
ATOM    536  CA  VAL B 245     281.552 425.0391354.013  1.00 37.38           C  
ATOM    537  CA  GLU B 246     278.320 423.8491355.515  1.00 38.86           C  
ATOM    538  CA  SER B 247     276.814 427.3301355.492  1.00 42.63           C  
ATOM    539  CA  ASP B 248     277.700 427.8671351.842  1.00 41.28           C  
ATOM    540  CA  ILE B 249     276.277 424.4411351.068  1.00 33.70           C  
ATOM    541  CA  SER B 250     272.988 425.3521352.764  1.00 36.12           C  
ATOM    542  CA  ALA B 251     272.831 428.6121350.868  1.00 38.26           C  
ATOM    543  CA  ILE B 252     273.616 427.0211347.512  1.00 33.42           C  
ATOM    544  CA  LYS B 253     271.020 424.2811348.070  1.00 36.12           C  
ATOM    545  CA  THR B 254     268.471 427.0431348.455  1.00 36.98           C  
ATOM    546  CA  SER B 255     269.621 428.8181345.329  1.00 34.22           C  
ATOM    547  CA  ILE B 256     269.305 425.7051343.321  1.00 31.70           C  
ATOM    548  CA  SER B 263     266.704 430.6671338.262  1.00 36.03           C  
ATOM    549  CA  ILE B 264     265.311 427.8201336.184  1.00 35.85           C  
ATOM    550  CA  ILE B 265     262.743 429.9061334.303  1.00 36.24           C  
ATOM    551  CA  THR B 266     265.241 432.6971333.763  1.00 33.52           C  
ATOM    552  CA  SER B 267     267.784 430.2901332.172  1.00 35.45           C  
ATOM    553  CA  VAL B 268     265.075 428.7561329.974  1.00 38.03           C  
ATOM    554  CA  ASN B 269     263.986 432.2641328.853  1.00 36.82           C  
ATOM    555  CA  THR B 270     267.484 433.5071327.992  1.00 34.99           C  
ATOM    556  CA  ASN B 271     267.765 430.2571326.084  1.00 38.90           C  
ATOM    557  CA  THR B 272     264.854 430.8681323.711  1.00 36.09           C  
ATOM    558  CA  ASP B 273     265.702 434.5061323.341  1.00 33.69           C  
ATOM    559  CA  ASN B 274     269.239 433.7031322.305  1.00 31.16           C  
ATOM    560  CA  ILE B 275     267.890 431.1701319.851  1.00 34.98           C  
ATOM    561  CA  ALA B 276     265.606 433.8681318.402  1.00 38.53           C  
ATOM    562  CA  SER B 277     268.165 436.6111317.973  1.00 37.38           C  
ATOM    563  CA  ILE B 278     270.289 434.0041316.299  1.00 38.86           C  
ATOM    564  CA  ASN B 279     267.656 433.2831313.665  1.00 42.63           C  
ATOM    565  CA  LEU B 280     267.267 436.9591312.813  1.00 41.28           C  
ATOM    566  CA  GLU B 281     271.045 437.2501312.666  1.00 33.70           C  
ATOM    567  CA  ILE B 288     271.967 438.1431308.051  1.00 66.02           C  
ATOM    568  CA  LYS B 289     270.945 436.0901304.950  1.00 64.90           C  
ATOM    569  CA  GLN B 290     268.698 438.9251303.716  1.00 64.92           C  
ATOM    570  CA  ARG B 291     271.522 441.4871303.732  1.00 63.61           C  
ATOM    571  CA  LEU B 292     273.910 438.9031302.213  1.00 63.93           C  
ATOM    572  CA  THR B 293     271.247 438.6671299.521  1.00 58.57           C  
ATOM    573  CA  VAL B 294     270.763 442.3891298.971  1.00 52.40           C  
ATOM    574  CA  ILE B 295     274.550 442.9931299.064  1.00 52.49           C  
ATOM    575  CA  GLU B 296     275.247 440.3541296.458  1.00 58.67           C  
ATOM    576  CA  THR B 297     272.563 441.8611294.219  1.00 55.76           C  
ATOM    577  CA  SER B 298     274.227 445.2331294.241  1.00 51.68           C  
ATOM    578  CA  ILE B 299     277.578 443.6731293.350  1.00 56.38           C  
ATOM    579  CA  ILE B 308     274.819 447.2101291.539  1.00 66.02           C  
ATOM    580  CA  LYS B 309     274.054 444.3431289.074  1.00 64.90           C  
ATOM    581  CA  GLY B 310     271.923 446.6661286.912  1.00 64.92           C  
ATOM    582  CA  GLN B 311     274.742 449.1881286.429  1.00 63.61           C  
ATOM    583  CA  ILE B 312     277.242 446.3331285.901  1.00 63.93           C  
ATOM    584  CA  LYS B 313     274.811 445.2891283.181  1.00 58.57           C  
ATOM    585  CA  ASP B 314     274.383 448.6931281.563  1.00 52.40           C  
ATOM    586  CA  ASN B 315     278.151 449.3801281.784  1.00 52.49           C  
ATOM    587  CA  THR B 316     279.056 446.1281280.097  1.00 58.67           C  
ATOM    588  CA  THR B 317     276.571 446.8841277.315  1.00 55.76           C  
ATOM    589  CA  SER B 318     278.235 450.1601276.516  1.00 51.68           C  
ATOM    590  CA  ILE B 319     281.645 448.4841276.375  1.00 56.38           C  
ATOM    591  CA  LEU B 334     279.237 451.3021274.273  1.00 66.02           C  
ATOM    592  CA  ARG B 335     279.519 448.3771271.775  1.00 64.90           C  
ATOM    593  CA  ALA B 336     276.986 450.0281269.436  1.00 64.92           C  
ATOM    594  CA  ASN B 337     278.992 453.2581269.160  1.00 63.61           C  
ATOM    595  CA  VAL B 338     282.239 451.2471268.849  1.00 63.93           C  
ATOM    596  CA  SER B 339     280.428 449.5961265.953  1.00 58.57           C  
ATOM    597  CA  TRP B 340     279.168 452.7611264.283  1.00 52.40           C  
ATOM    598  CA  LEU B 341     282.552 454.4941264.797  1.00 52.49           C  
ATOM    599  CA  ASN B 342     284.479 451.6651263.208  1.00 58.67           C  
ATOM    600  CA  GLN B 343     282.105 451.7231260.234  1.00 55.76           C  
ATOM    601  CA  ILE B 344     282.817 455.3511259.547  1.00 51.68           C  
ATOM    602  CA  VAL B 345     286.565 454.7251259.686  1.00 56.38           C  
ATOM    603  CA  SER B 359     280.620 457.0291257.665  1.00 36.03           C  
ATOM    604  CA  LEU B 360     283.765 455.2701256.488  1.00 35.85           C  
ATOM    605  CA  LEU B 361     282.355 454.1111253.148  1.00 36.24           C  
ATOM    606  CA  ASN B 362     280.731 457.4731252.538  1.00 33.52           C  
ATOM    607  CA  ARG B 363     284.064 459.3241253.051  1.00 35.45           C  
ATOM    608  CA  VAL B 364     285.874 456.8551250.784  1.00 38.03           C  
ATOM    609  CA  SER B 365     283.186 457.3501248.085  1.00 36.82           C  
ATOM    610  CA  THR B 366     283.241 461.1591248.168  1.00 34.99           C  
ATOM    611  CA  ILE B 367     286.988 460.7381247.905  1.00 38.90           C  
ATOM    612  CA  GLU B 368     287.006 458.8731244.587  1.00 36.09           C  
ATOM    613  CA  THR B 369     284.242 460.9921243.189  1.00 33.69           C  
ATOM    614  CA  SER B 370     286.139 464.1691243.923  1.00 31.16           C  
ATOM    615  CA  VAL B 371     283.711 464.5721244.565  1.00 66.02           C  
ATOM    616  CA  SER B 372     286.687 462.8581242.809  1.00 64.90           C  
ATOM    617  CA  GLY B 373     284.644 462.4141239.608  1.00 64.92           C  
ATOM    618  CA  LEU B 374     283.857 466.1331239.314  1.00 63.61           C  
ATOM    619  CA  ASN B 375     287.465 467.0001240.271  1.00 63.93           C  
ATOM    620  CA  ASN B 376     288.322 464.7531237.336  1.00 58.57           C  
ATOM    621  CA  ALA B 377     285.873 466.2311234.844  1.00 52.40           C  
ATOM    622  CA  VAL B 378     286.760 469.7981235.943  1.00 52.49           C  
ATOM    623  CA  GLN B 379     290.464 469.2461235.477  1.00 58.67           C  
ATOM    624  CA  ASN B 380     289.812 467.8251232.008  1.00 55.76           C  
ATOM    625  CA  LEU B 381     288.033 470.9471230.900  1.00 51.68           C  
ATOM    626  CA  GLN B 382     290.885 473.1181232.170  1.00 56.38           C  
ATOM    627  CA  VAL B 383     293.437 471.1791230.200  1.00 57.81           C  
ATOM    628  CA  GLU B 384     290.882 471.4271227.364  1.00 56.80           C  
ATOM    629  CA  ILE B 385     290.340 475.2071227.302  1.00 53.25           C  
ATOM    630  CA  GLY B 386     294.076 475.3331227.866  1.00 57.45           C  
ATOM    631  CA  ASN B 387     296.133 478.5021227.950  1.00 61.13           C  
ATOM    632  CA  ASN B 388     297.687 480.9511225.479  1.00 56.21           C  
ATOM    633  CA  SER B 389     300.007 478.2421224.411  1.00 52.91           C  
ATOM    634  CA  ALA B 390     297.722 475.2031224.339  1.00 49.07           C  
ATOM    635  CA  GLY B 391     294.178 473.9611224.000  1.00 46.98           C  
ATOM    636  CA  ILE B 392     291.310 475.9161222.572  1.00 43.17           C  
ATOM    637  CA  LYS B 393     292.696 479.1441224.020  1.00 44.95           C  
ATOM    638  CA  GLY B 394     295.990 478.4681222.249  1.00 41.35           C  
ATOM    639  CA  GLN B 395     294.422 477.7801218.868  1.00 42.54           C  
ATOM    640  CA  VAL B 396     292.317 480.9721219.008  1.00 37.57           C  
ATOM    641  CA  VAL B 397     295.300 483.1161220.067  1.00 36.68           C  
ATOM    642  CA  ALA B 398     297.140 481.9091216.979  1.00 36.11           C  
ATOM    643  CA  LEU B 399     294.077 482.6271214.842  1.00 36.19           C  
ATOM    644  CA  ASN B 400     293.943 486.2411216.057  1.00 41.94           C  
ATOM    645  CA  THR B 401     297.664 486.6701215.668  1.00 42.48           C  
ATOM    646  CA  LEU B 402     297.496 485.6581212.014  1.00 45.15           C  
ATOM    647  CA  VAL B 403     294.425 487.7671211.277  1.00 46.90           C  
ATOM    648  CA  ASN B 404     295.710 490.9731212.869  1.00 55.51           C  
ATOM    649  CA  GLY B 405     299.441 490.6481212.323  1.00 54.83           C  
ATOM    650  CA  THR B 406     302.703 491.1601214.247  1.00 57.60           C  
ATOM    651  CA  ASN B 407     304.095 494.1041212.394  1.00 60.39           C  
ATOM    652  CA  PRO B 408     301.875 496.1001210.046  1.00 64.08           C  
ATOM    653  CA  ASN B 409     304.826 497.6831208.189  1.00 66.30           C  
ATOM    654  CA  GLY B 410     306.149 494.1601207.975  1.00 61.13           C  
ATOM    655  CA  SER B 411     307.297 492.3511204.890  1.00 61.42           C  
ATOM    656  CA  THR B 412     305.317 489.0841205.143  1.00 52.20           C  
ATOM    657  CA  VAL B 413     301.635 488.2061204.987  1.00 48.08           C  
ATOM    658  CA  GLU B 414     301.874 486.7761208.541  1.00 46.50           C  
ATOM    659  CA  GLU B 415     303.610 489.9111209.766  1.00 45.01           C  
ATOM    660  CA  ARG B 416     301.002 492.2491208.295  1.00 40.02           C  
ATOM    661  CA  GLY B 417     298.117 489.9921209.228  1.00 35.39           C  
ATOM    662  CA  LEU B 418     295.535 488.5101206.868  1.00 36.03           C  
ATOM    663  CA  THR B 419     293.287 491.5591207.028  1.00 35.85           C  
ATOM    664  CA  ASN B 420     295.982 494.0971206.141  1.00 36.24           C  
ATOM    665  CA  SER B 421     297.343 491.8651203.405  1.00 33.52           C  
ATOM    666  CA  ILE B 422     293.888 491.5761201.740  1.00 35.45           C  
ATOM    667  CA  LYS B 423     293.358 495.3401202.008  1.00 38.03           C  
ATOM    668  CA  ALA B 424     296.801 495.9481200.420  1.00 36.82           C  
ATOM    669  CA  ASN B 425     296.308 493.5641197.487  1.00 34.99           C  
ATOM    670  CA  GLU B 426     293.014 495.3691197.059  1.00 38.90           C  
ATOM    671  CA  THR B 427     294.465 498.8431196.509  1.00 36.09           C  
ATOM    672  CA  ASN B 428     297.307 497.5131194.450  1.00 33.69           C  
ATOM    673  CA  ILE B 429     294.944 495.7341192.112  1.00 31.16           C  
ATOM    674  CA  ALA B 430     292.906 498.9021191.843  1.00 34.98           C  
ATOM    675  CA  SER B 431     296.087 500.8051190.918  1.00 38.53           C  
ATOM    676  CA  VAL B 432     297.395 498.4711188.255  1.00 37.38           C  
ATOM    677  CA  THR B 433     293.926 498.5961186.816  1.00 38.86           C  
ATOM    678  CA  GLN B 434     294.030 502.3661186.411  1.00 42.63           C  
ATOM    679  CA  GLU B 435     297.365 502.2431184.605  1.00 41.28           C  
ATOM    680  CA  VAL B 436     296.002 499.4561182.428  1.00 33.70           C  
ATOM    681  CA  ASN B 437     292.984 501.5831181.483  1.00 36.12           C  
ATOM    682  CA  THR B 438     295.216 504.5191180.680  1.00 38.26           C  
ATOM    683  CA  ALA B 439     297.642 502.4671178.604  1.00 33.42           C  
ATOM    684  CA  LYS B 440     294.789 500.8401176.661  1.00 36.12           C  
ATOM    685  CA  GLY B 441     293.729 504.3301175.675  1.00 36.98           C  
ATOM    686  CA  ASN B 442     297.224 505.3211174.651  1.00 34.22           C  
ATOM    687  CA  ILE B 443     297.537 502.3401172.451  1.00 31.70           C  
ATOM    688  CA  SER B 444     294.186 503.0791170.793  1.00 32.29           C  
ATOM    689  CA  SER B 445     295.417 506.4671169.807  1.00 32.47           C  
ATOM    690  CA  LEU B 446     298.635 504.8281168.671  1.00 28.05           C  
ATOM    691  CA  GLN B 447     296.833 502.4261166.385  1.00 29.60           C  
ATOM    692  CA  GLY B 448     294.972 505.2811164.754  1.00 29.46           C  
ATOM    693  CA  ASP B 449     298.178 507.2881164.323  1.00 29.14           C  
ATOM    694  CA  VAL B 450     299.835 504.3241162.583  1.00 32.26           C  
ATOM    695  CA  GLN B 451     296.704 503.6491160.526  1.00 38.22           C  
ATOM    696  CA  ALA B 452     296.866 507.2231159.320  1.00 35.96           C  
ATOM    697  CA  LEU B 453     300.572 507.0201158.366  1.00 34.01           C  
ATOM    698  CA  GLN B 454     299.987 503.6851156.588  1.00 34.42           C  
ATOM    699  CA  GLU B 455     297.052 505.1211154.576  1.00 35.15           C  
ATOM    700  CA  ALA B 456     298.973 508.2381153.717  1.00 31.68           C  
ATOM    701  CA  GLY B 457     300.553 506.8441150.542  1.00 32.56           C  
ATOM    702  CA  TYR B 458     304.035 508.1691151.033  1.00 31.35           C  
ATOM    703  CA  ILE B 459     306.646 507.4611148.452  1.00 31.40           C  
ATOM    704  CA  PRO B 460     310.014 505.8211149.032  1.00 32.94           C  
ATOM    705  CA  GLU B 461     313.408 507.0821147.967  1.00 33.93           C  
ATOM    706  CA  ALA B 462     314.214 507.2151144.225  1.00 35.50           C  
ATOM    707  CA  PRO B 463     317.240 505.1991142.937  1.00 37.70           C  
ATOM    708  CA  ARG B 464     320.669 506.6011143.865  1.00 43.46           C  
ATOM    709  CA  ASP B 465     322.583 506.1771140.597  1.00 42.68           C  
ATOM    710  CA  GLY B 466     323.729 509.6481139.558  1.00 41.53           C  
ATOM    711  CA  GLN B 467     320.558 510.2331137.569  1.00 39.66           C  
ATOM    712  CA  ALA B 468     317.599 512.6171137.904  1.00 34.55           C  
ATOM    713  CA  TYR B 469     314.106 511.1621138.364  1.00 33.51           C  
ATOM    714  CA  VAL B 470     310.544 512.5181138.217  1.00 33.42           C  
ATOM    715  CA  ARG B 471     307.188 511.0491139.378  1.00 35.41           C  
ATOM    716  CA  LYS B 472     304.898 509.1651136.936  1.00 39.68           C  
ATOM    717  CA  ASP B 473     302.262 506.3921137.555  1.00 41.29           C  
ATOM    718  CA  GLY B 474     303.701 504.9191140.769  1.00 41.26           C  
ATOM    719  CA  GLU B 475     307.191 504.5121139.239  1.00 40.70           C  
ATOM    720  CA  TRP B 476     310.218 506.8831139.309  1.00 41.16           C  
ATOM    721  CA  VAL B 477     311.170 507.7841135.689  1.00 40.33           C  
ATOM    722  CA  PHE B 478     314.410 509.2091134.311  1.00 34.39           C  
ATOM    723  CA  LEU B 479     314.027 512.9141133.684  1.00 36.69           C  
ATOM    724  CA  SER B 480     316.275 512.5681130.603  1.00 44.11           C  
ATOM    725  CA  THR B 481     313.433 510.5731128.950  1.00 50.73           C  
ATOM    726  CA  PHE B 482     311.599 513.9071128.484  1.00 57.21           C  
ATOM    727  CA  LEU B 483     314.634 516.2501128.451  1.00 61.29           C  
TER     728      LEU B 483                                                      
ATOM    729  CA  ASP C   2     238.642 442.0091380.118  1.00 46.92           C  
ATOM    730  CA  ILE C   3     235.321 443.0471381.685  1.00 34.11           C  
ATOM    731  CA  VAL C   4     232.763 440.2551382.085  1.00 28.51           C  
ATOM    732  CA  LEU C   5     229.099 441.2821382.218  1.00 24.61           C  
ATOM    733  CA  ASN C   6     225.962 439.1731382.765  1.00 23.35           C  
ATOM    734  CA  ASP C   7     223.764 438.2991379.774  1.00 22.18           C  
ATOM    735  CA  LEU C   8     220.069 439.2651380.082  1.00 18.58           C  
ATOM    736  CA  PRO C   9     218.063 436.2551381.374  1.00 16.95           C  
ATOM    737  CA  PHE C  10     214.948 436.8461379.245  1.00 15.82           C  
ATOM    738  CA  VAL C  11     214.748 437.6121375.512  1.00 14.91           C  
ATOM    739  CA  ASP C  12     211.931 438.2231373.041  1.00 17.94           C  
ATOM    740  CA  GLY C  13     213.253 435.7531370.470  1.00 19.17           C  
ATOM    741  CA  PRO C  14     215.260 432.4651370.188  1.00 19.29           C  
ATOM    742  CA  PRO C  15     217.329 432.1461373.362  1.00 19.60           C  
ATOM    743  CA  ALA C  16     221.053 431.5971373.604  1.00 21.64           C  
ATOM    744  CA  GLU C  17     222.947 429.8031376.379  1.00 23.66           C  
ATOM    745  CA  GLY C  18     221.587 430.6711379.842  1.00 23.60           C  
ATOM    746  CA  GLN C  19     218.561 432.5921378.539  1.00 20.26           C  
ATOM    747  CA  SER C  20     214.843 431.9151378.404  1.00 21.74           C  
ATOM    748  CA  ARG C  21     212.277 433.2311375.945  1.00 20.74           C  
ATOM    749  CA  ILE C  22     209.713 435.6361377.404  1.00 19.44           C  
ATOM    750  CA  SER C  23     206.195 434.2111377.497  1.00 20.45           C  
ATOM    751  CA  TRP C  24     203.716 436.9381376.505  1.00 18.66           C  
ATOM    752  CA  ILE C  25     200.067 436.7911377.557  1.00 22.73           C  
ATOM    753  CA  LYS C  26     198.116 434.6301375.115  1.00 28.17           C  
ATOM    754  CA  ASN C  27     194.456 434.6851374.187  1.00 34.03           C  
ATOM    755  CA  GLY C  28     192.701 431.5881375.473  1.00 39.29           C  
ATOM    756  CA  GLU C  29     194.902 431.6651378.538  1.00 40.23           C  
ATOM    757  CA  GLU C  30     193.487 432.1211382.033  1.00 40.77           C  
ATOM    758  CA  ILE C  31     193.954 435.7951383.053  1.00 37.71           C  
ATOM    759  CA  LEU C  32     195.078 435.6391386.696  1.00 32.76           C  
ATOM    760  CA  GLY C  33     196.926 437.7351389.267  1.00 27.76           C  
ATOM    761  CA  ALA C  34     198.685 436.8841392.558  1.00 27.47           C  
ATOM    762  CA  ASP C  35     197.117 435.3041395.651  1.00 33.69           C  
ATOM    763  CA  THR C  36     199.383 436.8901398.307  1.00 32.87           C  
ATOM    764  CA  GLN C  37     200.090 440.5311399.149  1.00 32.27           C  
ATOM    765  CA  TYR C  38     203.661 440.1491397.899  1.00 30.85           C  
ATOM    766  CA  GLY C  39     203.626 437.3691395.291  1.00 25.38           C  
ATOM    767  CA  SER C  40     204.162 437.9171391.556  1.00 24.14           C  
ATOM    768  CA  GLU C  41     202.376 434.8301390.214  1.00 25.45           C  
ATOM    769  CA  GLY C  42     199.661 435.0251387.568  1.00 25.08           C  
ATOM    770  CA  SER C  43     199.670 435.4661383.797  1.00 23.23           C  
ATOM    771  CA  MET C  44     198.856 439.1701384.122  1.00 23.26           C  
ATOM    772  CA  ASN C  45     202.184 439.7181385.896  1.00 21.52           C  
ATOM    773  CA  ARG C  46     204.345 437.1971384.023  1.00 19.86           C  
ATOM    774  CA  PRO C  47     205.853 439.2051381.192  1.00 18.04           C  
ATOM    775  CA  THR C  48     206.480 442.2251383.465  1.00 15.26           C  
ATOM    776  CA  VAL C  49     208.240 439.9911386.050  1.00 15.15           C  
ATOM    777  CA  SER C  50     210.532 438.7671383.225  1.00 16.25           C  
ATOM    778  CA  VAL C  51     211.366 442.3071382.151  1.00 12.03           C  
ATOM    779  CA  LEU C  52     212.099 443.2681385.796  1.00 12.21           C  
ATOM    780  CA  ARG C  53     214.541 440.3341386.031  1.00 12.71           C  
ATOM    781  CA  ASN C  54     216.414 441.8621383.072  1.00 12.32           C  
ATOM    782  CA  VAL C  55     216.342 445.2691384.787  1.00 12.32           C  
ATOM    783  CA  GLU C  56     217.919 443.7471387.933  1.00 13.65           C  
ATOM    784  CA AVAL C  57     220.724 442.2681385.796  0.60  7.63           C  
ATOM    785  CA  LEU C  58     221.308 445.5881384.028  1.00 12.48           C  
ATOM    786  CA  ASP C  59     221.627 447.2921387.424  1.00 15.15           C  
ATOM    787  CA  LYS C  60     224.343 444.7831388.427  1.00 17.96           C  
ATOM    788  CA  ASN C  61     226.149 445.2231385.106  1.00 14.05           C  
ATOM    789  CA  ILE C  62     226.279 448.9991385.685  1.00 15.66           C  
ATOM    790  CA  GLY C  63     227.754 448.3101389.123  1.00 17.96           C  
ATOM    791  CA  ILE C  64     230.480 446.1821387.523  1.00 19.80           C  
ATOM    792  CA  LEU C  65     231.335 449.0361385.088  1.00 18.59           C  
ATOM    793  CA  LYS C  66     231.309 451.5721387.932  1.00 20.06           C  
ATOM    794  CA  THR C  67     233.886 449.5811389.923  1.00 22.33           C  
ATOM    795  CA  SER C  68     236.165 449.2421386.930  1.00 20.95           C  
ATOM    796  CA  LEU C  69     235.860 452.9351386.065  1.00 19.55           C  
ATOM    797  CA  GLU C  70     236.658 453.9191389.665  1.00 20.63           C  
ATOM    798  CA  THR C  71     239.812 451.8381389.438  1.00 22.04           C  
ATOM    799  CA  ALA C  72     240.775 453.5421386.158  1.00 19.43           C  
ATOM    800  CA  ASN C  73     240.185 456.9901387.657  1.00 20.13           C  
ATOM    801  CA  SER C  74     242.425 456.0751390.591  1.00 20.92           C  
ATOM    802  CA  ASP C  75     245.171 454.7481388.277  1.00 20.16           C  
ATOM    803  CA  ILE C  76     245.015 457.9831386.252  1.00 18.71           C  
ATOM    804  CA  LYS C  77     245.328 460.1071389.385  1.00 22.05           C  
ATOM    805  CA  THR C  78     248.422 458.0721390.365  1.00 22.36           C  
ATOM    806  CA  ILE C  79     250.029 458.7461386.963  1.00 17.58           C  
ATOM    807  CA  GLN C  80     249.234 462.4871387.208  1.00 21.05           C  
ATOM    808  CA  ILE C  97     257.883 453.2071380.796  1.00 36.03           C  
ATOM    809  CA  ASN C  98     258.728 454.8801384.092  1.00 35.85           C  
ATOM    810  CA  LYS C  99     261.974 452.9851384.688  1.00 36.24           C  
ATOM    811  CA  LYS C 100     263.020 453.4121381.078  1.00 33.52           C  
ATOM    812  CA  ASP C 101     262.576 457.2291381.263  1.00 35.45           C  
ATOM    813  CA  ILE C 102     264.481 457.3681384.561  1.00 38.03           C  
ATOM    814  CA  SER C 103     267.326 455.3021383.015  1.00 36.82           C  
ATOM    815  CA  ASP C 104     267.664 457.4021379.852  1.00 34.99           C  
ATOM    816  CA  LEU C 105     267.723 460.3251382.249  1.00 38.90           C  
ATOM    817  CA  LYS C 106     270.809 459.2541384.200  1.00 36.09           C  
ATOM    818  CA  THR C 107     272.547 458.0311381.106  1.00 33.69           C  
ATOM    819  CA  LEU C 108     272.091 461.3571379.386  1.00 31.16           C  
ATOM    820  CA  THR C 109     273.386 463.0781382.487  1.00 34.98           C  
ATOM    821  CA  SER C 110     276.467 460.8231382.390  1.00 38.53           C  
ATOM    822  CA  GLU C 111     277.379 461.2591378.753  1.00 37.38           C  
ATOM    823  CA  HIS C 112     277.030 464.9461379.382  1.00 38.86           C  
ATOM    824  CA  THR C 113     279.652 464.9171382.123  1.00 42.63           C  
ATOM    825  CA  GLU C 114     282.155 463.0921379.931  1.00 41.28           C  
ATOM    826  CA  ILE C 115     281.379 465.5321377.137  1.00 33.70           C  
ATOM    827  CA  LEU C 116     282.099 468.4891379.432  1.00 36.12           C  
ATOM    828  CA  ASN C 117     285.344 466.9191380.552  1.00 38.26           C  
ATOM    829  CA  GLY C 118     286.484 466.0871377.027  1.00 33.42           C  
ATOM    830  CA  THR C 119     285.654 469.6061375.802  1.00 36.12           C  
ATOM    831  CA  ASN C 120     288.029 470.8791378.451  1.00 36.98           C  
ATOM    832  CA  ASN C 121     290.746 468.4501377.470  1.00 34.22           C  
ATOM    833  CA  THR C 122     290.546 469.5011373.910  1.00 31.70           C  
ATOM    834  CA  VAL C 123     290.768 473.1821374.873  1.00 32.29           C  
ATOM    835  CA  ASP C 124     294.007 472.5331376.618  1.00 32.47           C  
ATOM    836  CA  SER C 125     295.081 470.5111373.604  1.00 28.05           C  
ATOM    837  CA  ILE C 126     294.437 473.3631371.217  1.00 29.60           C  
ATOM    838  CA  LEU C 127     296.538 475.6861373.331  1.00 29.46           C  
ATOM    839  CA  ALA C 128     299.356 473.1361373.551  1.00 29.14           C  
ATOM    840  CA  ASP C 129     299.398 472.8081369.750  1.00 32.26           C  
ATOM    841  CA  ILE C 130     299.115 476.5791369.318  1.00 38.22           C  
ATOM    842  CA  ILE C 144     310.532 463.0031372.828  1.00 66.02           C  
ATOM    843  CA  ARG C 145     310.140 460.1171370.300  1.00 64.90           C  
ATOM    844  CA  ASN C 146     313.934 459.7721369.985  1.00 64.92           C  
ATOM    845  CA  ASP C 147     314.435 459.2641373.731  1.00 63.61           C  
ATOM    846  CA  LEU C 148     311.384 456.9491373.852  1.00 63.93           C  
ATOM    847  CA  LEU C 149     313.265 455.0471371.160  1.00 58.57           C  
ATOM    848  CA  TRP C 150     316.648 454.9711372.877  1.00 52.40           C  
ATOM    849  CA  ILE C 151     315.027 454.1111376.246  1.00 52.49           C  
ATOM    850  CA  LYS C 152     313.107 451.1941374.815  1.00 58.67           C  
ATOM    851  CA  ARG C 153     316.299 449.8851373.209  1.00 55.76           C  
ATOM    852  CA  GLU C 154     318.088 449.7591376.513  1.00 51.68           C  
ATOM    853  CA  LEU C 155     315.189 447.8821378.103  1.00 56.38           C  
ATOM    854  CA  MET C 176     326.772 449.0171381.261  1.00 36.03           C  
ATOM    855  CA  LYS C 177     326.219 448.2571384.933  1.00 35.85           C  
ATOM    856  CA  HIS C 178     322.609 447.1081384.572  1.00 36.24           C  
ATOM    857  CA  ARG C 179     323.442 445.0971381.477  1.00 33.52           C  
ATOM    858  CA  ILE C 180     326.237 443.1911383.305  1.00 35.45           C  
ATOM    859  CA  ILE C 181     323.956 442.5541386.291  1.00 38.03           C  
ATOM    860  CA  ASN C 182     321.225 441.2351383.935  1.00 36.82           C  
ATOM    861  CA  ASN C 183     323.494 438.8751381.985  1.00 34.99           C  
ATOM    862  CA  THR C 184     324.605 437.7161385.406  1.00 38.90           C  
ATOM    863  CA  ASP C 185     321.192 436.5541386.625  1.00 36.09           C  
ATOM    864  CA  VAL C 186     320.283 435.1511383.265  1.00 33.69           C  
ATOM    865  CA  ILE C 187     323.406 433.0381383.165  1.00 31.16           C  
ATOM    866  CA  THR C 188     322.658 431.8591386.673  1.00 34.98           C  
ATOM    867  CA  SER C 189     319.149 430.8641385.535  1.00 38.53           C  
ATOM    868  CA  GLN C 190     320.084 428.9421382.423  1.00 37.38           C  
ATOM    869  CA  GLY C 191     322.579 427.1601384.592  1.00 38.86           C  
ATOM    870  CA  ILE C 192     319.903 425.9341386.987  1.00 42.63           C  
ATOM    871  CA  ARG C 193     317.779 424.5571384.159  1.00 41.28           C  
ATOM    872  CA  LEU C 194     320.883 422.9301382.714  1.00 33.70           C  
ATOM    873  CA  SER C 208     315.224 414.5101380.289  1.00 66.02           C  
ATOM    874  CA  LEU C 209     312.541 413.3861382.823  1.00 64.90           C  
ATOM    875  CA  THR C 210     310.364 416.4121381.979  1.00 64.92           C  
ATOM    876  CA  ILE C 211     310.250 415.5891378.258  1.00 63.61           C  
ATOM    877  CA  GLU C 212     309.746 411.8781379.067  1.00 63.93           C  
ATOM    878  CA  VAL C 213     306.790 413.1631381.069  1.00 58.57           C  
ATOM    879  CA  GLY C 214     305.350 415.4581378.413  1.00 52.40           C  
ATOM    880  CA  ASN C 215     305.901 412.8111375.691  1.00 52.49           C  
ATOM    881  CA  LEU C 216     304.097 410.1291377.638  1.00 58.67           C  
ATOM    882  CA  ARG C 217     301.182 412.5091378.210  1.00 55.76           C  
ATOM    883  CA  GLU C 218     300.710 413.0551374.520  1.00 51.68           C  
ATOM    884  CA  GLU C 219     300.732 409.3061373.882  1.00 56.38           C  
ATOM    885  CA  LEU C 220     298.021 408.7071376.419  1.00 57.81           C  
ATOM    886  CA  VAL C 231     290.478 415.3501371.039  1.00 36.03           C  
ATOM    887  CA  TYR C 232     289.269 411.9001370.035  1.00 35.85           C  
ATOM    888  CA  SER C 233     285.562 412.7621370.000  1.00 36.24           C  
ATOM    889  CA  ARG C 234     286.225 416.0351368.219  1.00 33.52           C  
ATOM    890  CA  LEU C 235     288.150 414.2621365.400  1.00 35.45           C  
ATOM    891  CA  ASN C 236     285.413 411.6301365.080  1.00 38.03           C  
ATOM    892  CA  GLU C 237     282.761 414.4001364.872  1.00 36.82           C  
ATOM    893  CA  ILE C 238     284.554 416.4641362.218  1.00 34.99           C  
ATOM    894  CA  ASP C 239     284.861 413.1681360.395  1.00 38.90           C  
ATOM    895  CA  THR C 240     281.134 412.4581360.106  1.00 36.09           C  
ATOM    896  CA  LYS C 241     280.330 416.0601359.424  1.00 33.69           C  
ATOM    897  CA  GLN C 242     282.764 416.1861356.545  1.00 31.16           C  
ATOM    898  CA  THR C 243     281.278 412.9791355.216  1.00 34.98           C  
ATOM    899  CA  THR C 244     277.811 414.5751355.392  1.00 38.53           C  
ATOM    900  CA  VAL C 245     278.598 417.8401353.668  1.00 37.38           C  
ATOM    901  CA  GLU C 246     280.225 415.7401351.011  1.00 38.86           C  
ATOM    902  CA  SER C 247     277.031 413.8171350.313  1.00 42.63           C  
ATOM    903  CA  ASP C 248     275.003 417.0011349.935  1.00 41.28           C  
ATOM    904  CA  ILE C 249     277.724 418.3801347.683  1.00 33.70           C  
ATOM    905  CA  SER C 250     277.538 415.2911345.459  1.00 36.12           C  
ATOM    906  CA  ALA C 251     273.776 415.5551345.287  1.00 38.26           C  
ATOM    907  CA  ILE C 252     273.793 419.2701344.500  1.00 33.42           C  
ATOM    908  CA  LYS C 253     276.433 418.8031341.785  1.00 36.12           C  
ATOM    909  CA  THR C 254     274.033 416.3961340.136  1.00 36.98           C  
ATOM    910  CA  SER C 255     271.121 418.7771340.429  1.00 34.22           C  
ATOM    911  CA  ILE C 256     273.059 421.5101338.815  1.00 31.70           C  
ATOM    912  CA  SER C 263     271.689 424.9301335.709  1.00 36.03           C  
ATOM    913  CA  ILE C 264     275.435 425.5171335.665  1.00 35.85           C  
ATOM    914  CA  ILE C 265     276.036 424.0471332.206  1.00 36.24           C  
ATOM    915  CA  THR C 266     272.992 425.8051330.806  1.00 33.52           C  
ATOM    916  CA  SER C 267     274.237 429.2281332.043  1.00 35.45           C  
ATOM    917  CA  VAL C 268     277.721 428.5491330.656  1.00 38.03           C  
ATOM    918  CA  ASN C 269     276.193 427.5731327.271  1.00 36.82           C  
ATOM    919  CA  THR C 270     273.940 430.6311326.958  1.00 34.99           C  
ATOM    920  CA  ASN C 271     277.075 432.5631327.814  1.00 38.90           C  
ATOM    921  CA  THR C 272     279.159 431.3831324.856  1.00 36.09           C  
ATOM    922  CA  ASP C 273     276.230 431.5391322.515  1.00 33.69           C  
ATOM    923  CA  ASN C 274     275.546 435.1381323.413  1.00 31.16           C  
ATOM    924  CA  ILE C 275     279.210 435.9041322.917  1.00 34.98           C  
ATOM    925  CA  ALA C 276     279.021 434.3041319.453  1.00 38.53           C  
ATOM    926  CA  SER C 277     275.931 436.0601318.182  1.00 37.38           C  
ATOM    927  CA  ILE C 278     277.569 439.2291319.358  1.00 38.86           C  
ATOM    928  CA  ASN C 279     280.619 438.6861317.168  1.00 42.63           C  
ATOM    929  CA  LEU C 280     278.495 438.0971314.079  1.00 41.28           C  
ATOM    930  CA  GLU C 281     276.477 441.1811314.965  1.00 33.70           C  
ATOM    931  CA  ILE C 288     278.383 441.5381310.792  1.00 66.02           C  
ATOM    932  CA  LYS C 289     282.012 442.5991310.032  1.00 64.90           C  
ATOM    933  CA  GLN C 290     281.892 440.8601306.630  1.00 64.92           C  
ATOM    934  CA  ARG C 291     278.823 442.8081305.479  1.00 63.61           C  
ATOM    935  CA  LEU C 292     280.277 446.0291306.961  1.00 63.93           C  
ATOM    936  CA  THR C 293     283.241 445.1941304.743  1.00 58.57           C  
ATOM    937  CA  VAL C 294     281.296 444.4451301.573  1.00 52.40           C  
ATOM    938  CA  ILE C 295     279.033 447.4921302.127  1.00 52.49           C  
ATOM    939  CA  GLU C 296     281.951 449.8501302.532  1.00 58.67           C  
ATOM    940  CA  THR C 297     283.499 448.4771299.339  1.00 55.76           C  
ATOM    941  CA  SER C 298     280.438 449.3071297.320  1.00 51.68           C  
ATOM    942  CA  ILE C 299     280.390 452.8491298.702  1.00 56.38           C  
ATOM    943  CA  ILE C 308     280.992 451.3771293.713  1.00 66.02           C  
ATOM    944  CA  LYS C 309     284.675 452.2581292.979  1.00 64.90           C  
ATOM    945  CA  GLY C 310     284.834 449.6271290.209  1.00 64.92           C  
ATOM    946  CA  GLN C 311     281.875 451.1041288.312  1.00 63.61           C  
ATOM    947  CA  ILE C 312     283.209 454.6431288.933  1.00 63.93           C  
ATOM    948  CA  LYS C 313     286.344 453.2801287.288  1.00 58.57           C  
ATOM    949  CA  ASP C 314     284.668 451.6251284.314  1.00 52.40           C  
ATOM    950  CA  ASN C 315     282.374 454.6561283.799  1.00 52.49           C  
ATOM    951  CA  THR C 316     285.253 457.0941283.753  1.00 58.67           C  
ATOM    952  CA  THR C 317     287.059 454.9091281.214  1.00 55.76           C  
ATOM    953  CA  SER C 318     284.177 455.0691278.804  1.00 51.68           C  
ATOM    954  CA  ILE C 319     284.023 458.8561279.117  1.00 56.38           C  
ATOM    955  CA  LEU C 334     283.767 457.0271276.900  1.00 66.02           C  
ATOM    956  CA  ARG C 335     287.088 458.9371276.452  1.00 64.90           C  
ATOM    957  CA  ALA C 336     288.209 456.5071273.721  1.00 64.92           C  
ATOM    958  CA  ASN C 337     285.108 457.1061271.587  1.00 63.61           C  
ATOM    959  CA  VAL C 338     285.318 460.8681272.288  1.00 63.93           C  
ATOM    960  CA  SER C 339     288.831 460.4871270.904  1.00 58.57           C  
ATOM    961  CA  TRP C 340     287.935 458.4701267.818  1.00 52.40           C  
ATOM    962  CA  LEU C 341     284.915 460.7241267.104  1.00 52.49           C  
ATOM    963  CA  ASN C 342     286.969 463.8861267.269  1.00 58.67           C  
ATOM    964  CA  GLN C 343     289.516 462.3511264.896  1.00 55.76           C  
ATOM    965  CA  ILE C 344     286.905 461.7181262.264  1.00 51.68           C  
ATOM    966  CA  VAL C 345     285.648 465.2961262.539  1.00 56.38           C  
ATOM    967  CA  SER C 359     287.755 460.1671259.545  1.00 36.03           C  
ATOM    968  CA  LEU C 360     288.032 463.7801260.661  1.00 35.85           C  
ATOM    969  CA  LEU C 361     291.061 464.6351258.519  1.00 36.24           C  
ATOM    970  CA  ASN C 362     289.607 462.8161255.536  1.00 33.52           C  
ATOM    971  CA  ARG C 363     286.342 464.8401255.727  1.00 35.45           C  
ATOM    972  CA  VAL C 364     288.289 468.0941256.098  1.00 38.03           C  
ATOM    973  CA  SER C 365     290.428 467.1741253.044  1.00 36.82           C  
ATOM    974  CA  THR C 366     287.503 466.2641250.776  1.00 34.99           C  
ATOM    975  CA  ILE C 367     286.078 469.5761251.912  1.00 38.90           C  
ATOM    976  CA  GLU C 368     288.918 471.7591250.629  1.00 36.09           C  
ATOM    977  CA  THR C 369     289.306 469.7111247.507  1.00 33.69           C  
ATOM    978  CA  SER C 370     285.662 470.1261246.634  1.00 31.16           C  
ATOM    979  CA  VAL C 371     281.962 471.6351247.255  1.00 66.02           C  
ATOM    980  CA  SER C 372     282.994 475.3491247.395  1.00 64.90           C  
ATOM    981  CA  GLY C 373     286.261 474.5911245.559  1.00 64.92           C  
ATOM    982  CA  LEU C 374     284.492 472.9881242.587  1.00 63.61           C  
ATOM    983  CA  ASN C 375     281.848 475.7601242.629  1.00 63.93           C  
ATOM    984  CA  ASN C 376     284.866 478.0441242.351  1.00 58.57           C  
ATOM    985  CA  ALA C 377     286.636 476.1921239.553  1.00 52.40           C  
ATOM    986  CA  VAL C 378     283.340 475.7251237.646  1.00 52.49           C  
ATOM    987  CA  GLN C 379     282.491 479.3991237.795  1.00 58.67           C  
ATOM    988  CA  ASN C 380     285.974 480.2521236.525  1.00 55.76           C  
ATOM    989  CA  LEU C 381     285.527 478.1521233.439  1.00 51.68           C  
ATOM    990  CA  GLN C 382     282.175 479.7941232.711  1.00 56.38           C  
ATOM    991  CA  VAL C 383     283.663 483.2461232.871  1.00 57.81           C  
ATOM    992  CA  GLU C 384     286.465 481.7261230.756  1.00 56.80           C  
ATOM    993  CA  ILE C 385     284.403 480.2581227.897  1.00 53.25           C  
ATOM    994  CA  GLY C 386     282.427 483.4641228.230  1.00 57.45           C  
ATOM    995  CA  ASN C 387     279.586 484.4861225.957  1.00 61.13           C  
ATOM    996  CA  ASN C 388     279.120 486.0311222.506  1.00 56.21           C  
ATOM    997  CA  SER C 389     280.566 489.1921223.836  1.00 52.91           C  
ATOM    998  CA  ALA C 390     283.411 487.9241226.019  1.00 49.07           C  
ATOM    999  CA  GLY C 391     285.843 485.1171226.668  1.00 46.98           C  
ATOM   1000  CA  ILE C 392     286.771 482.4251224.221  1.00 43.17           C  
ATOM   1001  CA  LYS C 393     283.244 482.3971222.807  1.00 44.95           C  
ATOM   1002  CA  GLY C 394     283.520 486.1331222.170  1.00 41.35           C  
ATOM   1003  CA  GLN C 395     286.866 485.9301220.401  1.00 42.54           C  
ATOM   1004  CA  VAL C 396     285.663 483.1261218.092  1.00 37.57           C  
ATOM   1005  CA  VAL C 397     282.417 484.9601217.245  1.00 36.68           C  
ATOM   1006  CA  ALA C 398     284.501 487.9171216.104  1.00 36.11           C  
ATOM   1007  CA  LEU C 399     286.747 485.5931214.101  1.00 36.19           C  
ATOM   1008  CA  ASN C 400     283.758 484.1441212.224  1.00 41.94           C  
ATOM   1009  CA  THR C 401     282.247 487.5531211.694  1.00 42.48           C  
ATOM   1010  CA  LEU C 402     285.408 488.7991210.003  1.00 45.15           C  
ATOM   1011  CA  VAL C 403     285.856 485.6681207.901  1.00 46.90           C  
ATOM   1012  CA  ASN C 404     282.287 485.5081206.597  1.00 55.51           C  
ATOM   1013  CA  GLY C 405     281.340 489.1711206.523  1.00 54.83           C  
ATOM   1014  CA  THR C 406     278.401 491.4221207.473  1.00 57.60           C  
ATOM   1015  CA  ASN C 407     277.278 492.4961204.063  1.00 60.39           C  
ATOM   1016  CA  PRO C 408     278.540 490.6721200.979  1.00 64.08           C  
ATOM   1017  CA  ASN C 409     277.624 493.5291198.601  1.00 66.30           C  
ATOM   1018  CA  GLY C 410     279.398 495.7291201.096  1.00 61.13           C  
ATOM   1019  CA  SER C 411     282.129 498.2101200.395  1.00 61.42           C  
ATOM   1020  CA  THR C 412     284.771 497.1781202.967  1.00 52.20           C  
ATOM   1021  CA  VAL C 413     286.912 494.0931203.467  1.00 48.08           C  
ATOM   1022  CA  GLU C 414     285.291 493.5841206.909  1.00 46.50           C  
ATOM   1023  CA  GLU C 415     281.829 493.9671205.419  1.00 45.01           C  
ATOM   1024  CA  ARG C 416     282.446 491.4281202.661  1.00 40.02           C  
ATOM   1025  CA  GLY C 417     284.374 489.0941204.925  1.00 35.39           C  
ATOM   1026  CA  LEU C 418     287.929 487.8551204.415  1.00 36.03           C  
ATOM   1027  CA  THR C 419     286.859 484.9531202.225  1.00 35.85           C  
ATOM   1028  CA  ASN C 420     284.804 487.0241199.780  1.00 36.24           C  
ATOM   1029  CA  SER C 421     287.474 489.7021199.631  1.00 33.52           C  
ATOM   1030  CA  ILE C 422     290.180 487.1361198.686  1.00 35.45           C  
ATOM   1031  CA  LYS C 423     287.899 485.5821196.059  1.00 38.03           C  
ATOM   1032  CA  ALA C 424     287.202 489.0621194.592  1.00 36.82           C  
ATOM   1033  CA  ASN C 425     290.850 490.1461194.397  1.00 34.99           C  
ATOM   1034  CA  GLU C 426     291.368 486.7961192.725  1.00 38.90           C  
ATOM   1035  CA  THR C 427     289.014 487.3811189.793  1.00 36.09           C  
ATOM   1036  CA  ASN C 428     290.069 490.9661189.444  1.00 33.69           C  
ATOM   1037  CA  ILE C 429     293.705 489.9981189.173  1.00 31.16           C  
ATOM   1038  CA  ALA C 430     292.765 487.3891186.610  1.00 34.98           C  
ATOM   1039  CA  SER C 431     290.929 490.0831184.618  1.00 38.53           C  
ATOM   1040  CA  VAL C 432     293.634 492.7161184.593  1.00 37.38           C  
ATOM   1041  CA  THR C 433     295.938 489.9611183.491  1.00 38.86           C  
ATOM   1042  CA  GLN C 434     293.852 489.1931180.418  1.00 42.63           C  
ATOM   1043  CA  GLU C 435     293.794 492.8321179.347  1.00 41.28           C  
ATOM   1044  CA  VAL C 436     297.534 492.9931179.947  1.00 33.70           C  
ATOM   1045  CA  ASN C 437     298.090 489.9701177.693  1.00 36.12           C  
ATOM   1046  CA  THR C 438     295.921 491.4891175.003  1.00 38.26           C  
ATOM   1047  CA  ALA C 439     297.602 494.8891175.174  1.00 33.42           C  
ATOM   1048  CA  LYS C 440     301.074 493.3101175.047  1.00 36.12           C  
ATOM   1049  CA  GLY C 441     300.025 491.7331171.778  1.00 36.98           C  
ATOM   1050  CA  ASN C 442     298.689 494.9831170.403  1.00 34.22           C  
ATOM   1051  CA  ILE C 443     301.882 496.7341171.155  1.00 31.70           C  
ATOM   1052  CA  SER C 444     303.909 493.9931169.452  1.00 32.29           C  
ATOM   1053  CA  SER C 445     301.993 494.5361166.290  1.00 32.47           C  
ATOM   1054  CA  LEU C 446     302.461 498.2571166.793  1.00 28.05           C  
ATOM   1055  CA  GLN C 447     306.216 497.9501167.026  1.00 29.60           C  
ATOM   1056  CA  GLY C 448     306.319 496.0061163.788  1.00 29.46           C  
ATOM   1057  CA  ASP C 449     304.074 498.5441162.051  1.00 29.14           C  
ATOM   1058  CA  VAL C 450     306.401 501.3751163.115  1.00 32.26           C  
ATOM   1059  CA  GLN C 451     309.478 499.3291162.200  1.00 38.22           C  
ATOM   1060  CA  ALA C 452     308.030 498.9141158.739  1.00 35.96           C  
ATOM   1061  CA  LEU C 453     307.294 502.6501158.301  1.00 34.01           C  
ATOM   1062  CA  GLN C 454     310.785 503.5421159.586  1.00 34.42           C  
ATOM   1063  CA  GLU C 455     312.454 501.1071157.133  1.00 35.15           C  
ATOM   1064  CA  ALA C 456     310.339 502.3111154.267  1.00 31.68           C  
ATOM   1065  CA  GLY C 457     312.701 505.1051153.203  1.00 32.56           C  
ATOM   1066  CA  TYR C 458     310.139 507.7871152.593  1.00 31.35           C  
ATOM   1067  CA  ILE C 459     311.260 511.1601151.429  1.00 31.40           C  
ATOM   1068  CA  PRO C 460     310.508 514.4881153.082  1.00 32.94           C  
ATOM   1069  CA  GLU C 461     309.075 517.5891151.478  1.00 33.93           C  
ATOM   1070  CA  ALA C 462     311.197 519.4521148.889  1.00 35.50           C  
ATOM   1071  CA  PRO C 463     312.078 523.1441149.568  1.00 37.70           C  
ATOM   1072  CA  ARG C 464     309.197 525.6221149.191  1.00 43.46           C  
ATOM   1073  CA  ASP C 465     310.889 528.4961147.348  1.00 42.68           C  
ATOM   1074  CA  GLY C 466     308.992 528.9551144.088  1.00 41.53           C  
ATOM   1075  CA  GLN C 467     311.265 526.5211142.280  1.00 39.66           C  
ATOM   1076  CA  ALA C 468     310.774 523.0891140.691  1.00 34.55           C  
ATOM   1077  CA  TYR C 469     312.776 520.1351142.034  1.00 33.51           C  
ATOM   1078  CA  VAL C 470     313.488 516.5701140.879  1.00 33.42           C  
ATOM   1079  CA  ARG C 471     314.969 513.5301142.703  1.00 35.41           C  
ATOM   1080  CA  LYS C 472     318.708 512.6891142.442  1.00 39.68           C  
ATOM   1081  CA  ASP C 473     321.065 510.8151144.883  1.00 41.29           C  
ATOM   1082  CA  GLY C 474     319.213 511.5191148.146  1.00 41.26           C  
ATOM   1083  CA  GLU C 475     319.081 515.2901147.473  1.00 40.70           C  
ATOM   1084  CA  TRP C 476     316.347 517.4121145.796  1.00 41.16           C  
ATOM   1085  CA  VAL C 477     317.854 519.1691142.720  1.00 40.33           C  
ATOM   1086  CA  PHE C 478     316.594 522.1821140.782  1.00 34.39           C  
ATOM   1087  CA  LEU C 479     314.895 521.0551137.603  1.00 36.69           C  
ATOM   1088  CA  SER C 480     316.278 524.1571135.830  1.00 44.11           C  
ATOM   1089  CA  THR C 481     319.775 522.5961136.171  1.00 50.73           C  
ATOM   1090  CA  PHE C 482     318.786 520.1901133.357  1.00 57.21           C  
ATOM   1091  CA  LEU C 483     316.135 522.3581131.632  1.00 61.29           C  
TER    1092      LEU C 483                                                      
MASTER      507    0    0    0    0    0    0    6 1089    3    0  114          
END                                                                             
